STRUCTURAL STUDIES ON GLYCERALDEHYDE-PHOSPHATE DEHYDROGENASE FROM RAT SKELETAL-MUSCLEстатья
Информация о цитировании статьи получена из
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 19 сентября 2015 г.
Аннотация:The NH2-terminal amino acid sequence of rat skeletal muscle glyceraldehyde-phosphate dehydrogenase (d-glyceraldehyde-3-phosphate : NAD+ oxidoreductase(phosphorylating), EC 1.2.1.12) was determined to be
Val-Lys-Val-Gly-Val-Asn-Gly-Phe-Gly-Arg-Ile-Gly-Arg-Leu-Val-Thr-Arg-Ala-Ala-Phe-Ser-Ser-(-)-(-)-Val-Asx-Ile-Val-Ala-Ile.
The presence of Asn instead of Asp in position 6 differentiates this enzyme from other glyceraldehyde-3-phosphate dehydrogenases so far sequenced with the exception of the enzymes isolated from liver. The location of Asn in position 6 has been considered as a specific property of liver glyceraldehyde-3-phosphate dehydrogenase (Kulbe, K.D., Jackson, K.W. and Tang, J. (1975) Biochem. Biophys. Res. Commun. 67, 35–42); this suggestion is not sustained by the results of the present investigation.
The amino acid composition of the rat skeletal muscle dehydrogenase demonstrates the unusually low histidine content of this enzyme as compared to other mammalian muscle glyceraldehyde-phosphate dehydrogenases.