Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/ peptidases

Protein Science

Volumn 20, Issue 3, 2011, Pages 557-566

  Pai, Chien Hua ^a   Wu, Hsing Ju ^a   Lin, Chun Hung ^a   Wang, Andrew H J ^a,b  

^a INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^b ACADEMIA SINICA   (Taiwan)

Author keywords

Amidase; Cysteine; Glutathionylspermidine; Histidine dependent amidohydrolases peptidases; Mechanism; Regulation; Structure

Indexed keywords

AMIDASE; AMIDE; ASPARAGINE; CARBONYL DERIVATIVE; CYSTEINE; CYSTEINE PROTEINASE; DIMER; GLUTAMIC ACID; GLUTAMINE; GLUTATHIONE; GLUTATHIONYLSPERMIDINE AMIDASE; HISTIDINE; HISTIDINE AMMONIALYASE; HYDROGEN PEROXIDE; OXYGEN; PEPTIDASE; SPERMIDINE; SULFENIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROLYSIS; HYDROPHOBICITY; MUTATION; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; REGULATORY MECHANISM; SYNTHESIS;

AMIDE SYNTHASES; AMIDOHYDROLASES; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CYSTEINE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUTATHIONE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SPERMIDINE;

ESCHERICHIA COLI;

EID: 79952173520     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.589     Document Type: Article

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