The crystal structure of l-lactate oxidase from Aerococcus viridans at 2.1 Å resolution reveals the mechanism of strict substrate recognition

Biochemical and Biophysical Research Communications

Volumn 350, Issue 2, 2006, Pages 249-256

  Umena, Yasufumi ^a,b   Yorita, Kazuko ^c   Matsuoka, Takeshi ^d   Kita, Akiko ^a,e   Fukui, Kiyoshi ^c   Morimoto, Yukio ^a,e  

^a KYOTO UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c UNIVERSITY OF TOKUSHIMA   (Japan)

^d ASAHI KASEI PHARMA CORPORATION   (Japan)

^e RIKEN HARIMA INSTITUTE   (Japan)

Author keywords

Flavoprotein; Lactate oxidase; Substrate recognition; X ray structure analysis

Indexed keywords

LACTATE 2 MONOOXYGENASE;

AEROCOCCUS VIRIDANS; ARTICLE; CATALYSIS; COMPARATIVE STUDY; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIFFRACTION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN MOTIF; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

ALCOHOL OXIDOREDUCTASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY; STREPTOCOCCACEAE; SUBSTRATE SPECIFICITY; TEMPERATURE;

AEROCOCCUS VIRIDANS;

EID: 33749335515     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.025     Document Type: Article

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