Diaminopimelate decarboxylase
From Wikipedia, the free encyclopedia
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.
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[edit] 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.
[edit] References
- IUBMB entry for 4.1.1.20
- BRENDA references for 4.1.1.20 (Recommended.)
- PubMed references for 4.1.1.20
- PubMed Central references for 4.1.1.20
- Google Scholar references for 4.1.1.20
- DENMAN RF, HOARE DS, WORK E (1955). "Diaminopimelic acid decarboxylase in pyridoxin-deficient Escherichia coli". Biochim. Biophys. Acta. 16: 442–3. PMID 14378182.
[edit] External links
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- The CAS registry number for this enzyme class is 9024-75-3.