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Displaying entries 151-200 of 226.
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EC | 3.2.1.151 | ||||||||||||||||||
Accepted name: | xyloglucan-specific endo-β-1,4-glucanase | ||||||||||||||||||
Reaction: | xyloglucan + H2O = xyloglucan oligosaccharides | ||||||||||||||||||
Other name(s): | XEG; xyloglucan endo-β-1,4-glucanase; xyloglucanase; xyloglucanendohydrolase; XH; 1,4-β-D-glucan glucanohydrolase | ||||||||||||||||||
Systematic name: | [(1→6)-α-D-xylo]-(1→4)-β-D-glucan glucanohydrolase | ||||||||||||||||||
Comments: | The enzyme from Aspergillus aculeatus is specific for xyloglucan and does not hydrolyse other cell-wall components. The reaction involves endohydrolysis of 1,4-β-D-glucosidic linkages in xyloglucan with retention of the β-configuration of the glycosyl residues. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 76901-10-5 | ||||||||||||||||||
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EC | 3.2.1.152 | ||||||||||||||||||
Accepted name: | mannosylglycoprotein endo-β-mannosidase | ||||||||||||||||||
Reaction: | Hydrolysis of the α-D-mannosyl-(1→6)-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl sequence of glycoprotein to α-D-mannosyl-(1→6)-D-mannose and N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl sequences | ||||||||||||||||||
Other name(s): | endo-β-mannosidase | ||||||||||||||||||
Comments: | The substrate group is a substituent on N-4 of an asparagine residue in the glycoprotein. The mannose residue at the non-reducing end of the sequence may carry further α-D-mannosyl groups on O-3 or O-6, but such a substituent on O-3 of the β-D-mannosyl group prevents the action of the enzyme. The enzyme was obtained from the lily, Lilium longiflorum. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 141176-95-6 | ||||||||||||||||||
References: |
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EC | 3.2.1.153 | ||||||||||||||||||
Accepted name: | fructan β-(2,1)-fructosidase | ||||||||||||||||||
Reaction: | Hydrolysis of terminal, non-reducing (2→1)-linked β-D-fructofuranose residues in fructans | ||||||||||||||||||
For diagram of reaction, click here | |||||||||||||||||||
Other name(s): | β-(2-1)-D-fructan fructohydrolase; β-(2-1)fructan exohydrolase; inulinase; 1-FEH II; 1-fructan exohydrolase; 1-FEH w1; 1-FEH w2; β-(2-1)-linkage-specific fructan-β-fructosidase; β-(2,1)-D-fructan fructohydrolase | ||||||||||||||||||
Systematic name: | β-(2→1)-D-fructan fructohydrolase | ||||||||||||||||||
Comments: | Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the inulin-type fructans, such as 1-kestose [β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside] and 1,1-nystose [β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl-(2→1)-β-D-fructofuranosyl α-D-glucopyranoside], some (but not all) levan-type fructans can also be hydrolysed, but more slowly [see EC 3.2.1.154, fructan β-(2,6)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1000593-08-7 | ||||||||||||||||||
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EC | 3.2.1.154 | ||||||||||||||||||
Accepted name: | fructan β-(2,6)-fructosidase | ||||||||||||||||||
Reaction: | Hydrolysis of terminal, non-reducing (2→6)-linked β-D-fructofuranose residues in fructans | ||||||||||||||||||
For diagram of reaction, click here | |||||||||||||||||||
Other name(s): | β-(2-6)-fructan exohydrolase; levanase; 6-FEH; β-(2,6)-D-fructan fructohydrolase | ||||||||||||||||||
Systematic name: | (2→6)-β-D-fructan fructohydrolase | ||||||||||||||||||
Comments: | Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the levan-type fructans such as 6-kestotriose [β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl α-D-glucopyranoside] and 6,6-kestotetraose [β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl-(2→6)-β-D-fructofuranosyl α-D-glucopyranoside], some (but not all) inulin-type fructans can also be hydrolysed, but more slowly [cf. EC 3.2.1.153, fructan β-(2,1)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000597-62-5 | ||||||||||||||||||
References: |
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EC | 3.2.1.155 | ||||||||||||||||||
Accepted name: | xyloglucan-specific endo-processive β-1,4-glucanase | ||||||||||||||||||
Reaction: | Hydrolysis of (1→4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the newly-formed chain end after endo-initiation on a polymer molecule | ||||||||||||||||||
Other name(s): | Cel74A; [(1→6)-α-D-xylo]-(1→4)-β-D-glucan exo-glucohydrolase (ambiguous); xyloglucan-specific exo-β-1,4-glucanase (ambiguous) | ||||||||||||||||||
Systematic name: | [(1→6)-α-D-xylo]-(1→4)-β-D-glucan endo-processive glucohydrolase | ||||||||||||||||||
Comments: | The enzyme removes branched oligosaccharides, containing preferentially four glucoside residues in the main chain, from xyloglucan molecules in a processive manner after the initial endo-type attack on a polysaccharide [1-5]. Hydrolysis occurs at either the unsubstituted D-glucopyranose residue in the main backbone and/or the D-glucopyranose residue bearing a xylosyl group [1-5]. The enzyme does not display activity, or shows very low activity, towards other β-D-glucans [1,2,4,5]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000598-79-7 | ||||||||||||||||||
References: |
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EC | 3.2.1.156 | ||||||||||||||||||
Accepted name: | oligosaccharide reducing-end xylanase | ||||||||||||||||||
Reaction: | Hydrolysis of (1→4)-β-D-xylose residues from the reducing end of oligosaccharides | ||||||||||||||||||
Other name(s): | Rex; reducing end xylose-releasing exo-oligoxylanase | ||||||||||||||||||
Systematic name: | β-D-xylopyranosyl-(1→4)-β-D-xylopyranose reducing-end xylanase | ||||||||||||||||||
Comments: | The enzyme, originally isolated from the bacterium Bacillus halodurans C-125, releases the xylose unit at the reducing end of oligosaccharides ending with the structure β-D-xylopyranosyl-(1→4)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranose, leaving the new reducing end in the α configuration. It is specific for the β anomers of xylooligosaccharides whose degree of polymerization is equal to or greater than 3. The penultimate residue must be β-D-xylopyranose, but replacing either of the flanking residues with glucose merely slows the rate greatly. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 879497-03-7 | ||||||||||||||||||
References: |
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EC | 3.2.1.157 | ||||||||||||||||||
