Catalytic efficiency of HAP phytases is determined by a key residue in close proximity to the active site

Applied Microbiology and Biotechnology

Volumn 90, Issue 4, 2011, Pages 1295-1302

  Fu, Dawei ^a   Li, Zhongyuan ^a   Huang, Huoqing ^a   Yuan, Tiezheng ^a   Shi, Pengjun ^a   Luo, Huiying ^a   Meng, Kun ^a   Yang, Peilong ^a   Yao, Bin ^a  

^a INSTITUTE OF PLANT PROTECTION   (China)

Author keywords

Escherichia coli; Phytase; Site directed mutagenesis; Specific activity; Yersinia enterocolitica

Indexed keywords

ACID PHOSPHATASE; ACTIVE SITE; ACTIVITY LEVELS; AMINO ACID SEQUENCE; CATALYTIC EFFICIENCIES; CATALYTIC SITES; CLOSE PROXIMITY; MOLECULAR VOLUME; NON-CONSERVED RESIDUES; PHYTASE; PHYTASE ACTIVITY; PHYTASES; SEQUENCE ALIGNMENTS; SIDE CHAINS; SITE-DIRECTED MUTAGENESIS; SPECIFIC ACTIVITY; WILD TYPES; YERSINIA ENTEROCOLITICA;

CRYSTAL STRUCTURE; ESCHERICHIA COLI; MUTAGENESIS; PHOSPHATASES;

AMINO ACIDS;

AMINO ACID; ARGININE; ASPARTIC ACID; GLYCINE; HISTIDINE ACID PHOSPHATASE PHYTASE; LEUCINE; PHYTASE; SERINE; THREONINE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID; BACTERIUM; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; MOLECULAR ANALYSIS; MUTATION; PH; TEMPERATURE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; MOLECULAR MODEL; NUCLEOTIDE SEQUENCE; PH; PROTEIN ENGINEERING; SITE DIRECTED MUTAGENESIS; YERSINIA; YERSINIA ENTEROCOLITICA; YERSINIA KRISTEENSENII;

6-PHYTASE; ACID PHOSPHATASE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYSIS; CATALYTIC DOMAIN; CLONING, MOLECULAR; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; YERSINIA ENTEROCOLITICA;

ESCHERICHIA COLI; YERSINIA; YERSINIA ENTEROCOLITICA;

EID: 79955551347     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-011-3171-0     Document Type: Article

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