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Information on EC 1.1.1.24 - quinate dehydrogenase
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1.1.1.24 quinate dehydrogenaseIUBMB Comments
The enzyme is specific for quinate as substrate; phenylpyruvate, phenylalanine, cinnamate and shikimate will not act as substrates. NAD+ cannot be replaced by NADP+.
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Word Map
- 1.1.1.24
- shikimate
- phosphoglycerate
- crassa
-
neurospora
- qa
- dehydroquinate
- dehydroshikimate
-
quinoproteins
- gluconobacter
- 3-dehydroquinase
- calcoaceticus
- d-3-phosphoglycerate
-
one-carbon
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cglqsdh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cgl0424
CglQSDH
dehydrogenase, quinate
-
-
-
-
QDH
quinate dehydrogenase
quinate/shikimate dehydrogenase
quinate: oxidoreductase
-
-
-
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quinate:NAD oxidoreductase
-
-
-
-
quinic dehydrogenase
-
-
-
-
additional information
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the enzyme belongs to a functional class of the shikimate/quinate dehydrogenase family
quinate dehydrogenase
-
-
-
-
quinate/shikimate dehydrogenase
the enzyme also shows activity with shikimate
quinate/shikimate dehydrogenase
the enzyme also shows activity with shikimate
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-quinate + NAD+ = 3-dehydroquinate + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
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-
-
-
reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
L-quinate:NAD+ 3-oxidoreductase
The enzyme is specific for quinate as substrate; phenylpyruvate, phenylalanine, cinnamate and shikimate will not act as substrates. NAD+ cannot be replaced by NADP+.
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CAS REGISTRY NUMBER
COMMENTARY
9028-28-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
QDH plays a key role in the quinate-degradation pathway
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-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Thr88 and Thr221 are involved in quinate binding
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-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme also shows activity with shikimate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent
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-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
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-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
the enzyme also shows activity with shikimate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent
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-
r
p-hydroxybenzoate + O2
protocatechuic acid + H2O
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overview substrate specificity, some strains are using the substrate, some are not
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p-hydroxybenzoate + O2
protocatechuic acid + H2O
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overview substrate specificity, some strains are using the substrate, some are not
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quinate + NAD+
5-dehydroquinate + NADH + H+
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first reaction in inducible quinic acid catabolic pathway
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-
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quinate + NAD+
5-dehydroquinate + NADH + H+
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overview substrate specificity, some strains are using the substrate, some are not
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-
?
shikimate + NAD+
3-dehydroshikimate + NADPH + H+
the enzyme also shows high activity with quinate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADPH + H+
the enzyme also shows high activity with quinate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent
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r
additional information
?
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addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
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additional information
?
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the enzyme is involved in the quinate and shikimate metabolism, regulation, overview
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additional information
?
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the bifunctional enzyme shows quinate and shikimate dehydrogenase activities
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additional information
?
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the bifunctional enzyme shows quinate and shikimate dehydrogenase activities, interconversion of 5-dehydroquinate and 5-dehydroshikimate by dehydroquinase, EC 4.2.1.10, favouring 5-dehydroshikimate formation
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additional information
?
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structure of the potential binding site of quinate and shikimate includign the the completely conserved residues Lys92 and Asp102, overview. The crystal structure reveals that in contrast to shikimate, quinate forms a hydrogen bond to the NAD+. In addition, the hydroxyl group of a conserved active-site threonine hydrogen binds to quinate more effectively than to shikimate. Also, the hydroxyl group of a conserved tyrosine approaches the carboxylate group of quinate more closely than it does the carboxylate group of shikimate, active site structure, overview
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
QDH plays a key role in the quinate-degradation pathway
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Q9X5C9
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Q9X5C9
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
-
-
r
p-hydroxybenzoate + O2
protocatechuic acid + H2O
-
overview substrate specificity, some strains are using the substrate, some are not
-
-
-
p-hydroxybenzoate + O2
protocatechuic acid + H2O
-
overview substrate specificity, some strains are using the substrate, some are not
-
-
-
quinate + NAD+
5-dehydroquinate + NADH + H+
-
first reaction in inducible quinic acid catabolic pathway
-
-
-
additional information
?
