Information on EC 4.2.1.10 - 3-dehydroquinate dehydratase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.2.1.10
-
RECOMMENDED NAME
GeneOntology No.
3-dehydroquinate dehydratase
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydration
-, O30011
-
dehydration
-
-
dehydration
-
-
dehydration
Gluconobacter oxydans IFO 3244
-
-
-
elimination
-
-
-
-
elimination
-, O30011
-
elimination
-
-
elimination
Gluconobacter oxydans IFO 3244
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
chorismate biosynthesis from 3-dehydroquinate
-
gallate biosynthesis
-
Metabolic pathways
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
quinate degradation I
-
quinate degradation II
-
SYSTEMATIC NAME
IUBMB Comments
3-dehydroquinate hydro-lyase (3-dehydroshikimate-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-dehydroquinase
-
-
-
-
3-dehydroquinate dehydratase
-
-
-
-
3-dehydroquinate dehydratase
O30011
-
3-dehydroquinate dehydratase
-
-
3-dehydroquinate dehydratase
Gluconobacter oxydans IFO 3244
-
;
-
3-dehydroquinate dehydratase /shikimate dehydrogenase isoform 1
Q6PUF9
-
3-dehydroquinate dehydratase /shikimate dehydrogenase isoform 2
Q6PUG0
-
3-dehydroquinate dehydratase/shikimate dehydrogenase
Q6PUF9, Q6PUG0
-
3-dehydroquinate dehydratase/shikimate dehydrogenase
-
-
5-dehydroquinase
-
-
-
-
5-dehydroquinate dehydratase
-
-
-
-
5-dehydroquinate hydro-lyase
-
-
-
-
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplast
Q9SQT8
-
dehydratase, 3-dehydroquinate
-
-
-
-
dehydroquinase
-
-
-
-
dehydroquinase
O30011
-
dehydroquinase
-
-
dehydroquinase
Q48255
-
dehydroquinase
-
-
dehydroquinase
P0A4Z6
-
dehydroquinase
-
-
dehydroquinase
P15474
-
dehydroquinate dehydratase
-
-
-
-
dehydroquinate dehydratase
Clostridium difficile
-
-
dehydroquinate dehydratase
P58687
-
dehydroquinate dehydratase
Salmonella enterica LT2
P58687
-
-
dehydroquinate dehydratase-shikimate dehydrogenase
Q9SQT8
-
dehydroquinate synthase
-
-
DHD/SHD
Q6PUF9, Q6PUG0
-
DHQ synthase
-
-
-
-
DHQ-SDH
Q9SQT8
-
DHQ-SDH protein
Q9SQT8
-
DHQ/SDH
-
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
DHQ2
Q48255
-
DHQase
-
-
-
-
DHQase
Q48255
-
DHQase I
-
-
DHQase-SORase
Q9SQT8
-
DHQD
Clostridium difficile
-
-
DHQD
Salmonella enterica LT2
P58687
-
-
DQD
Gluconobacter oxydans IFO 3244
-
;
-
mDQD
Gluconobacter oxydans IFO 3244
-
-
-
membrane-bound 3-dehydroquinate dehydratase
-
-
NtDHD/SHD-1
Q6PUF9
-
NtDHD/SHD-2
Q6PUG0
cytosolic isoenzyme
pDQD
-
periplasmic 3-dehydroquinate dehydratase
pDQD
Gluconobacter oxydans IFO 3244
-
periplasmic 3-dehydroquinate dehydratase
-
sDQD
-
soluble, cytoplasmic 3-dehydroquinate dehydratase
sDQD
Gluconobacter oxydans IFO 3244
-
soluble, cytoplasmic 3-dehydroquinate dehydratase
-
Type I dehydroquinase
-
-
-
-
type I dehydroquinate dehydratase
Clostridium difficile
-
-
type I dehydroquinate dehydratase
P58687
-
type I dehydroquinate dehydratase
Salmonella enterica LT2
P58687
-
-
Type I DHQase
-
-
-
-
type I DHQD
Clostridium difficile
-
-
type I DHQD
P58687
-
type I DHQD
Salmonella enterica LT2
P58687
-
-
Type II dehydroquinase
-
-
-
-
Type II dehydroquinase
-
-
Type II dehydroquinase
Q48255
-
Type II DHQase
-
-
-
-
membrane-bound 3-dehydroquinate dehydratase
Gluconobacter oxydans IFO 3244
-
-
-
additional information
Q6PUG0
cf. EC 1.1.1.25
CAS REGISTRY NUMBER
COMMENTARY
9012-66-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
formerly Haemophilus pleuropneumoniae
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
168
-
-
Manually annotated by BRENDA team
cultivar: Yabukia, Sayamamidor, Hatsumomiji, Boh
-
-
Manually annotated by BRENDA team
Clostridium difficile
-
-
-
Manually annotated by BRENDA team
pentafunctional AROM protein with activities of EC 1.1.1.25, EC 4.2.1.10, 5-dehydroquinate synthetase, 3-enolpyruvylshikimic acid 5-phosphate synthetase and shikimic acid kinase
-
-
Manually annotated by BRENDA team
strain WA53
-
-
Manually annotated by BRENDA team
type II dehydroquinase
-
-
Manually annotated by BRENDA team
Emericella nidulans WA53
strain WA53
-
-
Manually annotated by BRENDA team
mutant strain 170-27
-
-
Manually annotated by BRENDA team
strain AB2848/pKS201
