Presteady State Kinetic Analysis of Riboflavin Synthase
نویسندگان
چکیده
منابع مشابه
Pre-steady-state kinetic analysis of riboflavin synthase using a pentacyclic reaction intermediate as substrate.
Riboflavin synthase catalyses a mechanistically complex dismutation affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H )-pyrimidinedione from 6,7-dimethyl-8-ribityllumazine. A pentacyclic adduct (compound 2 ) of two substrate molecules was used as substrate for pre-steady-state kinetic analysis. Whereas the wild-type enzyme catalyses the decomposition of compound 2 into a mixture of ribo...
متن کاملBiosynthesis of riboflavin. Single turnover kinetic analysis of 6,7-dimethyl-8-ribityllumazine synthase.
6,7-dimethyl-8-ribityllumazine synthase (lumazine synthase) catalyzes the condensation of 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione with 3,4-dihydroxy-2-butanone 4-phosphate, affording the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine. Single turnover experiments monitored by multiwavelength photometry were performed with the recombinant lumazine synthase of Bacillus subtilis. M...
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6,7-dimethyl-8-ribityllumazine synthase (lumazine synthase) catalyzes the condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione and 3,4-dihydroxy-2-butanone 4-phosphate. Presteady state kinetic experiments using the enzyme from the hyperthermophilic bacterium Aquifex aeolicus were monitored by multiwavelength photometry. An early optical transient absorbing around 330 nm is interpre...
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The catalytic mechanism of 3-deoxy-D-manno-2-octulosonate-8-phosphate (Kdo8P) synthase from Escherichia coli was investigated under pre-steady-state conditions using rapid chemical quench flow methods. The results suggest the formation of acyclic bisphosphate 1 as a reaction intermediate. © 1997 Elsevier Science Ltd. 3-Deoxy-D-manno-2-octulosonate-8-phosphate (Kdo8P) synthase (EC 4.1.2.16) is a...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2003
ISSN: 0021-9258
DOI: 10.1074/jbc.m305050200