arogenate dehydrogenase
ncADHArogenate dehydrogenaseSolanum lycopersicum
Arogenate dehydrogenase. Gene. ncADH. Organism. Solanum lycopersicum (Tomato) (Lycopersicon esculentum) Status. Unreviewed-Annotation score -Experimental evidence at transcript level i. Function i GOMolecular function i. arogenate dehydrogenase (NADP ) activity Source
Arogenate dehydrogenase NAD(P) SpringerLink
Arogenate dehydrogenase NAD(P) Chapter. 70 Downloads Part of the Springer Handbook of Enzymes book series (HDBKENZYMES volume S1) Keywords
62 Arogenate dehydrogenase from Phenylobacterium
· 62 Arogenate dehydrogenase from Phenylobacterium immobile. Author links open overlay panel Franz Lingens Eberhard Franz Lingens Eberhard
ENZYME1.3.1.78 Arogenate dehydrogenase (NADP( ))
TyrAAT2. Arogenate dehydrogenases may utilize NAD ( ) (EC 1.3.1.43 ) NADP ( ) (EC 1.3.1.78 ) or both (EC 1.3.1.79 ). NADP ( )-dependent enzymes usually predominate in higher plants. The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate
tyrCCyclohexadienyl dehydrogenaseZymomonas mobilis
· Can function as either prephenate dehydrogenase or as arogenate dehydrogenase in the biosynthesis of L-tyrosine. Catalyzes two analogous reactions converts prephenate to 4-hydroxyphenylpyruvate and transforms L-arogenate to L-tyrosine. Is not able to utilize NADP instead of NAD as cosubstrate.1 Publication
Information on EC 1.3.1.78arogenate dehydrogenase
Arogenate dehydrogenases may utilize NAD (EC 1.3.1.43) NADP (EC 1.3.1.78) or both (EC 1.3.1.79). NADP -dependent enzymes usually predominate in higher plants.The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate while the Arabidopsis isoform TyrAAT2 can use it very poorly
Molecular and biochemical characterization of an
The present study reports the first molecular characterization of a plant arogenate dehydrogenase the enzyme that catalyses the transformation of arogenate into tyrosine. The structure of the Arabidopsis thaliana tyrA gene is very peculiar since it encodes two highly similar and putatively active protein domains. PCR analyses confirmed the existence of a transcript encoding the two protein
Purification and properties of arogenate dehydrogenase
Arogenate dehydrogenase has been partially purified by a five-step procedure. The enzyme requires NAD as cofactor. The Km values for NAD and arogenate are 0.2 mM and 0.15 mM respectively. The molecular weight of arogenate dehydrogenase is about 68 000 and SDS gel electrophoresis indicates a composition of two identical subunits.
Biochemical characterization of TyrA dehydrogenases from
· Generally tyrosine can be synthesized via two pathways by prephenate dehydrogenase (TyrAp /PDH) a pathway found in most bacteria or by arogenate dehydrogenase (TyrA a /ADH) a pathway found mainly in plants. Both enzymes require the cofactor NAD or NADP and typically are strongly feedback inhibited by tyrosine.
Author Lopez-Nieves Anne Pringle Hiroshi A. Maeda
Purification and properties of arogenate dehydrogenase
Arogenate dehydrogenase has been partially purified by a five-step procedure. The enzyme requires NAD as cofactor. The Km values for NAD and arogenate are 0.2 mM and 0.15 mM respectively. The molecular weight of arogenate dehydrogenase is about 68 000 and SDS gel electrophoresis indicates a composition of two identical subunits.
