-
Identification, purification, and characterization of a D-arabinitol-specific dehydrogenase from Candida tropicalis.
Syva Company, Research Department, Palo Alto, CA 94304.
A novel D-arabinitol (DA) dehydrogenase was identified and purified more than 300-fold from Candida tropicalis. The enzyme is specific for DA and catalyzes the NAD(+)-dependent oxidation at carbon 4 to yield D-ribulose. Purification was accomplished by a combination of protamine sulfate and ammonium sulfate precipitation and dye ligand chromatography on a reactive yellow 86 column. The apparent Km of the enzyme for DA ([NAD+] = 2.2 mM) is 39.8 mM. The apparent Km for NAD+ ([DA] = 384 mM) is 0.12 mM. The pH-optimum for the enzymatic oxidation of DA is approximately 10. Cofactor stereospecificity studies demonstrate that the enzyme catalyzes transfer of the 4(S) hydrogen of NADH with D-ribulose as substrate. The polyol substrate specificity of the present DA dehydrogenase makes the enzyme potentially useful for the development of a simple and specific method for the measurement of DA, a metabolite of pathogenic Candida spp. which has been described as a marker for disseminated candidiasis.
PMID: 8250887 [PubMed - indexed for MEDLINE]
-
Cited by 3 PubMed Central articles
-
Characterization of a novel NADP(+)-dependent D-arabitol dehydrogenase from the plant pathogen Uromyces fabae.
Link T, Lohaus G, Heiser I, Mendgen K, Hahn M, Voegele RT.
Biochem J. 2005 Jul 15; 389(Pt 2):289-95.
[Biochem J. 2005]
-
ReviewCurrent status of nonculture methods for diagnosis of invasive fungal infections.
Yeo SF, Wong B.
Clin Microbiol Rev. 2002 Jul; 15(3):465-84.
[Clin Microbiol Rev. 2002]
-
An automated enzymatic method for measurement of D-arabinitol, a metabolite of pathogenic Candida species.
Switchenko AC, Miyada CG, Goodman TC, Walsh TJ, Wong B, Becker MJ, Ullman EF.
J Clin Microbiol. 1994 Jan; 32(1):92-7.
[J Clin Microbiol. 1994]