BRENDA - Enzyme Database

Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis

Larkin, A.; Chang, M.M.; Whitworth, G.E.; Imperiali, B.; Nat. Chem. Biol. 9, 367-373 (2013)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
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
Commentary
Organism
Structure
2.4.1.153
EDTA
-
Methanococcus voltae
Localization
EC Number
Localization
Commentary
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
Commentary
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]
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
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
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
732558
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
732558
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
732558
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
732558
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
732558
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
732558
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
732558
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
732558
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
-
732558
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
732558
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
732558
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
732558
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
732558
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
Commentary
Organism
2.4.1.153
?
x * 28175, calculated from sequence
Methanococcus voltae
2.4.1.335
?
x * 37328, calculated from sequence
Methanococcus voltae
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
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
Commentary
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
Cloned(Commentary) (protein specific)
EC Number
Commentary
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 (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
2.4.1.153
EDTA
-
Methanococcus voltae
Localization (protein specific)
EC Number
Localization
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
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] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
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) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
732558
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
732558
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
732558
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
732558
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
732558
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
732558
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
732558
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
732558
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
-
732558
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
732558
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
732558
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
732558
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
732558
Methanococcus voltae
dolichol + flagellum protein FlaB2 with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.4.1.153
?
x * 28175, calculated from sequence
Methanococcus voltae
2.4.1.335
?
x * 37328, calculated from sequence
Methanococcus voltae
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
2.4.1.153
25
-
assay at
Methanococcus voltae
2.4.1.335
25
-
assay at
Methanococcus voltae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
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
Commentary
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
General Information (protein specific)
EC Number
General Information
Commentary
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