Involvement of a residue at position 75 in the catalytic mechanism of a fungal aspartic proteinase, Rhizomucor pusillus pepsin. Replacement of tyrosine 75 on the flap by asparagine enhances catalytic efficiency

Protein Engineering

Volumn 9, Issue 10, 1996, Pages 869-875

  Park, Young Nam ^a   Aikawa, Jun Ichi ^b   Nishiyama, Makoto ^a   Horinouchi, Sueharu ^a   Beppu, Teruhiko ^c  

^a UNIVERSITY OF TOKYO   (Japan)

^b INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

^c NIHON UNIVERSITY   (Japan)

Author keywords

Aspartic proteinase; Catalytic mechanism; Rhizomucor pusillus pepsin; Site directed mutagenesis

Indexed keywords

ASPARAGINE; ASPARTIC PROTEINASE; FUNGAL PROTEIN; GLYCINE; HISTIDINE; MUTANT PROTEIN; PEPSIN A; PEPSTATIN; PHENYLALANINE; SYNTHETIC PEPTIDE; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ASPARAGINE; BASE SEQUENCE; BLOTTING, WESTERN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FUNGAL PROTEINS; GLYCOSYLATION; HYDROGEN BONDING; KINETICS; MUCORALES; MUTAGENESIS, SITE-DIRECTED; PEPSIN A; PEPSTATINS; PROTEASE INHIBITORS; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET; TYROSINE;

FELIS CATUS; FUNGI; RHIZOMUCOR PUSILLUS;

EID: 0029862567     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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