Cysteine oxidase and cysteine sulfinic acid decarboxylase in developing rat liver

Summary The patterns of development of cysteine oxidase (CO) and cysteine sulfinic acid decarboxylase (CSD) in rat liver are not similar. It was observed that CO is not under sex control as CSD is. The results obtained agree with the idea that, in liver, as well as in brain, CSD is the limiting factor for the regulation of taurine biosynthesis.Acknowledments: The authors thank CEA for financial support for the purchasing of labelled substrates.     

Activities of cystathionase,cysteine sulphinic acid decarboxylase and serine dehydrase in the liver of tumour-bearing rats

Résumé Dans le foie de rats porteurs de tumeurs (épithéliome de Guérin et sarcome de l'estomac), les activités de la cystathionase, de la décarboxylase de l'acide cysteine sulfinique et de la sérine déhydrase sont considérablement diminuées: cette diminution est de l'ordre de 50%, 15 jours après implantation de ces tumeurs. Si à ce moment le sarcome (qui ne provoque pas de métastases) est chirurgicalement extirpé, on observe une restauration des activités enzymatiques qui, après 15 jours, est totale pour la cystathionase et très significative pour la décarboxylase.

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Equipe de Recherche C.N.R.S. No. 43.     

Effects of pyridoxal phosphate andl-dopapyridoxal phosphate on DOPA decarboxylase activity

Sommaire Les résultats obtenus démontrent une inhibition de l'activité de la DOPA decarboxylase par de haute concentration de PLP ou de faible concentration del-DOPA plus PLP. Ceci pourrait expliquer les observations cliniques et expérimentales précédentes démontrant que la pyridoxine antagonise l'effet del-DOPA utilisé dans le traitement de la maladie de Parkinson.     

Effect of dietary cholic acid and cholesterol on liver and kidney cystathionase and cysteine sulfinate decarboxylase activities and taurine concentrations in the rat

Summary Hepatic cystathionase and cysteine sulfinate decarboxylase activities are drastically affected by cholic acid added to the diet without cholesterol. When cholic acid and cholesterol are given together, only cysteine sulfinate decarboxylase activity is changed. Neither kidney enzyme activity nor taurine concentrations in the liver and kidney are noticeably modified, whatever the diet.This research was supported by INSERM (Contract 78.152.3) and by CEA.     

Inactivation of N-assimilating enzymes and proteolytic activities in wheat leaf extracts: Effect of pyridine nucleotides and of adenylates

Summary Nitrate reductase was protected from inactivation in wheat leaf extracts by NADH, while NADPH was less effective. NAD, NADP or adenylates did not affect nitrate reductase inactivation in vitro. Glutamine synthetase was more stable than nitrate reductase and was protected from inactivation by ATP. ADP, AMP or pyridine nucleotides had no or only a minor effect on the decrease of glutamine synthetase activity in extracts. The caseolytic activity extracted from senescing leaves was slightly decreased by NADH and NADPH but this effect was not sufficient to explain the stabilization of nitrate reductase by NADH. Oxidized pyridine nucleotides and adenylates had no major effect on the caseolytic activity under the conditions used.This work was supported by grant 3.067-0.81 from the Swiss National Science Foundation. Author for correspondence: U.F.     

A comparison of pyridoxal 5′-phosphate dependent decarboxylase and transaminase enzymes at a molecular level

Pyridoxal 5′-phosphate is a coenzyme for a number of enzymes which catalyse reactions at C^α of amino acid substrates including transaminases, decarboxylases and serine hydroxymethyltransferase. Using the X-ray coordinates for a transaminase, aspartate aminotransferase, and the results of stereochemical and mechanistic studies for decarboxylases and serine hydroxymethyltransferase, an active-site structure for the decarboxylase group is constructed. The structure of the active-site is further refined through active-site pyridoxyllysine peptide sequence comparison and a 3-D catalytic mechanism for the L-α-amino acid decarboxylases is proposed. The chemistry of serine hydroxymethyltransferase is re-examined in the light of the proposed decarboxylase mechanism.     

A comparison of pyridoxal 5'-phosphate dependent decarboxylase and transaminase enzymes at a molecular level.

