N-Formimino-l-glutamate Iminohydrolase from Histidine-adapted Pseudomonas
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چکیده
منابع مشابه
Structure of N-Formimino-l-glutamate Iminohydrolase from Pseudomonas aeruginosa
N-Formimino-l-glutamate iminohydrolase (HutF), from Pseudomonas aeruginosa with a locus tag of Pa5106 ( gi|15600299 ), is a member of the amidohydrolase superfamily. This enzyme catalyzes the deamination of N-formimino-l-glutamate to N-formyl-l-glutamate and ammonia in the histidine degradation pathway. The crystal structure of Pa5106 was determined in the presence of the inhibitors N-formimino...
متن کاملMechanistic characterization of N-formimino-L-glutamate iminohydrolase from Pseudomonas aeruginosa.
N-Formimino-l-glutamate iminohydrolase (HutF) from Pseudomonas aeruginosa catalyzes the deimination of N-formimino-l-glutamate in the histidine degradation pathway. An amino acid sequence alignment between HutF and members of the amidohydrolase superfamily containing mononuclear metal centers indicated that residues Glu-235, His-269, and Asp-320 are involved in substrate binding and activation ...
متن کاملN-formimino-L-glutamate formiminohydrolase of Aerobacter aerogenes.
N-Formimino-n-glutamate is an intermediate in the degradation of n-histidine by such different types of cells as those of animal liver (1)) Pseudomonas jluorescens (2, 3), and Aerobacter aerogenes (3). The pathway leading from histidine to formiminoglutamate is the same in all cases and comprises three steps catalyzed by distinct enzymes: L-histidine is converted to urocanate and ammonia by his...
متن کاملAnnotating enzymes of unknown function: N-formimino-L-glutamate deiminase is a member of the amidohydrolase superfamily.
The functional assignment of enzymes that catalyze unknown chemical transformations is a difficult problem. The protein Pa5106 from Pseudomonas aeruginosa has been identified as a member of the amidohydrolase superfamily by a comprehensive amino acid sequence comparison with structurally authenticated members of this superfamily. The function of Pa5106 has been annotated as a probablechlorohydr...
متن کاملProduction of D-Glutamate from L-Glutamate with Glutamate Racemase and L-Glutamate Oxidase.
We studied production of D-glutamate from L-glutamate using a bioreactor consisting of two columns of sequentially connected immobilized glutamate racemase (EC 5.1.1.3, from Bacillus subtilis IFO 3336) and L-glutamate oxidase (EC 1.4.3.11, from Streptomyces sp. X119-6): L-glutamate was racemized by the glutamate racemase column, and then L-glutamate was oxidized by the L-glutamate oxidase colum...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)45599-3