By Gerhard Gottschalk (auth.)
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Extra resources for Bacterial Metabolism
If true this would also imply similarities in the mechanisms of electron transport phosphorylation in mitochondria and bacteria. D. Uncouplers and inhibitors In growing cells of E. coli the oxidation ofNADH 2 and the phosphorylation of ADP are coupled. This coupling is largely lost when subcellular fractions are prepared. As a result, the P:O ratio is low and only little ATP is formed during oxidation of NADH 2 . In vivo this uncoupling can also be achieved by the addition of certain compounds to cell suspensions.
It has been shown, first by Tempest and later by other investigators, that at low NH3 concentrations a combination of glutamine synthetase and glutamate synthase is responsible for glutamate formation from et-oxoglutarate and ammonia. 2. Assimilation of ammonia. (a) By glutamate dehydrogenase (1) and subsequent transfer of the amino group by a transaminase (2). (b) By glutamine synthetase/ glutamate synthase (GS/GOGAT). aminotransferase )-catalyzes the reductive transfer of the amido group of glutamine to a-oxoglutarate.
Sulfate (inside) sulfate (outside) ATP suI fury lase ATP + sulfate .. adenosine-S' -phosphosulfatc + PP i (APS) APS phosphokinase ATP + APS - - - - - - . ' (PAPS) PAPS reductase 2 RSH + PAPS - - -........ sulfite + AMP-3'-phosphate + RSSR sulfite reductase sulfite + 3 NADPH2 - - -........ 3. Assimilatory reduction of sulfate and formation of cysteine. RSH stands for thioredoxin ; its reduced form is regenerated from the oxidized form with N ADPH 2' 40 IV. 3. It is evident from this table that only a few compounds serve as substrates in amino acid synthesis.