| Value |
0.69
Hour^-1
Range: Table - link Hour^-1
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Hasona A, Kim Y, Healy FG, Ingram LO, Shanmugam KT. Pyruvate formate lyase and acetate kinase are essential for anaerobic growth of Escherichia coli on xylose. J Bacteriol. 2004 Nov186(22):7593-600. p.7596 table 2PubMed ID15516572
|
| Method |
P.7595 left column 2nd paragraph: "Cell density was determined as the OD at 420 nm after appropriate dilutions (Beckman DU640). Fermentation products and sugars were determined by high-pressure liquid chromatography, using HP 1090 (Hewlett-Packard) fitted with an Aminex HPX-87H column (Bio-Rad Laboratories). The mobile phase was 4 mM H2SO4 at 0.4 ml per min. Organic acids, sugars, and ethanol were detected by a filter photometric detector (210 nm) and/or a refractive index monitor, in series, as described previously (ref 34)." |
| Comments |
P.7596 left column bottom paragraph: "Acetate kinase-minus mutant is also xylose negative under anaerobic conditions: The results presented above suggest that the ATP derived from the pyruvate-to-acetyl-CoA-to-acetate pathway is a requirement for supporting anaerobic growth of E. coli on xylose. Since acetate kinase is the enzyme that converts acetyl phosphate to acetate and ATP, an ackA mutant is also expected to be defective in anaerobic growth on xylose. The results presented in Table 2 show that strain YK19, with the ackA202 mutation, also failed to grow with xylose under anaerobic conditions." |
| Entered by |
Uri M |
| ID |
108632 |