The Enzyme Database

Your query returned 9 entries.    printer_iconPrintable version

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]
[EC 6.3.2.46 created 2015]
 
 
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]
[EC 4.3.1.15 created 1999]
 
 
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
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.
[EC 2.3.1.58 created 1976]
 
 
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]
[EC 1.5.1.51 created 2017]
 
 
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]
[EC 6.3.2.54 created 2019]
 
 
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]
[EC 6.3.2.55 created 2019]
 
 
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]
[EC 2.7.1.225 created 2019]
 
 
EC 4.1.1.86     Relevance: 17.6%
Accepted name: diaminobutyrate decarboxylase
Reaction: L-2,4-diaminobutanoate = propane-1,3-diamine + CO2
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]
[EC 4.1.1.86 created 2006]
 
 
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]
[EC 6.3.2.47 created 2015, modified 2016]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald