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show all sequences of 2.2.1.10

Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids

Morar, M.; White, R.H.; Ealick, S.E.; Biochemistry 46, 10562-10571 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene mj0400, expression of N-terminally His-tagged ADHS in Escherichia coli strain B834-(DE3)
Methanocaldococcus jannaschii
Crystallization (Commentary)
Crystallization
Organism
purified recombinant detagged ADH synthase in complex with substrate analogue fructose 1,6-bisphosphate, with dihydroxyacetone phosphate, and with native structure-containing copurified ligands, modeled as dihydroxyacetone phosphate and glycerol, vapor diffusion hanging drop method, mixing of 0.002 ml of protein solution containing 20 mg/ml protein in 10 mM Tris, pH 7.5, with 0.002 ml of reservoir solution containing 4-8% 1,4-butanediol and 0.1 M acetate, pH 4.2-4.3, 1-2-days, soaking of crystals in motherliquor with 10 mM ligands, for 1 h, X-ray diffraction structure determination and analysis at 2.6-2.8 A resolution
Methanocaldococcus jannaschii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
Methanocaldococcus jannaschii
-
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanocaldococcus jannaschii
Q57843
gene mj0400
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged ADHS from Escherichia coli strain B834-(DE3) by nickel affinity chromatography, cleavage of the tag by thrombin, and further by strepavidin affinity chromatography to eliminate thrombin, followed by gel filtration/ultrafiltration
Methanocaldococcus jannaschii
Reaction
Reaction
Commentary
Organism
L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
possible catalytic residues are Lys184, which is responsible for formation of the Schiff base intermediate, and Asp33 and Tyr153, which are candidates for the general acid/base catalysis, ADHS active site structure, modeling of the DKFP Schiff base intermediate in the active site, overview
Methanocaldococcus jannaschii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
-
718845
Methanocaldococcus jannaschii
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodecamer
in the crystal structure ADHS forms a decamer. The decamer consists of two doughnut shaped pentamers with D5 symmetry, modeling, overview. The homodecamer contains the active site in the top of the barrel and forms a covalent adduct with a substrate utilizing a strictly conserved lysine residue located on strand beta6 of the barrel
Methanocaldococcus jannaschii
More
the enzyme monomer contains an (betaalpha)8-barrel structure, a pair of antiparallel strands, beta3a and beta3b, and additional helices that are not part of the (betaalpha)8-barrel fold, overview. The additional helix alpha1a and the pair of antiparallel beta-strands are also part of this interface
Methanocaldococcus jannaschii
Cloned(Commentary) (protein specific)
Commentary
Organism
gene mj0400, expression of N-terminally His-tagged ADHS in Escherichia coli strain B834-(DE3)
Methanocaldococcus jannaschii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant detagged ADH synthase in complex with substrate analogue fructose 1,6-bisphosphate, with dihydroxyacetone phosphate, and with native structure-containing copurified ligands, modeled as dihydroxyacetone phosphate and glycerol, vapor diffusion hanging drop method, mixing of 0.002 ml of protein solution containing 20 mg/ml protein in 10 mM Tris, pH 7.5, with 0.002 ml of reservoir solution containing 4-8% 1,4-butanediol and 0.1 M acetate, pH 4.2-4.3, 1-2-days, soaking of crystals in motherliquor with 10 mM ligands, for 1 h, X-ray diffraction structure determination and analysis at 2.6-2.8 A resolution
Methanocaldococcus jannaschii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
Methanocaldococcus jannaschii
-
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged ADHS from Escherichia coli strain B834-(DE3) by nickel affinity chromatography, cleavage of the tag by thrombin, and further by strepavidin affinity chromatography to eliminate thrombin, followed by gel filtration/ultrafiltration
Methanocaldococcus jannaschii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
-
718845
Methanocaldococcus jannaschii
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodecamer
in the crystal structure ADHS forms a decamer. The decamer consists of two doughnut shaped pentamers with D5 symmetry, modeling, overview. The homodecamer contains the active site in the top of the barrel and forms a covalent adduct with a substrate utilizing a strictly conserved lysine residue located on strand beta6 of the barrel
Methanocaldococcus jannaschii
More
the enzyme monomer contains an (betaalpha)8-barrel structure, a pair of antiparallel strands, beta3a and beta3b, and additional helices that are not part of the (betaalpha)8-barrel fold, overview. The additional helix alpha1a and the pair of antiparallel beta-strands are also part of this interface
Methanocaldococcus jannaschii
General Information
General Information
Commentary
Organism
evolution
ADH synthase is a member of the class I aldolase superfamily
Methanocaldococcus jannaschii
metabolism
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, the product of the Mj0400 gene, catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate and L-aspartate semialdehyde to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid, i.e. ADH. Dehydroquinate synthase II, the product of the Mj1249 gene, then catalyzes deamination and cyclization of ADH, resulting in DHQ, which is fed into the canonical pathway
Methanocaldococcus jannaschii
General Information (protein specific)
General Information
Commentary
Organism
evolution
ADH synthase is a member of the class I aldolase superfamily
Methanocaldococcus jannaschii
metabolism
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, the product of the Mj0400 gene, catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate and L-aspartate semialdehyde to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid, i.e. ADH. Dehydroquinate synthase II, the product of the Mj1249 gene, then catalyzes deamination and cyclization of ADH, resulting in DHQ, which is fed into the canonical pathway
Methanocaldococcus jannaschii
Other publictions for EC 2.2.1.10
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)
692386
Samland
MJ0400 from Methanocaldococcus ...
Methanocaldococcus jannaschii
FEMS Microbiol. Lett.
281
36-41
2008
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718845
Morar
Structure of 2-amino-3,7-dideo ...
Methanocaldococcus jannaschii
Biochemistry
46
10562-10571
2007
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718838
White
L-Aspartate semialdehyde and a ...
Methanocaldococcus jannaschii
Biochemistry
43
7618-7627
2004
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