BRENDA - Enzyme Database show
show all sequences of 2.4.99.21

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)
Commentary
Organism
overexpression in Escherichia coli with N-terminal T7 and C-terminal His6 tags
Methanococcus voltae
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the recombinant enzyme is purified from membrane fraction from Escherichia coli
Methanococcus voltae
16020
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanococcus voltae
Q2EMT4
-
-
Purification (Commentary)
Commentary
Organism
-
Methanococcus voltae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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 + ?
-
-
-
?
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
-
-
-
?
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
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Methanococcus voltae
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression in Escherichia coli with N-terminal T7 and C-terminal His6 tags
Methanococcus voltae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the recombinant enzyme is purified from membrane fraction from Escherichia coli
Methanococcus voltae
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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)
Commentary
Organism
-
Methanococcus voltae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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 + ?
-
-
-
?
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
-
-
-
?
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
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Methanococcus voltae
General Information
General Information
Commentary
Organism
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)
General Information
Commentary
Organism
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
Other publictions for EC 2.4.99.21
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738680
Esquivel
Identification of Haloferax vo ...
Haloferax volcanii
J. Biol. Chem.
291
10602-10614
2016
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738681
Taguchi
Comparative analysis of archae ...
Archaeoglobus fulgidus
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11042-11054
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733612
Fujinami
Structural elucidation of an a ...
Archaeoglobus fulgidus
Carbohydr. Res.
413
55-62
2015
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726749
Cohen-Rosenzweig
Substrate promiscuity: AglB, t ...
Haloarcula marismortui, Halobacterium salinarum, Halobacterium salinarum DSM 671, Haloferax mediterranei
Appl. Environ. Microbiol.
80
486-496
2014
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3
3
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734650
Meyer
AglB, catalyzing the oligosacc ...
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
MicrobiologyOpen
3
531-543
2014
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1
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732558
Larkin
Biochemical evidence for an al ...
Methanococcus voltae
Nat. Chem. Biol.
9
367-373
2013
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735172
Matsumoto
Crystal structures of an archa ...
Archaeoglobus fulgidus
Proc. Natl. Acad. Sci. USA
110
17868-17873
2013
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734470
Abu-Qarn
Haloferax volcanii AglB and Ag ...
Haloferax volcanii, Haloferax volcanii DSM 3757
J. Mol. Biol.
374
1224-1236
2007
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1
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732528
Chaban
Identification of genes involv ...
Methanococcus voltae
Mol. Microbiol.
61
259-268
2006
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