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DDAVP, dDAVP 1-deamino-8-D-arginine vasopressin; 1-deamino-8-N-arginine vasopressin
PYCR pyrroline-5-carboxylate reductase
AVP   1) Active non apeptide(?)
  2) Arginine Vaso-Pressin
AVT Arginine Vaso-Tocin
DDAVP 1-Desamino-8-D-Arginine Vasopressin
  = Desmopression
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OTC L-2-oxo-4-thiazolidine carboxylate
L-NAME L-arginine and NG-nitro-L-arginine methyl ester
ACC 1-Aminocyclopropane-1-carboxylate
P5C 1-Pyrroline-5-carboxylate
POCA 2-[5-(4-chlorophenyl)-pentyl]-oxirane-2-carboxylate
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CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
carboxylate reductase <enzyme> From pyrococcus furiosus; acts on glyceraldehyde to yield glycerate in a unique, partially nonphosphorylated, glycolytic pathway that generates acetyl-CoA from glucose without the participation of nicotinamide nucleotides
Registry number: EC 1.2.99.6
Synonym: glyceraldehyde ferredoxin oxidoreductase, tungsten-iron-sulfur protein, red tungsten protein
(26 Jun 1999)
pyrrole-2-carboxylate monooxygenase <enzyme> Consists of 18.7- and 54-kD subunits; the 18.7-kD subunit is an NADH-oxidase; the 54-kD subunit requires NADH and fad; isolated from rhodococcus
Registry number: EC 1.14.13.-
Synonym: pyrrole-2-cooh monooxygenase
(26 Jun 1999)
pyrrolidine-2-carboxylate <amino acid> One of the 20 amino acids directly coded for in proteins. Structure differs from all the others, in that its side chain is bonded to the nitrogen of the _ amino group, as well as the _ carbon. This makes the amino group a secondary amine and so proline is described as an imino acid. Has strong influence on secondary structure of proteins and is much more abundant in collagens than in other proteins, occurring especially in the sequence glycine proline hydroxyproline. A proline rich region seems to characterise the binding site of SH3 domains.
(18 Nov 1997)
pyrrolidone-5-carboxylate A keto derivative of proline that is formed nonenzymatically from glutamate, glutamine, and gamma-glutamylated peptides; it is also produced by the action of gamma-glutamylcyclotransferase; elevated levels of 5-oxoproline are often associated with problems of glutamine or glutathione metabolism.
Synonym: 5-pyrrolidone-2-carboxylic acid, pyroglutamic acid, pyrrolidone-5-carboxylate.
(05 Mar 2000)
pyrroline-2-carboxylate reductase An oxidoreductase reducing 1-pyrroline-2-carboxylate to l-proline with NAD(P)H.
Synonym: proline dehydrogenase, proline oxidase.
(05 Mar 2000)
pyrroline-5-carboxylate reductase An oxidoreductase reversibly reducing 1-pyrroline-5-carboxylate to l-proline with NAD(P)H; a deficiency of this enzyme is associated with type I hyperprolinaemia.
Synonym: proline dehydrogenase, proline oxidase.
(05 Mar 2000)
pyrroline carboxylate reductases <enzyme> A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(p)h. Includes both the 2-oxidoreductase (ec 1.5.1.1) and the 5-oxidoreductase (ec 1.5.1.2). The former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to hydroxyproline.
