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show all sequences of 1.3.1.101

Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids

Xu, Q.; Eguchi, T.; Mathews, I.I.; Rife, C.L.; Chiu, H.J.; Farr, C.L.; Feuerhelm, J.; Jaroszewski, L.; Klock, H.E.; Knuth, M.W.; Miller, M.D.; Weekes, D.; Elsliger, M.A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.; J. Mol. Biol. 404, 403-417 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Thermoplasma acidophilum
Crystallization (Commentary)
Crystallization
Organism
vapor-diffusion method, crystal structure at 1.6 A resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid
Thermoplasma acidophilum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+
Thermoplasma acidophilum
the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermoplasma acidophilum
Q9HKS9
-
-
Purification (Commentary)
Commentary
Organism
-
Thermoplasma acidophilum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+
the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
712772
Thermoplasma acidophilum
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
the sequence PxxYxWxFP defines a specificity pocket in the enzyme and precisely aligns the double bond of the geranyl group with respect to the FAD cofactor, thus providing a structural basis for the substrate specificity of geranylgeranyl reductases. FAD switches between two conformations that correspond to the reductive and oxidative half cycles. The structure provides evidence that substrate binding likely involves conformational changes, which are coupled to the two conformational states of the FAD
Thermoplasma acidophilum
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Thermoplasma acidophilum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
the sequence PxxYxWxFP defines a specificity pocket in the enzyme and precisely aligns the double bond of the geranyl group with respect to the FAD cofactor, thus providing a structural basis for the substrate specificity of geranylgeranyl reductases. FAD switches between two conformations that correspond to the reductive and oxidative half cycles. The structure provides evidence that substrate binding likely involves conformational changes, which are coupled to the two conformational states of the FAD
Thermoplasma acidophilum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
vapor-diffusion method, crystal structure at 1.6 A resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid
Thermoplasma acidophilum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+
Thermoplasma acidophilum
the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermoplasma acidophilum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+
the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
712772
Thermoplasma acidophilum
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
Thermoplasma acidophilum
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions
Thermoplasma acidophilum
Other publictions for EC 1.3.1.101
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)
712772
Xu
Insights into substrate specif ...
Thermoplasma acidophilum
J. Mol. Biol.
404
403-417
2010
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1
1
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-
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1
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5
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1
-
-
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-
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1
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-
-
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1
-
-
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1
1
1
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1
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1
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1
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-
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1
1
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719041
Nishimura
Stereochemistry of reduction i ...
Thermoplasma acidophilum
Bioorg. Chem.
35
276-283
2007
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-
1
-
-
-
-
-
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1
1
-
2
-
-
1
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-
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2
1
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-
-
-
-
-
1
-
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1
1
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-
-
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-
-
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1
1
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1
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2
1
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-
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719758
Nishimura
Biosynthesis of archaeal membr ...
Thermoplasma acidophilum
J. Biochem.
139
1073-1081
2006
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-
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1
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1
1
1
1
-
3
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1
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1
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6
1
1
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-
1
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-
2
-
-
-
-
-
-
2
-
-
-
-
1
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-
1
1
1
1
-
-
-
1
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-
1
-
6
1
1
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-
1
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