Identification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction.
The decarboxylation of L-aspartate by E. coli L-aspartate-alpha-decarboxylase (ADC) is shown to occur with retention of configuration; analysis of the protein structure identifies Tyr58 as the proton donor in the decarboxylation mechanism.
Saldanha
S A
SA
University Chemical Laboratory, Lensfield Road, Cambridge, UK CB2 1EW.
Birch
L M
LM
Webb
M E
ME
Nabbs
B K
BK
von Delft
F
F
Smith
A G
AG
Abell
C
C
D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology; D015964:Gene Expression Regulation, Bacterial; D005968:Glutamate Decarboxylase / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011522:Protons; D013237:Stereoisomerism; D014443:Tyrosine / Q000378:metabolism*
D011522:Protons; D014443:Tyrosine; C019104:aspartate-alpha-decarboxylase; D005968:Glutamate Decarboxylase