BRENDA - Enzyme Database
show all sequences of 2.4.1.153

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
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
-
Methanococcus voltae
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
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
-
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
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+
Methanococcus voltae
Mg2+
enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+
Methanococcus voltae
Mn2+
enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+
Methanococcus voltae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28175
-
x * 28175, calculated from sequence
Methanococcus voltae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
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
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanococcus voltae
B3VA58
-
-
Methanococcus voltae PS
B3VA58
-
-
Purification (Commentary)
Commentary
Organism
-
Methanococcus voltae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
the enzyme shows much higher activity with the shorter, native-like (C55–60) dolichyl monophosphate substrate compared with the longer (C85–105) 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
-
-
-
?
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
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
the enzyme shows much higher activity with the shorter, native-like (C55–60) dolichyl monophosphate substrate compared with the longer (C85–105) 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
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 28175, calculated from sequence
Methanococcus voltae
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Methanococcus voltae
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
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
-
Methanococcus voltae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
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
-
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
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+
Methanococcus voltae
Mg2+
enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+
Methanococcus voltae
Mn2+
enzymatic activity requires divalent metal cations Ca2+, Mn2+, or Mg2+
Methanococcus voltae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28175
-
x * 28175, calculated from sequence
Methanococcus voltae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
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
-
-
?
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
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
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
the enzyme shows much higher activity with the shorter, native-like (C55–60) dolichyl monophosphate substrate compared with the longer (C85–105) 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
-
-
-
?
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
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + dolichyl phosphate
the enzyme shows much higher activity with the shorter, native-like (C55–60) dolichyl monophosphate substrate compared with the longer (C85–105) 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
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 28175, calculated from sequence
Methanococcus voltae
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Methanococcus voltae
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 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
General Information (protein specific)
General Information
Commentary
Organism
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
Other publictions for EC 2.4.1.153
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)
732558
Larkin
Biochemical evidence for an al ...
Methanococcus voltae, Methanococcus voltae PS
Nat. Chem. Biol.
9
367-373
2013
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1
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2
3
1
2
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2
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1
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4
1
1
-
-
-
1
-
-
-
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-
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1
-
-
-
-
-
1
-
-
2
3
1
2
-
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-
1
-
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-
4
1
1
-
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1
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1
1
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660115
Koizumi
-
A chimeric tunicamycin resista ...
Arabidopsis thaliana
Plant Biotechnol.
20
305-309
2003
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1
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-
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1
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488620
Alhadeff
Lipid-mediated glycosylation i ...
Homo sapiens
Enzyme
31
90-103
1984
1
-
-
-
-
-
-
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1
1
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-
1
-
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1
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1
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1
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1
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-
-
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488621
Alhadeff
Dolichyl phosphate-mannosyltra ...
Homo sapiens
Clin. Chim. Acta
134
1-9
1983
2
-
-
-
-
-
-
-
-
1
-
1
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1
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1
1
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2
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1
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2
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1
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1
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1
1
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2
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1
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