Accepted name: | ι-carrageenase | ||||||||||||||||||
Reaction: | Endohydrolysis of (1→4)-β-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in ι-carrageenans | ||||||||||||||||||
For diagram of reaction, click here | |||||||||||||||||||
Glossary: | In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not. For example: ι-neocarrabiose = 3,6-anhydro-2-O-sulfo-α-D-galactopyranosyl-(1→3)-4-O-sulfo-D-galactose ι-carrabiose = 4-O-sulfo-β-D-galactopyranosyl-(1→4)-3,6-anhydro-2-O-sulfo-D-galactose |
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Systematic name: | ι-carrageenan 4-β-D-glycanohydrolase (configuration-inverting) | ||||||||||||||||||
Comments: | The main products of hydrolysis are ι-neocarratetraose sulfate and ι-neocarrahexaose sulfate. ι-Neocarraoctaose is the shortest substrate oligomer that can be cleaved. Unlike EC 3.2.1.81, β-agarase and EC 3.2.1.83, κ-carrageenase, this enzyme proceeds with inversion of the anomeric configuration. ι-Carrageenan differs from κ-carrageenan by possessing a sulfo group on O-2 of the 3,6-anhydro-D-galactose residues, in addition to that present in the κ-compound on O-4 of the D-galactose residues. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50936-37-3 | ||||||||||||||||||
References: |
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EC | 3.2.1.158 | ||||||||||||||||||
Accepted name: | α-agarase | ||||||||||||||||||
Reaction: | Endohydrolysis of (1→3)-α-L-galactosidic linkages in agarose, yielding agarotetraose as the major product | ||||||||||||||||||
Glossary: | agarose = a linear polysaccharide produced by some members of the Rhodophyta (red algae) made up from alternating D-galactose and 3,6-anhydro-α-L-galactopyranose residues joined by α-(1→3)- and β-(1→4)-linkages. In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not. For example: neoagarobiose = 3,6-anhydro-α-L-galactopyranosyl-(1→3)-D-galactose agarobiose = β-D-galactopyranosyl-(1→4)-3,6-anhydro-L-galactose |
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Other name(s): | agarase (ambiguous); agaraseA33 | ||||||||||||||||||
Systematic name: | agarose 3-glycanohydrolase | ||||||||||||||||||
Comments: | Requires Ca2+. The enzyme from Thalassomonas sp. can use agarose, agarohexaose and neoagarohexaose as substrate. The products of agarohexaose hydrolysis are dimers and tetramers, with agarotetraose being the predominant product, whereas hydrolysis of neoagarohexaose gives rise to two types of trimer. While the enzyme can also hydrolyse the highly sulfated agarose porphyran very efficiently, it cannot hydrolyse the related compounds κ-carrageenan (see EC 3.2.1.83) and ι-carrageenan (see EC 3.2.1.157) [2]. See also EC 3.2.1.81, β-agarase. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63952-00-1 | ||||||||||||||||||
References: |
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EC | 3.2.1.159 | ||||||||||||||||||
Accepted name: | α-neoagaro-oligosaccharide hydrolase | ||||||||||||||||||
Reaction: | Hydrolysis of the (1→3)-α-L-galactosidic linkages of neoagaro-oligosaccharides that are smaller than a hexamer, yielding 3,6-anhydro-L-galactose and D-galactose | ||||||||||||||||||
Glossary: | In the field of oligosaccharides derived from agarose, carrageenans, etc., in which alternate residues are 3,6-anhydro sugars, the prefix ’neo’ designates an oligosaccharide whose non-reducing end is the anhydro sugar, and the absence of this prefix means that it is not. For example: neoagarobiose = 3,6-anhydro-α-L-galactopyranosyl-(1→3)-D-galactose agarobiose = β-D-galactopyranosyl-(1→4)-3,6-anhydro-L-galactose |
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Other name(s): | α-neoagarooligosaccharide hydrolase; α-NAOS hydrolase | ||||||||||||||||||
Systematic name: | α-neoagaro-oligosaccharide 3-glycohydrolase | ||||||||||||||||||
Comments: | When neoagarohexaose is used as a substrate, the oligosaccharide is cleaved at the non-reducing end to produce 3,6-anhydro-L-galactose and agaropentaose, which is further hydrolysed to agarobiose and agarotriose. With neoagarotetraose as substrate, the products are predominantly agarotriose and 3,6-anhydro-L-galactose. In Vibrio sp. the actions of EC 3.2.1.81, β-agarase and EC 3.2.1.159 can be used to degrade agarose to 3,6-anhydro-L-galactose and D-galactose. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60063-77-6 | ||||||||||||||||||
References: |
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EC | 3.2.1.160 | ||||||||||||||||||
Deleted entry: | xyloglucan-specific exo-β-1,4-glucanase. The enzyme was shown to be identical to EC 3.2.1.155, xyloglucan-specific exo-β-1,4-glucanase, during the public-review process so was withdrawn before being made official | ||||||||||||||||||
EC | 3.2.1.161 | ||||||||||||||||||
Accepted name: | β-apiosyl-β-glucosidase | ||||||||||||||||||
Reaction: | 7-[β-D-apiofuranosyl-(1→6)-β-D-glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid + β-D-apiofuranosyl-(1→6)-D-glucose | ||||||||||||||||||
Other name(s): | isoflavonoid-7-O-β[D-apiosyl-(1→6)-β-D-glucoside] disaccharidase; isoflavonoid 7-O-β-apiosyl-glucoside β-glucosidase; furcatin hydrolase | ||||||||||||||||||
Systematic name: | 7-[β-D-apiofuranosyl-(1→6)-β-D-glucopyranosyloxy]isoflavonoid β-D-apiofuranosyl-(1→6)-D-glucohydrolase | ||||||||||||||||||
Comments: | The enzyme from the tropical tree Dalbergia nigrescens Kurz belongs in glycosyl hydrolase family 1. The enzyme removes disaccharides from the natural substrates dalpatein 7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside and 7-hydroxy-2′,4′,5′,6-tetramethoxy-7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside (dalnigrein 7-O-β-D-apiofuranosyl-(1→6)-β-D-glucopyranoside) although it can also remove a single glucose residue from isoflavonoid 7-O-glucosides [2]. Daidzin and genistin are also substrates. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 1000598-83-3 | ||||||||||||||||||
References: |
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EC | 3.2.1.162 | ||||||||||||||||||
Accepted name: | λ-carrageenase | ||||||||||||||||||
Reaction: | Endohydrolysis of (1→4)-β-linkages in the backbone of λ-carrageenan, resulting in the tetrasaccharide α-D-Galp2,6S2-(1→3)-β-D-Galp2S-(1→4)-α-D-Galp2,6S2-(1→3)-D-Galp2S | ||||||||||||||||||
For diagram of reaction, click here | |||||||||||||||||||
Glossary: | For diagram of the structures of carrageenans, click here | ||||||||||||||||||
Other name(s): | endo-β-1,4-carrageenose 2,6,2′-trisulfate-hydrolase | ||||||||||||||||||
Systematic name: | endo-(1→4)-β-carrageenose 2,6,2′-trisulfate-hydrolase | ||||||||||||||||||
