Enzymes
| UniProtKB help_outline | 1,317 proteins |
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Name help_outline
N,N'-diacetylchitobiosyldiphosphodolichol
Identifier
CHEBI:57269
Charge
-2
Formula
C36H62N2O17P2(C5H8)n
Search links
Involved in 2 reaction(s)
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Form(s) in this reaction:
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Identifier: RHEA-COMP:19510Polymer name: an N,N'-diacetylchitobiosyl-diphospho-di-trans,poly-cis-dolicholPolymerization index help_outline n-1Formula C36H62N2O17P2(C5H8)n-1Charge (-2)(0)n-1Mol File for the polymer
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- Name help_outline GDP-α-D-mannose Identifier CHEBI:57527 (Beilstein: 6630718) help_outline Charge -2 Formula C16H23N5O16P2 InChIKeyhelp_outline MVMSCBBUIHUTGJ-GDJBGNAASA-L SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]2O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 54 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
β-D-mannosyl-(1→4)-N,N'-diacetylchitobiosyldiphosphodolichol
Identifier
CHEBI:58472
Charge
-2
Formula
(C5H8)n.C42H72N2O22P2
Search links
Involved in 3 reaction(s)
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Form(s) in this reaction:
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Identifier: RHEA-COMP:19511Polymer name: a β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphospho-di-trans,poly-cis-dolicholPolymerization index help_outline n-1Formula C42H72N2O22P2(C5H8)n-1Charge (-2)(0)n-1Mol File for the polymer
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- Name help_outline GDP Identifier CHEBI:58189 Charge -3 Formula C10H12N5O11P2 InChIKeyhelp_outline QGWNDRXFNXRZMB-UUOKFMHZSA-K SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 184 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13865 | RHEA:13866 | RHEA:13867 | RHEA:13868 | |
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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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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.