Diaminopimelate decarboxylase

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diaminopimelate decarboxylase
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

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[edit]

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[edit]

  • 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.