Pyridoxal 5'-phosphate is a coenzyme for a number of enzymes which catalyse reactions at C alpha of amino acid substrates including transaminases, decarboxylases and serine hydroxymethyltransferase. Using the X-ray coordinates for a transaminase, aspartate aminotransferase, and the results of stereochemical and mechanistic studies for decarboxylases and serine hydroxymethyltransferase, an active-site structure for the decarboxylase group is constructed. The structure of the active-site is further refined through active-site pyridoxyllysine peptide sequence comparison and a 3-D catalytic mechanism for the L-alpha-amino acid decarboxylases is proposed. The chemistry of serine hydroxymethyltransferase is re-examined in the light of the proposed decarboxylase mechanism.     

Effect of temperature on the spectral properties of glutamic-aspartic transaminase and pyridoxal phosphate

Zusammenfassung Ein Zusammenhang zwischen optischen Eigenschaften und Stabilität der Transaminasen wird nachgewiesen. Temperaturabhängigkeit und Art der Partnerverbindung im Enzymsubstrat-Komplex (Aminooder -Ketoverbindung) einerseits und Konformation anderseits sind analog.

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Supported by research grant from the Royal Hellenic Research Foundation.     

Inactivation studies of angiotensin II by purified enzymes

Zusammenfassung Die hochgereinigte Arylamidase vom Schweinehirn spaltet, im Gegensatz zur ebenfalls isolierten Säureprotease und Aminopeptidase, Ile⁵-Angiotensin II, wobei die ersten 5 N-terminalen Aminosäuren von hydrolytischen Enzymen freigesetzt werden.     

Effect of X-rays on the proteolytic enzymes of granulocytes and on phagocytosis index in guinea-pigs

Résumé Après l'exposition du cobaye aux rayons X, nous avons constaté l'affaiblissement des enzymes granulocytaires suivants: la protéase acide, la protéase alcaline, le plasminogène, l'activateur du plasminogène, l'activité fibrinolytique spontanée. L'index de la phagocytose n'a diminué qu'au 20e jour après l'irradiation.     

Metabolism of pyridoxal phosphate in the liver of hypo- and hyperthyroid rats

Riassunto È stata determinata nel fegato di ratti normali, ipotiroidei ed ipertiroidei l'attività degli enzimi che portano alla sintesi del piridossalfosfato, la piridossalcinasi e la piridossaminfosfatoossidasi, e del primo enzima che ne catalizza la demolizione, una fosfatasi. In condizioni di ipertiroidismo sono aumentate la piridossalcinasi e la fosfatasi, mentre la ossidasi è invariata; nell'ipotiroidismo invece non si osservano modificazioni significative. La quantità di acido piridossico escreta con l'urina è diminuita nell'ipotiroidismo e aumentata nell'ipertiroidismo.

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This investigation was supported by Research Grant No. AM-05676 from the United States Public Health Service.     

Effect of phosphonic analogues of glutamic acid on glutamate decarboxylase

Among the phosphonic analogues of glutamic acid, only 4-amino-4-phosphono butyric acid, the compound which shows the highest affinity for pyridoxal phosphate, inhibits competitively both Escherichia coli and rat brain glutamate decarboxylases. Phosphinothricin, 2-amino-4-(methylphosphino)butyric acid, is a strong inhibitor of the mammalian enzyme.     

Effect of phosphonic analogues of glutamic acid on glutamate decarboxylase

Summary Among the phosphonic analogues of glutamic acid, only 4-amino-4-phosphono butyric acid, the compound which shows the highest affinity for pyridoxal phosphate, inhibits competitively bothEscherichia coli and rat brain glutamate decarboxylases. Phosphinothricin, 2-amino-4-(methylphosphino)butyric acid, is a strong inhibitor of the mammalian enzyme.We acknowledge the gift of a sample of phosphinothricin by Prof. Przemyslaw Mastalerz as well as the technical assistance of Denois.     

Pyridoxine and pyridoxal phosphate concentrations in the liver and heart of thyroxinized animals

Riassunto Negli animali trattati con tiroxina si rileva una considerevole diminuizione del contenuto in piridossale fosfato del fegato e del cuore. Tale diminuizione sembra principalmente connessa ad un difetto dei processi di fosforilazione piuttosto che ad una carenza di piridossina.