نتایج جستجو برای: pyridoxal phosphate
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Pyridoxal-5'-phosphate phosphatase (PLPP) catalyzes the dephosphorylation of pyridoxal-5'-phosphate (PLP). A human brain PLPP gene was fused with a PEP-1 peptide and produced a genetic in-frame PEP-1-PLPP fusion protein. The purified PEP-1-PLPP fusion protein was efficiently transduced into PC12 cells in a time- and dose-dependent manner when added exogenously to culture media. Once inside the ...
Non-enzymatic deamination of serine and cysteine is catalyzed by pyridoxal and certain metal salts at 100” (2). This finding suggested that pyridoxal phosphate might be involved in the enzymatic deamination of these amino acids. Vitamin B, has already been implicated in the desulfhydration of cysteine by rat liver (3) and of cysteine and homocysteine by bacteria (4). Several similarities of cys...
VITAMIN B6 REQUIREMENTS IN MAN I rc 1934 Gyorgy1 reported experimental studies on the relation of a dietary factor to rat dermatitis and established this nutrient as a new member of the B-Cornplex, calling it vitamin B6. The vitamin subsequently isolated26 and synthesized was found to be 2 methyl-3 hydroxy-4, 5 hydroxy methyl pyridine and called pyridoxine.7 By means of an elegant series of exp...
Non-enzymatic deamination of serine and cysteine is catalyzed by pyridoxal and certain metal salts at 100” (2). This finding suggested that pyridoxal phosphate might be involved in the enzymatic deamination of these amino acids. Vitamin B, has already been implicated in the desulfhydration of cysteine by rat liver (3) and of cysteine and homocysteine by bacteria (4). Several similarities of cys...
Lysine 5,6-aminomutase is an adenosylcobalamin and pyridoxal-5'-phosphate-dependent enzyme that catalyzes a 1,2 rearrangement of the terminal amino group of dl-lysine and of l-beta-lysine. We have solved the x-ray structure of a substrate-free form of lysine-5,6-aminomutase from Clostridium sticklandii. In this structure, a Rossmann domain covalently binds pyridoxal-5'-phosphate by means of lys...
5-Aminolevulinate synthase of Rhodopseudomonas spheroides interacts with its cofactor, pyridoxal phosphate, and shows an absorption maximum at 430 nm with a probable shoulder at 320--330 nm. The enzyme-PLP complex absorbing at 430 nm is the predominant species at pH 7.2 and can be reduced by NaBH4 at neutral pH with a spectral shift of the absorption maximum to 325 nm. These data suggests the f...
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