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Information on EC 1.1.1.24 - quinate/shikimate dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.24
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.24 quinate/shikimate dehydrogenase (NAD+)
IUBMB Comments
The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.24
- crassa
-
neurospora
- dehydratase
- dehydroquinate
- dehydroshikimate
- qa
- nidulans
- gluconobacter
-
quinoproteins
- calcoaceticus
- 3-dehydroquinase
- protocatechuate
- carrot
showSynonyms
quinate dehydrogenase, quinate/shikimate dehydrogenase, cglqsdh, quinate 5-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cgl0424
CglQSDH
dehydrogenase, quinate
-
-
-
-
QDH
quinate 5-dehydrogenase
-
-
ambiguous
-
quinate dehydrogenase
quinate/shikimate dehydrogenase
quinate: oxidoreductase
-
-
-
-
quinate:NAD oxidoreductase
-
-
-
-
quinate:NAD+ 5-oxidoreductase
-
-
-
-
quinic dehydrogenase
-
-
ambiguous
-
additional information
-
the enzyme belongs to a functional class of the shikimate/quinate dehydrogenase family
quinate dehydrogenase
-
-
ambiguous
-
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
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
shikimate degradation II
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SYSTEMATIC NAME
IUBMB Comments
L-quinate:NAD+ 3-oxidoreductase
The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
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CAS REGISTRY NUMBER
COMMENTARY
9028-28-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
Substrates: low activity
Products: -
Products: -
r
shikimate + NAD+
5-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-dehydroquinate + NADH
quinate + NAD+
-
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: QDH plays a key role in the quinate-degradation pathway
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: Thr88 and Thr221 are involved in quinate binding
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: 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
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: 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
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
p-hydroxybenzoate + O2
protocatechuic acid + H2O
-
Substrates: overview substrate specificity, some strains are using the substrate, some are not
Products: -
Products: -
?
p-hydroxybenzoate + O2
protocatechuic acid + H2O
-
Substrates: overview substrate specificity, some strains are using the substrate, some are not
Products: -
Products: -
?
quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: first reaction in inducible quinic acid catabolic pathway
Products: -
Products: -
?
quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: overview substrate specificity, some strains are using the substrate, some are not
Products: -
Products: -
?
quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: 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
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
Substrates: 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
Products: -
Products: -
r
additional information
?
-
-
Substrates: addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the quinate and shikimate metabolism, regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme shows quinate and shikimate dehydrogenase activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: product analysis by GC-MS
Products: -
Products: -
?
additional information
?
-
Substrates: product analysis by GC-MS
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
5-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-dehydroquinate + NADH
quinate + NAD+
-
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: QDH plays a key role in the quinate-degradation pathway
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
p-hydroxybenzoate + O2
protocatechuic acid + H2O
-
Substrates: overview substrate specificity, some strains are using the substrate, some are not
Products: -
Products: -
?
p-hydroxybenzoate + O2
protocatechuic acid + H2O
-
Substrates: overview substrate specificity, some strains are using the substrate, some are not
Products: -
Products: -
?
quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: first reaction in inducible quinic acid catabolic pathway
Products: -
Products: -
?
quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
quinate + NAD+
5-dehydroquinate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
quinic acid + NAD(P)+
dehydroquinic acid + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: addition of either shikimate or quinate to the assay does not increase the reaction rate when the other substrate is present alone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the quinate and shikimate metabolism, regulation, overview
Products: -
Products: -
?