-
-
addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
-
-
-
additional information
?
-
-
the enzyme is involved in the quinate and shikimate metabolism, regulation, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
erythrose 4-phosphate
-
erythrose 4-phosphate plus phosphoenolpyruvate increase quinate oxidizing activity by 25%
phosphoenolpyruvate
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erythrose 4-phosphate plus phosphoenolpyruvate increase quinate oxidizing activity by 25%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
quinic acid
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purification step Q1 HiTrapQ, cofactor NAD+; purification step Q2 HiTrapQ, cofactor NADP+
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
quinate dehydrogenase activity is highest early in fruit development abd declines in older fruit
additional information
-
quinate dehydrogenase activity is highest early in fruit development abd declines in older fruit
additional information
-
quinate dehydrogenase activity is highest early in fruit development and declines in older fruit
additional information
-
activity in infection-resistant hypocotyls remains constant, enzyme activity in hypocotyls susceptible to infection decreases about 50%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; bifunctional enzyme: quinate (shikimate) dehydrogenase, different from EC 1.1.1.25
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
quinate dehydrogenase activity is at a maximum around the time of greatest quinic acid accumulation in the early stages (less than 60 days after anthesis) of fruit development. It declines markedly in late fruit development
brenda
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; quinate dehydrogenase activity is at a maximum around the time of greatest quinic acid accumulation in the early stages (less than 60 days after anthesis) of fruit development. It declines markedly in late fruit development, and is higher in species that accumulate the largest amounts of quinic acid (Actinidia chinensis and Actinidia deliciosa)
brenda
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quinate dehydrogenase activity is at a maximum around the time of greatest quinic acid accumulation in the early stages (less than 60 days after anthesis) of fruit development. It declines markedly in late fruit development, and is higher in species that accumulate the largest amounts of quinic acid (Actinidia chinensis and Actinidia deliciosa)
brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
DHQA_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
329
0
36090
Swiss-Prot
DHQA_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
339
0
37271
Swiss-Prot
AROE_COREF
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
284
0
29938
Swiss-Prot
AROE_CORGL
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
283
0
29697
Swiss-Prot
A0A0E0UQN5_SINMB
Sinorhizobium meliloti (strain BL225C)
286
0
30636
TrEMBL
F5XJN1_MICPN
Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1)
289
0
30754
TrEMBL
A0A0F8AZG7_CERFI
330
0
36526
TrEMBL
A2QJS5_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
307
0
34164
TrEMBL
A2QGL3_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
344
0
37159
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
-
1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
additional information
-
transfer of carrot enzyme from dark to light conditions shifts MW from 42000 Da to 110000 Da, probably due to association of a regulatory subunit which may be a calciprotein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 41000, SDS-PAGE in presence of urea or electrophoresis in presence of cetyltrimethyl ammonium bromide
additional information
-
seconfdary and tertiary enzyme structures, the enzyme is composed of two alphabetaalpha domains containing two discontinuous segments, Asp22-Asn127 and Gly287-Leu302, overview
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
NAD+-dependent enzyme, X-ray diffraction structure determination and anaylsis at 1.64-8.0 A resolution, molecular replacement method, modelling of the ternary complexes, overview
-
vapor diffusion sitting-drop method at 20°C. Atomic resolution crystal structures of the enzyme in different functional states: with bound NAD+ (binary complex) and as ternary complexes with NADH plus either shikimate or quinate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme knockout results in loss of the ability to grow on quinate and/or shikimate
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
half-life of unprotected enzyme: 20 min, 180 min in presence of NaCl, completely stable in presence of quinate, shikimate or NADH
47
-
inactivation, kinetics vary in presence of quinate or shikimate, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high ionic strength, such as 0.1 M (NH4)2SO4, NaCl or phosphate buffer or the presence of 0.1 M quinate or shikimate protects against thermal inactivation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
partial from young kiwifruit by extraction and chromatography on Superdex G75 and HiTrapQ columns
-
separation from NADP+-linked shikimate dehydrogenase, EC 1.1.1.25, gel filtration
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hawkins, A.R.; Moore, J.D.; Adeokun, A.M.
