|
Your query returned 10 entries. Printable version
EC | 1.4.3.13 | ||||||||||||||||||
Accepted name: | protein-lysine 6-oxidase | ||||||||||||||||||
Reaction: | [protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2 | ||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-allysine | ||||||||||||||||||
Other name(s): | lysyl oxidase | ||||||||||||||||||
Systematic name: | protein-L-lysine:oxygen 6-oxidoreductase (deaminating) | ||||||||||||||||||
Comments: | Also acts on protein 5-hydroxylysine. This enzyme catalyses the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices [4]. These reactions play an important role for the development, elasticity and extensibility of connective tissue. The enzyme is also active on free amines, such as cadaverine or benzylamine [4,5]. Some isoforms can also use [protein]-N(6)-acetyl-L-lysine as substrate deacetamidating the substrate [6]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99676-44-5 | ||||||||||||||||||
References: |
| ||||||||||||||||||
EC | 1.4.3.20 | ||||||||||||||||||
Accepted name: | L-lysine 6-oxidase | ||||||||||||||||||
Reaction: | L-lysine + O2 + H2O = (S)-2-amino-6-oxohexanoate + H2O2 + NH3 | ||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine | ||||||||||||||||||
Other name(s): | L-lysine-ε-oxidase; Lod; LodA; marinocine | ||||||||||||||||||
Systematic name: | L-lysine:oxygen 6-oxidoreductase (deaminating) | ||||||||||||||||||
Comments: | Differs from EC 1.4.3.13, protein-lysine 6-oxidase, by using free L-lysine rather than the protein-bound form. N2-Acetyl-L-lysine is also a substrate, but N6-acetyl-L-lysine, which has an acetyl group at position 6, is not a substrate. Also acts on L-ornithine, D-lysine and 4-hydroxy-L-lysine, but more slowly. The amines cadaverine and putrescine are not substrates [2]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1116448-48-6 | ||||||||||||||||||
References: |
| ||||||||||||||||||
EC | 1.5.3.15 | ||||||||||||||||||
Accepted name: | N8-acetylspermidine oxidase (propane-1,3-diamine-forming) | ||||||||||||||||||
Reaction: | N8-acetylspermidine + O2 + H2O = propane-1,3-diamine + 4-acetamidobutanal + H2O2 | ||||||||||||||||||
Systematic name: | N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) | ||||||||||||||||||
Comments: | Also active with N1-acetylspermine, weak activity with N1,N12-diacetylspermine. No activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine. Absence of monoamine oxidase (EC 1.4.3.4) activity. Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
| ||||||||||||||||||
EC | 2.5.1.16 | ||||||||||||||||||
Accepted name: | spermidine synthase | ||||||||||||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5′-thioadenosine + spermidine | ||||||||||||||||||
For diagram of spermine biosynthesis, click here | |||||||||||||||||||
Glossary: | spermidine = N-(3-aminopropyl)butane-1,4-diamine spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine putrescine = butane-1,4-diamine S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium |
||||||||||||||||||
Other name(s): | aminopropyltransferase; putrescine aminopropyltransferase; spermidine synthetase; SpeE (ambiguous); S-adenosylmethioninamine:putrescine 3-aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase | ||||||||||||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:putrescine 3-aminopropyltransferase | ||||||||||||||||||
Comments: | The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [2,7]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [5,6]. cf. EC 2.5.1.22 (spermine synthase) and EC 2.5.1.23 (sym-norspermidine synthase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-82-0 | ||||||||||||||||||
References: |
| ||||||||||||||||||
EC | 2.5.1.104 | ||||||||||||||||||
Accepted name: | N1-aminopropylagmatine synthase | ||||||||||||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + agmatine = S-methyl-5′-thioadenosine + N1-(3-aminopropyl)agmatine | ||||||||||||||||||
For diagram of spermidine biosynthesis, click here | |||||||||||||||||||
Glossary: | S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium | ||||||||||||||||||
Other name(s): | agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE (ambiguous); agmatine aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:agmatine 3-aminopropyltransferase | ||||||||||||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:agmatine 3-aminopropyltransferase | ||||||||||||||||||
