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At least 1,063 records · Page 59Linked to original sources
PubMed1989

A novel biosynthesis of medium chain length alpha-ketodicarboxylic acids in methanogenic archaebacteria.

Gas chromatographic-mass spectrometric analysis on the distribution of alpha-ketodicarboxylic acids in various bacteria determined that alpha-ketoglutarate and alpha-ketoadipate are widely distributed in all the bacteria examined, whereas alpha-ketopimelate and alpha-ketosuberate are found only in the methanogenic archaebacteria. Labeling experiments with stable isotopes indicated that each of these acids arises from alpha-ketoglutarate by repeated alpha-ketoacid chain elongation. The final product in this series of reactions, alpha-ketosuberate, serves in the methanogenic bacteria as the biosynthetic precursor to the 7-mercaptoheptanoic acid portion of 7-mercaptoheptanoylthreonine phosphate, a methanogenic coenzyme.

Adipates↗
PubMed1975

Physiological basis for preferential uptake of D-alpha-aminoadipate over the L-isomer by Alcaligenes denitrificans.

Alcaligenes denitrificans, pre-incubated with D-alpha-aminoadipate and assayed for L-isomer uptake without removal of extracellular D-isomer, exhibits a reduced rate of uptake and a reduced level at which steady state is achieved. During D- or L-isomer uptake, intracellular alpha-aminoadipate is exclusively the L-configuration. These data are consistent with an intracellular, mediated reduction in L-isomer uptake as the physiological basis for preferential D-alpha-aminoadipate uptake by A. denitrificans growing on racemic alpha-aminoadipate. Translocated D-alpha-aminoadipate is rapidly metabolized to form an L-isomer pool which subsequently reduces the rate of L-isomer uptake and the level at which steady state occurs resulting in a preferred D-isomer uptake. Competitive inhibition of L-alpha-aminoadipate uptake by the D-isomer or a difference in the maximum rates of uptate uptake is an inducible process expressed only in the presence of that compound and while uptake of L-alpha-animoadipate is also inducible there is a low rate of constitutive uptake. While L-alpha-aminoadipate uptake occurs against a concentration gradient, uptake of the D-isomer is not against a gradient. D- and L-isomer uptake are active processes since both are inhibited by azide, cyanide and 2,4-dinitrophenol.

Adipates↗
PubMed1975

Immobilized glutamate oxaloacetate transaminase. Steady state kinetic analysis and stability studies.

1. Glutamate oxaloacetate transaminase (L-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) was immobilized on amino ethyl cellulose using the bifunctional reagent diethyl adipimidate. 2. The steady state kinetic analysis was performed for the particulate and the free enzyme, and the Michaelis constants measured for the amino ethyl cellulose derivative were not greatly different from those measured for the free glutamate oxaloacetate transaminase, while the latter were in good agreement with values in the literature. 3. The amino ethyl cellulose-glutamate oxaloacetate transaminase was slightly more stable than the free enzyme at 65 degrees C, but was stabilised less by polyethylene glycol than the free enzyme.

Adipates↗