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Literature summary extracted from
- Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis (2013), Nat. Chem. Biol., 9, 367-373.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 2.4.1.153 | overexpression in Escherichia coli with N-terminal T7 and C-terminal His6 tags | Methanococcus voltae |
| 2.4.1.335 | overexpression in Escherichia coli with N-terminal T7 and C-terminal His6 tags | Methanococcus voltae |
| 2.4.99.18 | expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells | Methanococcus voltae |
| 2.4.99.21 | overexpression in Escherichia coli with N-terminal T7 and C-terminal His6 tags | Methanococcus voltae |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 2.4.1.153 | EDTA | - |
Methanococcus voltae |  |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 2.4.1.153 | cytoplasm | the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-D-glucosamine to the membrane bound acceptor dolichyl phosphate. The recombinant enzyme produced in Escherichia coli sediments with the membrane fraction and requires detergent for solubility, suggesting it may contain hydrophobic regions that associate with the membrane | Methanococcus voltae | 5737 | - |
| 2.4.1.153 | membrane | the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-alpha-D-glucosamine to the membrane bound acceptor dolichyl phosphate. The recombinant enzyme produced in Escherichia coli sediments with the membrane fraction and requires detergent for solubility, suggesting it may contain hydrophobic regions that associate with the membrane | Methanococcus voltae | 16020 | - |
| 2.4.1.335 | membrane | the enzyme is purified from membrane fraction of recombinant Escherichia coli | Methanococcus voltae | 16020 | - |
| 2.4.99.21 | membrane | the recombinant enzyme is purified from membrane fraction from Escherichia coli | Methanococcus voltae | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 2.4.1.153 | Ca2+ | enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+ | Methanococcus voltae | |
| 2.4.1.153 | Mg2+ | enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+ | Methanococcus voltae | |
| 2.4.1.153 | Mn2+ | enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+ | Methanococcus voltae | |
| 2.4.99.18 | Mn2+ | the enzyme requires the addition of divalent metal cations such as Mn2+ | Methanococcus voltae | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.153 | 28175 | - |
x * 28175, calculated from sequence | Methanococcus voltae |
| 2.4.1.335 | 37328 | - |
x * 37328, calculated from sequence | Methanococcus voltae |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.1.153 | UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate | Methanococcus voltae | the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-alpha-D-glucosamine to the membrane bound acceptor dolichyl phosphate | UDP + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.153 | UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate | Methanococcus voltae PS | the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-alpha-D-glucosamine to the membrane bound acceptor dolichyl phosphate | UDP + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.335 | UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | Methanococcus voltae | the enzyme participates in the N-linked glycosylation in Methanococcus voltae. Methanococcus voltae generates N-linked glycoproteins with a unique trisaccharide composed of ManNAc(6Thr)A-beta1,4-Glc-2,3-diNAcA-beta1,3-GlcNAc in which threonine is linked via an amide to the terminal mannuronic acid | UDP + dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronsyl)-N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.335 | UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | Methanococcus voltae PS | the enzyme participates in the N-linked glycosylation in Methanococcus voltae. Methanococcus voltae generates N-linked glycoproteins with a unique trisaccharide composed of ManNAc(6Thr)A-beta1,4-Glc-2,3-diNAcA-beta1,3-GlcNAc in which threonine is linked via an amide to the terminal mannuronic acid | UDP + dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronsyl)-N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.99.21 | dolichyl phosphooligosaccharide + [flagellum protein FlaB2]-L-asparagine101 | Methanococcus voltae | the enzyme participates in the N-linked glycosylation in Methanococcus voltae. It catalyzes transfer of oligosaccharides from the dolichyl phosphate donor to asparagine in the acceptor proteins. The activity is dependent on the canonical AsnXaaSer/Thr sequon. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide, the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity | dolichol + flagellum protein FlaB2 with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.4.1.153 | Methanococcus voltae | B3VA58 | - |
