EC |
6.3.2.46 | Relevance: 100% |
Accepted name: |
fumarate—(S)-2,3-diaminopropanoate ligase |
Reaction: |
ATP + fumarate + L-2,3-diaminopropanoate = AMP + diphosphate + N3-fumaroyl-L-2,3-diaminopropanoate |
Glossary: |
N3-fumaroyl-L-2,3-diaminopropanoate = (2E)-4-{[(2S)-2-amino-2-carboxyethyl]amino}-4-oxobut-2-enoate
L-2,3-diaminopropanoate = (S)-2,3-diaminopropanoate |
Other name(s): |
DdaG; fumarate:(S)-2,3-diaminopropanoate ligase (AMP-forming) |
Systematic name: |
fumarate:L-2,3-diaminopropanoate ligase (AMP-forming) |
Comments: |
The enzyme, characterized from the bacterium Enterobacter agglomerans, is involved in biosynthesis of dapdiamide tripeptide antibiotics, a family of fumaramoyl- and epoxysuccinamoyl-peptides named for the presence of an L-2,3-diaminopropanoate (DAP) moiety and two amide linkages in their scaffold. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hollenhorst, M.A., Clardy, J. and Walsh, C.T. The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics. Biochemistry 48 (2009) 10467–10472. [DOI] [PMID: 19807062] |
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[EC 6.3.2.46 created 2015] |
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EC |
4.3.1.15 | Relevance: 45.7% |
Accepted name: |
diaminopropionate ammonia-lyase |
Reaction: |
2,3-diaminopropanoate + H2O = pyruvate + 2 NH3 |
Other name(s): |
diaminopropionatase; α,β-diaminopropionate ammonia-lyase; 2,3-diaminopropionate ammonia-lyase; 2,3-diaminopropanoate ammonia-lyase; 2,3-diaminopropanoate ammonia-lyase (adding H2O; pyruvate-forming) |
Systematic name: |
2,3-diaminopropanoate ammonia-lyase (adding water; pyruvate-forming) |
Comments: |
A pyridoxal phosphate enzyme. Active towards both D- and L-diaminopropanoate. D- and L-serine are poor substrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51901-19-0 |
References: |
1. |
Nagasawa, T., Tanizawa, K., Satoda, T., Yamada, H. Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme, and sequence determination of the pyridoxal 5′-phosphate binding peptide. J. Biol. Chem. 263 (1988) 958–964. [PMID: 3275662] |
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[EC 4.3.1.15 created 1999] |
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EC |
2.3.1.58 | Relevance: 44.6% |
Accepted name: |
2,3-diaminopropionate N-oxalyltransferase |
Reaction: |
oxalyl-CoA + L-2,3-diaminopropanoate = CoA + N3-oxalyl-L-2,3-diaminopropanoate |
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For diagram of O3-Acetyl-L-serine metabolism, click here |
Other name(s): |
oxalyldiaminopropionate synthase; ODAP synthase; oxalyl-CoA:L-α,β-diaminopropionic acid oxalyltransferase; oxalyldiaminopropionic synthase; oxalyl-CoA:L-2,3-diaminopropanoate 3-N-oxalyltransferase |
Systematic name: |
oxalyl-CoA:L-2,3-diaminopropanoate N3-oxalyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-48-3 |
References: |
1. |
Malathi, K., Padmanaban, G. and Sarma, P.S. Biosynthesis of β-N-oxalyl-L-α,β-diaminopropionic acid, the Lathyrus sativus neurotoxin. Phytochemistry 9 (1970) 1603–1610. |
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[EC 2.3.1.58 created 1976] |
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EC |
1.5.1.51 | Relevance: 34.2% |
Accepted name: |
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase |
Reaction: |
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O = 2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+ |
Other name(s): |
SbnB |
Systematic name: |
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate:NAD+ dehydrogenase (L-2,3-diaminopropanoate-forming) |
Comments: |
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Beasley, F.C., Cheung, J. and Heinrichs, D.E. Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus. BMC Microbiol. 11:199 (2011). [DOI] [PMID: 21906287] |
2. |
