Substrate specificity determinants of the methanogen homoaconitase enzyme: Structure and function of the small subunit

Biochemistry

Volumn 49, Issue 12, 2010, Pages 2687-2696

  Jeyakanthan, Jeyaraman ^a   Drevland, Randy M ^b   Gayathri, Dasara Raju ^c   Velmurugan, Devadasan ^c   Shinkai, Akeo ^d   Kuramitsu, Seiki ^d,e   Yokoyama, Shigeyuki ^f,g   Graham, David E ^b,h,i  

^a NATIONAL SYNCHROTRON RADIATION RESEARCH CENTER   (Taiwan)

^b UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^c UNIVERSITY OF MADRAS   (India)

^d RIKEN SPring 8 Center   (Japan)

^e OSAKA UNIVERSITY   (Japan)

^f RIKEN YOKOHAMA INSTITUTE   (Japan)

^g UNIVERSITY OF TOKYO   (Japan)

^h UNIVERSITY OF TENNESSEE   (United States)

ⁱ OAK RIDGE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACONITASE; CARBOXYLATE GROUPS; CHAIN GROUPS; CHEMO-ENZYMATIC SYNTHESIS; CONVERGENT EVOLUTION; DIASTEREOMERS; DICARBOXYLATES; EVOLUTIONARY POTENTIAL; GENE FUNCTION; GENOME SEQUENCES; HYDROXY ACIDS; ISOMERASES; LOOP REGIONS; LYASE ACTIVITY; SEQUENCE SIMILARITY; SITE DIRECTED MUTAGENESIS; SMALL SUBUNITS; STEREOSPECIFIC; STRUCTURAL MODELS; SUBSTRATE SPECIFICITY; WILD TYPES;

ACIDS; CARBOXYLATION; CARBOXYLIC ACIDS; CATALYST ACTIVITY; ELECTRON TRANSITIONS; ENZYME ACTIVITY; ENZYMES; GENES; ISOMERIZATION; ISOMERS; MODEL STRUCTURES; X RAY DIFFRACTION;

SUBSTRATES;

ACONITATE HYDRATASE; ARGININE; CARBOXYLIC ACID DERIVATIVE; GAMMA CARBOXYLATE; HOMOACONITASE; ISOMERASE; ISOPROPYLMALATE ISOMERASE; UNCLASSIFIED DRUG;

ARCHAEBACTERIUM; ARTICLE; CATALYSIS; CHEMICAL ANALYSIS; CONTROLLED STUDY; CRYSTALLIZATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; GENOME ANALYSIS; METHANOCOCCUS JANNASCHII; METHANOGEN; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; X RAY DIFFRACTION;

ACONITATE HYDRATASE; AMINO ACID SUBSTITUTION; ARCHAEAL PROTEINS; BASE SEQUENCE; BINDING SITES; CATALYSIS; EURYARCHAEOTA; EVOLUTION, MOLECULAR; HYDRO-LYASES; ISOMERASES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

METHANOCALDOCOCCUS JANNASCHII;

EID: 77949777049     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901766z     Document Type: Article

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