نتایج جستجو برای: amino acid dehydrogenase

تعداد نتایج: 865884  

Journal: :The Biochemical journal 1987
C S Tsai

A novel reaction catalysed by lipoamide dehydrogenase is described. In the presence of NADH, lipoamide dehydrogenase reduces the nitro group of 4-nitropyridine and 4-nitropyridine N-oxide. The elution profiles from a DEAE-cellulose column for the dehydrogenase and nitroreductase activities are identical. Chemical modifications of critical amino acid residues suggest that the two activities shar...

2002
FREDERICK E. EVANS

The nucleotides &amino-, 8-methylamino-, and &dimethylaminoadenylic acid have been synthesized and their preferred conformations about the glycosyl bond in aqueous solution have been determined by ‘H nuclear magnetic resonance spectroscopy. Paramagnetic relaxation studies, nuclear Overhauser enhancement measurements, chemical shifts, and coupling constant comparisons indicate that there is rota...

Journal: :The Biochemical journal 1999
T Lanisnik Rizner G Moeller H H Thole M Zakelj-Mavric J Adamski

17beta-Hydroxysteroid dehydrogenase (17beta-HSD) from the filamentous fungus Cochliobolus lunatus (17beta-HSDcl) catalyses the reduction of steroids and of several o- and p-quinones. After purification of the enzyme, its partial amino acid sequence was determined. A PCR fragment amplified with primers derived from peptide sequences was generated for screening the Coch. lunatus cDNA library. Thr...

Journal: :Applied and environmental microbiology 1998
J M Stoop H Mooibroek

Mannitol, a six-carbon sugar alcohol, is the main storage carbon in the button mushroom, Agaricus bisporus. Given the physiological importance of mannitol metabolism in growth, fruit body development, and salt tolerance of A. bisporus, the enzyme responsible for mannitol biosynthesis, NADP-dependent mannitol dehydrogenase (MtDH) (EC 1.1.1.138), was purified to homogeneity, and MtDH cDNA was clo...

Journal: :Journal of bacteriology 1994
S Hein A Steinbüchel

Sequence analysis of a 6.3-kbp genomic EcoRI-fragment of Alcaligenes eutrophus, which was recently identified by using a dihydrolipoamide dehydrogenase-specific DNA probe (A. Pries, S. Hein, and A. Steinbüchel, FEMS Microbiol. Lett. 97:227-234, 1992), and of an adjacent 1.0-kbp EcoRI fragment revealed the structural genes of the A. eutrophus pyruvate dehydrogenase complex, pdhA (2,685 bp), pdhB...

Journal: :Bioscience, biotechnology, and biochemistry 2003
Emran Kabir Chowdhury Yuka Akaishi Shinji Nagata Haruo Misono

The structural gene for NAD+-dependent 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) from Pseudomonas putida E23 was cloned in Escherichia coli cells to obtain a large amount of the enzyme and its nucleotides were sequenced to study its structural relationship with other proteins. The gene encoded a polypeptide containing 295 amino acid residues and was in a cluster with the gene for methylm...

2017
Jun-ichiro Hirano Hiromichi Ohta Shosuke Yoshida Kenji Miyamoto

From the standpoint of enzymatic organic synthesis, NADH oxidase (NOX) will be a key enzyme that plays an essential role in the cofactor regeneration of NAD+ dependent enzymatic reactions. For example, enzymatic enantioselective oxidations of racemic secondary alcohols (Geueke et al., 2003; Riebel et al., 2003; Hummel & Riebel, 1996) and amino acids (Hummel et al., 2003a) have been reported as ...

Journal: :The Biochemical journal 1974
J P Brown R N Perham

1. The two cysteine residues forming the disulphide bridge that comprises part of the active site of lipoamide dehydrogenase from pig heart were specifically labelled with iodo[2-(14)C]acetic acid. 2. A tryptic peptide containing these carboxymethylcysteine residues was isolated from digests of reduced and S-carboxymethylated lipoamide dehydrogenase and its amino acid sequence of 23 residues wa...

Journal: :The Journal of biological chemistry 1972
F M Veronese D Piszkiewicz E L Smith

By kinetic studies and the identification of the labeled peptide of the [WIKNCO-modified protein, the inactivation of bovine liver glutamate dehydrogenase by potassium cyanate can be attributed to the carbamylation of the e-amino group of lysine-97. Although the e-amino group of lysine-97 is the major site of carbamylation by cyanate, the oc-amino group of alanine-l and E-amino group of lysine-...

Journal: :Plants 2023

The agronomic potential of glutamate dehydrogenase 2 (GDH2) in maize kernel production was investigated by examining the impact a mutation on corresponding gene. Mu-insertion homozygous and heterozygous mutant lines lacking GDH2 activity were isolated characterized at biochemical, physiological levels. In comparison to wild type ghd2 mutants, gdh2 plants decrease root amino acid content, wherea...

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