The Enzyme Database

Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Proposed Changes to the Enzyme List

The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC-IUBMB by Kristian Axelsen, Richard Cammack, Ron Caspi, Masaaki Kotera, Andrew McDonald, Gerry Moss, Dietmar Schomburg, Ida Schomburg and Keith Tipton. Comments and suggestions on these draft entries should be sent to Dr Andrew McDonald (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland). The date on which an enzyme will be made official is appended after the EC number. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.


EC transferred
*EC phosphopolyprenol glucosyltransferase

Transferred entry: glutaryl-CoA dehydrogenase. Now EC, glutaryl-CoA dehydrogenase (decarboxylating)
[EC created 1972, deleted 2012]
Accepted name: phosphopolyprenol glucosyltransferase
Reaction: UDP-glucose + undecaprenyl phosphate = UDP + β-D-glucosyl-1-phosphoundecaprenol
Other name(s): gtrB (gene name); bactoprenol glucosyl transferase; polyisoprenyl-phosphate glycosyltransferase; uridine diphosphoglucose-polyprenol monophosphate glucosyltransferase; UDP-glucose:polyprenol monophosphate glucosyltransferase
Systematic name: UDP-glucose:undecaprenyl-phosphate D-glucosyltransferase (configuration- inverting)
Comments: The enzyme, characterized from the bacterium Shigella flexneri and its bacteriophages, catalyses the transfer of the glucose residue from UDP-glucose to the lipid carrier undecaprenyl phosphate. Following the flipping of the lipid-bound glucose across the cytoplasmic membrane, the glucose is used in the synthesis of the organism’s O-glycan in the periplasm.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 55576-46-0
1.  Jankowski, W., Mankowski, T. and Chojnacki, T. Formation of polyprenol monophosphate glucose in Shigella flexneri. Biochim. Biophys. Acta 337 (1974) 153–162. [DOI] [PMID: 4373050]
2.  Mavris, M., Manning, P.A. and Morona, R. Mechanism of bacteriophage SfII-mediated serotype conversion in Shigella flexneri. Mol. Microbiol. 26 (1997) 939–950. [PMID: 9426131]
3.  Allison, G.E. and Verma, N.K. Serotype-converting bacteriophages and O-antigen modification in Shigella flexneri. Trends Microbiol. 8 (2000) 17–23. [PMID: 10637639]
4.  Ardiccioni, C., Clarke, O.B., Tomasek, D., Issa, H.A., von Alpen, D.C., Pond, H.L., Banerjee, S., Rajashankar, K.R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., Manzini, M.C., Shapiro, L. and Mancia, F. Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat. Commun. 7:10175 (2016). [DOI] [PMID: 26729507]
[EC created 1976]

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