title: Identification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction.
abstract: 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.
authors.affiliation: University Chemical Laboratory, Lensfield Road, Cambridge, UK CB2 1EW.
authors.forename: S A
authors.initials: SA
authors.lastname: Saldanha
authors.forename: L M
authors.initials: LM
authors.lastname: Birch
authors.forename: M E
authors.initials: ME
authors.lastname: Webb
authors.forename: B K
authors.initials: BK
authors.lastname: Nabbs
authors.forename: F
authors.initials: F
authors.lastname: von Delft
authors.forename: A G
authors.initials: AG
authors.lastname: Smith
authors.forename: C
authors.initials: C
authors.lastname: Abell
mesh_terms: 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*
chemical_list: D011522:Protons; D014443:Tyrosine; C019104:aspartate-alpha-decarboxylase; D005968:Glutamate Decarboxylase