Open AccessEnzymes involved in the formation of glycerol 3‐phosphate and the by‐products dihydroxyacetone and glycerol in Zymomonas mobilis
Author(s) -
Horbach Silke,
Strohhäcker Joachim,
Welle Roland,
Graaf Albert,
Sahm Hermann
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07004.x
Subject(s) - dihydroxyacetone phosphate , dihydroxyacetone , zymomonas mobilis , triosephosphate isomerase , glyceraldehyde , glycerol , biochemistry , aldolase a , glycerol 3 phosphate dehydrogenase , transaldolase , enzyme , glycolaldehyde , fructose , chemistry , dehydrogenase , biology , pentose phosphate pathway , glycolysis , ethanol , catalysis , ethanol fuel
In Zymomonas mobilis a novel pathway for the formation of glycerol 3‐phosphate was identified by enzymatic studies and nuclear magnetic resonance spectroscopy. This pathway branches off from the Entner‐Doudoroff pathway at the intermediate glyceraldehyde 3‐phosphate and proceedes via dihydroxyacetone phosphate, dihydroxyacetone, glycerol to glycerol 3‐phosphate. The reaction sequence is catalyzed by the enzymes triosephosphate isomerase (0.4 U (mg protein) −1 ), dihydroxyacetone phosphatase (0.31 U (mg protein) −1 ), dihydroxyacetone reductase (0.25 U (mg protein) −1 ), and glycerokinase (0.08 mU (mg protein) −1 ), respectively. The action of a postulated aldolase catalyzing the cleavage of fructose 6‐phosphate to dihydroxyacetone and glyceraldehyde 3‐phosphate could be excluded.