BRENDA - Enzyme Database show
show all sequences of 2.4.99.21

Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation

Matsumoto, S.; Shimada, A.; Nyirenda, J.; Igura, M.; Kawano, Y.; Kohda, D.; Proc. Natl. Acad. Sci. USA 110, 17868-17873 (2013)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
protein consists of the transmembrane domain, about 400-500 residues, 13 transmembrane helices and long external loops EL1 and EL5 and the CC structural unit in the C-terminal globular domain. The key amino acid residue is the conserved Glu residue in the TIXE/SVXE motif in the EL5 loop
Archaeoglobus fulgidus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Archaeoglobus fulgidus
O29867
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
lipid-linked oligosaccharide + [peptide]-L-asparagine
-
735172
Archaeoglobus fulgidus
lipid + a glycopeptide with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
the glycan structure is estimated to be a branched heptasaccharide
-
-
?
Crystallization (Commentary) (protein specific)
Crystallization
Organism
protein consists of the transmembrane domain, about 400-500 residues, 13 transmembrane helices and long external loops EL1 and EL5 and the CC structural unit in the C-terminal globular domain. The key amino acid residue is the conserved Glu residue in the TIXE/SVXE motif in the EL5 loop
Archaeoglobus fulgidus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
lipid-linked oligosaccharide + [peptide]-L-asparagine
-
735172
Archaeoglobus fulgidus
lipid + a glycopeptide with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
the glycan structure is estimated to be a branched heptasaccharide
-
-
?
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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1
1
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738681
Taguchi
Comparative analysis of archae ...
Archaeoglobus fulgidus
J. Biol. Chem.
291
11042-11054
2016
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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
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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1
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3
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1
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1
1
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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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1
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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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2
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1
1
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732528
Chaban
Identification of genes involv ...
Methanococcus voltae
Mol. Microbiol.
61
259-268
2006
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2
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