Enzymes
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Name help_outline
dolichyl phosphate
Identifier
CHEBI:57683
Charge
-2
Formula
C20H35O4P(C5H8)n
Search links
Involved in 24 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9517Polymer name: a dolichyl phosphatePolymerization index help_outline nFormula C20H35O4P(C5H8)nCharge (-2)(0)nMol File for the polymer
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- Name help_outline UDP-N-acetyl-α-D-glucosamine Identifier CHEBI:57705 (Beilstein: 4286654) help_outline Charge -2 Formula C17H25N3O17P2 InChIKeyhelp_outline LFTYTUAZOPRMMI-CFRASDGPSA-L SMILEShelp_outline CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 88 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
N-acetyl-α-D-glucosaminyldiphosphodolichol
Identifier
CHEBI:58427
Charge
-2
Formula
(C5H8)n.C28H49NO12P2
Search links
Involved in 2 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9519Polymer name: N-acetyl-α-D-glucosaminyl-diphosphodolicholPolymerization index help_outline nFormula C28H49NO12P2(C5H8)nCharge (-2)(0)nMol File for the polymer
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- Name help_outline UMP Identifier CHEBI:57865 (Beilstein: 3570858) help_outline Charge -2 Formula C9H11N2O9P InChIKeyhelp_outline DJJCXFVJDGTHFX-XVFCMESISA-L SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 51 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13289 | RHEA:13290 | RHEA:13291 | RHEA:13292 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Properties of a soluble polyprenyl phosphate. UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate transferase.
Villemez C.L., Carlo P.L.
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Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast.
Sharma C.B., Lehle L., Tanner W.
Preparation and purification of substrate amounts of radioactive as well as non-radioactive dolichyl diphosphate N-acetylglucosamine and dolichyl diphosphate chitobiose made it possible to test and characterize tentatively the first three reactions of the dolichol pathway (enzyme I-III). The test ... >> More
Preparation and purification of substrate amounts of radioactive as well as non-radioactive dolichyl diphosphate N-acetylglucosamine and dolichyl diphosphate chitobiose made it possible to test and characterize tentatively the first three reactions of the dolichol pathway (enzyme I-III). The test conditions are described in detail. All three enzymes were solubilized from yeast membranes with detergents. Enzyme II and III were purified to give a purification factor of 35-fold and 70-fold, respectively. The reactions required divalent metal ions with an optimum concentration of 10 mM Mg2+. Enzyme II was stimulated almost to the same extent also by Ca2+. The Km values for UDP-N-acetylglucosamine for enzyme I and II were 15 and 10 muM, respectively, and for GDP-mannose (enzyme III) 7 muM. The apparent Km values for the lipophilic acceptor was 180 muM for enzyme I (dolichyl phosphate), 40 muM for enzyme II (dolichyl diphosphate N-acetylglucosamine) and 17 muM for enzyme III (dolichyl diphosphate chitobiose). The corresponding V values were approximately 1, 10, and 50 nmol X h-1 X mg protein-1. All reactions were inhibited by nucleoside diphosphates. << Less
Eur J Biochem 126:319-325(1982) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.