Histidines 345 and 378 of Bacillus stearotheromophilus leucine aminopeptidase II are essential for the catalytic activity of the enzyme

Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology

Volumn 87, Issue 4, 2005, Pages 355-359

  Hwang, Guang Yuh ^a   Kuo, Lih Ying ^a,b   Tsai, Ming Ru ^b   Yang, Shin Ling ^c   Lin, Long Liu ^c  

^a TUNGHAI UNIVERSITY   (Taiwan)

^b HUNGKUANG UNIVERSITY   (Taiwan)

^c NATIONAL CHIAYI UNIVERSITY   (Taiwan)

Author keywords

Bacillus stearothermophilus; Histidine; Leucine aminopeptidase; Site directed mutagenesis

Indexed keywords

BACTERIAL ENZYME; CYTOSOL AMINOPEPTIDASE; HISTIDINE DERIVATIVE; NICKEL COMPLEX;

ENZYME ACTIVITY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CHROMATOGRAPHY; ENZYME ACTIVITY; GENE OVEREXPRESSION; GEOBACILLUS STEAROTHERMOPHILUS; MOLECULAR WEIGHT; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS; WILD TYPE;

AMINO ACID SEQUENCE; BACILLUS STEAROTHERMOPHILUS; BASE SEQUENCE; CATALYSIS; CONSERVED SEQUENCE; DNA PRIMERS; HISTIDINE; KINETICS; LEUCYL AMINOPEPTIDASE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 25144490209     PISSN: 00036072     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10482-004-5777-z     Document Type: Article

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