Diaminopimelate decarboxylase
| diaminopimelate decarboxylase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.1.1.20 | ||||||||
| CAS number | 9024-75-3 | ||||||||
| 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 / EGO | ||||||||
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In enzymology, a diaminopimelate decarboxylase (EC 4.1.1.20) is an enzyme that catalyzes the chemical reaction
- meso-2,6-diaminoheptanedioate
L-lysine + CO2
Hence, this enzyme has one substrate, meso-2,6-diaminoheptanedioate, and two products, L-lysine and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is meso-2,6-diaminoheptanedioate carboxy-lyase (L-lysine-forming). Other names in common use include diaminopimelic acid decarboxylase, meso-diaminopimelate decarboxylase, DAP-decarboxylase, and meso-2,6-diaminoheptanedioate carboxy-lyase. This enzyme participates in lysine biosynthesis. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1HKV, 1HKW, 1KNW, 1KO0, 1TUF, 1TWI, 2O0T, and 2P3E.
References
- Denman, R.; Hoare, D.; Work, E. (1955). "Diaminopimelic acid decarboxylase in pyridoxin-deficient Escherichia coli". Biochimica et Biophysica Acta 16 (3): 442–3. doi:10.1016/0006-3002(55)90257-2. PMID 14378182.
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