Characterization of two important histidine residues in the active site of xylanase A from Streptomyces lividans, a family 10 glycanase

Biochemistry

Volumn 36, Issue 25, 1997, Pages 7769-7775

  Roberge, M ^a   Shareck, F ^a   Morosoli, R ^a   Kluepfel, D ^a   Dupont, C ^a  

^a UNIVERSITÉ LAVAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

GLUCAN SYNTHASE; HISTIDINE; MUTANT PROTEIN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ENZYME DENATURATION; ENZYME MECHANISM; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; STREPTOMYCES LIVIDANS;

AMINO ACID SEQUENCE; BINDING SITES; ENDO-1,4-BETA XYLANASES; GLYCOSIDE HYDROLASES; HEAT; HISTIDINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; STREPTOMYCES; XYLOSIDASES;

FELIS CATUS; STREPTOMYCES LIVIDANS;

EID: 0030842357     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9703296     Document Type: Article

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