Amino acid substitutions in mutant forms of histidinol dehydrogenase from Neurospora crassa
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منابع مشابه
The purification and properties of histidinol dehydrogenase from Neurospora crassa.
1. A procedure is described for the purification of l-histidinol dehydrogenase (l-histidinol-NAD oxidoreductase, EC 1.1.1.23) from Neurospora crassa. 2. The enzyme, as purified, has a sedimentation coefficient, S(20), of 7.1s and a molecular weight of 81 000. Considerable variation is possible in the state of polymerization of the enzyme, giving rise to observed molecular weights from 40 000 to...
متن کاملMutants of NEUROSPORA CRASSA Permeable to Histidinol.
I N Neurospora, L-histidinol is the immediate precursor of L-histidine, as shown by the isolation of L-histidinol dehydrogenase and the study of its catalytic functions (AMES 1957; CREASER, BENNETT and DRYSDALE 1965). The failure of histidine mutants, with the histidinol dehydrogenase function intact, to grow on histidinol, suggests that histidinol cannot enter the cell. However, CATCHESIDE ( 1...
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histidinol dehydrogenase. The wild type sequence, Arg ( > Lys Glu-Gln-Ala, has been replaced by the sequence -Lys-AlaSer-Leu-Thr in the hisD2352 dehydrogenase. The permuted amino acid sequence may be explained if hisD2352 is a two-base deletion near the end of the hisD gene. A unique nucleotide sequence may be written for this region which indicates that the normal termination signal of the his...
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The amino-acid sequence of tyrosinase from Neurospora crassa (monophenol,dihydroxyphenylalanine:oxygen oxidoreductase, EC 1.14.18.1) is reported. This copper-containing oxidase consists of a single polypeptide chain of 407 amino acids. The primary structure was determined by automated and manual sequence analysis on fragments produced by cleavage with cyanogen bromide and on peptides obtained b...
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A tentative primary structure of the NADP-specific glutamate dehydrogenase [L-glutamate: NADP oxidoreductase (deaminating), EC 1.4.1.4] from Neurospora crassa has been determined. The proposed sequence contains 452 amino-acid residues in each of the identical subunits of the hexameric enzyme. Comparison of the sequence with that of the bovine liver enzyme reveals considerable homology in the am...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1967
ISSN: 0306-3283
DOI: 10.1042/bj1050039