Comments: | The enzyme from Pseudoalteromonas sp. is specific for λ-carrageenan. ι-Carrageenan (see EC 3.2.1.157, ι-carrageenase), κ-carrageenan (see EC 3.2.1.83, κ-carrageenase), agarose and porphyran are not substrates. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.163 | ||||||||||||||||||
Accepted name: | 1,6-α-D-mannosidase | ||||||||||||||||||
Reaction: | Hydrolysis of the (1→6)-linked α-D-mannose residues in α-D-Manp-(1→6)-D-Manp | ||||||||||||||||||
Systematic name: | (1→6)-α-mannosyl α-D-mannohydrolase | ||||||||||||||||||
Comments: | The enzyme is specific for (1→6)-linked mannobiose and has no activity towards any other linkages, or towards p-nitrophenyl-α-D-mannopyranoside or baker’s yeast mannan. It is strongly inhibited by Mn2+ but does not require Ca2+ or any other metal cofactor for activity. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY | ||||||||||||||||||
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EC | 3.2.1.164 | ||||||||||||||||||
Accepted name: | galactan endo-1,6-β-galactosidase | ||||||||||||||||||
Reaction: | Endohydrolysis of (1→6)-β-D-galactosidic linkages in arabinogalactan proteins and (1→3):(1→6)-β-galactans to yield galactose and (1→6)-β-galactobiose as the final products | ||||||||||||||||||
Other name(s): | endo-1,6-β-galactanase | ||||||||||||||||||
Systematic name: | endo-β-(1→6)-galactanase | ||||||||||||||||||
Comments: | The enzyme specifically hydrolyses 1,6-β-D-galactooligosaccharides with a degree of polymerization (DP) higher than 3, and their acidic derivatives with 4-O-methylglucosyluronate or glucosyluronate groups at the non-reducing terminals [2]. 1,3-β-D- and 1,4-β-D-galactosyl residues cannot act as substrates. The enzyme can also hydrolyse α-L-arabinofuranosidase-treated arabinogalactan protein (AGP) extracted from radish roots [2,3]. AGPs are thought to be involved in many physiological events, such as cell division, cell expansion and cell death [3]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.165 | ||||||||||||||||||
Accepted name: | exo-1,4-β-D-glucosaminidase | ||||||||||||||||||
Reaction: | Hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini | ||||||||||||||||||
Glossary: | GlcN = D-glucosamine = 2-amino-2-deoxy-D-glucopyranose GlcNAc = N-acetyl-D-glucosamine |
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Other name(s): | CsxA; GlcNase; exochitosanase; GlmA; exo-β-D-glucosaminidase; chitosan exo-1,4-β-D-glucosaminidase | ||||||||||||||||||
Systematic name: | chitosan exo-(1→4)-β-D-glucosaminidase | ||||||||||||||||||
Comments: | Chitosan is a partially or totally N-deacetylated chitin derivative that is found in the cell walls of some phytopathogenic fungi and comprises D-glucosamine residues with a variable content of GlcNAc residues [4]. Acts specifically on chitooligosaccharides and chitosan, having maximal activity on chitotetraose, chitopentaose and their corresponding alcohols [1]. The enzyme can degrade GlcN-GlcNAc but not GlcNAc-GlcNAc [3]. A member of the glycoside hydrolase family 2 (GH-2) [4]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.166 | ||||||||||||||||||
Accepted name: | heparanase | ||||||||||||||||||
Reaction: | endohydrolysis of (1→4)-β-D-glycosidic bonds of heparan sulfate chains in heparan sulfate proteoglycan | ||||||||||||||||||
Other name(s): | Hpa1 heparanase; Hpa1; heparanase 1; heparanase-1; C1A heparanase; HPSE | ||||||||||||||||||
Systematic name: | heparan sulfate N-sulfo-D-glucosamine endoglucanase | ||||||||||||||||||
Comments: | Heparanase cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group [2]. Heparanase-1 cuts macromolecular heparin into fragments of 5000–20000 Da [5]. The enzyme cleaves the heparan sulfate glycosaminoglycans from proteoglycan core proteins and degrades them to small oligosaccharides. Inside cells, the enzyme is important for the normal catabolism of heparan sulfate proteoglycans, generating glycosaminoglycan fragments that are then transported to lysosomes and completely degraded. When secreted, heparanase degrades basement membrane heparan sulfate glycosaminoglycans at sites of injury or inflammation, allowing extravasion of immune cells into nonvascular spaces and releasing factors that regulate cell proliferation and angiogenesis [1]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
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EC | 3.2.1.167 | ||||||||||||||||||
Accepted name: | baicalin-β-D-glucuronidase | ||||||||||||||||||
Reaction: | baicalin + H2O = baicalein + D-glucuronate | ||||||||||||||||||
Glossary: | baicalin = 5,6,7-trihydroxyflavone-7-O-β-D-glucuronate = 5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl β-D-glucupyranosiduronic acid baicalein = 5,6,7-trihydroxyflavone = 5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one wogonin = 5,7-dihydroxy-8-methoxyflavone = 5,7-dihydroxy-8-methoxy-2-phenyl-4H-chromen-4-one oroxylin = 5,7-dihydroxy-6-methoxyflavone = 5,7-dihydroxy-6-methoxy-2-phenyl-4H-1-benzopyran-4-one |
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Other name(s): | baicalinase | ||||||||||||||||||
Systematic name: | 5,6,7-trihydroxyflavone-7-O-β-D-glucupyranosiduronate glucuronosylhydrolase | ||||||||||||||||||
Comments: | The enzyme also hydrolyses wogonin 7-O-β-D-glucuronide and oroxylin 7-O-β-D-glucuronide with lower efficiency [4]. Neglegible activity with p-nitrophenyl-β-D-glucuronide [2]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.168 | ||||||||||||||||||
Accepted name: | hesperidin 6-O-α-L-rhamnosyl-β-D-glucosidase | ||||||||||||||||||
Reaction: | hesperidin + H2O = hesperetin + rutinose | ||||||||||||||||||
Glossary: | hesperetin = 5,7,3′-trihydroxy-4′-methoxyflavanone hesperidin = hesperetin 7-(6-O-α-L-rhamnopyranosyl-β-D-glucopyranoside) rutinose = 6-O-α-L-rhamnopyranosyl-D-glucose |
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Other name(s): | AnRut; rutinosidase | ||||||||||||||||||
Systematic name: | hesperetin 7-(6-O-α-L-rhamnopyranosyl-β-D-glucopyranoside) 6-O-α-rhamnopyranosyl-β-glucohydrolase | ||||||||||||||||||
Comments: | The enzyme exhibits high specificity towards 7-O-linked flavonoid β-rutinosides. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.169 | ||||||||||||||||||
Accepted name: | protein O-GlcNAcase | ||||||||||||||||||
Reaction: | (1) [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine (2) [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-theronine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine |
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Other name(s): | OGA; glycoside hydrolase O-GlcNAcase; O-GlcNAcase; BtGH84; O-GlcNAc hydrolase | ||||||||||||||||||
Systematic name: | [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase | ||||||||||||||||||
Comments: | Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.170 | ||||||||||||||||||
Accepted name: | mannosylglycerate hydrolase | ||||||||||||||||||
Reaction: | 2-O-(α-D-mannopyranosyl)-D-glycerate + H2O = D-mannopyranose + D-glycerate | ||||||||||||||||||
Other name(s): | MgH | ||||||||||||||||||
Systematic name: | 2-O-(α-D-mannopyranosyl)-D-glycerate D-mannohydrolase | ||||||||||||||||||
Comments: | The enzyme occurs in thermophilic bacteria and has been characterized in Thermus thermophilus and Rubrobacter radiotolerans. It also has been identified in the moss Selaginella moellendorffii. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.171 | ||||||||||||||||||
Accepted name: | rhamnogalacturonan hydrolase | ||||||||||||||||||
Reaction: | Endohydrolysis of α-D-GalA-(1→2)-α-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with β-D-GalA at the reducing end. | ||||||||||||||||||
Other name(s): | rhamnogalacturonase A; RGase A; RG-hydrolase | ||||||||||||||||||
Systematic name: | rhamnogalacturonan α-D-GalA-(1→2)-α-L-Rha hydrolase | ||||||||||||||||||
Comments: | The enzyme is part of the degradation system for rhamnogalacturonan I in Aspergillus aculeatus. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.172 | ||||||||||||||||||
Accepted name: | unsaturated rhamnogalacturonyl hydrolase | ||||||||||||||||||
Reaction: | 2-O-(4-deoxy-β-L-threo-hex-4-enopyranuronosyl)-α-L-rhamnopyranose + H2O = 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose | ||||||||||||||||||
For diagram of ramnosylgalacturan degradation, click here | |||||||||||||||||||
Glossary: | 6-deoxy-2-O-(4-deoxy-β-L-threo-hex-4-enopyranuronosyl)-α-L-mannopyranose = 2-O-(4-deoxy-β-L-threo-hex-4-enopyranuronosyl)-α-L-rhamnopyranose 5-dehydro-4-deoxy-D-glucuronate = (4S,5R)-4,5-dihydroxy-2,6-dioxohexanoate |
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Other name(s): | YteR; YesR | ||||||||||||||||||
Systematic name: | 2-O-(4-deoxy-β-L-threo-hex-4-enopyranuronosyl)-α-L-rhamnopyranose hydrolase | ||||||||||||||||||
Comments: | The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.173 | ||||||||||||||||||
Accepted name: | rhamnogalacturonan galacturonohydrolase | ||||||||||||||||||
Reaction: | Exohydrolysis of the α-D-GalA-(1→2)-α-L-Rha bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing D-galacturonic acid from the non-reducing end of rhamnogalacturonan oligosaccharides. | ||||||||||||||||||
Other name(s): | RG-galacturonohydrolase | ||||||||||||||||||
Systematic name: | rhamnogalacturonan oligosaccharide α-D-GalA-(1→2)-α-L-Rha galacturonohydrolase | ||||||||||||||||||
Comments: | The enzyme is part of the degradation system for rhamnogalacturonan I in Aspergillus aculeatus. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.174 | ||||||||||||||||||
Accepted name: | rhamnogalacturonan rhamnohydrolase | ||||||||||||||||||
Reaction: | Exohydrolysis of the α-L-Rha-(1→4)-α-D-GalA bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing β-L-rhamnose from the non-reducing end of rhamnogalacturonan oligosaccharides. | ||||||||||||||||||
Other name(s): | RG-rhamnohydrolase; RG α-L-rhamnopyranohydrolase | ||||||||||||||||||
Systematic name: | rhamnogalacturonan oligosaccharide α-L-Rha-(1→4)-α-D-GalA rhamnohydrolase | ||||||||||||||||||
Comments: | The enzyme is part of the degradation system for rhamnogalacturonan I in Aspergillus aculeatus. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.175 | ||||||||||||||||||
Accepted name: | β-D-glucopyranosyl abscisate β-glucosidase | ||||||||||||||||||
Reaction: | D-glucopyranosyl abscisate + H2O = D-glucose + abscisate | ||||||||||||||||||
For diagram of abscisic-acid biosynthesis, click here | |||||||||||||||||||
Other name(s): | AtBG1; ABA-β-D-glucosidase; ABA-specific β-glucosidase; ABA-GE hydrolase; β-D-glucopyranosyl abscisate hydrolase | ||||||||||||||||||
Systematic name: | β-D-glucopyranosyl abscisate glucohydrolase | ||||||||||||||||||
Comments: | The enzyme hydrolzes the biologically inactive β-D-glucopyranosyl ester of abscisic acid to produce active abscisate. Abscisate is a phytohormone critical for plant growth, development and adaption to various stress conditions. The enzyme does not hydrolyse β-D-glucopyranosyl zeatin [1]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.176 | ||||||||||||||||||
Accepted name: | cellulose 1,4-β-cellobiosidase (reducing end) | ||||||||||||||||||
Reaction: | Hydrolysis of (1→4)-β-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains. | ||||||||||||||||||
Other name(s): | CelS; CelSS; endoglucanase SS; cellulase SS; cellobiohydrolase CelS; Cel48A | ||||||||||||||||||
Systematic name: | 4-β-D-glucan cellobiohydrolase (reducing end) | ||||||||||||||||||
Comments: | Some exocellulases, most of which belong to the glycoside hydrolase family 48 (GH48, formerly known as cellulase family L), act at the reducing ends of cellulose and similar substrates. The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism [2]. Different from EC 3.2.1.91, which attacks cellulose from the non-reducing end. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.177 | ||||||||||||||||||
Accepted name: | α-D-xyloside xylohydrolase | ||||||||||||||||||
Reaction: | Hydrolysis of terminal, non-reducing α-D-xylose residues with release of α-D-xylose. | ||||||||||||||||||
Other name(s): | α-xylosidase | ||||||||||||||||||
Systematic name: | α-D-xyloside xylohydrolase | ||||||||||||||||||
Comments: | The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide. Representative α-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.178 | ||||||||||||||||||
Accepted name: | β-porphyranase | ||||||||||||||||||
Reaction: | Hydrolysis of β-D-galactopyranose-(1→4)-α-L-galactopyranose-6-sulfate linkages in porphyran | ||||||||||||||||||
Other name(s): | porphyranase; PorA; PorB; endo-β-porphyranase | ||||||||||||||||||
Systematic name: | porphyran β-D-galactopyranose-(1→4)-α-L-galactopyranose-6-sulfate 4-glycanohydrolase | ||||||||||||||||||
