Escherichia coli acetate kinase

ACETATE KINASE. MacNeal et first proposed the use of Escherichia coli acetate kinase as a nearly ideal... 

Wong, S.S. Wong, L.-J.C. Inactivation of Escherichia coli acetate kinase by N-ethylmaleimide. Protection by substrates and products. Biochim. Biophys. Acta, 615, 121-131 (1980)... 

Fox, D.K. Roseman, S. Isolation and characterization of homogeneous acetate kinase from Salmonella typhimurium and Escherichia coli. J. Biol. Chem., 261, 13487-13497 (1986)... 

Figure 1 Fermentation pathways of Escherichia coli. Gene symbols ackA, acetate kinase adhE, alcohol dehydrogenase fdh, formate dehydrogenase of FHL complex fhn, nitrate-inducible formate dehydrogenase hyd, hydrogenase 3 of FHL complex IdhA, NAD+-dependent D-(-)-lactate dehydrogenase pfl, pyruvate formate-lyase pta, phosphotransacetylase. FHL, formate hydrogenlyase. Redrawn from reference 29...

Lee, T.-Y., Makino, K., Shinagawa, H. and Nakata, A. (1990). Overproduction of acetate kinase activates the phosphate regulation in the absence of the phoK phoM functions in Escherichia coli.J. Bacterial. 172, 2245-2249. 

Wanner, B.L. and Wilmes-Riesenberg, M.R. (1992). Involvement of phospho-transacetylase, acetate kinase, and acetyl phosphate synthesis in control of the phosphate regulon in Escherichia coli.J. Bacteriol. 174, 2124 2130. 

Figure 17.7 Aerobic metaboiic pathways involved in SA production in wiid-type Escherichia coli. PEP, phosphoenoipyru-vate OAA, oxaioacetate MAE, maiate FUM, fumarate Suc-CoA, succinyi-CoA a-KG, a-ketoglutarate iCT, isocitrate CiT, citrate GOX, glyoxylate IdhA, iactate dehydrogenase pfIB, pyruvate formateiyase pta, phosphate acetyi-transferase ackA, acetate kinase poxB, pyruvate dehydrogenase ppc, PEP carboxykinase ...

Isoenzymes of enzymes involved in the first step of a branched biosynthetic pathway may differ in their sensitivity to inhibitors. Thus the enzyme aspartate kinase catalyses in Escherichia coli the first step in the synthesis of lysine, methionine and threonine. Three isoenzymes occur, the synthesis and activity of one is suppressed by L-lysine, the activity of the second is depressed by L-threonine and the activity of the third by homoserine (an intermediate in methionine biosynthesis). Thus accumulation of L-lysine or L-threonine suppresses their own further S3mthesis but does not prevent the activity of the aspartokinase isoenzyme involved in methionine synthesis. Again peroxidase isoenzymes differ in their activity in destroying indol-3yl-acetic acid (lAA) and the pattern of peroxidase isoenzymes can be altered by feeding lAA or gibberellic acid (GA) to plant tissues. 

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