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・ 3-Methyl-2-pentanol
・ 3-Methyl-2-pentanone
・ 3-Methyl-3-octanol
・ 3-Methyl-3-pentanol
・ 3-Methyl-3-penten-2-one
・ 3-demethylubiquinone-9 3-O-methyltransferase
・ 3-Demon
・ 3-Deoxy-2-octulosonidase
・ 3-deoxy-8-phosphooctulonate synthase
・ 3-Deoxy-D-arabino-heptulosonic acid 7-phosphate
・ 3-Deoxy-D-manno-oct-2-ulosonic acid
・ 3-deoxy-D-manno-oct-2-ulosonic acid transferase
・ 3-deoxy-D-manno-octulosonate aldolase
・ 3-Deoxy-D-manno-octulosonic acid kinase
・ 3-Deoxy-D-pentulosonic acid aldolase
3-deoxy-manno-octulosonate cytidylyltransferase
・ 3-deoxy-manno-octulosonate-8-phosphatase
・ 3-deoxy-manno-octulosonic acid transferase
・ 3-Deoxyanthocyanidin
・ 3-Deoxyglucosone
・ 3-deoxyoctulosonase
・ 3-dimensional matching
・ 3-Epi-6-deoxocathasterone 23-monooxygenase
・ 3-ethylmalate synthase
・ 3-Ethylpentan-3-ol
・ 3-Ethylpentane
・ 3-Ethylphenol
・ 3-Faced Elva
・ 3-Fluoroamphetamine
・ 3-Fluoroethamphetamine


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3-deoxy-manno-octulosonate cytidylyltransferase : ウィキペディア英語版
3-deoxy-manno-octulosonate cytidylyltransferase

In enzymology, a 3-deoxy-manno-octulosonate cytidylyltransferase () is an enzyme that catalyzes the chemical reaction
:CTP + 3-deoxy-D-manno-octulosonate \rightleftharpoons diphosphate + CMP-3-deoxy-D-manno-octulosonate
Thus, the two substrates of this enzyme are CTP and 3-deoxy-D-manno-octulosonate, whereas its two products are diphosphate and CMP-3-deoxy-D-manno-octulosonate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:3-deoxy-D-manno-octulosonate cytidylyltransferase. Other names in common use include CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase, 2-keto-3-deoxyoctonate cytidylyltransferase, 3-Deoxy-D-manno-octulosonate cytidylyltransferase, CMP-3-deoxy-D-manno-octulosonate synthetase, CMP-KDO synthetase, CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase, and cytidine monophospho-3-deoxy-D-manno-octulosonate pyrophosphorylase. This enzyme participates in lipopolysaccharide biosynthesis.
==Structural studies==

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .

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