Comments: | The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
| ||||||||||||||||||
EC | 2.6.1.82 | ||||||||||||||||||
Accepted name: | putrescine—2-oxoglutarate transaminase | ||||||||||||||||||
Reaction: | putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate | ||||||||||||||||||
For diagram of arginine catabolism, click here | |||||||||||||||||||
Glossary: | putrescine = butane-1,4-diamine 1-pyrroline = 3,4-dihydro-2H-pyrrole |
||||||||||||||||||
Other name(s): | putrescine-α-ketoglutarate transaminase; YgjG; putrescine:α-ketoglutarate aminotransferase; PAT (ambiguous); putrescine transaminase (ambiguous); putrescine aminotransferase (ambiguous); butane-1,4-diamine:2-oxoglutarate aminotransferase | ||||||||||||||||||
Systematic name: | putrescine:2-oxoglutarate aminotransferase | ||||||||||||||||||
Comments: | A pyridoxal 5′-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which may be the actual substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates [3]. Forms part of the arginine-catabolism pathway [2]. cf. EC 2.6.1.113, putrescine—pyruvate transaminase. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 98982-73-1 | ||||||||||||||||||
References: |
| ||||||||||||||||||
EC | 3.5.1.62 | ||||||||||||||||||
Accepted name: | acetylputrescine deacetylase | ||||||||||||||||||
Reaction: | N-acetylputrescine + H2O = acetate + putrescine | ||||||||||||||||||
Glossary: | putrescine = butane-1,4-diamine spermidine = N-(3-aminopropyl)butane-1,4-diamine |
||||||||||||||||||
Systematic name: | N-acetylputrescine acetylhydrolase | ||||||||||||||||||
Comments: | The enzyme from Micrococcus luteus also acts on N8-acetylspermidine and acetylcadaverine, but more slowly. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 103679-48-7 | ||||||||||||||||||
References: |
| ||||||||||||||||||
EC | 4.1.1.18 | ||||||||||||||||||
Accepted name: | lysine decarboxylase | ||||||||||||||||||
Reaction: | L-lysine = cadaverine + CO2 | ||||||||||||||||||
Other name(s): | L-lysine carboxy-lyase | ||||||||||||||||||
Systematic name: | L-lysine carboxy-lyase (cadaverine-forming) | ||||||||||||||||||
Comments: | A pyridoxal-phosphate protein. Also acts on 5-hydroxy-L-lysine. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-76-4 | ||||||||||||||||||
References: |
| ||||||||||||||||||
EC | 4.1.1.116 | ||||||||||||||||||
Accepted name: | D-ornithine/D-lysine decarboxylase | ||||||||||||||||||
Reaction: | (1) D-ornithine = putrescine + CO2 (2) D-lysine = cadaverine + CO2 |
||||||||||||||||||
For diagram of spermine biosynthesis, click here | |||||||||||||||||||
Glossary: | cadaverine = pentane-1,5-diamine putrescine = butane-1,4-diamine |
||||||||||||||||||
Other name(s): | dokD (gene name); DOKDC | ||||||||||||||||||
Systematic name: | D-ornithine/D-lysine carboxy-lyase | ||||||||||||||||||
Comments: | The enzyme, characterized from the bacterium Salmonella typhimurium LT2, is specific for D-ornithine and D-lysine. Requires pyridoxal 5′-phosphate. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
| ||||||||||||||||||
EC | 6.3.2.64 | ||||||||||||||||||
Accepted name: | bisucaberin synthase | ||||||||||||||||||
Reaction: | 2 ATP + 2 N1-hydroxy-N1-succinylcadaverine = 2 AMP + 2 diphosphate + bisucaberin (overall reaction) (1a) ATP + 2 N1-hydroxy-N1-succinylcadaverine = AMP + diphosphate + bisucaberin B (1b) ATP + bisucaberin B = AMP + diphosphate + bisucaberin |
||||||||||||||||||
Glossary: | bisucaberin B = pre-bisucaberin = 3-[(5-{3-[(5-aminopentyl)(hydroxy)carbamoyl]propanamido}pentyl)(hydroxy)carbamoyl]propanoate bisucaberin = 1,12-dihydroxy-1,6,12,17-tetrazacyclodocosane-2,5,13,16-tetrone |
||||||||||||||||||
Other name(s): | pubC (gene name); BibC C-terminal domain | ||||||||||||||||||
Systematic name: | N1-hydroxy-N1-succinylcadaverine:N1-hydroxy-N1-succinylcadaverine ligase | ||||||||||||||||||
Comments: | Requires Mg2+. The enzyme, characterized from the bacterium Aliivibrio salmonicida, catalyses the last step in the biosynthesis of the siderophore bisucaberin. The enzyme catalyses the reaction in two steps - concatenation of two molecules of N1-hydroxy-N1-succinylcadaverine, followed by cyclization. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
| ||||||||||||||||||