Back to Search Start Over

Purification and characterization of two dihydroxyacetone kinases from Schizosaccharomyces pombe IFO 0354

Authors :
Yoshihara, Kyoko
Shimada, Yuzo
Karita, Shuichi
Kimura, Tetsuya
Sakka, Kazuo
Ohmiyo, Kunio
Source :
Applied and Environmental Microbiology. Dec, 1996, Vol. 62 Issue 12, p4663, 3 p.
Publication Year :
1996

Abstract

The characterization of two dihydroxyacetone kinases (DHAKs), DHAK I and DHAK II, purified from Schizosaccharomyces pombe IFO 0354, shows that they are immunologically different from each other. DHAK II is more important than DHAK I for the dissimilation of glycerol via dihydroxyacetone. When the enzyme activity is measured in a mixed buffer, DHAK I shows optimum activity at pH 6.0 and DHAK II at pH 7.0. The optimum temperature for the activity of DHAK I is 50 degree celsius (C)and that for the activity for DHAK II is 60 degree C.

Details

ISSN :
00992240
Volume :
62
Issue :
12
Database :
Gale General OneFile
Journal :
Applied and Environmental Microbiology
Publication Type :
Academic Journal
Accession number :
edsgcl.19005195