BRENDA - Enzyme Database show

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)
EC Number
Commentary
Organism
2.2.1.10
gene mj0400, expression of N-terminally His-tagged ADHS in Escherichia coli strain B834-(DE3)
Methanocaldococcus jannaschii
Crystallization (Commentary)
EC Number
Crystallization
Organism
2.2.1.10
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.2.1.10
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
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.4.1.24
Methanocaldococcus jannaschii
P81230
-
-
1.4.1.24
Methanocaldococcus jannaschii DSM 2661
P81230
-
-
2.2.1.10
Methanocaldococcus jannaschii
Q57843
gene mj0400
-
Purification (Commentary)
EC Number
Commentary
Organism
2.2.1.10
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
EC Number
Reaction
Commentary
Organism
2.2.1.10
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)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.4.1.24
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+
-
718845
Methanocaldococcus jannaschii
3-dehydroquinate + NH3 + NADH + H+
-
-
-
?
1.4.1.24
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+
-
718845
Methanocaldococcus jannaschii DSM 2661
3-dehydroquinate + NH3 + NADH + H+
-
-
-
?
2.2.1.10
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
EC Number
Subunits
Commentary
Organism
2.2.1.10
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
2.2.1.10
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)
EC Number
Commentary
Organism
2.2.1.10
gene mj0400, expression of N-terminally His-tagged ADHS in Escherichia coli strain B834-(DE3)
Methanocaldococcus jannaschii
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
2.2.1.10
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.2.1.10
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)
EC Number
Commentary
Organism
2.2.1.10
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)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.4.1.24
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+
-
718845
Methanocaldococcus jannaschii
3-dehydroquinate + NH3 + NADH + H+
-
-
-
?
1.4.1.24
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+
-
718845
Methanocaldococcus jannaschii DSM 2661
3-dehydroquinate + NH3 + NADH + H+
-
-
-
?
2.2.1.10
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)
EC Number
Subunits
Commentary
Organism
2.2.1.10
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
2.2.1.10
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
EC Number
General Information
Commentary
Organism
2.2.1.10
evolution
ADH synthase is a member of the class I aldolase superfamily
Methanocaldococcus jannaschii
2.2.1.10
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)
EC Number
General Information
Commentary
Organism
2.2.1.10
evolution
ADH synthase is a member of the class I aldolase superfamily
Methanocaldococcus jannaschii
2.2.1.10
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