Cosubstrate binding site of Pseudomonas sp. AK1 gamma-butyrobetaine hydroxylase. Interactions with structural analogs of alpha-ketoglutarate
نویسندگان
چکیده
منابع مشابه
Ejection of structural zinc leads to inhibition of γ-butyrobetaine hydroxylase.
γ-Butyrobetaine hydroxylase (BBOX) is a 2-oxoglutarate and Fe(II) dependent oxygenase that catalyses an essential step during carnitine biosynthesis in animals. BBOX is inhibited by ejection of structural zinc by a set of selenium containing analogues. Previous structural analyses indicated that an undisrupted N-terminal zinc binding domain of BBOX is required for catalysis. Ebselen is a relati...
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Taurinealpha-ketoglutarate (alphaKG) dioxygenase, or TauD, is a mononuclear non-heme iron hydroxylase that couples the oxidative decarboxylation of alphaKG to the decomposition of taurine, forming sulfite and aminoacetaldehyde. Prior studies revealed that taurine-free TauD catalyzes an O(2)- and alphaKG-dependent self-hydroxylation reaction involving Tyr-73, yielding an Fe(III)-catecholate chro...
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γ-Butyrobetaine hydroxylase (BBOX) is a non-heme Fe(II) - and 2-oxoglutarate-dependent oxygenase that catalyzes the stereoselective hydroxylation of an unactivated C-H bond of γ-butyrobetaine (γBB) in the final step of carnitine biosynthesis. BBOX contains an aromatic cage for the recognition of the positively charged trimethylammonium group of the γBB substrate. Enzyme binding and kinetic anal...
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The hydroxylation of y-butyrobetaine (4-trimethylaminobutyrate) to carnitine (3-hydroxy-4-trimethylaminobutyrate) is catalyzed by a soluble enzyme from rat liver which has been partially purified. The enzyme which previously has been shown to require molecular oxygen and ferrous ion has a specific requirement for 2-ketoglutarate. Several reductams stimulate the formation of hydroxylated product...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)52326-7