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<em>Rhodotorula toruloides</em> (Banno) Wang et al.
<em>Rhodotorula toruloides</em> (Banno) Wang et al.
規(guī)格:
貨期:
編號(hào):B169980
品牌:Mingzhoubio

標(biāo)準(zhǔn)菌株
定量菌液
DNA
RNA

規(guī)格:
凍干粉
斜面
甘油
平板


產(chǎn)品名稱 Rhodotorula toruloides (Banno) Wang et al.
商品貨號(hào) B169980
Deposited As Rhodotorula gracilis Rennerfelt
Classification Sporidiobolales, Sporidiobolaceae
Strain Designations Pan
Application

Produces D-amino acid oxidase

Oxidation of cephalosporin C to glutaryl-7-aminocephalosporanic acid by D-amino acid oxidase

Biosafety Level 1

Biosafety classification is based on U.S. Public Health Service Guidelines, it is the responsibility of the customer to ensure that their facilities comply with biosafety regulations for their own country.

Product Format freeze-dried
Storage Conditions Frozen: -80°C or colder
Freeze-Dried: 2°C to 8°C
Live Culture: See Propagation Section
Type Strain no
Preceptrol&reg; no
Comments
Physiology
Pyrimidine utilization
Characterization of D-amino acid oxidase
Kinetic mechanism of D-amino acid oxidase
Inactivation of oxidase by phenylglyoxal
Medium ATCC® Medium 28: Emmons' modification of Sabouraud's agar
ATCC® Medium 200: YM agar or YM broth
ATCC® Medium 323: Malt agar medium
Growth Conditions
Temperature: 24°C to 26°C
Atmosphere: Typical aerobic
Name of Depositor MC Cocucci
Chain of Custody
ATCC <-- MC Cocucci <-- Inst. Agr. Microbiol., Milan
Cross References

Nucleotide (GenBank) : Z71657 Rhodotorula gracilis mRNA for D-amino acid oxidase.

Nucleotide (GenBank) : U60066 Rhodosporidium toruloides D-amino acid oxidase mRNA, complete cds.

References

Faotto L, et al. The primary structure of D-amino acid oxidase from Rhodotorula gracilis. Biotechnol Lett 17: 193-198, 1995.

Pilone MS, Butò S, Pollegioni L. A process for bioconversion of cephalosporin C by Rhodotorula gracilis D-amino acid oxidase. Biotechnol Lett 17: 199-204, 1995.

Buto S, et al. Evaluation of D-amino acid oxidase from Rhodotorula gracilis for the production of alpha-Keto acids: A reactor system. Biotechnol. Bioeng. 44: 1288-1294, 1994.

Gadda G, et al. Reaction of phenylglyoxal with arginine groups in D-amino-acid oxidase from Rhodotorula gracilis. J. Biol. Chem. 269: 17809-17814, 1994. PubMed: 7913089

Pollegioni L, et al. Kinetic mechanism of D-amino acid oxidases from Rhodotorula gracilis and Trigonopsis variabilis. J. Biol. Chem. 268: 13850-13857, 1993. PubMed: 8100225

Pollegioni L, Simonetta MP. Immunochemical studies on Rhodotorula gracilis D-amino acid oxidase. Experientia 47: 232-235, 1991. PubMed: 1672654

Pilone Simonetta M, et al. Properties of D-amino-acid oxidase from Rhodotorula gracilis. Eur. J. Biochem. 180: 199-204, 1989. PubMed: 2565232

Cocucci SM, Gianani L. Pyrimidine utilization by exponentially growing and starved cells of Rhodotorula gracilis. Experientia 30: 337-338, 1974. PubMed: 4858191

Cocucci MC, Marrè E. The effects of cycloheximide on respiration, protein synthesis and adenosine nucleotide levels in Rhodotorula gracilis. Plant Sci Lett 1: 293-301, 1973.

Cocucci MC, Rossi G. Biochemical and morphological aspects of zinc deficiency in Rhodotorula gracilis. Arch. Mikrobiol. 85: 267-279, 1972. PubMed: 4347451

Guerritore A, Hanozet GM. Presence and adaptive changes of citrate cleavage enzyme in the yeast Rhodotorula gracilis. Experientia 26: 28-30, 1970. PubMed: 5460902

Guerritore A, et al. Regulation of isocitrate lyase level in yeast growing on external carbon sources or on lipid reserves. Experientia 25: 131-132, 1969. PubMed: 5815004

Plant Sci. Lett. 1: 425-431, 1973.

Simonetta MP, et al. D-amino acid oxidase activity in the yeast Rhodotorula gracilis. FEMS Microbiol. Lett. 15: 27-31, 1982.

Pilone Simonetta M, et al. Induction of D-amino-acid oxidase by D-alanine in Rhodotorula gracilis grown in defined medium. J. Gen. Microbiol. 135: 593-600, 1989.

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