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Literature summary for 2.2.1.10 extracted from

  • Morar, M.; White, R.H.; Ealick, S.E.
    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 (2007), Biochemistry, 46, 10562-10571.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene mj0400, expression of N-terminally His-tagged ADHS in Escherichia coli strain B834-(DE3) Methanocaldococcus jannaschii

Crystallization (Commentary)

Crystallization (Comment) 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate Methanocaldococcus jannaschii
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2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
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?

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q57843 gene mj0400
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Purification (Commentary)

Purification (Comment) 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 Comment Organism Reaction ID
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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
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Methanocaldococcus jannaschii 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
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?

Subunits

Subunits Comment 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

Synonyms

Synonyms Comment Organism
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase
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Methanocaldococcus jannaschii
ADH synthase
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Methanocaldococcus jannaschii
ADHS
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Methanocaldococcus jannaschii

General Information

General Information Comment 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