GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase

Search
PMC	articles
PubMed	articles
NCBI	proteins

GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase
GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase
Identifiers
EC no.	2.4.1.252
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Last updated January 24, 2024

GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase (EC 2.4.1.252, GumH, AceA, alpha1,3-mannosyltransferase AceA) is an enzyme with systematic name GDP-mannose:D-Glc-beta-(1->4)-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 3-alpha-mannosyltransferase .^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

GDP-mannose + D-Glc-beta-(1->4)-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol

\rightleftharpoons

GDP + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol

In the bacterium Gluconacetobacter xylinus the enzyme is involved in the biosynthesis of the exopolysaccharide acetan.

Related Research Articles

In enzymology, a chitobiosyldiphosphodolichol beta-mannosyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a dolichyl-phosphate beta-D-mannosyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, an undecaprenyl-phosphate mannosyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, an initiation-specific alpha-1,6-mannosyltransferase is an enzyme that catalyzes the chemical reaction in which an alpha-D-mannosyl residue is transferred from GDP-mannose to a lipid-linked oligosaccharide, being linked by an alpha-1,6-D-mannosyl-D-mannose bond.

In enzymology, a glycolipid 3-alpha-mannosyltransferase is an enzyme that catalyzes the chemical reaction in which an alpha-D-mannosyl residue is transferred from GDP-mannose to a lipid-linked oligosaccharide, being attached by an alpha-1,3-D-mannosyl-D-mannose bond.

Mannosylfructose-phosphate synthase is an enzyme with systematic name GDP-mannose:D-fructose-6-phosphate 2-alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction

GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 4-beta-mannosyltransferase is an enzyme with systematic name GDP-mannose:GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 4-beta-mannosyltransferase. This enzyme catalyses the following chemical reaction

GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase is an enzyme with systematic name GDP-D-mannose:D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-6-mannosyltransferase. This enzyme catalyses the following chemical reaction

Dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase is an enzyme with systematic name dolichyl beta-D-mannosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha- )-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-mannosyltransferase. This enzyme catalyses the following chemical reaction

D-Man-alpha-(1->3) -D-Glc-beta-(1->4) -D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase is an enzyme with the systematic name UDP-glucuronate: D-Man-alpha-(1->3) -D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol beta-1,2-glucuronyltransferase. This enzyme catalyses the following chemical reaction:

Mannosylglycerate synthase is an enzyme with systematic name GDP-mannose:D-glycerate 2-alpha-D-mannosyltransferase. This enzyme catalyses the following chemical reaction

Rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,3/1,4-galactofuranosyltransferase is an enzyme with systematic name UDP-alpha-D-galactofuranose:alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol 3-beta/4-beta-galactofuranosyltransferase. This enzyme catalyses the following chemical reaction

Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase is an enzyme with systematic name UDP-alpha-D-galactofuranose:beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol 4-beta/5-beta-D-galactofuranosyltransferase. This enzyme catalyses the following chemical reaction

N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase is an enzyme with systematic name dTDP-6-deoxy-beta-L-mannose:N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol 3-alpha-L-rhamnosyltransferase. This enzyme catalyses the following chemical reaction

GalNAc5-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase is an enzyme with systematic name UDP-alpha-D-glucose:(GalNAc-alpha- )4-GalNAc-alpha-(1->3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol 3-beta-D-glucosyltransferase. This enzyme catalyses the following chemical reaction

Galactan 5-O-arabinofuranosyltransferase is an enzyme with systematic name galactofuranan:trans,octacis-decaprenylphospho-beta-D-arabinofuranose 5-O-alpha-D-arabinofuranosyltransferase. This enzyme catalyses the following chemical reaction

Xanthan ketal pyruvate transferase is an enzyme with systematic name phosphoenolpyruvate:D-Man-beta-(1->4)-GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 4,6-O-(1-carboxyethan-1,1-diyl)transferase. This enzyme catalyses the following chemical reaction

Undecaprenyl-phosphate glucose phosphotransferase is an enzyme with systematic name UDP-glucose:ditrans,octacis-undecaprenyl-phosphate glucose phosphotransferase. This enzyme catalyses the following chemical reaction

UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-alpha-D-glucosaminephosphotransferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Methyltransferase/kinase WbdD</span>

Methyltransferase/kinase WbdD EC 2.1.1.294 and EC 2.7.1.181WbdD is a bifunctional enzyme that regulates the length of the LPS O-antigen polysaccharide chain. Stops the polymerization of the chain by phosphorylating and then methylating the phosphate on the terminal sugar. This terminal modification is essential for export of the O-antigen across the inner membrane. WbdD is also required for correct localization of the WbdA mannosyltransferase.

