BRENDA - Enzyme Database
show all sequences of 1.1.1.282

Hydroaromatic metabolism in Rhodococcus rhodochrous: purification and characterization of its NAD-dependent quinate dehydrogenase

Bruce, N.C.; Cain, R.B.; Arch. Microbiol. 154, 179-186 (1990)
No PubMed abstract available

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.15
-
beta-NAD+
pH 10, cosubstrate (-)-quinate
Rhodococcus rhodochrous
0.48
-
nicotinamide hypoxanthine dinucleotide
pH 10, cosubstrate (-)-quinate
Rhodococcus rhodochrous
0.51
-
oxidized nicotinamide 1,N6-ethanoadenine dinucleotide
pH 10, cosubstrate (-)-quinate
Rhodococcus rhodochrous
0.65
-
3-acetylpyridine adenine dinucleotide
pH 10, cosubstrate (-)-quinate
Rhodococcus rhodochrous
2.47
-
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate
pH 10, (-)-enantiomer, cosubstrate NAD+
Rhodococcus rhodochrous
2.56
-
dihydroshikimate
pH 10, (-)-enantiomer, cosubstrate NAD+
Rhodococcus rhodochrous
2.95
-
L-quinate
pH 10, (-)-enantiomer, cosubstrate NAD+
Rhodococcus rhodochrous
5.25
-
shikimate
pH 10, (-)-enantiomer, cosubstrate NAD+
Rhodococcus rhodochrous
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
31500
-
1 * 31500, SDS-PAGE
Rhodococcus rhodochrous
44000
-
gel filtration
Rhodococcus rhodochrous
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Rhodococcus rhodochrous
initial enzyme of the hydroaromatic pathway
?
-
-
?
additional information
Rhodococcus rhodochrous N75
initial enzyme of the hydroaromatic pathway
?
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Rhodococcus rhodochrous
-
-
-
Rhodococcus rhodochrous N75
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
188fold
Rhodococcus rhodochrous
Reaction
Reaction
Commentary
Organism
Reaction ID
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
stereospecificity
Rhodococcus rhodochrous
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+
stereospecificity
Rhodococcus rhodochrous
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Rhodococcus rhodochrous
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
dihydroshikimate + NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, 38% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
(-)-enantiomer, reverse reaction: 3.3fold higher activity than with (-)-3-dehydroquinate
-
-
r
dihydroshikimate + NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, 38% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous N75
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
(-)-enantiomer, reverse reaction: 3.3fold higher activity than with (-)-3-dehydroquinate
-
-
r
L-quinate + 3-acetylpyridine adenine dinucleotide
67% of the activity with NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + ?
-
-
-
?
L-quinate + 3-acetylpyridine adenine dinucleotide
67% of the activity with NAD+
654384
Rhodococcus rhodochrous N75
3-dehydroquinate + ?
-
-
-
?
L-quinate + beta-NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity
654384
Rhodococcus rhodochrous
3-dehydroquinate + beta-NADH + H+
(-)-enantiomer, reverse reaction: lower activity than with t-4,c-5-dihydroxy-3-oxocyclohexane-c-1-carboxylate or 4-hydroxy-3-oxocyclohexane-c-1-carboxylate
-
-
r
L-quinate + beta-NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity
654384
Rhodococcus rhodochrous N75
3-dehydroquinate + beta-NADH + H+
(-)-enantiomer, reverse reaction: lower activity than with t-4,c-5-dihydroxy-3-oxocyclohexane-c-1-carboxylate or 4-hydroxy-3-oxocyclohexane-c-1-carboxylate
-
-
r
L-quinate + NADP+
0.3% of the activity with NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + NADPH + H+
-
-
-
?
L-quinate + nicotinamide 1,N6-ethenoadenine dinucleotide
69% of the activity with NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + ?
-
-
-
?
L-quinate + nicotinamide hypoxanthine dinucleotide
1.3fold higher activity than with NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + ?
-
-
-
?
L-quinate + oxidized nicotinamide 1,N6-ethanoadenine dinucleotide
69% activity compared to NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + reduced nicotinamide 1,N6-ethanoadenine dinucleotide
-
-
-
r
additional information
initial enzyme of the hydroaromatic pathway
654384
Rhodococcus rhodochrous
?
-
-
-
?
additional information
substrate specificity, enzyme is highly stereospecific with regard to hydroaromatic substrates, oxidizing only the axial hydroxyl group at C-3 of (-)-enantiomer of quinate, shikimate, dihydroshikimate and t-3,t-4-dihydroxycyclohexane-c-1-carboxylate, enzyme shows activity with several NAD+ analogues, reverse reaction: not 4-hydroxy-3-oxocyclohex-4-ene-c-1-carboxylate, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
654384
Rhodococcus rhodochrous
?
-
-
-
?
additional information
initial enzyme of the hydroaromatic pathway
654384
Rhodococcus rhodochrous N75
?
-
-
-
?
additional information
