Biology:Aerobactin synthase
From HandWiki
Short description: Class of enzymes
| aerobactin synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.2.39 | ||||||||
| CAS number | 94047-30-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an aerobactin synthase (EC 6.3.2.39) is an enzyme that catalyzes the chemical reaction
- 4 ATP + citrate + 2 N6-acetyl-N6-hydroxy-L-lysine + 2 H2O [math]\displaystyle{ \rightleftharpoons }[/math] 4 ADP + 4 phosphate + aerobactin
The 4 substrates of this enzyme are ATP, citrate, N6-acetyl-N6-hydroxy-L-lysine, and H2O, whereas its 3 products are ADP, phosphate, and aerobactin.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (ADP-forming). This enzyme is also called citrate:6-N-acetyl-6-N-hydroxy-L-lysine ligase (ADP-forming). This enzyme participates in lysine degradation.
References
- "Aerobactin synthesis in a cell-free system of Aerobacter aerogenes 62-1". Biochim. Biophys. Acta 801: 437–443. 1984. doi:10.1016/0304-4165(84)90150-8.
- "The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I". Biochim. Biophys. Acta 192 (2): 175–84. 1969. doi:10.1016/0304-4165(69)90353-5. PMID 4313071.
- "Microbial iron chelators: total synthesis of aerobactin and its constituent amino acid, N6-acetyl-N6-hydroxylysine". J. Am. Chem. Soc. 104 (11): 3096–3101. 1982. doi:10.1021/ja00375a025.
- "Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12". J. Bacteriol. 165 (2): 570–8. 1986. doi:10.1128/jb.165.2.570-578.1986. PMID 2935523.
- Challis GL (2005). "A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases". ChemBioChem 6 (4): 601–11. doi:10.1002/cbic.200400283. PMID 15719346.
 |  |