Kobylarz, M.J., Grigg, J.C., Takayama, S.J., Rai, D.K., Heinrichs, D.E. and Murphy, M.E. Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor. Chem. Biol. 21 (2014) 379–388. [DOI] [PMID: 24485762] |
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[EC 1.5.1.51 created 2017] |
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EC |
6.3.2.54 | Relevance: 31.8% |
Accepted name: |
L-2,3-diaminopropanoate—citrate ligase |
Reaction: |
ATP + L-2,3-diaminopropanoate + citrate = AMP + diphosphate + 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate |
Glossary: |
staphyloferrin B = 5-[(2-{[(3S)-5-{[(2S)-2-amino-2-carboxyethyl]amino}-3-carboxy-3-hydroxy-5-oxopentanoyl]amino}ethyl)amino]-2,5-dioxopentanoate |
Other name(s): |
sbnE (gene name); 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate synthtase |
Systematic name: |
L-2,3-diaminopropanoate:citrate ligase (2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate-forming) |
Comments: |
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Dale, S.E., Doherty-Kirby, A., Lajoie, G. and Heinrichs, D.E. Role of siderophore biosynthesis in virulence of Staphylococcus aureus: identification and characterization of genes involved in production of a siderophore. Infect. Immun. 72 (2004) 29–37. [PMID: 14688077] |
2. |
Cheung, J., Beasley, F.C., Liu, S., Lajoie, G.A. and Heinrichs, D.E. Molecular characterization of staphyloferrin B biosynthesis in Staphylococcus aureus. Mol. Microbiol. 74 (2009) 594–608. [PMID: 19775248] |
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[EC 6.3.2.54 created 2019] |
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EC |
6.3.2.55 | Relevance: 25.5% |
Accepted name: |
2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate synthase |
Reaction: |
ATP + 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate + L-2,3-diaminopropanoate = AMP + diphosphate + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate |
Glossary: |
staphyloferrin B = 5-[(2-{[(3S)-5-{[(2S)-2-amino-2-carboxyethyl]amino}-3-carboxy-3-hydroxy-5-oxopentanoyl]amino}ethyl)amino]-2,5-dioxopentanoate |
Other name(s): |
sbnF (gene name) |
Systematic name: |
2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate:L-2,3-diaminopropanoate ligase {2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate-forming} |
Comments: |
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B. It belongs to a class of siderophore synthases known as type C nonribosomal peptide synthase-independent synthases (NIS). Type C NIS enzymes recognize esterified or amidated derivatives of carboxylic acids. The enzyme likely forms a 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cheung, J., Beasley, F.C., Liu, S., Lajoie, G.A. and Heinrichs, D.E. Molecular characterization of staphyloferrin B biosynthesis in Staphylococcus aureus. Mol. Microbiol. 74 (2009) 594–608. [PMID: 19775248] |
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[EC 6.3.2.55 created 2019] |
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EC |
2.7.1.225 | Relevance: 22.5% |
Accepted name: |
L-serine kinase (ATP) |
Reaction: |
ATP + L-serine = ADP + O-phospho-L-serine |
Other name(s): |
sbnI (gene name) |
Systematic name: |
ATP:L-serine 3-phosphotransferase |
Comments: |
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of L-2,3-diaminopropanoate, which is used by that organism as a precursor for the biosynthesis of the siderophore staphyloferrin B. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Verstraete, M.M., Perez-Borrajero, C., Brown, K.L., Heinrichs, D.E. and Murphy, M.EP. SbnI is a free serine kinase that generates O -phospho-l-serine for staphyloferrin B biosynthesis in Staphylococcus aureus. J. Biol. Chem. 293 (2018) 6147–6160. [PMID: 29483190] |
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[EC 2.7.1.225 created 2019] |
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EC |
4.1.1.86 | Relevance: 17.6% |
Accepted name: |
diaminobutyrate decarboxylase |
Reaction: |
L-2,4-diaminobutanoate = propane-1,3-diamine + CO2 |
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For diagram of ectoine biosynthesis, click here |
Other name(s): |
DABA DC; L-2,4-diaminobutyrate decarboxylase; L-2,4-diaminobutanoate carboxy-lyase |
Systematic name: |
L-2,4-diaminobutanoate carboxy-lyase (propane-1,3-diamine-forming) |
Comments: |
A pyridoxal-phosphate protein that requires a divalent cation for activity [1]. N4-Acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates. Found in the proteobacteria Haemophilus influenzae and Acinetobacter baumannii. In the latter, this enzyme is cotranscribed with the dat gene that encodes EC 2.6.1.76, diaminobutyrate—2-oxoglutarate transaminase, which can supply the substrate for this enzyme. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Yamamoto, S., Tsuzaki, Y., Tougou, K. and Shinoda, S. Purification and characterization of L-2,4-diaminobutyrate decarboxylase
from Acinetobacter calcoaceticus. J. Gen. Microbiol. 138 (1992) 1461–1465. [DOI] [PMID: 1512577] |
2. |
Ikai, H. and Yamamoto, S. Cloning and expression in Escherichia coli of the gene encoding a novel L-2,4-diaminobutyrate decarboxylase of Acinetobacter baumannii. FEMS Microbiol. Lett. 124 (1994) 225–228. [DOI] [PMID: 7813892] |
3. |
Ikai, H. and Yamamoto, S. Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii. J. Bacteriol. 179 (1997) 5118–5125. [DOI] [PMID: 9260954] |
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[EC 4.1.1.86 created 2006] |
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EC |
6.3.2.47 | Relevance: 13.9% |
Accepted name: |
dapdiamide synthase |
Reaction: |
(1) ATP + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine + L-valine = ADP + phosphate + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-valine (2) ATP + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine + L-isoleucine = ADP + phosphate + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-isoleucine (3) ATP + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine + L-leucine = ADP + phosphate + 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-leucine (4) ATP + 3-({[(2R,3R)-3-carbamoyloxiran-2-yl]carbonyl}amino)-L-alanine + L-valine = ADP + phosphate + 3-({[(2R,3R)-3-carbamoyloxiran-2-yl]carbonyl}amino)-L-alanyl-L-valine |
Glossary: |
dapdiamide A = 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-valine
dapdiamide B = 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-isoleucine
dapdiamide C = 3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanyl-L-leucine |
Other name(s): |
DdaF; dapdiamide A synthase |
Systematic name: |
3-{[(2E)-4-amino-4-oxobut-2-enoyl]amino}-L-alanine:L-valine ligase (ADP-forming) |
Comments: |
The enzyme, characterized from the bacterium Pantoea agglomerans, is involved in biosynthesis of dapdiamide tripeptide antibiotics, a family of fumaramoyl- and epoxysuccinamoyl-peptides named for the presence of an (S)-2,3-diaminopropanoate (DAP) moiety and two amide linkages in their scaffold. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hollenhorst, M.A., Clardy, J. and Walsh, C.T. The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics. Biochemistry 48 (2009) 10467–10472. [DOI] [PMID: 19807062] |
2. |
Hollenhorst, M.A., Bumpus, S.B., Matthews, M.L., Bollinger, J.M., Jr., Kelleher, N.L. and Walsh, C.T. The nonribosomal peptide synthetase enzyme DdaD tethers N(β)-fumaramoyl-L-2,3-diaminopropionate for Fe(II)/α-ketoglutarate-dependent epoxidation by DdaC during dapdiamide antibiotic biosynthesis. J. Am. Chem. Soc. 132 (2010) 15773–15781. [DOI] [PMID: 20945916] |
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[EC 6.3.2.47 created 2015, modified 2016] |
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