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Information on EC 2.2.1.10 - 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57843

for references in articles please use BRENDA:EC2.2.1.10
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EC Tree
IUBMB Comments
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.
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Methanocaldococcus jannaschii
UNIPROT: Q57843
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
adhs, mj0400, adh synthase, 2-amino-3,7-dideoxy-d-threo-hept-6-ulosonic acid synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase
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ADHS
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-
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ADH synthase
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-
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MJ0400
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-
-
-
additional information
cf. EC 4.1.2.13
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
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
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.
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 SUBSTRATE
NATURAL 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
-
-
-
?
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
-
-
-
?
L-aspartate semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate
?
show the reaction diagram
1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate and L-aspartate semialdehyde are precursors to 3-dehydroquinate, DHQ
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-O-phosphonato-D-erythrose
competitive inhibition of aldolase activity
glycylglycine
slightly inhibiting as buffer at 50 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
4-O-phosphonato-D-erythrose
recombinant enzyme, pH 7.5, 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.033
purified recombinant enzyme, pH 7.5, 50°C, 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
10% activity at 25°C, higher activity at 50°C, optimal activity probably at or above the optimal growth temperature of 85°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
optimal growth temperature is 85°C
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
ADH synthase is a member of the class I aldolase superfamily
metabolism
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
10 mg/ml purified recombinant His6-tagged enzyme, 50 mM Tris-HCl, pH 7.5, 1 mM DTT, half-life is 1 h
80
10 mg/ml purified recombinant His6-tagged enzyme, 50 mM Tris-HCl, pH 7.5, 1 mM DTT, half-life is 37 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by heat treatment and anion exchange chromatography
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
soluble fraction of recombinant His6-tagged MJ0400 from Escherichia coli strain Rosetta(DE3) by nickel affinity chromatography to over 97% purity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Mj0400, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
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
gene mj0400, expression of N-terminally His-tagged ADHS in Escherichia coli strain B834-(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Samland, A.K.; Wang, M.; Sprenger, G.A.
MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity
FEMS Microbiol. Lett.
281
36-41
2008
Methanocaldococcus jannaschii (Q57843), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
White, R.H.
L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii
Biochemistry
43
7618-7627
2004
Methanocaldococcus jannaschii (Q57843), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
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
Biochemistry
46
10562-10571
2007
Methanocaldococcus jannaschii (Q57843), Methanocaldococcus jannaschii
Manually annotated by BRENDA team