ENZYME1.3.1.79 Arogenate dehydrogenase (NAD(P)( ))
ENZYME entry EC 1.3.1.79. Arogenate dehydrogenase (NAD (P) ( )). Arogenic dehydrogenase. Cyclohexadienyl dehydrogenase. Pretyrosine dehydrogenase. Arogenate dehydrogenases may utilize NAD ( ) (EC 1.3.1.43 ) NADP ( ) (EC 1.3.1.78 ) or both (EC 1.3.1.79 ). Enzymes that can utilize both cofactors have been reported from some Proteobacteria
TYRAAT2Arogenate dehydrogenase 2 chloroplastic
Proteins known to be involved in this subpathway in this organism are Arogenate dehydrogenase 1 chloroplastic (TYRAAT1) Arogenate dehydrogenase 2 chloroplastic (TYRAAT2) This subpathway is part of the pathway L-tyrosine biosynthesis which is itself part of Amino-acid biosynthesis.
Arogenate dehydrogenase (NADP )
· In enzymology an arogenate dehydrogenase (NADP ) (EC number1.3.1.78) is an enzyme that catalyzes the chemical reaction L-arogenate NADP ightleftharpoons L-tyrosine NADPH CO 2. Thus the two substrates of this enzyme are L-arogenate and NADP whereas its 3 products are L-tyrosine NADPH and CO 2.. This enzyme belongs to the family of oxidoreductase s specifically
Information on EC 1.3.1.79arogenate dehydrogenase
arogenate dehydrogenase arogenate dehydrogenase isoform 2 cyclohexadienyl dehydrogenase tyrA TyrAc TyrC ZmTyrA more top print hide show all columns Go to Synonym Search Please wait a moment until the data is sorted.
ENZYME1.3.1.43 Arogenate dehydrogenase
Pretyrosine dehydrogenase. Arogenate dehydrogenases may utilize NAD ( ) (EC 1.3.1.43 ) NADP ( ) (EC 1.3.1.78 ) or both (EC 1.3.1.79 ). NAD ( )-specific enzymes have been reported from some bacteria and plants. Some enzymes also possess the activity of EC 1.3.1.12 . All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.3.1.-.
The prephenate dehydrogenase component of the bifunctional
· Arogenate dehydrogenase activity was not detected in other column fractions with either NAD or NADP present. Similar results were obtained with E. coli C (not shown). 136 The elution profiles of enzymes from K. pneumor iae that were obtained following DE52 chromatography of crude extracts are shown in fig.3. Two peaks of chorismate mutase
BRENDAInformation on EC 1.3.1.43arogenate dehydrogenase
Arogenate dehydrogenases may utilize NAD (EC 1.3.1.43) NADP (EC 1.3.1.78) or both (EC 1.3.1.79). NAD -specific enzymes have been reported from some bacteria and plants . Some enzymes also possess the activity of EC 1.3.1.12 prephenate dehydrogenase. To select more than one organism hold the CTRL key and click the items in the list.
ENZYME1.3.1.78 Arogenate dehydrogenase (NADP( ))
TyrAAT2. Arogenate dehydrogenases may utilize NAD ( ) (EC 1.3.1.43 ) NADP ( ) (EC 1.3.1.78 ) or both (EC 1.3.1.79 ). NADP ( )-dependent enzymes usually predominate in higher plants. The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate
Purification of arogenate dehydrogenase from
· Fractions containing arogenate dehydrogenase ac- tivity were pooled and adjusted to a protein con- centration of 2 mg/ml. 2.4.2. (NH4)zS04 fractionation The resulting protein solution was fractionated by addition of solid (NN4)2804. Arogenate dehydrogenase was discovered in the 35-80 precipitate and was collected by centrifugation.
