Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase

Journal of Biological Chemistry

Volumn 280, Issue 17, 2005, Pages 17392-17396

  Jones, Limei H ^a   Pearson, Arwen R ^b   Tang, Yu ^a   Wilmot, Carrie M ^b   Davidson, Victor L ^a  

^a UNIVERSITY OF MISSISSIPPI MEDICAL CENTER   (United States)

^b UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BIOCHEMISTRY; BIOSYNTHESIS; MOLECULAR BIOLOGY; OXYGEN;

COVALENT CROSSLINKING; METHYLAMINE DEHYDROGENASE (MADH);

ENZYMES;

AMINE DEHYDROGENASE; ASPARTIC ACID; CYSTEINE; HEMOPROTEIN; OXYGEN; QUINOHEMOPROTEIN; QUINOHEMOPROTEIN AMINE DEHYDROGENASE; QUINONE DERIVATIVE; TRYPTOPHAN; TRYPTOPHAN TRYPTOPHYLQUINONE; UNCLASSIFIED DRUG; DISULFIDE; DRUG DERIVATIVE; INDOLE DERIVATIVE; METHYLAMINE; OXIDOREDUCTASE;

ARTICLE; BIOGENESIS; COVALENT BOND; CROSS LINKING; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME SYNTHESIS; GENE MUTATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; STEADY STATE; BINDING SITE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; MASS SPECTROMETRY; METABOLISM; MUTATION; PARACOCCUS DENITRIFICANS; PROTEIN CONFORMATION; STATISTICAL MODEL; X RAY CRYSTALLOGRAPHY;

ASPARTIC ACID; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DISULFIDES; INDOLEQUINONES; KINETICS; MASS SPECTROMETRY; METHYLAMINES; MODELS, CHEMICAL; MODELS, MOLECULAR; MODELS, STATISTICAL; MUTATION; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; OXYGEN; PARACOCCUS DENITRIFICANS; PROTEIN CONFORMATION; TRYPTOPHAN;

EID: 20444466042     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M500943200     Document Type: Article

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