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Purification and characterization of a cysteine dioxygenase from the yeast phase of Histoplasma capsulatum
- Source :
- Biochemistry. 22:762-768
- Publication Year :
- 1983
- Publisher :
- American Chemical Society (ACS), 1983.
-
Abstract
- A cysteine dioxygenase, cysteine oxidase (EC 1.13.11.20), has been purified from the cytosolic fraction of yeast phase cells of the dimorphic fungus Histoplasma capsulatum. The cysteine oxidase is an iron-containing dioxygenase with a molecular weight of 10500 (±1500) and is present only in the yeast phase of the fungus. The enzyme is highly specific for l-cysteine, with a Km of 2 × 10−5 M in vitro. The product of cysteine oxidation is cysteinesulfinic acid, as analyzed by thin-layer chromatography and mass spectroscopy. To our knowledge, this is the first cysteine oxidase isolated from a fungus, and it probably plays an important role in the mycelial to yeast phase transition of H. capsulatum during which redox potential and cysteine levels are crucial factors. © 1983, American Chemical Society. All rights reserved.
- Subjects :
- chemistry.chemical_classification
biology
Chemistry
Histoplasma
Cysteine Dioxygenase
Cysteine dioxygenase
Fungus
biology.organism_classification
Biochemistry
Peptide Fragments
In vitro
Dioxygenases
Substrate Specificity
Enzyme
Dioxygenase
Flavin-Adenine Dinucleotide
Oxygenases
biology.protein
Dimorphic fungus
Mycelium
Cysteine
Subjects
Details
- ISSN :
- 15204995 and 00062960
- Volume :
- 22
- Database :
- OpenAIRE
- Journal :
- Biochemistry
- Accession number :
- edsair.doi.dedup.....af361ec3f3ab75dd8d07866ca6934e96
- Full Text :
- https://doi.org/10.1021/bi00273a009