Molecular and biochemical characterization of an
The present study reports the first molecular characterization of a plant arogenate dehydrogenase the enzyme that catalyses the transformation of arogenate into tyrosine. The structure of the Arabidopsis thaliana tyrA gene is very peculiar since it encodes two highly similar and putatively active protein domains. PCR analyses confirmed the existence of a transcript encoding the two protein
L-Tyrosine regulation and biosynthesis via arogenate
actually more effective as an inhibitor of arogenate dehydrogenase than was L-tyrosine. Since MFT was found to be a potent antimetabolite inhibitor of growth in N. silvestris and since inhibition was specifically and effectively reversed by L-tyrosine arogenate dehydrogenase is an outstanding candi date as the in vivo target of analog action. Al
ENZYME1.3.1.43 Arogenate dehydrogenase
Pretyrosine dehydrogenase. Arogenate dehydrogenases may utilize NAD ( ) (EC 1.3.1.43 ) NADP ( ) (EC 1.3.1.78 ) or both (EC 1.3.1.79 ). NAD ( )-specific enzymes have been reported from some bacteria and plants. Some enzymes also possess the activity of EC 1.3.1.12 . All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.3.1.-.
Purification of arogenate dehydrogenase from
· Purification of arogenate dehydrogenase from Phenylobacterium immobile. Mayer E Waldner-Sander S Keller B Keller E Lingens F. Phenylobacterium immobile a bacterium which is able to degrade the herbicide chloridazon utilizes for L-tyrosine synthesis arogenate as an obligatory intermediate which is converted in the final biosynthetic step
Biochemical Characterization and Crystal Structure of
· As observed for Arabidopsis thaliana arogenate dehydrogenase when NADP is used at low concentrations (between 4 and 12 μM) with arogenate as the variable substrate sigmoidal curves were obtained indicating positive kinetic cooperativity (n H = 1.4) with respect to the binding of arogenate for both enzymes. When NADP was the variable
The prephenate dehydrogenase component of the bifunctional
· Arogenate dehydrogenase activity was not detected in other column fractions with either NAD or NADP present. Similar results were obtained with E. coli C (not shown). 136 The elution profiles of enzymes from K. pneumor iae that were obtained following DE52 chromatography of crude extracts are shown in fig.3. Two peaks of chorismate mutase
Molecular and biochemical characterization of an
The present study reports the first molecular characterization of a plant arogenate dehydrogenase the enzyme that catalyses the transformation of arogenate into tyrosine. The structure of the Arabidopsis thaliana tyrA gene is very peculiar since it encodes two highly similar and putatively active
Biochemical characterization and crystal structure of
The extreme diversity in substrate specificity and in the regulation mechanism of arogenate/prephenate dehydrogenase enzymes in nature makes a comparative structural study of these enzymes of great interest. We report here on the biochemical and structural characterization of arogenate dehydrogenase from Synechocystis sp. (TyrAsy).
Information on EC 1.3.1.79arogenate dehydrogenase
arogenate dehydrogenase arogenate dehydrogenase isoform 2 cyclohexadienyl dehydrogenase tyrA TyrAc TyrC ZmTyrA more top print hide show all columns Go to Synonym Search Please wait a moment until the data is sorted.
TYRAAT1Arogenate dehydrogenase 1 chloroplastic
· This protein is involved in step 1 of the subpathway that synthesizes L-tyrosine from L-arogenate (NADP ( ) route). This subpathway is part of the pathway L-tyrosine biosynthesis which is itself part of Amino-acid biosynthesis.
ENZYME1.3.1.43 Arogenate dehydrogenase
Pretyrosine dehydrogenase. Arogenate dehydrogenases may utilize NAD ( ) (EC 1.3.1.43 ) NADP ( ) (EC 1.3.1.78 ) or both (EC 1.3.1.79 ). NAD ( )-specific enzymes have been reported from some bacteria and plants. Some enzymes also possess the activity of EC 1.3.1.12 . All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.3.1.-.
Information on EC 1.3.1.79arogenate dehydrogenase
arogenate dehydrogenase arogenate dehydrogenase isoform 2 cyclohexadienyl dehydrogenase tyrA TyrAc TyrC ZmTyrA more top print hide show all columns Go to Synonym Search Please wait a moment until the data is sorted.
Arogenate dehydrogenase NAD(P) SpringerLink
Arogenate dehydrogenase NAD(P) Chapter. 70 Downloads Part of the Springer Handbook of Enzymes book series (HDBKENZYMES volume S1) Keywords