Characterization of the 3-dehydroquinase domain of the pentafunctional AROM protein, and the quinate dehydrogenase from Aspergillus nidulans, and the overproduction of the type II 3-dehydroquinase from Neurospora crassa
Biochem. J.
296
451-457
1993
Aspergillus nidulans
brenda
Barea, J.L.; Giles, N.H.
Purification and characterization of quinate (shikimate) dehydrogenase, an enzyme in the inducible quinic acid catabolic pathway of Neurospora crassa
Biochim. Biophys. Acta
524
1-14
1978
Neurospora crassa
brenda
Cain, R.B.
The identity of shikimate dehydrogenase and quinate dehydrogenase in Aspergillus niger
Biochem. J.
127
15P
1972
Aspergillus niger
brenda
Gamborg, O.L.
Aromatic metabolism in plants III. Quinate dehydrogenase from mung bean cell suspension cultures
Biochim. Biophys. Acta
128
483-491
1966
Vigna radiata var. radiata
-
brenda
Graziana, A.; Ranjeva, R.; Salimath, B.P.; Boudet, A.M.
The reversible association of quinate:NAD+ oxidoreductase from carrot cells with a putative regulatory subunit depends on light conditions
FEBS Lett.
163
306-311
1983
Daucus carota
-
brenda
Davies, B.D.; Gilvarg, C.; Mitsuhyshi, S.
Enzymes of aromatic biosynthesis C. quinic dehydrogenase from Aerobacter aerogenes
Methods Enzymol.
2
307-311
1955
Klebsiella aerogenes
-
brenda
Kang, X.; Neuhaus, E.; Scheibe, R.
Subcellular localization of quinate: oxidoreductase from Phaseolus mungo L. sprouts
Z. Naturforsch. C
49
415-420
1994
Vigna radiata var. radiata
-
brenda
Grund, E.; Kutzner, H.J.
Utilization of quinate and p-hydroxybenzoate by actinomycetes: key enzymes and taxonomic relevance
J. Basic Microbiol.
38
241-255
1998
Pseudonocardia sp., Rhodococcus rhodochrous, Streptomyces sp.
brenda
Ossipov, V.; Bonner, C.; Ossipova, S.; Jensen, R.
Broad-specificity quinate (shikimate) dehydrogenase from Pinus taeda needles
Plant Physiol.
38
923-928
2000
Daucus carota, Pinus taeda
-
brenda
Kang, X.; Scheibe, R.
Purification and characterization of the quinate: oxidoreductase from Phaseolus mungo sprouts
Phytochemistry
33
769-773
1993
Vigna radiata var. radiata
-
brenda
Shein, I.V.; Shibistova, O.B.; Zrazhevskaya, G.K.; Astrakhantseva, N.G.; Polyakova, G.G.
The content of phenolic compounds and the activity of key enzymes of their synthesis in Scots pine hypocotyls infected with Fusarium
Russ. J. Plant Physiol.
50
516-521
2003
Pinus sylvestris
-
brenda
Schoepe, J.; Niefind, K.; Schomburg, D.
1.6 A structure of an NAD(+)-dependent quinate dehydrogenase from Corynebacterium glutamicum
Acta Crystallogr. Sect. D
64
803-809
2008
Corynebacterium glutamicum
brenda
Cain, R.B.
Metabolism of shikimate and quinate by Aspergillus niger and its regulation
Biochem. J.
127
15P-16P
1972
Aspergillus niger
brenda
Marsh, K.; Boldingh, H.; Shilton, R.; Laing, W.
Changes in quinic acid metabolism during fruit development in three kiwifruit species
Funct. Plant Biol.
36
463-470
2009
Actinidia arguta, Actinidia arguta var. arguta, Actinidia chinensis, Actinidia deliciosa, Actinidia deliciosa var. deliciosa
brenda
Höppner, A.; Schomburg, D.; Niefind, K.
Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination
Biol. Chem.
394
1505-1516
2013
Corynebacterium glutamicum, Corynebacterium glutamicum (Q9X5C9), Corynebacterium glutamicum ATCC 13032 (Q9X5C9)
brenda
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