Archaeal MO-containing glyceraldehyde oxidoreductase isozymes exhibit diverse substrate specificities through unique subunit assemblies

PLoS ONE

Volumn 11, Issue 1, 2016, Pages

  Wakagi, Takayoshi ^a   Nishimasu, Hiroshi ^a,b   Miyake, Masayuki ^a   Fushinobu, Shinya ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE REDUCTASE; ARCHAEAL PROTEIN; GLYCERALDEHYDE REDUCTASE; IRON SULFUR PROTEIN; ISOENZYME; MOLYBDENUM; PROTEIN SUBUNIT; RIBOFLAVIN DERIVATIVE; XANTHINE DEHYDROGENASE;

AMINO ACID SEQUENCE; CHEMISTRY; CLASSIFICATION; COMPARATIVE STUDY; ENZYME SPECIFICITY; ENZYMOLOGY; GLYCOLYSIS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; MOLECULAR MODEL; MOLECULAR WEIGHT; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN SUBUNIT; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SULFOLOBUS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; FLAVINS; GLYCOLYSIS; IRON-SULFUR PROTEINS; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MOLYBDENUM; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN SUBUNITS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; SUGAR ALCOHOL DEHYDROGENASES; SULFOLOBUS; XANTHINE DEHYDROGENASE;

EID: 84996452920     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0147333     Document Type: Article

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