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Carboxylase

Lyases. These enzymes cleave C-C, C-0, C-N and other bonds by elimination leaving double bonds or conversely add groups to double bonds. This group includes decarboxylases, hydratases, dehydratases and some carboxylases. [Pg.159]

Ligases (syniheiases). Enzymes catalysing the joining together of two molecules coupled with the hydrolysis of a pyrophosphate bond in ADP or a similar triphosphate. They include some carboxylases and many enzymes known as synthetases. [Pg.159]

Refs. 21, 22, 155. Abbreviations AHV, a-amino-(3-hydroxyvaleric acid Horn, L-homoserine AEG, (3 -(2-aminoethyl)-L-cysteine ppc, phosphoenolpymvate carboxylase the strain improvement largely depends on the transduction technology sensitive resistant —, auxotroph or deficient , leaky auxotroph +, prototrophic revertant. Table 7. Amino Acid Production from Hydrocarbons ... [Pg.289]

Gene symbols are according to those of E. coli. (173). Abbreviations Horn, Homoserine Ant, Anthranilic acid PR, Phosphoribosyl ppc, Phosphoenolpyruvate carboxylase PRDH, prephenate dehydrogenase. [Pg.290]

Figure 4.8 The active site in all a/p barrels is in a pocket formed by the loop regions that connect the carboxy ends of the p strands with the adjacent a helices, as shown schematically in (a), where only two such loops are shown, (b) A view from the top of the barrel of the active site of the enzyme RuBisCo (ribulose bisphosphate carboxylase), which is involved in CO2 fixation in plants. A substrate analog (red) binds across the barrel with the two phosphate groups, PI and P2, on opposite sides of the pocket. A number of charged side chains (blue) from different loops as welt as a Mg ion (yellow) form the substrate-binding site and provide catalytic groups. The structure of this 500 kD enzyme was determined to 2.4 A resolution in the laboratory of Carl Branden, in Uppsala, Sweden. (Adapted from an original drawing provided by Bo Furugren.)... Figure 4.8 The active site in all a/p barrels is in a pocket formed by the loop regions that connect the carboxy ends of the p strands with the adjacent a helices, as shown schematically in (a), where only two such loops are shown, (b) A view from the top of the barrel of the active site of the enzyme RuBisCo (ribulose bisphosphate carboxylase), which is involved in CO2 fixation in plants. A substrate analog (red) binds across the barrel with the two phosphate groups, PI and P2, on opposite sides of the pocket. A number of charged side chains (blue) from different loops as welt as a Mg ion (yellow) form the substrate-binding site and provide catalytic groups. The structure of this 500 kD enzyme was determined to 2.4 A resolution in the laboratory of Carl Branden, in Uppsala, Sweden. (Adapted from an original drawing provided by Bo Furugren.)...
Knight, S., Andersson, I., Branden, C.-I. Crystallographic analysis of ribulose-l,5-bisphosphate carboxylase from spinach at 2.4 A resolution. Subunit interactions and active site. /. Mol. Biol. 215 113-160,... [Pg.65]

Schneider, G., Lindqvist, Y., Lundqvlst, T. Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 A resolution. J. Mol. Biol. [Pg.65]

Zn-+ DNA polymerase Coenzyme A (CoA) Acyl groups Acetyl-CoA carboxylase... [Pg.430]

Glncose-6-phosphatase Biotin (biocytin) CO, Propionyl-CoA carboxylase... [Pg.430]

FIGURE 18.40 The glutamyl carboxylase reaction is vitamin K-dependent. This enzyme activity is essential for the formation of 7-car-boxyglutamyl residues in several proteins of the blood-clotting cascade (Figure 15.5), accounting for the vitamin K dependence of coagulation. [Pg.607]

In a sort of reciprocal arrangement, the cell also feeds many intermediates back into the TCA cycle from other reactions. Since such reactions replenish the TCA cycle intermediates, Hans Kornberg proposed that they be called anaplerotie reactions (literally, the filling up reactions). Thus, PEP carboxylase and pyruvate carboxylase synthesize oxaloacetate from pyruvate (Figure 20.24). [Pg.663]