Comments: | The backbone of porphyran consists largely (~70%) of (1→3)-linked β-D-galactopyranose followed by (1→4)-linked α-L-galactopyranose-6-sulfate [the other 30% are mostly agarobiose repeating units of (1→3)-linked β-D-galactopyranose followed by (1→4)-linked 3,6-anhydro-α-L-galactopyranose] [2]. This enzyme cleaves the (1→4) linkages between β-D-galactopyranose and α-L-galactopyranose-6-sulfate, forming mostly the disaccharide α-L-galactopyranose-6-sulfate-(1→3)-β-D-galactose, although some longer oligosaccharides of even number of residues are also observed. Since the enzyme is inactive on the non-sulfated agarose portion of the porphyran backbone, some agarose fragments are also included in the products [1]. Methylation of the D-galactose prevents the enzyme from Zobellia galactanivorans, but not that from Wenyingzhuangia fucanilytica, from binding at subsite -1 [2,3]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.179 | ||||||||||||||||||
Accepted name: | gellan tetrasaccharide unsaturated glucuronosyl hydrolase | ||||||||||||||||||
Reaction: | β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp + H2O = 5-dehydro-4-deoxy-D-glucuronate + β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp | ||||||||||||||||||
Glossary: | 5-dehydro-4-deoxy-D-glucuronate = (4S,5R)-4,5-dihydroxy-2,6-dioxohexanoate β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GalNAc = 3-(4-deoxy-β-D-gluc-4-enuronosyl)-N-acetyl-D-galactosamine = 3-(4-deoxy-α-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-galactose |
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Other name(s): | UGL (ambiguous); unsaturated glucuronyl hydrolase (ambiguous); gellan tetrasaccharide unsaturated glucuronyl hydrolase | ||||||||||||||||||
Systematic name: | β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp β-D-4-deoxy-Δ4-GlcAp hydrolase | ||||||||||||||||||
Comments: | The enzyme releases 4-deoxy-4(5)-unsaturated D-glucuronic acid from oligosaccharides produced by polysaccharide lyases, e.g. the tetrasaccharide β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp produced by EC 4.2.2.25, gellan lyase. The enzyme can also hydrolyse unsaturated chondroitin and hyaluronate disaccharides (β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GalNAc, β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GalNAc6S, β-D-4-deoxy-Δ4-GlcAp2S-(1→3)-D-GalNAc, β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GlcNAc), preferring the unsulfated disaccharides to the sulfated disaccharides. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.180 | ||||||||||||||||||
Accepted name: | unsaturated chondroitin disaccharide hydrolase | ||||||||||||||||||
Reaction: | β-D-4-deoxy-Δ4-GlcAp-(1→3)-β-D-GalNAc6S + H2O = 5-dehydro-4-deoxy-D-glucuronate + N-acetyl-β-D-galactosamine-6-O-sulfate | ||||||||||||||||||
Glossary: | 5-dehydro-4-deoxy-D-glucuronate = (4S,5R)-4,5-dihydroxy-2,6-dioxohexanoate | ||||||||||||||||||
Other name(s): | UGL (ambiguous); unsaturated glucuronyl hydrolase (ambiguous) | ||||||||||||||||||
Systematic name: | β-D-4-deoxy-Δ4-GlcAp-(1→3)-β-D-GalNAc6S hydrolase | ||||||||||||||||||
Comments: | The enzyme releases 4-deoxy-4,5-didehydro D-glucuronic acid or 4-deoxy-4,5-didehydro L-iduronic acid from chondroitin disaccharides, hyaluronan disaccharides and heparin disaccharides and cleaves both glycosidic (1→3) and (1→4) bonds. It prefers the sulfated disaccharides to the unsulfated disaccharides. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.181 | ||||||||||||||||||
Accepted name: | galactan endo-β-1,3-galactanase | ||||||||||||||||||
Reaction: | The enzyme specifically hydrolyses β-1,3-galactan and β-1,3-galactooligosaccharides | ||||||||||||||||||
Other name(s): | endo-β-1,3-galactanase | ||||||||||||||||||
Systematic name: | arabinogalactan 3-β-D-galactanohydrolase | ||||||||||||||||||
Comments: | The enzyme from the fungus Flammulina velutipes (winter mushroom) hydrolyses the β(1→3) bonds found in type II plant arabinogalactans, which occur in cell walls of dicots and cereals. The enzyme is an endohydrolase, and requires at least 3 contiguous β-1,3-residues. cf. EC 3.2.1.89, arabinogalactan endo-β-1,4-galactanase and EC 3.2.1.145, galactan 1,3-β-galactosidase. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.182 | ||||||||||||||||||
Accepted name: | 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside β-D-glucosidase | ||||||||||||||||||
Reaction: | (1) (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + H2O =
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + D-glucose (2) (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside + H2O = 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + D-glucose |
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Glossary: | DIMBOA glucoside = (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside DIBOA glucoside = (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside |
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Other name(s): | DIMBOAGlc hydrolase; DIMBOA glucosidase | ||||||||||||||||||
Systematic name: | (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl β-D-glucopyranoside β-D-glucosidase | ||||||||||||||||||
Comments: | The enzyme from Triticum aestivum (wheat) has a higher affinity for DIMBOA glucoside than DIBOA glucoside. With Secale cereale (rye) the preference is reversed. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.183 | ||||||||||||||||||
Accepted name: | UDP-N-acetylglucosamine 2-epimerase (hydrolysing) | ||||||||||||||||||
Reaction: | UDP-N-acetyl-α-D-glucosamine + H2O = N-acetyl-D-mannosamine + UDP | ||||||||||||||||||
For diagram of N-acetylneuraminic acid biosynthesis, click here, and for mechanism, click here | |||||||||||||||||||
Other name(s): | UDP-N-acetylglucosamine 2-epimerase (ambiguous); GNE (gene name); siaA (gene name); neuC (gene name) | ||||||||||||||||||
Systematic name: | UDP-N-acetyl-α-D-glucosamine hydrolase (2-epimerising) | ||||||||||||||||||
Comments: | The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus. It catalyses the first step of sialic acid (N-acetylneuraminic acid) biosynthesis. The initial product formed is the α anomer, which rapidly mutarotates to a mixture of anomers [2]. The mammalian enzyme is bifunctional and also catalyses EC 2.7.1.60, N-acetylmannosamine kinase. cf. EC 5.1.3.14, UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.184 | ||||||||||||||||||
Accepted name: | UDP-N,N′-diacetylbacillosamine 2-epimerase (hydrolysing) | ||||||||||||||||||
Reaction: | UDP-N,N′-diacetylbacillosamine + H2O = UDP + 2,4-diacetamido-2,4,6-trideoxy-D-mannopyranose | ||||||||||||||||||
For diagram of legionaminic acid biosynthesis, click here, and for mechanism, click here | |||||||||||||||||||
Glossary: | UDP-N,N′-diacetylbacillosamine = UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose | ||||||||||||||||||
