IscS functions as a primary sulfur-donating enzyme by interacting specifically with moeb and moad in the biosynthesis of molybdopterin in escherichia coli

Journal of Biological Chemistry

Volumn 285, Issue 4, 2010, Pages 2302-2308

  Zhang, Wanjiao ^a   Urban, Alexander ^c   Mihara, Hisaaki ^b   Leimkühler, Silke ^c   Kurihara, Tatsuo ^a   Esaki, Nobuyoshi ^a  

^a KYOTO UNIVERSITY   (Japan)

^b RITSUMEIKAN UNIVERSITY   (Japan)

^c UNIVERSITY OF POTSDAM   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ADENYLATE; BIOSYNTHETIC PATHWAY; C TERMINUS; COFACTORS; CYSTEINE RESIDUES; DIRECT OXIDATION; DITHIOLENE; E. COLI; IN-VITRO; L-CYSTEINE; MOLYBDENUM-COFACTOR; MOLYBDOPTERIN; SURFACE PLASMONS; SYNTHASES; THIOCARBOXYLATE;

BIOCHEMISTRY; BIOSYNTHESIS; ENZYMES; ESCHERICHIA COLI; MOLYBDENUM; STRAIN; SULFUR; SURFACE PLASMON RESONANCE;

PLASMA JETS;

BACTERIAL PROTEIN; CARBOXYLIC ACID DERIVATIVE; CYSTATHIONINE GAMMA LYASE; CYSTEINE DESULFURASE A; MOLYBDOPTERIN; MOLYBDOPTERIN SYNTHASE; PROTEIN ISCS; PROTEIN MOAD; PROTEIN MOEB; PROTEIN SUFS; SULFUR; SYNTHETASE; THIOCARBOXYLATE; UNCLASSIFIED DRUG; CYSTEINE; ESCHERICHIA COLI PROTEIN; LYASE; METALLOPROTEIN; MOEB PROTEIN, E COLI; MOLYBDENUM COFACTOR; NUCLEOTIDYLTRANSFERASE; PTERIDINE DERIVATIVE; SULFUR DERIVATIVE; SULFURTRANSFERASE;

ARTICLE; BACTERIAL METABOLISM; BACTERIAL STRAIN; CONTROLLED STUDY; ENZYME ACTIVATION; ESCHERICHIA COLI; GENE DELETION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN SYNTHESIS; SULFATION; SURFACE PLASMON RESONANCE; BIOSYNTHESIS; CHEMISTRY; COENZYME; ENZYME ACTIVE SITE; ENZYMOLOGY; METABOLISM; PROTEIN BINDING; SPECIES DIFFERENCE;

ESCHERICHIA COLI;

CARBON-SULFUR LYASES; CATALYTIC DOMAIN; COENZYMES; CYSTEINE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; METALLOPROTEINS; NUCLEOTIDYLTRANSFERASES; PROTEIN BINDING; PTERIDINES; SPECIES SPECIFICITY; SULFUR; SULFUR COMPOUNDS; SULFURTRANSFERASES; SURFACE PLASMON RESONANCE;

EID: 77449106447     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.082172     Document Type: Article

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