Pyruvate carboxylase is the most important of the anaplerotie reactions. It exists in the mitochondria of animal cells but not in plants, and it provides a direct link between glycolysis and the TCA cycle. The enzyme is tetrameric and contains covalently bound biotin and an Mg site on each subunit. (It is examined in greater detail in our discussion of gluconeogenesis in Chapter 23.) Pyruvate carboxylase has an absolute allosteric requirement for acetyl-CoA. Thus, when acetyl-CoA levels exceed the oxaloacetate supply, allosteric activation of pyruvate carboxylase by acetyl-CoA raises oxaloacetate levels, so that the excess acetyl-CoA can enter the TCA cycle. [Pg.663]

FIGURE 20.24 Phosphoenolpyruvate (PEP) carboxylase, pyrnvate carboxylase, and malic enzyme catalyze anaplerotlc reactions, replenishing TCA cycle Intermediates. [Pg.664]

PEP carboxylase occurs in yeast, bacteria, and higher plants, but not in animals. The enzyme is specifically inhibited by aspartate, which is produced by transamination of oxaloacetate. Thus, organisms utilizing this enzyme control aspartate production by regulation of PEP carboxylase. Malic enzyme is found in the cytosol or mitochondria of many animal and plant ceils and is an NADPIT-dependent enzyme. [Pg.665]

H,COPO Ribulose-1,5-bis-phosphate (RuBP) carboxylase HCOH 1, H,C0P05 Two 3-Phospho- kinase 1,3-Blsphospho-glvcerate (BPG) dehydrogenase Glyceraldehydi 3-phosphate (G3P)... [Pg.734]

As indicated, ribulose bisphosphate carboxylase/oxygenase catalyzes an alternative reaction in which Og replaces COg as the substrate added to RuBP (Figure 22.29a). The ribulose-l,5-bisphosphate oxygenase rezLCtion diminishes plant... [Pg.737]


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AIR carboxylase

Acetyl CoA carboxylase (ACC

Acetyl CoA carboxylase fatty acid synthesis

Acetyl carboxylase

Acetyl coenzyme carboxylase

Acetyl coenzyme carboxylase inhibitors

Acetyl-CoA carboxylase

Acetyl-CoA carboxylase ACCase)

