Sorbitol dehydrogenase of Drosophila -: Gene, protein, and expression data show a two-gene system

被引:16
作者
Luque, T
Hjelmqvist, L
Marfany, G
Danielsson, O
El-Ahmad, M
Persson, B
Jörnvall, H [1 ]
Gonzàlez-Duarte, R
机构
[1] Karolinska Inst, Dept Med Biochem & Biophys, S-17177 Stockholm, Sweden
[2] Univ Barcelona, Fac Biol, Dept Genet, E-08071 Barcelona, Spain
关键词
D O I
10.1074/jbc.273.51.34293
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Drosophila melanogaster sorbitol dehydrogenase (SDH) is characterized as a two-enzyme system of the medium chain dehydrogenase/reductase family (MDR). The SDH-1 enzyme has an enzymology with K-m and k(cat) values an order of magnitude higher than those for the human enzyme but with a similar K-cat/K-m ratio. It is a tetramer with identical subunits of similar to 38 kDa. At the genomic level, two genes, Sdh-1 and Sdh-2, have a single transcriptional start site and no functional TATA box. Expression is greater in larvae and adults than in pupae, where it is very low. At all three stages, Sdh-1. constitutes the major transcript. Sdh-1 and Sdh-2 genes were located at positions 84E-F and 86D in polytene chromosomes. The deduced amino acid sequences of the two genes show 90% residue identity. Evaluation of the sequence and modeling of the structure toward that of class I alcohol dehydrogenase (ADH) show altered loop and gap arrangements as in mammalian SDH and establishes that SDH, despite gene multiplicity and larger variability than the "constant" ADH of class III, is an enzyme conserved over wide ranges.
引用
收藏
页码:34293 / 34301
页数:9
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