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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
-
erythrose 4-phosphate plus phosphoenolpyruvate increase quinate oxidizing activity by 25%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics
-
1.4
3-dehydroquinate
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
0.164
L-quinate
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
0.0537
NAD+
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
0.102
NADH
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
281
3-dehydroquinate
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
298
NADH
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
127
L-quinate
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
139
NAD+
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
200.7
3-dehydroquinate
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
2921.6
NADH
pH 7.5, 30°C, EcDQD/SDH4a, quinate formation
774.4
L-quinate
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
2588.5
NAD+
pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation
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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
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
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
-
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
-
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
additional information
comparison of EcDQD/SDH, UGT84A25a/b, and UGT84A26a/b expression patterns in Eucalyptus camaldulensis, relative EcDQD/SDH mRNA levels in the leaves, stems, and roots are plotted against the relative UGT84A25a/b and UGT84A26a/b mRNA levels in the same samples, and determination of concentrations of the metabolites in the different tissues, overview
brenda
additional information
comparison of EcDQD/SDH, UGT84A25a/b, and UGT84A26a/b expression patterns in Eucalyptus camaldulensis, relative EcDQD/SDH mRNA levels in the leaves, stems, and roots are plotted against the relative UGT84A25a/b and UGT84A26a/b mRNA levels in the same samples, and determination of concentrations of the metabolites in the different tissues, overview
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
evolution
plant SDH enzymes are fused to dehydroquinate dehydratases (DQDs, EC 4.2.1.10) to form bifunctional DQD/SDH enzymes. The DQD activity is observed for EcDQD/SDH1, 2, and 3, but not for EcDQD/SDH4a. Among the active enzymes, EcDQD/SDH1 exhibits the highest DQD activity, followed by EcDQD/SDH2 (about 50% of the EcDQD/SDH1 activity) and EcDQD/SDH3 (about 5% of the EcDQD/SDH1 activity). For shikimate formation from 3-DHS as well as shikimate oxidation to 3-DHS, measurable catalytic activities are detected for EcDQD/SDH1-3, but the activities of EcDQD/SDH2 and 3 are less than 20% of those of EcDQD/SDH1. Regarding the cofactor, EcDQD/SDH1-3 have a clear preference for NADPH/NADP+ over NADH/ NAD+. In contrast, EcDQD/SDH4a and b lack shikimate formation activity. For the reverse reaction, the conversion of shikimate to 3-DHS, EcDQD/SDH4a and b display low enzymatic activity with a preference for NAD+ as the cofactor. Both EcDQD/SDH2 and 3 exhibit relatively high gallate formation activity, in contrast to the low activity of EcDQD/SDH1. The preferred cofactor in this reaction is NADP+. The reversible quinate formation from 3-DHQ is catalyzed only by EcDQD/SDH4a/b, with NADH/NAD+ as the preferred cofactor. The reaction specificity of EcDQD/SDH4a confirms the sequence-based prediction that EcDQD/SDH4a is a functional QDH enzyme. This enzyme should be renamed EcQDHa and its closest relative, EcDQD/SDH4b, should be renamed EcQDHb. The EcDQD/SDH4a and EcDQD/SDH4b genes may represent allelic variants encoding enzymes with 99.2% amino acid identity
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
Show AA Sequence and Transmembrane Helices (225 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
-
recombinant GST-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by glutathione affinity chromatography and tag cleavage through thrombin
separation from NADP+-linked shikimate dehydrogenase, EC 1.1.1.25, gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene EcDQD/SDH4a, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL, quantitative real-time RT-PCR enzyme expression analysis
gene EcDQD/SDH4b, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL, quantitative real-time RT-PCR enzyme expression analysis
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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
Streptomyces sp., Pseudonocardia sp., Rhodococcus rhodochrous
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
Hppner, 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 (Q9X5C9), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q9X5C9)
brenda
Carrington, Y.; Guo, J.; Le, C.H.; Fillo, A.; Kwon, J.; Tran, L.T.; Ehlting, J.
Evolution of a secondary metabolic pathway from primary metabolism shikimate and quinate biosynthesis in plants
Plant J.
95
823-833
2018
Populus trichocarpa
brenda
Tahara, K.; Nishiguchi, M.; Funke, E.; Miyazawa, S.I.; Miyama, T.; Milkowski, C.
Dehydroquinate dehydratase/shikimate dehydrogenases involved in gallate biosynthesis of the aluminum-tolerant tree species Eucalyptus camaldulensis
Planta
253
3
2020
Eucalyptus camaldulensis (A0A5H2WXM2), Eucalyptus camaldulensis (A0A5H2X0F8)
brenda
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