4-Acetamidobutyrate Deacetylase in the Yeast Candida boidinii Grown on Putrescine or Spermidine as Sole Nitrogen Source and Its Probable Role in Polyamine Catabolism

One hundred and fourteen bacterial cultures representing most of the species in the Bacillus genus were tested for the production of extracellular barley gum cytase. Assays were made on shake-flask cultures grown on a medium containing glucose and yeast extract. Although all the organisms had some enzymatic activity, certain strains of Bacillus subtilis gave the best yields of cytase. On a medium with asparagine as the sole nitrogen source even higher yields were obtained. The crude cytase preparations were stable and after freeze-drying most of the original activity remained.

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Monomethylamine as a Nitrogen Source for a Nonmethylotrophic Bacterium, Agrobacterium tumefaciens

Applied and Environmental Microbiology ◽

10.1128/aem.00469-10 ◽

2010 ◽

Vol 76 (12) ◽

pp. 4102-4104 ◽

Cited By ~ 24

Author(s):

Yin Chen ◽

Kathryn L. McAleer ◽

J. Colin Murrell

Keyword(s):

Agrobacterium Tumefaciens ◽

Carbon Source ◽

Nitrogen Source ◽

Sole Nitrogen Source ◽

Key Enzymes ◽

Genes Encoding

ABSTRACT Monomethylamine can be used by nonmethylotrophs as a sole nitrogen source but not as a carbon source; however, little is known about the genes and enzymes involved. The γ-glutamylmethylamide/N-methylglutamate pathway for monomethylamine utilization by methylotrophs has recently been resolved. We have identified genes encoding key enzymes of this pathway in nonmethylotrophs (e.g., Agrobacterium tumefaciens) and demonstrated that this pathway is also involved in the utilization of monomethylamine as a nitrogen source by nonmethylotrophs.

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Mutants affecting histidine utilization inAspergillus nidulans

Genetics Research ◽

10.1017/s0016672300015524 ◽

1975 ◽

Vol 25 (2) ◽

pp. 119-135 ◽

Cited By ~ 8

Author(s):

Meryl Polkinghorne ◽

M. J. Hynes

Keyword(s):

Carbon Source ◽

Nitrogen Source ◽

Sole Carbon Source ◽

Nitrogen Sources ◽

Limiting Factor ◽

Sole Nitrogen Source ◽

Wild Type ◽

Exogenous Substrate ◽

Growth Properties ◽

Type Strains

SUMMARYWild-type strains ofAspergillus nidulansgrow poorly onL-histidine as a sole nitrogen source. The synthesis of the enzyme histidase (EC. 4.3.1.3) appears to be a limiting factor in the growth of the wild type, as strains carrying the mutantareA102 allele have elevated histidase levels and grow strongly on histidine as a sole nitrogen source.L-Histidine is an extremely weak sole carbon source for all strains.Ammonium repression has an important role in the regulation of histidase synthesis and the relief of ammonium repression is dependent on the availability of a good carbon source. The level of histidase synthesis does not respond to the addition of exogenous substrate.Mutants carrying lesions in thesarA orsarB loci (suppressor ofareA102) have been isolated. The growth properties of these mutants on histidine as a sole nitrogen source correlate with the levels of histidase synthesized. Mutation at thesarA andsarB loci also reduces the utilization of a number of other nitrogen sources. The data suggest that these two genes may code for regulatory products involved in nitrogen catabolism. No histidase structural gene mutants were identified and possible explanations of this are discussed.

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Biosynthesis of higher alcohol flavour compounds by the yeastSaccharomyces cerevisiae: impact of oxygen availability and responses to glucose pulse in minimal growth medium with leucine as sole nitrogen source.

Yeast ◽

10.1002/yea.3045 ◽

2014 ◽

pp. n/a-n/a ◽

Cited By ~ 2

Author(s):

Esteban Espinosa Vidal ◽

Marcos Antonio de Morais Junior ◽

Jean Marie François ◽

Gustavo M. de Billerbeck

Keyword(s):

Nitrogen Source ◽

Growth Medium ◽

Oxygen Availability ◽

Sole Nitrogen Source ◽

Minimal Growth ◽

Higher Alcohol ◽

Flavour Compounds ◽

Glucose Pulse

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Purification of arginase from Aspergillus nidulans.

Acta Biochimica Polonica ◽

10.18388/abp.1994_4700 ◽

1994 ◽

Vol 41 (4) ◽

pp. 467-471 ◽

Cited By ~ 4

Author(s):

A Dzikowska ◽

J P Le Caer ◽

P Jonczyk ◽

P Wëgleński

Keyword(s):

Saccharomyces Cerevisiae ◽

Neurospora Crassa ◽

Molecular Mass ◽

Nitrogen Source ◽

Aspergillus Nidulans ◽

Sole Nitrogen Source ◽

Mass Ratio ◽

Conserved Domains ◽

Native Molecular Mass ◽

High Degree

Arginase (EC 3.5.3.1) of Aspergillus nidulans, the enzyme which enables the fungus to use arginine as the sole nitrogen source was purified to homogeneity. Molecular mass of the purified arginase subunit is 40 kDa and is similar to that reported for the Neurospora crassa (38.3 kDa) and Saccharomyces cerevisiae (39 kDa) enzymes. The native molecular mass of arginase is 125 kDa. The subunit/native molecular mass ratio suggests a trimeric form of the protein. The arginase protein was cleaved and partially sequenced. Two out of the six polypeptides sequenced show a high degree of homology to conserved domains in arginases from other species.

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