Other name(s): | UDP-Bac2Ac4Ac 2-epimerase; NeuC | ||||||||||||||||||
Systematic name: | UDP-N,N′-diacetylbacillosamine hydrolase (2-epimerising) | ||||||||||||||||||
Comments: | Requires Mg2+. Involved in biosynthesis of legionaminic acid, a nonulosonate derivative that is incorporated by some bacteria into assorted virulence-associated cell surface glycoconjugates. The initial product formed by the enzyme from Legionella pneumophila, which incorporates legionaminic acid into the O-antigen moiety of its lipopolysaccharide, is 2,4-diacetamido-2,4,6-trideoxy-α-D-mannopyranose, which rapidly mutarotates to a mixture of anomers [1]. The enzyme from Campylobacter jejuni, which incorporates legionaminic acid into flagellin, prefers GDP-N,N′-diacetylbacillosamine [2]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.185 | ||||||||||||||||||
Accepted name: | non-reducing end β-L-arabinofuranosidase | ||||||||||||||||||
Reaction: | β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose + H2O = 2 β-L-arabinofuranose | ||||||||||||||||||
Other name(s): | HypBA1 | ||||||||||||||||||
Systematic name: | β-L-arabinofuranoside non-reducing end β-L-arabinofuranosidase | ||||||||||||||||||
Comments: | The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, removes the β-L-arabinofuranose residue from the non-reducing end of multiple substrates, including β-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara2-Hyp, Ara3-Hyp, and β-L-arabinofuranosyl-(1→2)-1-O-methyl-β-L-arabinofuranose.In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. cf. EC 3.2.1.55, non-reducing end α-L-arabinofuranosidase | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.186 | ||||||||||||||||||
Accepted name: | protodioscin 26-O-β-D-glucosidase | ||||||||||||||||||
Reaction: | protodioscin + H2O = 26-deglucoprotodioscin + D-glucose | ||||||||||||||||||
Other name(s): | F26G; torvosidase; CSF26G1; furostanol glycoside 26-O-β-D-glucosidase; furostanol 26-O-β-D-glucoside glucohydrolase | ||||||||||||||||||
Systematic name: | protodioscin glucohydrolase | ||||||||||||||||||
Comments: | The enzyme has been characterized from the plants Cheilocostus speciosus and Solanum torvum. It also hydrolyses the 26-β-D-glucose group from related steroid glucosides such as protogracillin, torvoside A and torvoside H. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.187 | ||||||||||||||||||
Accepted name: | (Ara-f)3-Hyp β-L-arabinobiosidase | ||||||||||||||||||
Reaction: | 4-O-(β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + H2O = 4-O-(β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose | ||||||||||||||||||
Glossary: | 4-O-(β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline = (Ara-f)3-Hyp | ||||||||||||||||||
Other name(s): | hypBA2 (gene name); β-L-arabinobiosidase | ||||||||||||||||||
Systematic name: | 4-O-(β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline β-L-arabinofuranosyl-(1→2)-β-L-arabinofuranose hydrolase | ||||||||||||||||||
Comments: | The enzyme, which was identified in the bacterium Bifidobacterium longum JCM1217, is specific for (Ara-f)3-Hyp, a sugar chain found in hydroxyproline-rich glyoproteins such as extensin and lectin. The enzyme was not able to accept (Ara-f)2-Hyp or (Ara-f)4-Hyp as substrates. In the presence of 1-alkanols, the enzyme demonstrates transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.188 | ||||||||||||||||||
Accepted name: | avenacosidase | ||||||||||||||||||
Reaction: | avenacoside B + H2O = 26-desgluco-avenacoside B + D-glucose | ||||||||||||||||||
Glossary: | avenacoside B = (22S,25S)-3β-{β-D-glucopyranosyl-(1→3)-β-D-glucopyranosyl-(1→4)-[α-L-rhamnopyranosyl-(1→2)]-β-D-glucopyranosyloxy}-26-(β-D-glucopyranosyloxy)-22,25-epoxyfurost-5-ene 26-desgluco-avenacoside B = (22S,25S)-3β-{β-D-glucopyranosyl-(1→3)-β-D-glucopyranosyl-(1→4)-[α-L-rhamnopyranosyl-(1→2)]-β-D-glucopyranosyloxy}-22,25-epoxyfurost-5-en-26-ol |
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Other name(s): | As-P60 | ||||||||||||||||||
Systematic name: | avenacoside B 26-β-D-glucohydrolase | ||||||||||||||||||
Comments: | Isolated from oat (Avena sativa) seedlings. The product acts as a defense system against fungal infection. Also acts on avenacoside A. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.189 | ||||||||||||||||||
Accepted name: | dioscin glycosidase (diosgenin-forming) | ||||||||||||||||||
Reaction: | 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin + 3 H2O = D-glucose + 2 L-rhamnose + diosgenin | ||||||||||||||||||
For diagram of diosgenin catabolism, click here | |||||||||||||||||||
Glossary: | 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin = (3β,25R)-spirost-5-en-3-yl 6-deoxy-α-L-mannopyranosyl-(1→2)-[6-deoxy-α-L-mannopyranosyl-(1→4)]-β-D-glucopyranoside = dioscin diosgenin = (3β,25R)-spirost-5-en-3-ol |
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Other name(s): | dioscin glycosidase (aglycone-forming) | ||||||||||||||||||
Systematic name: | 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin hydrolase (diosgenin-forming) | ||||||||||||||||||
Comments: | The enzyme is involved in degradation of the steroid saponin dioscin by some fungi of the Absidia genus. The enzyme can also hydrolyse 3-O-[α-L-Ara-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin into diosgenin and free sugars as the final products. cf. EC 3.2.1.190, dioscin glycosidase (3-O-β-D-Glc-diosgenin-forming). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.190 | ||||||||||||||||||
Accepted name: | dioscin glycosidase (3-O-β-D-Glc-diosgenin-forming) | ||||||||||||||||||
Reaction: | 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin + 2 H2O = 2 L-rhamnopyranose + diosgenin 3-O-β-D-glucopyranoside | ||||||||||||||||||
For diagram of diosgenin catabolism, click here | |||||||||||||||||||
Glossary: | 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin = (3β,25R)-spirost-5-en-3-yl 6-deoxy-α-L-mannopyranosyl-(1→2)-[6-deoxy-α-L-mannopyranosyl-(1→4)]-β-D-glucopyranoside = dioscin diosgenin = (3β,25R)-spirost-5-en-3-ol |
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Other name(s): | dioscin-α-L-rhamnosidase | ||||||||||||||||||
Systematic name: | 3-O-[α-L-Rha-(1→4)-[α-L-Rha-(1→2)]-β-D-Glc]diosgenin (3-O-β-D-Glc-diosgenin-forming) | ||||||||||||||||||
Comments: | The enzyme is involved in the hydrolysis of the steroid saponin dioscin by the digestive system of Sus scrofa (pig). cf. EC 3.2.1.189, dioscin glycosidase (diosgenin-forming). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.191 | ||||||||||||||||||
