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Literature summary for 2.5.1.87 extracted from

  • Matsuoka, S.; Sagami, H.; Kurisaki, A.; Ogura, K.
    Variable product specificity of microsomal dehydrodolichyl diphosphate synthase from rat liver (1991), J. Biol. Chem., 266, 3464-3468.
    View publication on PubMed
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Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required. Native microsomal enzyme exists in association with lipid and Mg2+ Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Source Tissue

Source Tissue Comment Organism Textmining
brain
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 Rattus norvegicus
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liver
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 Rattus norvegicus
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testis
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 Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate chain length of products shifts downward from C90 and C95 with increasing concentration of the detergents. Maximum activation is observed at the concentration of 2% Triton X-100, 30 mM octyl glucoside, 30 mM 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, and 10 mM deoxycholate with the product chain length being C80-C85, C65-C75, C70-C75, and C55-C65, respectively. The activity of Triton X-100 solubilized enzyme is decreased by asolectin, phosphatidylethanolamine, and phosphatidylcholine. The chain lengths of products formed in the presence of these phospholipids are C85 and C90. In the presence of both phosphatidylcholine and Mg2+ the solubilized enzyme is able to produce C90 and C95 dehydrodolichyl diphosphates like native microsomal enzyme Rattus norvegicus diphosphate + di-trans,poly-cis-polyprenyl diphosphate
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