References

↑ Geremia RA, Roux M, Ferreiro DU, Dauphin-Dubois R, Lellouch AC, Ielpi L (July 1999). "Expression and biochemical characterisation of recombinant AceA, a bacterial alpha-mannosyltransferase". Molecular & General Genetics. 261 (6): 933–40. doi:10.1007/s004380051040. PMID 10485283.
↑ Abdian PL, Lellouch AC, Gautier C, Ielpi L, Geremia RA (December 2000). "Identification of essential amino acids in the bacterial alpha -mannosyltransferase aceA". The Journal of Biological Chemistry. 275 (51): 40568–75. doi: 10.1074/jbc.M007496200 . hdl: 11336/47751 . PMID 11001941.
↑ Petroni EA, Ielpi L (August 1996). "Isolation and nucleotide sequence of the GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase gene from Acetobacter xylinum". Journal of Bacteriology. 178 (16): 4814–21. doi:10.1128/jb.178.16.4814-4821.1996. PMC 178262 . PMID 8759843.
↑ Lellouch AC, Watt GM, Geremia RA, Flitsch SL (May 2000). "Phytanyl-pyrophosphate-linked substrate for a bacterial alpha-mannosyltransferase". Biochemical and Biophysical Research Communications. 272 (1): 290–2. doi:10.1006/bbrc.2000.2771. PMID 10872841.
↑ Katzen, F.; Ferreiro, D.U.; Oddo, C.G.; Ielmini, M.V.; Becker, A.; Puhler, A.; Ielpi, L. (1998). "Xanthomonas campestris pv. campestris gum mutants: effects on xanthan biosynthesis and plant virulence". J. Bacteriol. 180 (7): 1607–1617. PMC 107069 . PMID 9537354.

External links

GDP-mannose:cellobiosyl-diphosphopolyprenol+alpha-mannosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.

[1] Geremia RA, Roux M, Ferreiro DU, Dauphin-Dubois R, Lellouch AC, Ielpi L (July 1999). "Expression and biochemical characterisation of recombinant AceA, a bacterial alpha-mannosyltransferase". Molecular & General Genetics. 261 (6): 933–40. doi:10.1007/s004380051040. PMID 10485283.

[2] Abdian PL, Lellouch AC, Gautier C, Ielpi L, Geremia RA (December 2000). "Identification of essential amino acids in the bacterial alpha -mannosyltransferase aceA". The Journal of Biological Chemistry. 275 (51): 40568–75. doi: 10.1074/jbc.M007496200 . hdl: 11336/47751 . PMID 11001941.

[3] Petroni EA, Ielpi L (August 1996). "Isolation and nucleotide sequence of the GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase gene from Acetobacter xylinum". Journal of Bacteriology. 178 (16): 4814–21. doi:10.1128/jb.178.16.4814-4821.1996. PMC 178262 . PMID 8759843.

[4] Lellouch AC, Watt GM, Geremia RA, Flitsch SL (May 2000). "Phytanyl-pyrophosphate-linked substrate for a bacterial alpha-mannosyltransferase". Biochemical and Biophysical Research Communications. 272 (1): 290–2. doi:10.1006/bbrc.2000.2771. PMID 10872841.

[5] Katzen, F.; Ferreiro, D.U.; Oddo, C.G.; Ielmini, M.V.; Becker, A.; Puhler, A.; Ielpi, L. (1998). "Xanthomonas campestris pv. campestris gum mutants: effects on xanthan biosynthesis and plant virulence". J. Bacteriol. 180 (7): 1607–1617. PMC 107069 . PMID 9537354.

[1]

[2]

[3]

[4]

[5]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)