THE SITE OF BINDING OF PYRIDOXAL-5'-PHOSPHATE TO HEAR GLUTAMIC-ASPARTIC TRANSAMINASE
نویسندگان
چکیده
منابع مشابه
Glutamic Aspartic Transaminase
Aspartate and glutamate react instantaneously with the pyridoxal form of the pig heart glutamic aspartic transaminase (1) to yield the corresponding keto acid, converting the enzymebound pyridoxal phosphate to bound pyridoxamine phosphate (2). Other amino acids such as methionine sulfoxide, methionine sulfone, and alanine react much more slowly with the enzyme, but the reaction itself appears t...
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 کاملThe pyridoxal-binding site in pyridoxamine-pyruvate transaminase.
The enzyme-substrate complex formed between pyridoxamine-pyruvate transaminase (EC 2.6.1.30) and pyridoxal was reduced with NaBH4. After carboxymethylation and tryptic digestion, pyridoxyl-lysine-containing peptides were isolated by a combination of Sephadex and Dowex 50 chromatography. Analysis of these peptides shows the structure around the pyridoxal-binding lysine residues to be Ala-Asp-Ile...
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: Proceedings of the National Academy of Sciences
سال: 1962
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.48.9.1615