Tryptophan Synthetase β2 Subunit
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چکیده
منابع مشابه
Tryptophan Synthetase ,& Subunit
Radioactivity incorporated into an e-N-5’-phosphopyridoxyllysine residue of the /3 chain by reduction of the flZ holoenzyme with tritiated sodium borohydride appears in two tryptic peptides. These pyridoxyl peptides differ by only a single arginyl residue. As expected, tryptic digests of normal protein contain two peptides that together make up the pyridoxyl peptide region. The primary structur...
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The A protein subunit of the Escherichia coli tryptophan synthetase catalyzes the reversible conversion of indoleglycerol phosphate to indole and 3-phosphoglyceraldehyde (I). This enzyme has been highly purified and consists of a single polypeptide chain with no associated metal (2, 3). Extensive genetic and biochemical studies have been carried out in order to determine specific relationships ...
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There is 50% identity in the sequences of the first 50 residues of the a chains of Escherichia coli and Pseudomonas putida. No deletions or additions of residues are found in this region, except for the N-terminal methionine residue which is missing in the polypeptide isolated from P. putida. Most of the residues which differ are chemically dissimilar, and half of them are specified by codons w...
متن کاملThe formation and properties of dimers of the tryptophan synthetase alpha subunit of Escherichia coli.
The normally monomeric 01 subunit of Escherichia coti tryptophan synthetase forms dimers and higher order aggregates following exposure to high urea concentrations and removal of the urea by dialysis. The maximum yield of cx chain dimers is approximately 2%. Dimers of certain combinations of different enzymatically inactive mutant (Y monomers exhibit the missing enzymatic activity. In such hete...
متن کاملThe Formation and Properties of Dimers of the Tryptophan Synthetase a Subunit of Escherichia coZi*
The normally monomeric 01 subunit of Escherichia coti tryptophan synthetase forms dimers and higher order aggregates following exposure to high urea concentrations and removal of the urea by dialysis. The maximum yield of cx chain dimers is approximately 2%. Dimers of certain combinations of different enzymatically inactive mutant (Y monomers exhibit the missing enzymatic activity. In such hete...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)34160-2