MUTANT ACCESSION NUMBER: 74
PROTEIN NAME: Aspartate aminotransferase (EC 2.6.1.1) (Transaminase A) (ASPAT).
SWISS PROT ENTRY:
AAT_ECOLI
ORGANISM: ESCHERICHIA COLI
GENE NAME: ASPC B0928
VARIANT OR MUTAGEN:Mutagen
PMD ENTRY: A931045
MUTATIONS:
POINT Asp 211 Ala
EFFECTS: Absorption spectra, fluorescence excitation spectra, and CD
spectra of the wild-type enzyme reconstituted with pyridoxal
5''-phosphate (PLP), the mutant PLP form, and the mutant
reconstituted with N(1)-methylated PLP (N-MePLP form) were
studied.: X-ray crystallographic (2.0 A resolution) and CD
spectroscopic studies suggest that the coenzyme analog is not
held in a proper orientation within the active site of the
N-MePLP form.
FUNCTION kmax for aspartate of PLP form [- - -], and of N-MePLP form
[- -]: Kd for aspartate of PLP form [+], and of N-MePLP form
[+]: kmax/Kd for aspartate of PLP form [- - - -], and of
N-MePLP form [- - -] (compared with the wild type(PLP))
COMMENT The numbering is base on the sequence of E.coli enzyme in
SwissProt and different from that in the article.
REFERENCE:
PUBMED ID:
8263922
TITLE:Role of an active site residue analyzed by combination of mutagenesis and coenzyme analog.
AUTHOR:Yano T, Hinoue Y, Chen VJ, Metzler DE, Miyahara I, Hirotsu K, Kagamiyama H.
REFERENCE:J Mol Biol. 1993 Dec 20;234(4):1218-29
3D STRUCTURE:1AAM 1AAW 1AIA 1AIB 1AIC 1AMQ 1AMR 1AMS 1ARS 1ART 1ASA 1ASB 1ASC 1ASD 1ASE 1ASF 1ASG 1ASL 1ASM 1ASN 1B4X 1BQA 1BQD 1C9C 1CQ6 1CQ7 1CQ8 1CZC 1CZE 1G4V 1G4X 1G7W 1G7X 1IX6 1IX7 1IX8 1QIR 1QIS 1QIT 1SPA 1YOO 2AAT 3AAT 5EAA
© copyright 2003
|
