| EC |
2.7.8.15 |
| Accepted name: |
UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase |
| Reaction: |
UDP-N-acetyl-α-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphosphodolichol |
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For diagram of dolichyltetradecasaccharide biosynthesis, click here |
| Other name(s): |
UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase; UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase; uridine diphosphoacetylglucosamine-dolichyl phosphate acetylglucosamine-1-phosphotransferase; chitobiosylpyrophosphoryldolichol synthase; dolichol phosphate N-acetylglucosamine-1-phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase |
| Systematic name: |
UDP-N-α-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase (configuration-retaining) |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 70431-08-2 |
| References: |
| 1. |
Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319–325. [DOI] [PMID: 6215245] |
| 2. |
Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate. UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate transferase. J. Biol. Chem. 255 (1980) 8174–8178. [PMID: 6447695] |
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| [EC 2.7.8.15 created 1983] |
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