Accepted name: | ginsenosidase type III | ||||||||||||||||||
Reaction: | a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + 2 H2O = a protopanaxadiol-type ginsenoside with no glycosidic modification at position 3 + 2 D-glucopyranose (overall reaction) (1a) a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + H2O a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + D-glucopyranose (1b) a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + H2O = a protopanaxadiol-type ginsenoside with no glycosidic modification at position 3 + D-glucopyranose |
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For diagram of protopanaxadiol ginsenosides ginsenosidases, click here | |||||||||||||||||||
Glossary: | ginsenoside Rb1 = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol gypenoside XVII = 3β-(β-D-glucopyranosyloxy)-20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol gypenoside LXXV = 20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-ene-3β,12β-diol |
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Systematic name: | protopanaxadiol-type ginsenoside 3-β-D-hydrolase | ||||||||||||||||||
Comments: | Ginsenosidase type III catalyses the sequential hydrolysis of the 3-O-β-D-(1→2)-glucopyranosyl bond followed by hydrolysis of the 3-O-β-D-glucopyranosyl bond of protopanaxadiol ginsenosides. When acting for example on ginsenoside Rb1 the enzyme first generates ginsenoside XVII, and subsequently ginsenoside LXXV. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.192 | ||||||||||||||||||
Accepted name: | ginsenoside Rb1 β-glucosidase | ||||||||||||||||||
Reaction: | ginsenoside Rb1 + 2 H2O = ginsenoside Rg3 + 2 D-glucopyranose (overall reaction) (1a) ginsenoside Rb1 + H2O = ginsenoside Rd + D-glucopyranose (1b) ginsenoside Rd + H2O = ginsenoside Rg3 + D-glucopyranose |
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For diagram of protopanaxadiol ginsenosides ginsenosidases, click here | |||||||||||||||||||
Glossary: | ginsenoside Rb1 = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol ginsenoside Rd = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-(β-D-glucopyranosyloxy)dammar-24-en-12β-ol ginsenoside F2 = 3β,20-bis(β-D-glucopyranosyloxy)dammar-24-en-12β-ol |
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Systematic name: | ginsenoside Rb1 glucohydrolase | ||||||||||||||||||
Comments: | Ginsenosidases catalyse the hydrolysis of glycosyl moieties attached to the C-3, C-6 or C-20 position of ginsenosides. They are specific with respect to the nature of the glycosidic linkage, the position and the order in which the linkages are cleaved. Ginsenoside Rb1 β-glucosidase specifically and sequentially hydrolyses the 20-[β-D-glucopyranosyl-(1→6)-β-D glucopyranosyloxy] residues attached to position 20 by first hydrolysing the (1→6)-glucosidic bond to generate ginsenoside Rd as an intermediate, followed by hydrolysis of the remaining 20-O-β-D-glucosidic bond. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.193 | ||||||||||||||||||
Accepted name: | ginsenosidase type I | ||||||||||||||||||
Reaction: | (1) a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + H2O = a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + D-glucopyranose (2) a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + H2O = a protopanaxadiol-type ginsenoside with no glycosidic modifications at position 3 + D-glucopyranose (3) a protopanaxadiol-type ginsenoside with two glycosyl residues at position 20 + H2O = a protopanaxadiol-type ginsenoside with a single glucosyl residue at position 20 + a monosaccharide |
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For diagram of protopanaxadiol ginsenosides ginsenosidases, click here | |||||||||||||||||||
Glossary: | ginsenoside Rb1 = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol ginsenoside Rb2 = 3β-[β-D-glucopyranosyl-(1→2)-β-D glucopyranosyloxy]-20-[α-L-arabinopyranosyl-(1→6)-β-D glucopyranosyloxy]dammar-24-en-12β-ol ginsenoside Rb3 = 3β-[β-D-glucopyranosyl-(1→2)-β-D glucopyranosyloxy]-20-[β-D-xylopyranosyl-(1→6)-β-D glucopyranosyloxy]dammar-24-en-12β-ol ginsenoside Rc = 3β-[β-D-glucopyranosyl-(1→2)-β-D glucopyranosyloxy]-20-[α-L-arabinofuranosyl-(1→6)-β-D glucopyranosyloxy]dammar-24-en-12β-ol ginsenoside Rd = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-(β-D-glucopyranosyloxy)dammar-24-en-12β-ol ginsenoside F2 = 3β,20-bis(β-D-glucopyranosyloxy)dammar-24-en-12β-ol ginsenoside C-K = 20β-(β-D-glucopyranosyloxy)dammar-24-ene-3β,12β-diol ginsenoside Rh2 = 3β-(β-D-glucopyranosyloxy)dammar-24-ene-12β,20-diol |
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Systematic name: | ginsenoside glucohydrolase | ||||||||||||||||||
Comments: | Ginsenosidase type I is slightly activated by Mg2+ or Ca2+ [1]. The enzyme hydrolyses the 3-O-β-D-(1→2)-glucosidic bond, the 3-O-β-D-glucopyranosyl bond and the 20-O-β-D-(1→6)-glycosidic bond of protopanaxadiol-type ginsenosides. It usually leaves a single glucosyl residue attached at position 20 and one or no glucosyl residues at position 3. Starting with a ginsenoside that is glycosylated at both positions (e.g. ginsenoside Rb1, Rb2, Rb3, Rc or Rd), the most common products are ginsenoside F2 and ginsenoside C-K, with low amounts of ginsenoside Rh2. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.194 | ||||||||||||||||||
Accepted name: | ginsenosidase type IV | ||||||||||||||||||
Reaction: | a protopanaxatriol-type ginsenoside with two glycosyl residues at position 6 + 2 H2O = a protopanaxatriol-type ginsenoside with no glycosidic modification at position 6 + D-glucopyranose + a monosaccharide (overall reaction) (1a) a protopanaxatriol-type ginsenoside with two glycosyl residues at position 6 + H2O = a protopanaxatriol-type ginsenoside with a single glucosyl at position 6 + a monosaccharide (1b) a protopanaxatriol-type ginsenoside with a single glucosyl at position 6 + H2O = a protopanaxatriol-type ginsenoside with no glycosidic modification at position 6 + D-glucopyranose |
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For diagram of protopanaxatriol ginsenosides ginsenosidases, click here | |||||||||||||||||||
Glossary: | ginsenoside Re = 20-(β-D-glucopyranosyl)oxy-6α-[α-L-rhamnopyranosyl-(1→2)-β-D-glucopyranosyloxy]dammar-24-en-3β,12β-diol ginsenoside Rg1 = 6α,20-bis(β-D-glucopyranosyl)oxy-dammar-24-en-3β,12β-diol ginsenoside F1 = 20-(β-D-glucopyranosyloxy)dammar-24-en-3β,6α,12β-triol |
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Systematic name: | protopanaxatriol-type ginsenoside 6-β-D-glucohydrolase | ||||||||||||||||||
