GalNAc-alpha-(1-4)-GalNAc-alpha-(1-3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase

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GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase
GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase
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EC no.	2.4.1.292
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BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
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PDB structures	RCSB PDB PDBe PDBsum
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Last updated January 24, 2024

GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase (EC 2.4.1.292, PglH) is an enzyme with systematic name UDP-N-acetyl-alpha-D-galactosamine:GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 4-alpha-N-acetyl-D-galactosaminyltransferase.^[1]^[2]^[3] This enzyme catalyses the following chemical reaction

3 UDP-N-acetyl-alpha-D-galactosamine + GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol

\rightleftharpoons

3 UDP + [GalNAc-alpha-(1->4)]4-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol

This enzyme is solated from Campylobacter jejuni .

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Polypeptide N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the GALNT2 gene.

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(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:1-O-(O- - -O-beta-D-galactopyranosyl- -beta-D-glucopyranosyl)-ceramide 4-beta-N-acetyl-D-galactosaminyltransferase. This enzyme catalyses the following chemical reaction:

N-acetylneuraminylgalactosylglucosylceramide beta-1,4-N-acetylgalactosaminyltransferase (EC 2.4.1.165, is an enzyme that catalyses the following chemical reaction:

N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:N-acetyl-beta-D-glucosaminyl-group 4-beta-N-acetylgalactosaminyltransferase. This enzyme catalyses the following chemical reaction

N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-galactosamine:N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-alpha-N-acetyl-D-galactosaminyltransferase. This enzyme catalyses the following chemical reaction

N-acetylgalactosamine-N, N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-galactosamine:N-acetylgalactosaminyl-alpha-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-alpha-N-acetyl-D-galactosaminyltransferase. 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

UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase is an enzyme with systematic name UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction

UDP-N-acetylgalactosamine diphosphorylase is an enzyme with systematic name UTP:N-acetyl-alpha-D-galactosamine-1-phosphate uridylyltransferase. This enzyme catalyses the following chemical reaction

Phosphoglycosyl transferase C (PglC) is an enzyme belonging to a class known as monotopic phosphoglycosyl transferases (PGT). PGTs are required for the synthesis of glycoconjugates on the membrane surface of bacteria. Glycoconjugates, such as glycoproteins, are imperative for bacterial communication as well as host cell interactions between prokaryotic and eukaryotic cells lending to bacteria's pathogenicity.

UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) (EC 4.2.1.135, PglF) is an enzyme with systematic name UDP-N-acetyl-α-Dglucosamine hydro-lyase (configuration-retaining; UDP-2-acetamido-2,6-dideoxy-α-Dxylo-hex-4-ulose-forming). This enzyme catalyses the following chemical reaction

References

↑ Glover KJ, Weerapana E, Imperiali B (October 2005). "In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation". Proceedings of the National Academy of Sciences of the United States of America. 102 (40): 14255–9. Bibcode:2005PNAS..10214255G. doi: 10.1073/pnas.0507311102 . PMC 1242339 . PMID 16186480.
↑ Troutman JM, Imperiali B (March 2009). "Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions". Biochemistry. 48 (12): 2807–16. doi:10.1021/bi802284d. PMC 2736683 . PMID 19159314.
↑ Børud B, Viburiene R, Hartley MD, Paulsen BS, Egge-Jacobsen W, Imperiali B, Koomey M (June 2011). "Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system". Proceedings of the National Academy of Sciences of the United States of America. 108 (23): 9643–8. Bibcode:2011PNAS..108.9643B. doi: 10.1073/pnas.1103321108 . PMC 3111294 . PMID 21606362.

External links

GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol+alpha-1,4-N-acetyl-D-galactosaminyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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[1] Glover KJ, Weerapana E, Imperiali B (October 2005). "In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation". Proceedings of the National Academy of Sciences of the United States of America. 102 (40): 14255–9. Bibcode:2005PNAS..10214255G. doi: 10.1073/pnas.0507311102 . PMC 1242339 . PMID 16186480.

[2] Troutman JM, Imperiali B (March 2009). "Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions". Biochemistry. 48 (12): 2807–16. doi:10.1021/bi802284d. PMC 2736683 . PMID 19159314.

[3] Børud B, Viburiene R, Hartley MD, Paulsen BS, Egge-Jacobsen W, Imperiali B, Koomey M (June 2011). "Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system". Proceedings of the National Academy of Sciences of the United States of America. 108 (23): 9643–8. Bibcode:2011PNAS..108.9643B. doi: 10.1073/pnas.1103321108 . PMC 3111294 . PMID 21606362.

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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)