Nitrogen regulation of amino acid utilization by Neurospora crassa
نویسندگان
چکیده
منابع مشابه
Peptide utilization by nitrogen-starved Neurospora crassa.
Peptides ranging in size from a mean number of 30 residues down to dipeptides supported growth of a leucine auxotroph when used as both a nitrogen and leucine source. Under nitrogen-limiting conditions, the peptides induced extracellular peptidohydrolytic activity, hydrolyzing peptides to monomer amino acids. Growth of a leu-2 mutant of Neurospora crassa on those peptides transportable by the o...
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Conidia of Neurospora crassa exhibit an ability to transport various amino acids against a concentration gradient. The conidial transport system has previously been characterized in terms of kinetics, competitions, and genetic control. This study describes the development of a new and highly active transport capability which is elaborated during the early stages of development but prior to evid...
متن کاملSize restriction on utilization of peptides by amino acid auxotrophs of Neurospora crassa.
Growth of an amino acid auxotroph of Neurospora crassa on oligopeptides is shown to occur by extracellular hydrolysis, with subsequent utilization of monomer amino acid residues, and by transport of peptides. Peptides with a hydrodynamic volume greater than that of trileucine are not transported, and this lack of transport is shown to be due to restriction by the oligopeptide transport system r...
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The ability of Neurospora crassa FGSC 4335 in the biotransformation of hydrocortisone was investigated. The microorganism produced two major metabolites after incubation with the substrate for seven days. Each microbial product was purified chromatographically and identified on the basis of spectral data. The products were identified as 11?,17?,20?,21-tetrahydroxypregn-4-en-3-one (II) and 11?-h...
متن کاملAmino acid sequence of tyrosinase from Neurospora crassa.
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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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1984
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.160.2.493-498.1984