ExplorEnz: EC 2.4.1.3*

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2.4.1.389

Accepted name:

solabiose phosphorylase

Reaction:

solabiose + phosphate = D-galactose + α-D-glucose 1-phosphate

Glossary:

solabiose = β-D-glucopyranosyl-(1→3)-D-galactose

Systematic name:

solabiose:phosphate α-D-glucosyltransferase

Comments:

The enzyme, characterized from the bacterium Paenibacillus borealis, belongs to glycoside hydrolase family 94 (GH94).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Saburi, W., Nihira, T., Nakai, H., Kitaoka, M. and Mori, H. Discovery of solabiose phosphorylase and its application for enzymatic synthesis of solabiose from sucrose and lactose. Sci. Rep. 12:259 (2022). [DOI] [PMID: 34997180]

[EC 2.4.1.389 created 2022]

2.4.1.390

Accepted name:

4,3-α-glucanotransferase

Reaction:

formation of a mixed (1→4)/(1→3)-α-D-glucan from (1→4)-α-D-glucans

Other name(s):

gtfB (gene name) (ambiguous)

Systematic name:

(1→4)-α-D-glucan:(1→4)/(1→3)-α-D-glucan 3-α-D-glucosyltransferase

Comments:

The enzyme, characterized from the bacterium Lactobacillus fermentum NCC 2970, possesses hydrolysis and transglycosylase activities on malto-oligosaccharides with a degree of polymerization of at least 6, as well as polymers such as amylose, potato starch, and amylopectin. The enzyme, which belongs to glycoside hydrolase 70 (GH70) family, attaches the glucosyl residues by α(1→3) linkages in both linear and branched orientations. While capable of forming large polymers, the enzyme produces mainly oligosaccharides in vitro.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Gangoiti, J., van Leeuwen, S.S., Gerwig, G.J., Duboux, S., Vafiadi, C., Pijning, T. and Dijkhuizen, L. 4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H. Sci. Rep. 7:39761 (2017). [DOI] [PMID: 28059108]
2.	Pijning, T., Gangoiti, J., Te Poele, E.M., Borner, T. and Dijkhuizen, L. Insights into broad-specificity starch modification from the crystal structure of Limosilactobacillus reuteri NCC 2613 4,6-α-glucanotransferase GtfB. J. Agric. Food Chem. 69 (2021) 13235–13245. [DOI] [PMID: 34708648]

[EC 2.4.1.390 created 2022]

2.4.1.391

Accepted name:

β-1,2-glucosyltransferase

Reaction:

[(1→2)-β-D-glucosyl]_n + a D-glucoside = [(1→2)-β-D-glucosyl]_n-1 + a β-D-glucosyl-(1→2)-D-glucoside

Systematic name:

1,2-β-D-glucan:D-glucoside 2-β-D-glucosyltransferase (configuration-retaining)

Comments:

The enzyme, characterized from the bacterium Ignavibacterium album, transfers a glucosyl residue from the non-reducing end of a 1,2-β-D-glucan to a glucose residue of an acceptor molecule, forming a β(1,2) linkage. The donor molecule can be as small as sophorose (which contains two glucosyl residues). The enzyme has a very broad specificity for the acceptor, and can act on various aryl- and alkyl-glucosides. In addition, the accepting glucose unit can be in either α or β configuration.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Kobayashi, K., Shimizu, H., Tanaka, N., Kuramochi, K., Nakai, H., Nakajima, M. and Taguchi, H. Characterization and structural analyses of a novel glycosyltransferase acting on the β-1,2-glucosidic linkages. J. Biol. Chem. 298:101606 (2022). [DOI] [PMID: 35065074]

[EC 2.4.1.391 created 2022]

2.4.1.392

Accepted name:

3-O-β-D-glucopyranosyl-β-D-glucuronide phosphorylase

Reaction:

a 3-O-β-D-glucosyl-β-D-glucuronoside + phosphate = a β-D-glucuronoside + α-D-glucopyranose 1-phosphate

Other name(s):

PBOR_13355 (locus name)

Systematic name:

3-O-β-D-glucopyranosyl-β-D-glucuronide:phosphate α-D-glucosyltransferase

Comments:

The enzyme, characterized from the bacterium Paenibacillus borealis, catalyses a reversible reaction, transferring a glucosyl residue attached by a β(1,3) linkage to a D-glucuronate residue (either free or as a part of a β-D-glucuronide) to a free phosphate, generating α-D-glucopyranose 1-phosphate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Isono, N., Mizutani, E., Hayashida, H., Katsuzaki, H. and Saburi, W. Functional characterization of a novel GH94 glycoside phosphorylase, 3-O-β-D-glucopyranosyl β-D-glucuronide phosphorylase, and implication of the metabolic pathway of acidic carbohydrates in Paenibacillus borealis. Biochem. Biophys. Res. Commun. 625 (2022) 60–65. [DOI] [PMID: 35947916]

[EC 2.4.1.392 created 2022]

2.4.1.393

Accepted name:

MMP α-(1→4)-mannosyltransferase

Reaction:

GDP-α-D-mannose + [3-O-methyl-α-D-mannosyl-(1→4)]_n-3-O-methyl-α-D-mannose = α-D-mannosyl-(1→4)-[3-O-methyl-α-D-mannosyl-(1→4)]_n-3-O-methyl-α-D-mannose + GDP

Glossary:

MMP = α-D-mannosyl-(1→4)-[3-O-methyl-α-D-mannosyl-(1→4)]_n-1-O,3-O-dimethyl-α-D-mannose

Other name(s):

manT (gene name)

Systematic name:

GDP-α-D-mannose:[3-O-methyl-α-D-mannosyl-(1→4)]_n-3-O-methyl-α-D-mannose [(1→4)-α-D-mannosyl]transferase

Comments:

The enzyme, present in mycobacterial species that produce a 3-O-methylmannose polysaccharide (MMP), is involved in recycling and biosynthesis of the polymer. The enzyme has the highest activity with 3-O-methylated mannosides with 4-6 residues. The residue at the reducing end of the substrate is often dimethylated, with the second methyl group attached at the O-1 position.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Maranha, A., Costa, M., Ripoll-Rozada, J., Manso, J.A., Miranda, V., Mendes, V.M., Manadas, B., Macedo-Ribeiro, S., Ventura, M.R., Pereira, P.JB. and Empadinhas, N. Self-recycling and partially conservative replication of mycobacterial methylmannose polysaccharides. Commun Biol 6:108 (2023). [DOI] [PMID: 36707645]

[EC 2.4.1.393 created 2023]

2.4.1.394

Accepted name:

4,6-α-glucanotransferase (linear substrates/linear products)

Reaction:

formation of a linear isomalto/malto-polysaccharide from linear malto-oligosaccharides

Other name(s):

gtfB (gene name) (ambiguous); gtfC (gene name)

Systematic name:

linear (1→4)-α-D-glucan:(1→4)/(1→6)-α-D-glucan 6-α-D-glucosyltransferase

Comments:

The enzyme, originally discovered in lactic acid bacteria but later found in other organisms, is similar to EC 2.4.1.395, reuteransucrase, yet is not able to act on sucrose. The enzyme, which belongs to the glycoside hydrolase 70 (GH70) family, possesses both hydrolase and transglycosylase activities, cleaving α(1→4) linkages from the non-reducing end of linear maltooligosaccharides and synthesizing linear α(1→6)-glucan chains. It also possesses an endo-α(1→4)-glycosidase activity. Due to its narrow binding groove, it is not able to act on branched substrates. cf. EC 2.4.1.396, 4,6-α-glucanotransferase (linear and branched substrates, branched products).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Kralj, S., van Geel-Schutten, G.H., Dondorff, M.MG., Kirsanovs, S., van der Maarel, M.JE.C. and Dijkhuizen, L. Glucan synthesis in the genus Lactobacillus: isolation and characterization of glucansucrase genes, enzymes and glucan products from six different strains. Microbiology (Reading) 150 (2004) 3681–3690. [DOI] [PMID: 15528655]
2.	Kralj, S., Grijpstra, P., van Leeuwen, S.S., Leemhuis, H., Dobruchowska, J.M., van der Kaaij, R.M., Malik, A., Oetari, A., Kamerling, J.P. and Dijkhuizen, L. 4,6-α-glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70. Appl. Environ. Microbiol. 77 (2011) 8154–8163. [DOI] [PMID: 21948833]
3.	Dobruchowska, J.M., Gerwig, G.J., Kralj, S., Grijpstra, P., Leemhuis, H., Dijkhuizen, L. and Kamerling, J.P. Structural characterization of linear isomalto-/malto-oligomer products synthesized by the novel GTFB 4,6-α-glucanotransferase enzyme from Lactobacillus reuteri 121. Glycobiology 22 (2012) 517–528. [DOI] [PMID: 22138321]
4.	Leemhuis, H., Dijkman, W.P., Dobruchowska, J.M., Pijning, T., Grijpstra, P., Kralj, S., Kamerling, J.P. and Dijkhuizen, L. 4,6-α-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily. Appl. Microbiol. Biotechnol. 97 (2013) 181–193. [DOI] [PMID: 22361861]
5.	Gangoiti, J., Pijning, T. and Dijkhuizen, L. The Exiguobacterium sibiricum 255-15 GtfC enzyme represents a novel glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes. Appl. Environ. Microbiol. 82 (2016) 756–766. [DOI] [PMID: 26590275]
6.	Bai, Y., Gangoiti, J., Dijkstra, B.W., Dijkhuizen, L. and Pijning, T. Crystal structure of 4,6-α-glucanotransferase supports diet-driven evolution of GH70 enzymes from α-amylases in oral bacteria. Structure 25 (2017) 231–242. [DOI] [PMID: 28065507]
7.	Te Poele, E.M., van der Hoek, S.E., Chatziioannou, A.C., Gerwig, G.J., Duisterwinkel, W.J., Oudhuis, L.AA.CM., Gangoiti, J., Dijkhuizen, L. and Leemhuis, H. GtfC enzyme of Geobacillus sp. 12AMOR1 represents a novel thermostable type of GH70 4,6-α-glucanotransferase that synthesizes a linear alternating (α1→6)/(α1→4) α-glucan and delays bread staling. J. Agric. Food Chem. 69 (2021) 9859–9868. [DOI] [PMID: 34427087]

