| IGD | idiopathic growth hormone deficiency; interglobal distance; isolated gonadotropin deficiency |
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| DDC | L-Dopa De-Carboxylase |
| ACC | accommodation; acetyl coenzyme A carboxylase; acinic cell carcinoma; acute care center; adenoid cyst... |
| BMCC | beta-methylcrotonyl coenzyme A carboxylase |
| GGC | gamma-glutamyl carboxylase |
| ribulose bisphosphate carboxylase | <enzyme> A copper protein that catalyses the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide and is responsible for carbon dioxide fixation in photosynthesis. Carbon dioxide is combined with ribulose diphosphate to give two molecules of 3 phosphoglycerate, as part of the Calvin Benson cycle. It is the sole carbon dioxide fixing enzyme in C3 plants and collaborates with PEP carboxylase in carbon dioxide fixation in C4 plants. In the presence of oxygen the products of the reaction are one molecule of phosphoglyceric acid and one molecule of phosphoglycolic acid. The latter is the initial substrate for photorespiration and this oxygenase function occurs in C3 plants where the enzyme is not protected from ambient oxygen, in C4 plants the enzyme acts exclusively as a carboxylase since it is protected from oxygen. Also called Fraction 1 protein, the major protein of leaves. Chemical name: 3-Phospho-D-glycerate carboxy-lyase (dimerizing) Registry number: EC 4.1.1.39 (12 Dec 1998) |
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| ribulosebisphosphate carboxylase-oxygenase activase | <chemical> Requires ATP; amino acid sequence given in first source Synonym: rubisco activase, rca protein (26 Jun 1999) |
| ribulose diphosphate carboxylase | <enzyme> A copper protein that catalyses the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide and is responsible for carbon dioxide fixation in photosynthesis. Carbon dioxide is combined with ribulose diphosphate to give two molecules of 3 phosphoglycerate, as part of the Calvin Benson cycle. It is the sole carbon dioxide fixing enzyme in C3 plants and collaborates with PEP carboxylase in carbon dioxide fixation in C4 plants. In the presence of oxygen the products of the reaction are one molecule of phosphoglyceric acid and one molecule of phosphoglycolic acid. The latter is the initial substrate for photorespiration and this oxygenase function occurs in C3 plants where the enzyme is not protected from ambient oxygen, in C4 plants the enzyme acts exclusively as a carboxylase since it is protected from oxygen. Also called Fraction 1 protein, the major protein of leaves. Chemical name: 3-Phospho-D-glycerate carboxy-lyase (dimerizing) Registry number: EC 4.1.1.39 (12 Dec 1998) |
| RuDP carboxylase | <enzyme> A copper protein that catalyses the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide and is responsible for carbon dioxide fixation in photosynthesis. Carbon dioxide is combined with ribulose diphosphate to give two molecules of 3 phosphoglycerate, as part of the Calvin Benson cycle. It is the sole carbon dioxide fixing enzyme in C3 plants and collaborates with PEP carboxylase in carbon dioxide fixation in C4 plants. In the presence of oxygen the products of the reaction are one molecule of phosphoglyceric acid and one molecule of phosphoglycolic acid. The latter is the initial substrate for photorespiration and this oxygenase function occurs in C3 plants where the enzyme is not protected from ambient oxygen, in C4 plants the enzyme acts exclusively as a carboxylase since it is protected from oxygen. Also called Fraction 1 protein, the major protein of leaves. Chemical name: 3-Phospho-D-glycerate carboxy-lyase (dimerizing) Registry number: EC 4.1.1.39 (12 Dec 1998) |
| phosphoenolpyruvate carboxylase | <enzyme> An enzyme with high affinity for carbon dioxide. It catalyses irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesis of glucose. Chemical name: Orthophosphate:oxaloacetate carboxy-lyase (phosphorylating) Registry number: EC 4.1.1.31 (12 Dec 1998) |
| phosphoenolpyruvate carboxylase kinase | <enzyme> From bryophyllum fedtschenkoi plant and maise; phosphorylates phosphoenolpyruvate carboxylase on serine near the n-terminus; activity controlled by circadian rhythms Registry number: EC 2.7.10.- Synonym: pep carboxylase kinase, pepc kinase (26 Jun 1999) |
| polyprenyl-4-hydroxybenzoate carboxylase | <enzyme> Involved in polyprenylphenol synthesis; implicated in flagellation of salmonella typhimurium Registry number: EC 4.1.1.- Synonym: ppphb carboxylase, polyprenyl-p-hydroxybenzoate carboxylase (26 Jun 1999) |
| preprothrombin carboxylase | <enzyme> Vitamin k-dependent, membrane-bound Registry number: EC 4.1.1.- (26 Jun 1999) |
| propionyl-CoA carboxylase | <enzyme> See also propionyl CoA carboxylase (ATP-hydrolyzing) (EC 6.4.1.4) Registry number: EC 4.1.1.41 Synonym: methylmalonyl-CoA decarboxylase, propionyl-coenzyme a carboxylase (26 Jun 1999) |
| pyruvic-malic carboxylase | <enzyme> An enzyme that catalyses the conversion of (s)-malate and NAD+ to oxaloacetate and NADH. Chemical name: (S)-Malate:NAD+ oxidoreductase Registry number: EC 1.1.1.37 (12 Dec 1998) |
| oxalosuccinic carboxylase | <enzyme> An enzyme of the oxidoreductase class that catalyses the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires magnesium, mn2+; it is activated by ADP, citrate, and calcium, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (the NADP+ enzyme is EC 1.1.1.42.) Chemical name: Isocitrate:NAD+ oxidoreductase (decarboxylating) Registry number: EC 1.1.1.41 (12 Dec 1998) |
| active pyruvate | An intermediate formed in the oxidative decarboxylation of pyruvate. Compare: pyruvate dehydrogenase (lipoamide). Synonym: alpha-lactyl-thiamin pyrophosphate. (05 Mar 2000) |
| beta-alanine-pyruvate aminotransferase | <enzyme> An enzyme that reversibly transfers the amino group of beta-alanine to paruvate, thus producing l-alanine and malonate saemialdehyde. A deficiency of this enzyme is believed to be the cause of hyper-beta-alaninaemia. (05 Mar 2000) |
| beta-aminoisobutyrate:pyruvate aminotransferase | Beta-aminosiobutyrate:pyruvate transaminase;an enzyme that catalyses the reversible transfer of an amino group from beta-aminoisobutyrate to pyruvate, producing l-alanine and methylmalonate saemialdehyde. A step in valine degradation. A deficiency of beta-aminoisobutyrate:pyruvate aminotransferase results in hyper-beta-aminoisobutyric aciduria. (05 Mar 2000) |
| valine-pyruvate transaminase | <enzyme> E coli enzyme catalyzing the terminal step of valine biosynthesis; consider also EC 2.6.1.42, branched-chain-amino-acid transaminase; alanine-alpha-oxoisovalerate aminotransferase and alanine-alpha-ketoisovalerate aminotransferase were ens to alanine aminotransferase 1981-93 Registry number: EC 2.6.1.66 Synonym: alanine-valine transaminase, transaminase c, alanine alpha-ketoisovalerate aminotransferase, alanine-alpha-oxoisovalerate aminotransferase, alanine-alpha-ketoisovalerate aminotransferase (26 Jun 1999) |