EC Number | Cloned (Comment) | Organism |
---|---|---|
2.2.1.10 | gene mj0400, expression of N-terminally His-tagged ADHS in Escherichia coli strain B834-(DE3) | Methanocaldococcus jannaschii |
EC Number | Crystallization (Comment) | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | - |
? |
EC Number | Organism | UniProt | Comment | 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 | - |
EC Number | Purification (Comment) | 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 |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.1.24 | 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+ | - |
Methanocaldococcus jannaschii | 3-dehydroquinate + NH3 + NADH + H+ | - |
? | |
1.4.1.24 | 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+ | - |
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 | - |
Methanocaldococcus jannaschii | 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate | - |
? |
EC Number | Subunits | Comment | 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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.1.24 | dehydroquinate synthase II | - |
Methanocaldococcus jannaschii |
1.4.1.24 | MJ1249 | - |
Methanocaldococcus jannaschii |
2.2.1.10 | 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase | - |
Methanocaldococcus jannaschii |
2.2.1.10 | ADH synthase | - |
Methanocaldococcus jannaschii |
2.2.1.10 | ADHS | - |
Methanocaldococcus jannaschii |
EC Number | General Information | Comment | 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 |