Effect of metal binding and posttranslational lysine carboxylation on the activity of recombinant hydantoinase

Journal of Biological Inorganic Chemistry

Volumn 14, Issue 1, 2009, Pages 111-121

  Huang, Cheng Yang ^a   Hsu, Ching Chen ^a   Chen, Mei Chun ^a   Yang, Yuh Shyong ^a,b  

^a NATIONAL CHIAO TUNG UNIVERSITY   (Taiwan)

^b INSTRUMENT TECHNOLOGY RESEARCH CENTER   (Taiwan)

Author keywords

Carboxylated lysine; Hydantoinase; Metalloenzyme; Site directed mutagenesis; Structure function relationship

Indexed keywords

CARBOXYLIC ACID; COBALT; DIHYDROPYRIMIDINASE; IRON; LYSINE; MANGANESE; ZINC;

ARTICLE; BINDING SITE; CARBOXYLATION; CATALYSIS; CELL CULTURE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; ESCHERICHIA COLI; METAL BINDING; MUTATION; PH MEASUREMENT; PRIORITY JOURNAL; RHIZOBIUM RADIOBACTER;

AMIDOHYDROLASES; BINDING SITES; CARBOXYLIC ACIDS; CATALYSIS; COBALT; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; LYSINE; MOLECULAR STRUCTURE; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT PROTEINS; RHIZOBIUM; STRUCTURE-ACTIVITY RELATIONSHIP; ZINC;

AGROBACTERIUM TUMEFACIENS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 57149125703     PISSN: 09498257     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00775-008-0428-x     Document Type: Article

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