Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes.

Article Details

Citation

Bashir Q, Rashid N, Akhtar M

Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes.

Chem Commun (Camb). 2006 Dec 28;(48):5065-7. Epub 2006 Oct 13.

PubMed ID
17146529 [ View in PubMed
]
Abstract

The condensation process catalysed by 2-amino-3-oxobutyrate CoA ligase (KBL; also known as 2-amino-3-ketobutyrate ligase) involves the loss of the pro-R hydrogen atom of glycine and occurs with the inversion of stereochemistry; a similar scenario is envisaged for the condensation step of other alpha-oxoamine synthases.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
Glycine2-amino-3-ketobutyrate coenzyme A ligase, mitochondrialProteinHumans
Unknown
Substrate
Details