Acetyl-CoA carboxylase N-acetyltransferase

Acetyl-CoA carboxylase activation

Acetyl-CoA carboxylase biotin subunit

Acetyl-CoA carboxylase complex

Acetyl-CoA carboxylase inactivation

Acetyl-CoA carboxylase inhibitors

Acetyl-CoA carboxylase kinases

Acetyl-CoA carboxylase phosphatase

Acetyl-CoA carboxylase regulation

Acetyl-CoA carboxylase structure

Acetyl-CoA carboxylase, ATP-citrate lyase

Acetyl-CoA carboxylases

Acetyl-coenzyme A carboxylase

Acetyl-coenzyme A carboxylase inhibitors

AcetylCoA carboxylase

Acyl-CoA carboxylase

Biotin carboxylase

Biotin carboxylase domain

Biotin carboxylases

Biotin methylcrotonyl CoA carboxylase

Biotin propionyl CoA carboxylase

Biotin pyruvate carboxylase

Biotin-dependent carboxylase

Biotin-dependent carboxylases

Carboxylase acetivity

Carboxylase activity

Carboxylase and

Carboxylase enzymes

Carboxylase plant

Carboxylases

Carboxylases

Carboxylases and

Carboxylases and Carboxyltransferases

Carboxylases biotin metabolism

Carboxylases biotinidase

Carboxylases biotinylation

Carboxylation carboxylase

Chloroplast ribulose bisphosphate carboxylase

Citrate cycle Pyruvate carboxylase

Citric acid cycle pyruvate carboxylase

Co-carboxylase

Combined carboxylase deficiency,

Concentration Dependence of KIE Phosphoenolpyruvate Carboxylase

Enzyme pyruvate carboxylase

Enzymes phosphoenol pyruvate carboxylase

Escherichia coli acetyl-CoA carboxylase

Geranoyl-CoA carboxylase

Gluconeogenesis Pyruvic carboxylase

Gluconeogenesis pyruvate carboxylase activation

Gluconeogenesis, biotin pyruvate carboxylase

Glutamic acid carboxylase

Glutamyl carboxylase

Glycolysis Pyruvic carboxylase

Inhibition acetyl CoA carboxylase

Insulin effects on acetyl-CoA carboxylase

Liver acetyl coenzyme A carboxylase

Liver acetyl-CoA carboxylase

Methylcrotonyl carboxylase

Methylcrotonyl-CoA carboxylase

Methylmalonyl CoA carboxylase mutase

Mitochondria carboxylases

Mitochondria pyruvate carboxylase

Multiple carboxylase

Multiple carboxylase deficiency

NAD picolinate carboxylase

Nicotinamide picolinate carboxylase

Ornithine carboxylase

Orotidylate carboxylase

Oxalacetate 0-carboxylase

Oxalacetic carboxylase

Oxaloacetate pyruvate carboxylase deficiency

PEP-Carboxylase

Phenolphosphate carboxylase (EC 4.1.1.-) in Thauera aromatica

Phenylphosphate carboxylase

Phosphoenol-pyruvate carboxylase

Phosphoenolpyruvate carboxylase

Phosphoenolpyruvate carboxylase (PPC

Phosphoenolpyruvate carboxylase PEPC)

Phosphoenolpyruvate carboxylase, pyruvate

Phosphoenolpyruvate carboxylase, pyruvate decarboxylation

Phosphoenolpyruvate carboxylase, reaction catalyzed

Phosphoenolpyruvic carboxylases

Phosphoenolpyruvic carboxylases photosynthesis

Phosphopyruvate carboxylase

Phosphoribosyl aminoimidazole carboxylase

Phosphoribosylaminoimidazole carboxylase

Photosynthesis carboxylase)

Photosynthesis carboxylase/oxygenase

Picolinate Carboxylase and Nonenzymic Cyclization to Quinolinic Acid

Picolinate carboxylase

Picolinic acid carboxylase

Picolinic carboxylase

Propionyl carboxylase

Propionyl carboxylase, mitochondrial

Propionyl coenzyme A carboxylase

Propionyl coenzyme A carboxylase and

Propionyl-CoA carboxylase

Propionyl-CoA carboxylase deficiency

Pyruvate carboxylase

Pyruvate carboxylase (PYC

Pyruvate carboxylase biotin dependent

Pyruvate carboxylase biotin metabolism

Pyruvate carboxylase catalyses

Pyruvate carboxylase control mechanisms

Pyruvate carboxylase deficiency

Pyruvate carboxylase first partial reaction

Pyruvate carboxylase gluconeogenesis

Pyruvate carboxylase lipoic acid

Pyruvate carboxylase model

Pyruvate carboxylase modification

Pyruvate carboxylase modifiers

Pyruvate carboxylase partial reactions

Pyruvate carboxylase reaction catalyzed

Pyruvate carboxylase regulation

Pyruvate carboxylase requirements

Pyruvate carboxylase stimulation

Pyruvate carboxylase structure

Pyruvate carboxylase substrate cycle

Pyruvate carboxylase temperature

Pyruvate carboxylase, activity

Pyruvate carboxylase, function

Pyruvate carboxylases and

Pyruvic carboxylase

Ribosome Ribulose bisphosphate carboxylase

Ribosome carboxylase

Ribulose bisphosphate carboxylase

Ribulose bisphosphate carboxylase spinach, active site

Ribulose diphosphate carboxylase and

Ribulose diphosphate carboxylase/oxygenase

Ribulose-1, -diphosphate carboxylase

Ribulose-1, -diphosphate carboxylase carbon dioxide

Ribulose-1,5 -biphosphate carboxylase

Ribulose-1,5 -biphosphate carboxylase oxygenase

Ribulose-1,5 -bisphosphate carboxylase oxygenase

Ribulose-1,5-bisphosphate carboxylase regulation

Ribulose-Bisphosphate Carboxylase-Oxygenase Photorespiration and the C-4 Cycle

Ribulose-bisphosphate carboxylase photosynthesis

Ribulose-l,5-bisphosphate Carboxylase

Ribuloses carboxylase

RuBP carboxylase

RuDP carboxylase

Rubisco carboxylase

Rubisco, ribulose bisphosphate carboxylase

Salmonella PEP carboxylase

Spinach ribulose bisphosphate carboxylase

The First Step in Fatty Acid Synthesis Is Catalyzed by Acetyl-CoA Carboxylase

The Vitamin K-Dependent Carboxylase

Thiamine pyruvate with carboxylase

Thiamine with carboxylase

Urea carboxylase

Vitamin K-dependent carboxylase

Vitamin carboxylase

Wheat germ carboxylase

Y-glutamyl carboxylase

Yeast, carboxylase

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