Kinetics of the Binding of Pyridoxal 5'-Phosphate to Glutamate Decarboxylase
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چکیده
منابع مشابه
Pyridoxal 5”Phosphate-dependent Histidine Decarboxylase
Pyridoxal phosphate-dependent histidine decarboxylase from Morganella morganii AM-15 was inactivated by (a-a-fluoromethylhistidine by a pseudo firstorder reaction, with KI and kinact values of 0 . 1 mM and 32.2 min-l, respectively, and was most efficient at pH 6.5-7.0. Both L-histidine and the competitive inhibitor, L-histidine methyl ester, protected against inactivation. The apoenzyme was not...
متن کاملBinding of Pyridoxal 5'-Phosphate
1. The a and ,B subforms of aspartate aminotransferase were purified from pig heart. 2. The a subform contained 2mol of pyridoxal 5'-phosphate. The apo-(a subform) could be fully reactived by combination with 2mol of cofactor. 3. The protein fluorescence of the apo(a subform) decreased non-linearly with increase in enzyme activity and concentration of bound cofactor. 4. It is concluded that the...
متن کاملBinding of pyridoxal 5-phosphate to cystathionase.
The binding of pyridoxal 5-phosphate to the apoprotein of the enzyme cystathionase from rat liver was investigated by two independent methods, absorption and fluorescence spectroscopy. The increase in absorbance at 525 nm associated with Schiff’s base formation was used to investigate the binding of pyridoxal-5-P at a protein concentration of 1 X 10e5 M. A model based on two classes of independ...
متن کاملPyridoxal phosphate-sensitized photoinactivation of glutamate decarboxylase from Clostridium perfringens.
1. l-Glutamate decarboxylase (EC 4.1.1.15) from Clostridium perfringens was inactivated by exposure to visible light at pH6.2. 2. Inactivation does not occur at pH4.6 or in the absence of bound pyridoxal phosphate. 3. On prolonged photo-oxidation six histidine residues per molecule of enzyme were destroyed. 4. The loss of six cysteine residues per molecule occurred both in irradiated samples an...
متن کاملMode of binding of pyridoxal phosphate to 5-aminolevulinate synthase.
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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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62522-0