- |
| 2.4.1.153 | Methanococcus voltae PS | B3VA58 | - |
- |
| 2.4.1.335 | Methanococcus voltae | B3VA59 | - |
- |
| 2.4.1.335 | Methanococcus voltae PS | B3VA59 | - |
- |
| 2.4.99.18 | Methanococcus voltae | - |
- |
- |
| 2.4.99.21 | Methanococcus voltae | Q2EMT4 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 2.4.1.153 | - |
Methanococcus voltae |
| 2.4.1.335 | - |
Methanococcus voltae |
| 2.4.99.18 | Ni-NTA resin column chromatography | Methanococcus voltae |
| 2.4.99.21 | - |
Methanococcus voltae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.1.153 | UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate | the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-alpha-D-glucosamine to the membrane bound acceptor dolichyl phosphate | Methanococcus voltae | UDP + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.153 | UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate | the enzyme shows much higher activity with the shorter, native-like (C5560) dolichyl monophosphate substrate compared with the longer (C85105) dolichyl monophosphate, indicating a strong preference of the enzyme for the shorter dolichols found in archaea | Methanococcus voltae | UDP + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.153 | UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate | the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-alpha-D-glucosamine to the membrane bound acceptor dolichyl phosphate | Methanococcus voltae PS | UDP + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.153 | UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate | the enzyme shows much higher activity with the shorter, native-like (C5560) dolichyl monophosphate substrate compared with the longer (C85105) dolichyl monophosphate, indicating a strong preference of the enzyme for the shorter dolichols found in archaea | Methanococcus voltae PS | UDP + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.335 | UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | the enzyme participates in the N-linked glycosylation in Methanococcus voltae. Methanococcus voltae generates N-linked glycoproteins with a unique trisaccharide composed of ManNAc(6Thr)A-beta1,4-Glc-2,3-diNAcA-beta1,3-GlcNAc in which threonine is linked via an amide to the terminal mannuronic acid | Methanococcus voltae | UDP + dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronsyl)-N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.335 | UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | the enzyme is specific for dolichyl N-acetyl-alpha-D-glucosaminyl phosphate, as no conversion is observed with Dol-P or Dol-PP-GlcNAc. No activity with UDP-Glc, UDP-GalNAc or UDP-Gal. Although the full length N-glycan generated by Methanococcus voltae is a trisaccharide (composed of ManNAc(6Thr)A-beta1,4-Glc-2,3-diNAcA-beta1,3-GlcNAc in which threonine is linked via an amide to the terminal mannuronic acid) the disaccharide-linked | Methanococcus voltae | UDP + dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronsyl)-N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.335 | UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | the enzyme participates in the N-linked glycosylation in Methanococcus voltae. Methanococcus voltae generates N-linked glycoproteins with a unique trisaccharide composed of ManNAc(6Thr)A-beta1,4-Glc-2,3-diNAcA-beta1,3-GlcNAc in which threonine is linked via an amide to the terminal mannuronic acid | Methanococcus voltae PS | UDP + dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronsyl)-N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.1.335 | UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate + dolichyl N-acetyl-alpha-D-glucosaminyl phosphate | the enzyme is specific for dolichyl N-acetyl-alpha-D-glucosaminyl phosphate, as no conversion is observed with Dol-P or Dol-PP-GlcNAc. No activity with UDP-Glc, UDP-GalNAc or UDP-Gal. Although the full length N-glycan generated by Methanococcus voltae is a trisaccharide (composed of ManNAc(6Thr)A-beta1,4-Glc-2,3-diNAcA-beta1,3-GlcNAc in which threonine is linked via an amide to the terminal mannuronic acid) the disaccharide-linked | Methanococcus voltae PS | UDP + dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronsyl)-N-acetyl-alpha-D-glucosaminyl phosphate | - |
