Information on EC 2.2.1.10 - 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase

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The expected taxonomic range for this enzyme is: Methanocaldococcus jannaschii

EC NUMBER
COMMENTARY hide
2.2.1.10
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RECOMMENDED NAME
GeneOntology No.
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-dehydroquinate biosynthesis II (archaea)
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Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Phenylalanine, tyrosine and tryptophan biosynthesis
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chorismate metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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ADH synthase is a member of the class I aldolase superfamily
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
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?
L-aspartate 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
show the reaction diagram
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?
L-aspartate semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
?
show the reaction diagram
pyruvate + D-erythrose 4-phosphate
?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
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?
L-aspartate 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
show the reaction diagram
Q57843
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?
L-aspartate semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
?
show the reaction diagram
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1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate and L-aspartate semialdehyde are precursors to 3-dehydroquinate, DHQ
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-O-phosphonato-D-erythrose
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competitive inhibition of aldolase activity
glycylglycine
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slightly inhibiting as buffer at 50 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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MJ0400-His6 exhibits Michaelis-Menten kinetics in the aldolase reaction
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
4-O-phosphonato-D-erythrose
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recombinant enzyme, pH 7.5, 50C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.033
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purified recombinant enzyme, pH 7.5, 50C, buffer Tris-HCl, HEPES/NaOH, or Na-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 85
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10% activity at 25C, higher activity at 50C, optimal activity probably at or above the optimal growth temperature of 85C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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optimal growth temperature is 85C
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodecamer
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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
additional information
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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
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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10 mg/ml purified recombinant His6-tagged enzyme, 50 mM Tris-HCl, pH 7.5, 1 mM DTT, half-life is 37 h
100
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10 mg/ml purified recombinant His6-tagged enzyme, 50 mM Tris-HCl, pH 7.5, 1 mM DTT, half-life is 1 h
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by heat treatment and anion exchange chromatography
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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
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soluble fraction of recombinant His6-tagged MJ0400 from Escherichia coli strain Rosetta(DE3) by nickel affinity chromatography to over 97% purity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene Mj0400, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
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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
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gene mj0400, expression of N-terminally His-tagged ADHS in Escherichia coli strain B834-(DE3)
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