Aspzincin, a family of metalloendopeptidases with a new zinc-binding motif. Identification of new zinc-binding sites (His-128, His-132, and Asp-164) and three catalytically crucial residues (Glu-129, Asp-143, and Tyr-106) of deuterolysin from Aspergillus oryzae by site-directed mutagenesis

Journal of Biological Chemistry

Volumn 274, Issue 34, 1999, Pages 24195-24201

  Fushimi, Naoya ^a   Ee, Ch'ng Ewe ^a   Nakajima, Tasuku ^a   Ichishima, Eiji ^a,b  

^a TOHOKU UNIVERSITY   (Japan)

^b SOKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARAGINE; ASPARTIC ACID; ASPZINCIN; DEUTEROLYSIN; GLUTAMIC ACID; GLUTAMINE; HISTIDINE; METALLOPROTEINASE; MUTANT PROTEIN; PHENYLALANINE; TYROSINE; UNCLASSIFIED DRUG; ZINC;

AMINO ACID SUBSTITUTION; ARTICLE; ASPERGILLUS ORYZAE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; SEQUENCE HOMOLOGY; STRAIN DIFFERENCE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ASPERGILLUS ORYZAE; BINDING SITES; CATALYSIS; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; STRUCTURE-ACTIVITY RELATIONSHIP; ZINC;

EID: 0039110574     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.34.24195     Document Type: Article

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