PMID:10419973

Citation	Chiu, CH, Lee, CZ, Lin, KS, Tam, MF and Lin, LY (1999) Amino acid residues involved in the functional integrity of Escherichia coli methionine aminopeptidase. J. Bacteriol. 181:4686-9
Abstract	Amino acid residues in the metal-binding and putative substrate-binding sites of Escherichia coli methionine aminopeptidase (MAP) were mutated, and their effects on the function of the enzyme were investigated. Substitution of any amino acid residue at the metal-binding site resulted in complete loss of the two cobalt ions bound to the protein and diminished the enzyme activity. However, only Cys70 and Trp221 at the putative substrate-binding site are involved in the catalytic activity of MAP. Changing either of them caused partial loss of enzyme activity, while mutations at both positions abolished MAP function. Both residues are found to be conserved in type I but not type II MAPs.
Links	PubMed PMC103606
Keywords	Amino Acid Substitution; Aminopeptidases/chemistry; Aminopeptidases/genetics; Aminopeptidases/metabolism; Binding Sites; Cobalt/analysis; Cobalt/metabolism; Cysteine; DNA Primers; Escherichia coli/enzymology; Escherichia coli/genetics; Kinetics; Methionyl Aminopeptidases; Mutagenesis, Site-Directed; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Tryptophan
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.