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PubMed1976

The "phosphoryl-enzyme" from phosphoglycerate kinase.

The "phosphoryl-enzyme" prepared from phosphoglycerate kinase and adenosine 5'-triphosphate in the presence of an adenosine 5'-diphosphate trap is shown to contain stoichiometric amounts of 3-phosphoglycerate. This "phosphoryl-enzyme" is chemically competent, but is probably just a tight complex between 1,3-bisphosphoglycerate and the enzyme. The two partial exchange reactions (between adenosine 5'-diphosphate, and adenosine 5'-triphosphate, and between 3-phosphoglycerate and 1,3-bisphosphoglycerate) can both be observed, but their rates are very much slower than the rate of overall catalysis. No substrate analogue was found that accelerated the partial exchange reactions. Catalysis of each of the two exchange reactions and of the kinase reaction coincides after isoelectric focusing of purified enzyme, but the amount of cosubstrate necessary to cause the observed partial exchange rates is so small that these reactions may well be artifactual. The balance of evidence does not support a ping-pong pathway via phosphoryl-enzyme, and the reaction may be a sequential one in which the phosphoryl group is transferred between substrates in a ternary complex. The results point to the dangers in the interpretation of experiments where very small amounts of contaminating cosubstrate can lead to large kinetic effects, and to the possibility of mistaken deductions about the identity of reaction intermediates.

Adenosine Diphosphate↗
PubMed1997

[Mechanisms of shedding of a soluble form of the TSH receptor].

The thyrotropin (TSH) receptor in human-thyroid glands is cleaved into an extracellular alpha subunit and a transmembrane beta subunit held together by disulfide bridges. An excess of the latter component relative to the former suggests shedding of the ectodomain. Indeed we observed such shedding in cultures of human thyrocytes and permanently transfected L or Chinese hamster ovary cells. Shedding was increased by inhibitors of endocytosis, recycling and lysosomal degradation suggesting that it was dependent on receptor residency at the cell surface. It was slightly increased by TSH and phorbol esters whereas forskolin and 8 bromo cAMP were without effect. The complete inhibition of soluble TSH receptor shedding by the specific inhibitor BB-2116 indicated that the cleavage reaction is catalyzed probably at the cell surface by a matrix metalloprotease-like enzyme. Shedding of the TSH receptor alpha domain is the consequence of two events: cleavage of the proreceptor into alpha and beta subunits and reduction of the disulfide bridge(s). The use of different specific inhibitors including monoclonal antibodies allowed us to implicate the enzyme protein disulfide isomerase in the reduction of TSHR disulfide bounds. The shed alpha subunit probably results in circulating TSH receptor ectodomain detected in human blood. This shedding mechanism might be implicated in the development of autoimmune diseases.

Animals↗
PubMed2004

[Metabolic flux analysis of L-valine fermentation in Corynebacterium glutamicum].

In industrial fermentation of amino acids the cells are often forced to synthesize the biochemicals excessive of their physiological needs. The knowledge of metabolic networks and their regulation relevant usually come from biochemical research, especially from enzymology, not from engineering study. To enrich the knowledge of metabolic sub-network of L-valine syntheses for higher production of L-valine, Corynebacterium glutamicum AS1.495 and its genetic derivatives AA361, AAT231, AATV341 were used for metabolic flux analysis. AS1.495 is a leucine auxotrophic (Leu-), and the three derivatives carry additional mutations. AA361 contains D-aspartic acid-beta-hydroxamate supersensitive marker (Leu-, L-AAHss), AAT231 (Leu-, L-AAHss, 2-TAr) is D-aspartic acid-beta-hydroxamate supersensitive and 2-thiazole alanine resistant, and AAT341 (Leu-, L-AAHss, 2-TAr, Vd-) is a D-aspartic acid-beta-hydroxamate supersensitive, 2-thiazole alanine resistant and valine-decompose-ability imperfect (Vd-). The concentrations of extra-cellular metabolites were determined under sub-steady-state of the batch culture. The metabolic flux distribution maps of the four strains were obtained, compared and analyzed. Our analysis showed that the flux ratio of EMP and HMP from the glucose-6-phosphate had increased from 0.205 in the parental strain AS1.495 to 0.321 in the multiple-mutation strain AATV341; the flux ratio of L-valine synthesis branch and the rest branches from the pyruvate node increased from 0.188 in AS1.495 to 3.29 in AATV341; the flux of lactic acid synthesis branch decreased from 11.1 in AS1.495 to 1.16 in AATV341; the flux of L-valine synthesis branch increased from 5.37 in AS1.495 to 37.3 in AATV341; and the productivity of L-valine correspondently increased from 4 g/L in AS1.495 to 24.5 g/L in AATV341. These results indicate that the introduction of analog supersensitive marker L-AAH55 and/or analog resistant marker 2-TAr skew the metabolic flux towards the formation of L-valine. This study revealed the usefulness of the metabolic flux analysis as a tool for verification of existing production strains. The analysis may play an important role in helping us b to rationally re-design metabolism for further improvement of fermentation process.

Corynebacterium glutamicum↗
PubMed1992

Inhibition of assimilatory nitrate reductase activity in soil by glutamine and ammonium analogs.

Recent work in our laboratory indicated that the inhibitory effect of ammonium (NH4+) on assimilatory nitrate reductase (ANR) activity in soil is not due to NH4+ per se but to glutamine formed by microbial assimilation of NH4+. To test this conclusion, we studied the effects of eight analogs of L-glutamine (L-glutamic acid gamma-methyl ester, L-glutamic acid gamma-hydrazide, L-glutamic acid gamma-hydroxamate, L-glutamic acid gamma-ethyl ester, L-glutamic acid dimethyl ester, L-asparagine, L-aspartic acid beta-methyl ester, and L-aspartic acid beta-hydroxamate) and two analogs of ammonium (hydroxylamine and methylamine) on ANR activity in soil slurries. The studies with the L-glutamine analogs showed that all except L-glutamic acid dimethyl ester inhibited ANR activity in soil. The sharp contrast observed between the strong inhibitory effect of L-glutamic acid gamma-methyl ester on ANR activity and the complete lack of an inhibitory effect with the corresponding dimethyl ester suggests that only the free-acid form of glutamine effectively inhibits ANR activity. The studies with hydroxylamine and methylamine showed that both of these ammonium analogs inhibited ANR activity in soil and that this inhibition was dependent upon glutamine synthetase activity. This dependence indicates that inhibition of ANR activity by hydroxylamine and methylamine was due to formation of the glutamine analogs L-glutamic acid gamma-hydroxamate and L-glutamic acid gamma-methylamide, respectively. These observations support the conclusion that the inhibitory effect of NH4+ on ANR activity in soil is due to glutamine formed by microbial assimilation of NH4+.

Journal Article↗