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Characterization of glycerol kinase and NAD‐independent glycerol‐3‐phosphate dehydrogenase from Pediococcus pentosaceus N5p
Author(s) -
Pasteris S.E.,
De Saad A.M. Strasser
Publication year - 1998
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1472-765x.1998.00391.x
Subject(s) - glycerol , nad+ kinase , dehydrogenase , biology , biochemistry , enzyme
The pathway involved in glycerol dissimilation in Pediococcus pentosaceus N5p, a strain isolated from wine, includes glycerol kinase and NAD‐independent glycerol‐3P dehydrogenase. The properties of these enzymes were studied. Glycerol kinase activity was maximal at 28 °C and pH 7·5 in 50 mmol l −1 Tris‐HCl buffer. The end‐products of the reaction acted as competitive inhibitors while fructose‐1,6‐diphosphate was a non‐competitive inhibitor. Mg 2+ was required for optimal enzyme activity. The Km values for both substrates were 0·11 and 0·37 mmol l −1 for glycerol and ATP, respectively. NAD‐independent glycerol‐3P dehydrogenase activity was maximal at 37 °C and pH 7·5 in 100 mmol l −1 Tris‐HCl buffer. The enzymatic activity was activated by KCN and bivalent cations as Mg 2+ and Ca 2+ , but it was strongly inhibited by others. Dihydroxyacetone phosphate acted as competitive inhibitor while ATP and phosphenolpyruvate were non‐competitive inhibitors.