-
-
Manually annotated by BRENDA team
type I dehydroquinase
-
-
Manually annotated by BRENDA team
Escherichia coli AB2848/pKS201
strain AB2848/pKS201
-
-
Manually annotated by BRENDA team
strain IFO 3244
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 3244
-
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 3244
strain IFO 3244
-
-
Manually annotated by BRENDA team
Hansenula henricii
-
-
-
Manually annotated by BRENDA team
dehydroquinase type II
-
-
Manually annotated by BRENDA team
dehydroquinase type II
-
-
Manually annotated by BRENDA team
dehydroquinase type II
UniProt
Manually annotated by BRENDA team
gene Rv2537c or aroD
UniProt
Manually annotated by BRENDA team
2 isoenzymes: the catabolic dehydroquinase is produced by the qa-2 gene and the biosynthetic dehydroquinase is produced by the constitutive aro cluster
-
-
Manually annotated by BRENDA team
type II dehydroquinase
-
-
Manually annotated by BRENDA team
wild type strain 74A, multienzyme complex with the activities of ec 1.1.1.25, ec 4.2.1.10, 5-dehydroquinate synthetase, 3-enolpyruvylshikimic acid 5-phosphate synthetase and shikimic acid kinase
-
-
Manually annotated by BRENDA team
cv. Samsun NN
Q6PUF9
SwissProt
Manually annotated by BRENDA team
cv. Samsun NN; DHD/SHD-2; cytosolic isozyme
SwissProt
Manually annotated by BRENDA team
no activity in Homo sapiens
-
-
-
Manually annotated by BRENDA team
bifunctional enzyme with activities of ec 1.1.1.25 and ec 4.2.1.10
-
-
Manually annotated by BRENDA team
bifunctional enzyme ec 4.2.1.10/ec 1.1.1.25
-
-
Manually annotated by BRENDA team
Saccharomycopsis lipolytica
-
-
-
Manually annotated by BRENDA team
Salmonella enterica LT2
-
UniProt
Manually annotated by BRENDA team
bifunctional enzyme ec 4.2.1.10/ec 1.1.1.25
-
-
Manually annotated by BRENDA team
dehydroquinase type II
-
-
Manually annotated by BRENDA team
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
KCl
-
facilitates mDQD enzyme purification/solubilization by detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside as a chaotropic agent
Mg2+
-
required
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9
-
pH 6.5: about 65% of maximal activity, pH 9.0: about 95% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-, O30011
calculated pI-value
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus subtilis (strain 168)
Bifidobacterium longum subsp. longum (strain JDM301)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Clostridium difficile (strain 630)
Clostridium difficile (strain 630)
Geobacillus kaustophilus (strain HTA426)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Salmonella typhi
Salmonella typhi
Salmonella typhi
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
reversible dissociation into inactive subunits
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
57
-
-
Tm: 57C, irreversible thermal denaturation
70
-
-
10 min, stable
70
-
-
10 min, not stable
82
-
-
irreversible thermal denaturation involves at least three transitions. The first is a broad shoulder at approximately 82C, the second is a shoarp doublet at 86C and the final transition occurs at 95C
additional information
-
-
extremly resistant to thermal denaturation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
guanidine hydrochloride, the type II enzyme from Aspergillus nidulans unfolds at concentrations of denaturant 4fold greater than type I enzyme from E. coli and through a series of discrete transitions, while the type I enzyme from E. coli unfolds in a single transition
-
extremly resistant to denaturation by urea and guanidine hydrochloride at 25C
-
irreversible inactivation by SDS and guanidine hydrochloride at 55C
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isozyme 3 is down-regulated (28%) at 4C
-
the expression of SVCR3 is not affected by light intensity alone up to 0.2 mM photon m-2 s-1 at temperatures higher than 10C, very little SVCR3 is expressed at 20C regardless of the light intensity
-
when combined with light (above 0.05 mM photon m-2 s-1) the expression of SVCR3 increases more at 4C. Isozymes 1 and 2 are up-regulated (38% and 24%, respectively) at 4C
-