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・ 2-acylglycerol-3-phosphate O-acyltransferase
・ 2-acylglycerophosphocholine O-acyltransferase
・ 2-alkenal reductase
・ 2-alkyn-1-ol dehydrogenase
・ 2-Amino-1,2-dihydronaphthalene
・ 2-Amino-1-methyl-6-phenylimidazo(4,5-b)pyridine
・ 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
・ 2-Amino-3-carboxymuconic semialdehyde
・ 2-Amino-4-deoxychorismate dehydrogenase
・ 2-Amino-4-deoxychorismate synthase
・ 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
・ 2-Amino-4-hydroxy-6-pyrophosphoryl-methylpteridine
・ 2-Amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one
・ 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase
・ 2-Aminoacridine
2-aminoadipate transaminase
・ 2-aminobenzenesulfonate 2,3-dioxygenase
・ 2-Aminoethoxydiphenyl borate
・ 2-aminoethylphosphonate—pyruvate transaminase
・ 2-aminohexano-6-lactam racemase
・ 2-aminohexanoate transaminase
・ 2-Aminoindane
・ 2-Aminoisobutyric acid
・ 2-aminomuconate deaminase
・ 2-Aminomuconic acid
・ 2-Aminomuconic semialdehyde
・ 2-Aminophenol
・ 2-Aminopurine
・ 2-Aminopyridine
・ 2-Aminotetralin


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2-aminoadipate transaminase : ウィキペディア英語版
2-aminoadipate transaminase

In enzymology, a 2-aminoadipate transaminase () is an enzyme that catalyzes the chemical reaction
:L-2-aminoadipate + 2-oxoglutarate \rightleftharpoons 2-oxoadipate + L-glutamate
Thus, the two substrates of this enzyme are L-2-aminoadipate and 2-oxoglutarate, whereas its two products are 2-oxoadipate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-2-aminoadipate:2-oxoglutarate aminotransferase. Other names in common use include alpha-aminoadipate aminotransferase, 2-aminoadipate aminotransferase, 2-aminoadipic aminotransferase, glutamic-ketoadipic transaminase, and glutamate-alpha-ketoadipate transaminase. This enzyme participates in lysine biosynthesis and lysine degradation. It employs one cofactor, pyridoxal phosphate.
==Structural studies==

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .

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