Characterization of chondroitin sulfate lyase ABC from Bacteroides thetaiotaomicron WAL2926

Biochemistry

Volumn 47, Issue 25, 2008, Pages 6650-6661

  Shaya, David ^a   Hahn, Bum Soo ^b   Nam, Young Park ^c   Sim, Joon Soo ^b   Yeong, Shik Kim ^c   Cygler, Miroslaw ^a,d  

^a MCGILL UNIVERSITY   (Canada)

^b National Institute of Animal Science   (South Korea)

^c Seoul National University   (South Korea)

^d NATIONAL RESEARCH COUNCIL CANADA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE RESIDUES; BACTEROIDES THETAIOTAOMICRON; BIOCHEMICAL CHARACTERIZATIONS; CATALYTIC RESIDUES; CHONDROITIN SULFATE (CHSA); DERMATAN SULFATE (DS); EPIMERS; GLUCURONIC ACIDS; GLYCOSAMINOGLYCANS (GAG); GLYCOSIDIC BONDS; IDURONIC ACIDS; SITE DIRECTED MUTAGENESIS; THREE-DIMENSIONAL (3D) STRUCTURING; URONIC ACIDS;

BIOCHEMICAL ENGINEERING; CALCIUM; CARBOXYLIC ACIDS; CESIUM; DIELECTRIC RELAXATION; FOOD ADDITIVES; GLUCOSE; SULFUR COMPOUNDS; THREE DIMENSIONAL;

SULFATE MINERALS;

CALCIUM ION; CHONDROITIN SULFATE; CHONDROITIN SULFATE ABC LYASE; DERMATAN SULFATE; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HEPARIN; HYALURONIC ACID; LYASE; MAGNESIUM ION; URONIC ACID;

ARTICLE; ASYMMETRIC CATALYSIS; BACTEROIDES THETAIOTAOMICRON; DEPOLYMERIZATION; ENZYMATIC DEGRADATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; EPIMER; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTON TRANSPORT; SENSITIVITY AND SPECIFICITY; SITE DIRECTED MUTAGENESIS; THREE DIMENSIONAL IMAGING;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; BACTEROIDES; BINDING SITES; CALCIUM; CARBOHYDRATE SEQUENCE; CATALYSIS; CATALYTIC DOMAIN; CHONDROITIN ABC LYASE; CHONDROITIN SULFATES; GLYCOSAMINOGLYCANS; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; OSMOLAR CONCENTRATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TEMPERATURE; TYROSINE;

BACTEROIDES THETAIOTAOMICRON;

EID: 45749084849     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800353g     Document Type: Article

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