Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes.
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.
Bashir
Qamar
Q
School of Biological Sciences, University of the Punjab, New Campus, Lahore, 54590, Pakistan.
Rashid
Naeem
N
Akhtar
Muhammad
M
D000624:5-Aminolevulinate Synthetase / Q000737:chemistry*; D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics; D000217:Acyltransferases / Q000737:chemistry*; D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000235:genetics; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D005998:Glycine / Q000737:chemistry; D006859:Hydrogen / Q000737:chemistry; D008968:Molecular Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D013237:Stereoisomerism; D013912:Threonine / Q000096:biosynthesis / Q000737:chemistry
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D013912:Threonine; D006859:Hydrogen; D000429:Alcohol Oxidoreductases; C023159:L-threonine 3-dehydrogenase; D000217:Acyltransferases; D000123:Acetyltransferases; C020679:glycine acetyltransferase; D000624:5-Aminolevulinate Synthetase; D005998:Glycine