Back to Search Start Over

Purification and characterization of a cysteine dioxygenase from the yeast phase of Histoplasma capsulatum

Authors :
Gerald Medoff
Vijaya Kumar
Robert Goewert
George S. Kobayashi
Margherita Sacco
Bruno Maresca
Kumar, Bv
Maresca, B
Sacco, Margherita
Goewert, R
Kobayashi, G
Medoff, M.
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.

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