Comments: | Ginsenosidase type IV catalyses the sequential hydrolysis of the 6-O-β-D-(1→2)-glycosidic bond or the 6-O-α-D-(1→2)-glycosidic bond in protopanaxatriol-type ginsenosides with a disacchride attached to the C6 position, followed by the hydrolysis of the remaining 6-O-β-D-glycosidic bond (e.g. ginsenoside Re → ginsenoside Rg1 → ginsenoside F1). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.195 | ||||||||||||||||||
Accepted name: | 20-O-multi-glycoside ginsenosidase | ||||||||||||||||||
Reaction: | a protopanaxadiol-type ginsenoside with two glycosyl residues at position 20 + H2O = a protopanaxadiol-type ginsenoside with a single glucosyl residue at position 20 + a monosaccharide | ||||||||||||||||||
For diagram of protopanaxadiol ginsenosides ginsenosidases, click here | |||||||||||||||||||
Glossary: | ginsenoside Rb1 = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol ginsenoside Rb2 = 3β-[β-D-glucopyranosyl-(1→2)-β-D glucopyranosyloxy]-20-[α-L-arabinopyranosyl-(1→6)-β-D glucopyranosyloxy]dammar-24-en-12β-ol ginsenoside Rb3 = 3β-[β-D-glucopyranosyl-(1→2)-β-D glucopyranosyloxy]-20-[β-D-xylopyranosyl-(1→6)-β-D glucopyranosyloxy]dammar-24-en-12β-ol ginsenoside Rc = 3β-[β-D-glucopyranosyl-(1→2)-β-D glucopyranosyloxy]-20-[α-L-arabinofuranosyl-(1→6)-β-D glucopyranosyloxy]dammar-24-en-12β-ol ginsenoside Rd = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-(β-D-glucopyranosyloxy)dammar-24-en-12β-ol ginsenoside Rg3 = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-(β-D-glucopyranosyloxy)dammar-24-ene-12β,20-diol |
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Other name(s): | ginsenosidase type II (erroneous) | ||||||||||||||||||
Systematic name: | protopanaxadiol-type ginsenoside 20-β-D-glucohydrolase | ||||||||||||||||||
Comments: | The 20-O-multi-glycoside ginsenosidase catalyses the hydrolysis of the 20-O-α-(1→6)-glycosidic bond and the 20-O-β-(1→6)-glycosidic bond of protopanaxadiol-type ginsenosides. The enzyme usually leaves a single glucosyl residue attached at position 20, although it can cleave the remaining glucosyl residue with a lower efficiency. Starting with a ginsenoside that is glycosylated at positions 3 and 20, such as ginsenosides Rb1, Rb2, Rb3 and Rc, the most common product is ginsenoside Rd, with a low amount of ginsenoside Rg3 also formed. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.196 | ||||||||||||||||||
Accepted name: | limit dextrin α-1,6-maltotetraose-hydrolase | ||||||||||||||||||
Reaction: | Hydrolysis of (1→6)-α-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin. | ||||||||||||||||||
Other name(s): | glgX (gene name); glycogen debranching enzyme (ambiguous) | ||||||||||||||||||
Systematic name: | glycogen phosphorylase-limit dextrin maltotetraose-hydrolase | ||||||||||||||||||
Comments: | This bacterial enzyme catalyses a reaction similar to EC 3.2.1.33, amylo-α-1,6-glucosidase (one of the activities of the eukaryotic glycogen debranching enzyme). However, while EC 3.2.1.33 removes single glucose residues linked by 1,6-α-linkage, and thus requires the additional activity of 4-α-glucanotransferase (EC 2.4.1.25) to act on limit dextrins formed by glycogen phosphorylase (EC 2.4.1.1), this enzyme removes maltotriose and maltotetraose chains that are attached by 1,6-α-linkage to the limit dextrin main chain, generating a debranched limit dextrin without a need for another enzyme. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.197 | ||||||||||||||||||
Accepted name: | β-1,2-mannosidase | ||||||||||||||||||
Reaction: | β-D-mannopyranosyl-(1→2)-β-D-mannopyranosyl-(1→2)-D-mannopyranose + H2O = β-D-mannopyranosyl-(1→2)-D-mannopyranose + α-D-mannopyranose | ||||||||||||||||||
Systematic name: | β-1,2-D-mannoside mannohydrolase | ||||||||||||||||||
Comments: | The enzyme, characterized from multiple bacterial species, catalyses the hydrolysis of terminal, non-reducing D-mannose residues from β-1,2-mannotriose and β-1,2-mannobiose. The mechanism involves anomeric inversion, resulting in the release of α-D-mannopyranose. Activity with β-1,2-mannotriose or higher oligosaccharides is higher than that with β-1,2-mannobiose. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.198 | ||||||||||||||||||
Accepted name: | α-mannan endo-1,2-α-mannanase | ||||||||||||||||||
Reaction: | Hydrolysis of the terminal α-D-mannosyl-(1→3)-α-D-mannose disaccharide from α-D-mannosyl-(1→3)-α-D-mannosyl-(1→2)-α-D-mannosyl-(1→2)-α-D-mannosyl side chains in fungal cell wall α-mannans. | ||||||||||||||||||
Systematic name: | α-mannan 1,2-[α-D-mannosyl-(1→3)-α-D-mannose] hydrolase | ||||||||||||||||||
Comments: | The enzyme, characterized from the gut bacteria Bacteroides thetaiotaomicron and Bacteroides xylanisolvens, can also catalyse the reaction of EC 3.2.1.130, glycoprotein endo-α-1,2-mannosidase. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.2.1.199 | ||||||||||||||||||
Accepted name: | sulfoquinovosidase | ||||||||||||||||||
Reaction: | a 6-sulfo-α-D-quinovosyl diacylglycerol + H2O = 6-sulfo-α-D-quinovose + a 1,2-diacylglycerol | ||||||||||||||||||
Glossary: | quinovose = 6-deoxy-D-glucopyranose | ||||||||||||||||||
Other name(s): | yihQ (gene name); 6-sulfo-α-D-quinovosyl diacylglycerol 6-sulfo-D-quinovohydrolase | ||||||||||||||||||
Systematic name: | 6-sulfo-α-D-quinovosyl diacylglycerol 6-sulfo-D-quinovohydrolase (configuration-retaining) | ||||||||||||||||||
Comments: | The enzyme, characterized from the bacteria Escherichia coli and Pseudomonas putida, hydrolyses terminal non-reducing α-sulfoquinovoside residues in α-sulfoquinovosyl diacylglycerides and α-sulfoquinovosyl glycerol using a retaining mechanism. The enzyme belongs to the glycosyl hydrolase GH31 family. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 3.2.1.200 | ||||||||||||||||||
Accepted name: | exo-chitinase (non-reducing end) | ||||||||||||||||||
Reaction: | Hydrolysis of N,N′-diacetylchitobiose from the non-reducing end of chitin and chitodextrins. | ||||||||||||||||||
Other name(s): | chiB (gene name) | ||||||||||||||||||
Systematic name: | (1→4)-2-acetamido-2-deoxy-β-D-glucan diacetylchitobiohydrolase (non-reducing end) | ||||||||||||||||||
Comments: | The enzyme hydrolyses the second glycosidic (1→4) linkage from non-reducing ends of chitin and chitodextrin molecules, liberating N,N′-diacetylchitobiose disaccharides. cf. EC 3.2.1.201, exo-chitinase (reducing end). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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