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・ Dihydroisocoumarin
・ Dihydroisoindole
・ Dihydrokaempferide
・ Dihydrokaempferol 4-reductase
・ Dihydrokanakugiol
・ Dihydrokavain
・ Dihydrolipoamide
・ Dihydrolipoamide dehydrogenase
・ Dihydrolipoic acid
・ Dihydrolipoyl transacetylase
・ Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
・ Dihydrolipoyllysine-residue succinyltransferase
・ Dihydromethysticin
・ Dihydromorin
・ Dihydromorphine
Dihydroneopterin aldolase
・ Dihydronicotinamide adenine dinucleotide-coenzyme Q reductase
・ Dihydroorotase
・ Dihydroorotate dehydrogenase
・ Dihydroorotate dehydrogenase (fumarate)
・ Dihydroorotate dehydrogenase (quinone)
・ Dihydrophloroglucinol
・ Dihydroprogesterone
・ Dihydropteroate
・ Dihydropteroate synthase
・ Dihydropteroate synthase inhibitor
・ Dihydropyran
・ Dihydropyridine
・ Dihydropyrimidinase
・ Dihydropyrimidine dehydrogenase


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Dihydroneopterin aldolase : ウィキペディア英語版
Dihydroneopterin aldolase

In enzymology, a dihydroneopterin aldolase () is an enzyme that catalyzes the chemical reaction
:2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine \rightleftharpoons 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
Thus, the substrate (biochemistry) of this enzyme is 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine, whereas its two products are 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine and glycolaldehyde.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropt eridine glycolaldehyde-lyase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-forming). Other names in common use include 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-, and dihydropteridine glycolaldehyde-lyase. This enzyme participates in folate biosynthesis.
==Structural studies==

As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .

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