Registry number: EC 1.5.1.-
(12 Dec 1998)
delta-1-piperideine-6-carboxylate dehydrogenase <enzyme> From streptomyces clavuligerus and other cephamycin c-producing actinomycetes; converts delta-1-piperideine-6-carboxylate to alpha-aminoadipic acid
Registry number: EC 1.5.1.-
Synonym: p6c dehydrogenase
(26 Jun 1999)
1-pyrroline-5-carboxylate dehydrogenase <enzyme> Catalyses the oxidation of 1-pyrroline-5-carboxylate to l-glutamate in the presence of nad; see also record for glutamate-saemialdehyde dehydrogenase which converts 5-glutamyl phosphate to glutamate 5-saemialdehyde and phosphate in the presence of NADPH
Registry number: EC 1.5.1.12
Synonym: delta(1)-pyrroline-5-carboxylate dehydrogenase, glutamic-gamma-saemialdehyde dehydrogenase, nadp+ specific 8-glutamate saemialdehyde dehydrogenase, ggs dehydrogenase, delta-1-pyrroline-5-carboxylate synthetase, p5cs enzyme, glutamyl-gamma-saemialdehyde dehydrogenase
(26 Jun 1999)
2-hydroxychromene-2-carboxylate isomerase <enzyme> Catalyses the conversion of 2-hydroxychromene-2-carboxylate to cis-o-hydroxybenzylidenepyruvate--a step in the bacterial degradation of naphthalene to salicylate
Registry number: EC 5.3.99.-
Synonym: o-hydroxychromene-2-carboxylate isomerase, hcca isomerase
(26 Jun 1999)
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase <enzyme> E coli enzyme; catalyses formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate from 2-ketoglutarate and isochorismate; requires thiamine pyrophosphate and liberates pyruvate from the isochorismate molecule; see also o-succinylbenzoate synthase
Registry number: EC 4.1.3.-
Synonym: shchc synthase
(26 Jun 1999)
3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase <enzyme> Catalyses the oxidation of 3,5-cyclohexadiene-1,2-diol-1-carboxylate in presence of nad to yield catechol, carbon dioxide and NADH
Registry number: EC 1.3.1.25
Synonym: dihydrodihydroxybenzoate dehydrogenase
(26 Jun 1999)
arginine <amino acid> An essential amino acid, a major component of proteins and contains the guanido group that has a pKa of greater than 12, so that it carries a permanent positive charge at physiological pH. It becomes an essential amino acid when the body is under stress or is in an injured state.
Depressed growth results from lack of dietary arginine. Arginine deficiency syndrome is observed in human babies born with a phosphate synthetase deficiency. Normal growth and development in these infants are achieved by adding arginine to their diet. Arginine deficiency leads to carbamyl phosphate overproduction in the mitochondria due to inadequate ornithine supply. Arginine-deficient diets in males causes decreased sperm counts. Free and bound arginine are found in abundance in human male sperm and arginine has been found to stimulate sperm motility.
There are two sources of arginine, arginine in the food chain and free-form arginine from supplements. Food-source arginine is found in abundance in turkey, chicken and other meats. Nonfood-source arginine is called L-arginine and is created through a fermentation process which separates arginine from all other proteins. In the presence of food and other amino acids, L-arginine will act like food-source arginine but when L-arginine is separated from its nutrient boundaries by the removal of all other amino acids, then L-arginine undertakes a different role, becoming capable of crossing the blood-brain barrier and stimulating growth hormone release secreted by the anterior pituitary.
Growth hormone serum levels peak during adolescence and begin to drop after age 23. Aging reduces natural growth hormone production, which results in added body fat, reduced muscle tissue, slowed healing, lack of elasticity in the skin and reduced immune function. Human pituitary growth hormone secretion is evidenced in human males, females and children following intravenous administration of 30 grams of arginine (in 30 minutes) in adults and 0.5 grams/kilogram of bodyweight in children. Female response is somewhat higher than male response. Oral administration of L-arginine also results in the release of Human Growth Hormone.
Tumour suppression is evidenced in the presence of L-arginine. In the Barbul study, tumours recurred in 100% of the control animals. But in the arginine-supplemented group, only about 60% of the tumours recurred and the animals with tumours survived longer. Supplementation of arginine in the diet inhibits development and increase in size of cancerous tumours, both chemically induced and naturally occurring.
Insulin can block growth hormone release, so high serum insulin levels are counterproductive to GH release. Insulin itself is capable of stimulating muscle growth, but it also strongly stimulates fat storage. Muscle growth stimulation from insulin is minuscule compared to muscle growth stimulated by growth hormone.
(13 Nov 1997)
arginine 2-monooxygenase <enzyme> Catalyses oxidative decarboxylation or arginine to form gamma-guanidinobutyramide (4-guanidinobutanamide)
Registry number: EC 1.13.12.1
Synonym: arginine decarboxyoxidase
(26 Jun 1999)
arginine amidase <enzyme> A ureahydrolase that catalyses the hydrolysis of arginine and canavanine to yield l-ornithine and urea.
Chemical name: L-Arginine amidinohydrolase
Registry number: EC 3.5.3.1
(12 Dec 1998)
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