[EC 2.4.1.394 created 2023]

2.4.1.395

Accepted name:

reuteransucrase

Reaction:

formation of reuteran from sucrose

Glossary:

reuteran = a high-molecular-mass branched α-glucan produced by the lactic acid bacterium Limosilactobacillus reuteri.

Systematic name:

sucrose:α-D-glucan 4-α/6-α-D-glucosyltransferase

Comments:

The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage of the transferred glucosyl residue. The enzyme, characterized from the lactic acid bacterium Limosilactobacillus reuteri strain 121, catalyses the hydrolysis of sucrose and the transfer of the D-glucose moiety to suitable acceptors (inclduing sucrose), forming the glucan reuteran, which is typical for these strains. The enzyme forms mostly α(1→4) glucosidic linkages, but also α(1→6) linkages. The presence of maltose significantly accelerate the initial rate of the reaction. See EC 2.4.1.5, dextransucrase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Kralj, S., van Geel-Schutten, G.H., Rahaoui, H., Leer, R.J., Faber, E.J., van der Maarel, M.J. and Dijkhuizen, L. Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with α-(1→4) and α-(1→6) glucosidic bonds. Appl. Environ. Microbiol. 68 (2002) 4283–4291. [DOI] [PMID: 12200277]
2.	Kralj, S., van Geel-Schutten, G.H., van der Maarel, M.JE.C. and Dijkhuizen, L. Biochemical and molecular characterization of Lactobacillus reuteri 121 reuteransucrase. Microbiology (Reading) 150 (2004) 2099–2112. [DOI] [PMID: 15256553]
3.	Kralj, S., Stripling, E., Sanders, P., van Geel-Schutten, G.H. and Dijkhuizen, L. Highly hydrolytic reuteransucrase from probiotic Lactobacillus reuteri strain ATCC 55730. Appl. Environ. Microbiol. 71 (2005) 3942–3950. [DOI] [PMID: 16000808]

[EC 2.4.1.395 created 2023]

2.4.1.396

Accepted name:

4,6-α-glucanotransferase (linear and branched substrates, branched products)

Reaction:

formation of a branched isomalto/malto-polysaccharide from branched malto-oligosaccharides

Other name(s):

gtfB (gene name) (ambiguous); gtfD (gene name)

Systematic name:

branched (1→4)-α-D-glucan:(1→4)/(1→6)-α-D-glucan 6-α-D-glucosyltransferase

Comments:

The enzyme, discovered in several bacterial species, is similar to EC 2.4.1.395, reuteransucrase, yet is not able to act on sucrose. The enzyme, which belongs to the glycoside hydrolase 70 (GH70) family, possesses both hydrolase and transglycosylase activities, cleaving endo α(1→4) linkages from the non-reducing end of maltooligosaccharides and adding the resulting oligosaccharides to the non-reducing end of α-D-glucan chains that terminate with a residue linked by an α-(1→4) linkage, forming an α(1→6) linkage. The enzyme is not able to form successive α(1→6) linkages. Unlike EC 2.4.1.394, 4,6-α-glucanotransferase (linear substrates/linear products), which can only act on linear substrates, this enzyme is able to act on both linear and branched substrates, and can form the branched reuteran type of α-glucan.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Gangoiti, J., van Leeuwen, S.S., Vafiadi, C. and Dijkhuizen, L. The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-α-glucanotransferase enzyme (GtfD) to synthesize a reuteran like polymer from maltodextrins and starch. Biochim. Biophys Acta 1860 (2016) 1224–1236. [DOI] [PMID: 26868718]
2.	Gangoiti, J., van Leeuwen, S.S., Meng, X., Duboux, S., Vafiadi, C., Pijning, T. and Dijkhuizen, L. Mining novel starch-converting glycoside hydrolase 70 enzymes from the Nestle Culture Collection genome database: the Lactobacillus reuteri NCC 2613 GtfB. Sci. Rep. 7:9947 (2017). [DOI] [PMID: 28855510]
3.	Pijning, T., Gangoiti, J., Te Poele, E.M., Borner, T. and Dijkhuizen, L. Insights into broad-specificity starch modification from the crystal structure of Limosilactobacillus reuteri NCC 2613 4,6-α-glucanotransferase GtfB. J. Agric. Food Chem. 69 (2021) 13235–13245. [DOI] [PMID: 34708648]

[EC 2.4.1.396 created 2023]

2.4.1.397

Accepted name:

cyclic β-1,2-glucan glucanotransferase

Reaction:

Cyclizes part of a (1→2)-β-D-glucan chain by formation of a (1→2)-β-D-glucosidic bond

Systematic name:

(1→2)-β-D-glucan:(1→2)-β-D-glucan 2-β-D-[(1→2)-β-D-glucano]-transferase (cyclizing and configuration-retaining)

Comments:

This enzyme is the cyclization domain of cyclic β-1,2-glucan synthase. Enzymes from Brucella abortus and Thermoanaerobacter italicus were characterized. The cyclization domain of cyclic β-1,2-glucan synthase is flanked by an N-terminal β-1,2-glucosyltransferase domain (a UDP-α-D-glucose-dependent synthase, not EC 2.4.1.391) and a C-terminal β-1,2-glucoside phosphorylase domain (cf. EC 2.4.1.333), with the former responsible for elongation and the latter for chain length control. The cyclization domain of Thermoanaerobacter italicus cyclizes linear oligosaccharides with a degree of polymerization (DP) of 21 or higher to produce cyclic glucans with DP 17 or higher. The cyclization domain also disproportionates linear β-1,2-glucooligosaccharides without cycling. The entire cyclic β-1,2-glucan synthase from Brucella abortus synthesizes cyclic β-1,2-glucans with DP 17-22.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Inon de Iannino, N., Briones, G., Tolmasky, M. and Ugalde, R.A. Molecular cloning and characterization of cgs, the Brucella abortus cyclic β(1-2) glucan synthetase gene: genetic complementation of Rhizobium meliloti ndvB and Agrobacterium tumefaciens chvB mutants. J. Bacteriol. 180 (1998) 4392–4400. [DOI] [PMID: 9721274]
2.	Guidolin, L.S., Ciocchini, A.E., Inon de Iannino, N. and Ugalde, R.A. Functional mapping of Brucella abortus cyclic β-1,2-glucan synthase: identification of the protein domain required for cyclization. J. Bacteriol. 191 (2009) 1230–1238. [DOI] [PMID: 19074375]
3.	Guidolin, L.S., Morrone Seijo, S.M., Guaimas, F.F., Comerci, D.J. and Ciocchini, A.E. Interaction network and localization of Brucella abortus membrane proteins involved in the synthesis, transport, and succinylation of cyclic β-1,2-glucans. J. Bacteriol. 197 (2015) 1640–1648. [DOI] [PMID: 25733613]
4.	Tanaka, N., Saito, R., Kobayashi, K., Nakai, H., Kamo, S., Kuramochi, K., Taguchi, H., Nakajima, M. and Masaike, T. Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase. Appl. Microbiol. Biotechnol. 108:187 (2024). [DOI] [PMID: 38300345]

[EC 2.4.1.397 created 2024]