The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.
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
The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.
GC-MS analysis of reaction intermediates, overview. The enzyme is active as aldose with erythrose 4-phosphate and pyruvate producing a different stereoisomer from 3-deoxy-D-arabino-2-heptulosonate-7-phosphate
GC-MS analysis of reaction intermediates, overview. The enzyme is active as aldose with erythrose 4-phosphate and pyruvate producing a different stereoisomer from 3-deoxy-D-arabino-2-heptulosonate-7-phosphate
MJ0400 acts as an 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, catalyzing the reaction of L-aspartate semialdehyde and 6-deoxy-5-ketofructose-1-phosphate to 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid, but the recombinant His6-tagged MJ0400 also catalyzes the cleavage of fructose-1,6-bisphosphate to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate, exhibiting fructose-1,6-bisphosphate aldolase, FBP aldolase, activity, EC 4.1.2.13, or the transaldolase reaction with D-fructose-6-phosphate and D-erythose-4-phosphate as substrates. The enzyme shows high substrate specificity for fructose-6-phosphate
MJ0400 acts as an 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, catalyzing the reaction of L-aspartate semialdehyde and 6-deoxy-5-ketofructose-1-phosphate to 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid, but the recombinant His6-tagged MJ0400 also catalyzes the cleavage of fructose-1,6-bisphosphate to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate, exhibiting fructose-1,6-bisphosphate aldolase, FBP aldolase, activity, EC 4.1.2.13, or the transaldolase reaction with D-fructose-6-phosphate and D-erythose-4-phosphate as substrates. The enzyme shows high substrate specificity for fructose-6-phosphate
Expression pattern, ethanol-metabolizing activities, and cellular localization of alcohol and aldehyde dehydrogenases in human large bowel: association of the functional polymorphisms of ADH and ALDH genes with hemorrhoids and colorectal cancer.
Expression pattern, ethanol-metabolizing activities, and cellular localization of alcohol and aldehyde dehydrogenases in human large bowel: association of the functional polymorphisms of ADH and ALDH genes with hemorrhoids and colorectal cancer.
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
Mj0400 is involved in the biosynthesis of aromatic compounds, including 3-dehydroquinate via an undetermined intermediate and 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid, which is formed by NAD+-dependent Mj1249 from the intermediate compound. Also 4,5-dihydroxy-6-methylpipecolinic acid is formed from the intermediate. Pathway analysis, detailed overview
the enzyme is involved in both carbon metabolism and amino acid biosynthesis, it catalyzes as transaldolase a step leading to biosynthesis of 3-dehydroquinate, which enters the shikimate pathway, and also shows activity as fructose 1,6-bisphosphate aldolase in carbon metabolism, overview
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
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
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
gene Mj0400, DNA and amino acid sequence determination and analysis, overexpression of the His6-tagged enzyme in Escherichia coli strain Rosetta2(DE3)pLysS as mainly insoluble protein
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