D-Amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217
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منابع مشابه
D-amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217.
The complete nucleotide sequence of the DAO1 gene encoding D-amino-acid oxidase (DAAO) in the yeast Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217 has been determined. The primary structure of DAAO was deduced from the nucleotide sequence of a cDNA clone that covered the entire amino acid coding sequence. Comparison of cDNA and genomic sequences of DAO1 revealed the presence of fiv...
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The variation of kinetic parameters of d-amino acid oxidase from Rhodotorula gracilis with pH was used to gain information about the chemical mechanism of the oxidation of D-amino acids catalysed by this flavoenzyme. d-Alanine was the substrate used. The pH dependence of Vmax and Vmax/Km for alanine as substrate showed that a group with a pK value of 6.26-7.95 (pK1) must be unprotonated and a g...
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The wide range of chemical reactivity exhibited by flavoprotein enzymes is determined fundamentally by the nature of the protein moiety. Studies on the interactions of the isoalloxazine nucleus of flavin with the enzyme are therefore ~ important in understanding this reactivitYi flavin analogues are extremely useful probes for elucidating structure-function relationships (1, 2). We have used a ...
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a c i d a H a s a p r o t o n v i a t h e s o c a l l e d " c a r b a n i o n m e c h a n i s m " . a p r o c e s s t h a t r e q u i r e s a n a c t i v e s i t e b a s e . O n t h e o t h e r h a n d , t h e w o r k o n p k D A A O r e c o n s t i t u t e d w i t h t h e a r t i f i c i a l f 1 a v i n 5 < l e a z a F A D ( 3 ) f a v o r e d a h y d r i d e m e c h a n i s m p r o c e e d i n...
متن کاملKinetic mechanism of D-amino acid oxidases from Rhodotorula gracilis and Trigonopsis variabilis.
The reaction of two D-amino acid oxidases from the yeasts Rhodotorula gracilis and Trigonopsis variabilis with the substrates alanine and valine in their 2-1H and 2-2H forms was studied employing the stopped-flow spectrophotometric technique. The turnover numbers at infinite substrate and oxygen concentrations were: 20,700/4,250 and 1,730/360 ([2-1H]/[2-2H]alanine and valine, respectively) for ...
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ژورنال
عنوان ژورنال: Microbiology
سال: 1998
ISSN: 1350-0872,1465-2080
DOI: 10.1099/00221287-144-4-1095