? | |
| 2.4.99.18 | dolichyl monophosphate GlcNAc-Glc-2,3-diNAcA + [protein]-L-asparagine | - |
Methanococcus voltae | ? | - |
? | |
| 2.4.99.18 | additional information | minimal activity with alpha-linked dolichyl monophosphate N-acetylglucosamine and no glycosylation activity with peptide Ac(YKYQESSYKpNF)NH2 | Methanococcus voltae | ? | - |
? | |
| 2.4.99.21 | dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl phosphate + Ac-YKYQESSYK-(4-nitro)F-NH2 | the peptide is based on the sequence of the natively glycosylated flagellum protein FlaB2. The enzyme shows no activity with the peptide Ac-YKYQESSYK-(4-nitro)F-NH2, lacking the key asparagine residue. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity | Methanococcus voltae | dolichol + ? | - |
? | |
| 2.4.99.21 | dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl phosphate + [flagellum protein FlaB2]-L-asparagine | the enzyme is incubated with the acceptor peptide Ac-YKYQESSYK-(4-nitro)F-NH2, which is based the natively glycosylated flagellum protein FlaB2 sequence. The activity is dependent on the canonical AsnXaaSer/Thr sequon. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity | Methanococcus voltae | dolichol + 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl-[flagellum protein FlaB2]-L-asparagine | - |
? | |
| 2.4.99.21 | dolichyl phosphooligosaccharide + [flagellum protein FlaB2]-L-asparagine101 | the enzyme participates in the N-linked glycosylation in Methanococcus voltae. It catalyzes transfer of oligosaccharides from the dolichyl phosphate donor to asparagine in the acceptor proteins. The activity is dependent on the canonical AsnXaaSer/Thr sequon. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide, the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity | Methanococcus voltae | dolichol + flagellum protein FlaB2 with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 2.4.1.153 | ? | x * 28175, calculated from sequence | Methanococcus voltae |
| 2.4.1.335 | ? | x * 37328, calculated from sequence | Methanococcus voltae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.4.1.153 | AglK | - |
Methanococcus voltae |
| 2.4.1.153 | Dol-P-GlcNAc synthase | - |
Methanococcus voltae |
| 2.4.1.335 | AglC | - |
Methanococcus voltae |
| 2.4.1.335 | Mv990 | locus name | Methanococcus voltae |
| 2.4.1.335 | UDP-Glc-2,3-diNAcA glycosyltransferase | - |
Methanococcus voltae |
| 2.4.99.18 | AglB | - |
Methanococcus voltae |
| 2.4.99.18 | OTase | - |
Methanococcus voltae |
| 2.4.99.21 | AglB | - |
Methanococcus voltae |
| 2.4.99.21 | archaeal oligosaccharyl transferase | - |
Methanococcus voltae |
| 2.4.99.21 | dolichyl-monophosphooligosaccharide-protein glycotransferase | - |
Methanococcus voltae |
| 2.4.99.21 | MVO1749 | locus name | Methanococcus voltae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.153 | 25 | - |
assay at | Methanococcus voltae |
| 2.4.1.335 | 25 | - |
assay at | Methanococcus voltae |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.153 | 7.5 | - |
assay at | Methanococcus voltae |
| 2.4.1.335 | 7.5 | - |
assay at | Methanococcus voltae |
| 2.4.99.21 | 7.5 | - |
assay at | Methanococcus voltae |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 2.4.1.153 | metabolism | the enzyme initiates the N-linked glycan biosynthesis in the cytoplasm by transfer of N-acetyl-alpha-D-glucosamine to the membrane bound acceptor dolichyl phosphate | Methanococcus voltae |
| 2.4.1.335 | metabolism | the enzyme participates in the N-linked glycosylation in Methanococcus voltae. Methanococcus voltae generates N-linked glycoproteins with a unique trisaccharide composed of ManNAc(6Thr)A-beta1,4-Glc-2,3-diNAcA-beta1,3-GlcNAc in which threonine is linked via an amide to the terminal mannuronic acid | Methanococcus voltae |
| 2.4.99.21 | metabolism | the enzyme participates in the N-linked glycosylation in Methanococcus voltae. It catalyzes transfer of oligosaccharides from the dolichyl phosphate donor to asparagine in the acceptor proteins. Methanococcus voltae generates N-linked glycoproteins with a unique trisaccharide (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) | Methanococcus voltae |
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