D-glyceraldehyde-3-phosphate dehydrogenase. Amino-acid sequence of the enzyme from the extreme thermophile Thermus aquaticus
1. The amino acid sequence of D‐glyceraldehyde‐3‐phosphate dehydrogenase from the extreme thermophile Thermus aquaticus has been elucidated. 2. The polypeptide contains 332 amino acids and its sequence is 70% identical with that of the enzyme from the moderate thermophile Bacillus stearothermophilus...
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Veröffentlicht in: | European journal of biochemistry 1980-07, Vol.108 (2), p.567-579 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 1. The amino acid sequence of D‐glyceraldehyde‐3‐phosphate dehydrogenase from the extreme thermophile Thermus aquaticus has been elucidated.
2. The polypeptide contains 332 amino acids and its sequence is 70% identical with that of the enzyme from the moderate thermophile Bacillus stearothermophilus.
3. In contrast to less thermostable forms of the enzymes from B. stearothermophilus, pig, lobster and yeast, the T. aquaticus enzyme has only one cysteine residue, namely cysteine‐149 which is required for catalysis. |
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ISSN: | 0014-2956 1432-1033 |
DOI: | 10.1111/j.1432-1033.1980.tb04752.x |