Document Detail

D-serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants.
MedLine Citation:
PMID:  3053699     Owner:  NLM     Status:  MEDLINE    
We have identified two glycyl residues whose integrity is essential for the catalytic competence of a model pyridoxal 5'-phosphate requiring enzyme, D-serine dehydratase from Escherichia coli. This was accomplished by isolating and sequencing the structural gene from wild type E. coli and from two mutant strains that produce inactive D-serine dehydratase. DNA sequencing indicated the presence of a single glycine to aspartic acid replacement in each variant. The amino acid replacements lie in a glycine-rich region of D-serine dehydratase well removed from pyridoxal 5'-phosphate-binding lysine 118 in the primary structure of the enzyme. The striking effect of these two glycine to aspartic acid replacements on catalytic activity, the conservation of the glycine-rich region in several pyridoxal 5'-phosphate-dependent enzymes that catalyze alpha/beta-eliminations, and the placement of similar glycine-rich sequences in well-characterized active site structures suggest that the glycine-rich region interacts with the cofactor at the active site of the enzyme.
M Marceau; E McFall; S D Lewis; J A Shafer
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  263     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1988 Nov 
Date Detail:
Created Date:  1988-12-14     Completed Date:  1988-12-14     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  16926-33     Citation Subset:  IM    
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.
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MeSH Terms
Amino Acid Sequence
Aspartic Acid / analysis*
DNA, Bacterial / analysis*
Escherichia coli / enzymology*
Glycine / analysis*
L-Serine Dehydratase / analysis,  genetics*
Molecular Sequence Data
Nucleotide Mapping
Protein Conformation
Grant Support
Reg. No./Substance:
0/DNA, Bacterial; 56-40-6/Glycine; 56-84-8/Aspartic Acid; EC Dehydratase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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