substrate specificity, enzyme is highly stereospecific with regard to hydroaromatic substrates, oxidizing only the axial hydroxyl group at C-3 of (-)-enantiomer of quinate, shikimate, dihydroshikimate and t-3,t-4-dihydroxycyclohexane-c-1-carboxylate, enzyme shows activity with several NAD+ analogues, reverse reaction: not 4-hydroxy-3-oxocyclohex-4-ene-c-1-carboxylate, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
654384
Rhodococcus rhodochrous N75
?
-
-
-
?
shikimate + NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity, 72% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous
3-dehydroshikimate + NADH + H+
(-)-enantiomer, reverse reaction: 15% of the activity with (-)-3-dehydroquinate
-
-
r
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate + NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, 44% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous
4-hydroxy-3-oxocyclohexane-c-1-carboxylate + NADH + H+
(-)-isomer, reverse reaction: 2.2fold higher activity than with (-)-3-dehydroquinate
-
-
r
t-3-hydroxy-4-oxocyclohexane-c-1-carboxylate + NAD+
6% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 31500, SDS-PAGE
Rhodococcus rhodochrous
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
45
-
t1/2: 1.85 min
Rhodococcus rhodochrous
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
reduction reaction, assay at
Rhodococcus rhodochrous
10
-
oxidation reaction, quinate or shikimate as substrates, 50 mM glycine-KOH
Rhodococcus rhodochrous
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7
8.5
the rate of activity decreases more rapidly, maximal 25% at pH 7.5, at pH values from 8.5 to 7 when shikimate rather than quinate is used as substrate
Rhodococcus rhodochrous
Cofactor
Cofactor
Commentary
Organism
Structure
3-acetylpyridine adenine dinucleotide
67% of the activity with NAD+
Rhodococcus rhodochrous
additional information
absolute requirement for a nicotinamide nucleotide cofactor for the oxidation of quinate or shikimate, cofactor specificity, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
Rhodococcus rhodochrous
NAD+
-
Rhodococcus rhodochrous
NADH
-
Rhodococcus rhodochrous
NADP+
0.3% of the activity with NAD+
Rhodococcus rhodochrous
nicotinamide 1,N6-ethenoadenine dinucleotide
69% of the activity with NAD+
Rhodococcus rhodochrous
nicotinamide hypoxanthine dinucleotide
1.3fold higher activity than with NAD+
Rhodococcus rhodochrous
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
3-acetylpyridine adenine dinucleotide
67% of the activity with NAD+
Rhodococcus rhodochrous
additional information
absolute requirement for a nicotinamide nucleotide cofactor for the oxidation of quinate or shikimate, cofactor specificity, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
Rhodococcus rhodochrous
NAD+
-
Rhodococcus rhodochrous
NADH
-
Rhodococcus rhodochrous
NADP+
0.3% of the activity with NAD+
Rhodococcus rhodochrous
nicotinamide 1,N6-ethenoadenine dinucleotide
69% of the activity with NAD+
Rhodococcus rhodochrous
nicotinamide hypoxanthine dinucleotide
1.3fold higher activity than with NAD+
Rhodococcus rhodochrous
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.15
-
beta-NAD+
pH 10, cosubstrate (-)-quinate
Rhodococcus rhodochrous
0.48
-
nicotinamide hypoxanthine dinucleotide
pH 10, cosubstrate (-)-quinate
Rhodococcus rhodochrous
0.51
-
oxidized nicotinamide 1,N6-ethanoadenine dinucleotide
pH 10, cosubstrate (-)-quinate
Rhodococcus rhodochrous
0.65
-
3-acetylpyridine adenine dinucleotide
pH 10, cosubstrate (-)-quinate
Rhodococcus rhodochrous
2.47
-
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate
pH 10, (-)-enantiomer, cosubstrate NAD+
Rhodococcus rhodochrous
2.56
-
dihydroshikimate
pH 10, (-)-enantiomer, cosubstrate NAD+
Rhodococcus rhodochrous
2.95
-
L-quinate
pH 10, (-)-enantiomer, cosubstrate NAD+
Rhodococcus rhodochrous
5.25
-
shikimate
pH 10, (-)-enantiomer, cosubstrate NAD+
Rhodococcus rhodochrous
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
31500
-
1 * 31500, SDS-PAGE
Rhodococcus rhodochrous
44000
-
gel filtration
Rhodococcus rhodochrous
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Rhodococcus rhodochrous
initial enzyme of the hydroaromatic pathway
?
-
-
?
additional information
Rhodococcus rhodochrous N75
initial enzyme of the hydroaromatic pathway
?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
188fold
Rhodococcus rhodochrous
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Rhodococcus rhodochrous
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
dihydroshikimate + NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, 38% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
(-)-enantiomer, reverse reaction: 3.3fold higher activity than with (-)-3-dehydroquinate
-
-
r
dihydroshikimate + NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, 38% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous N75
(1S,3R,4S)-3,4-dihydroxy-5-oxocyclohexanecarboxylic acid + NADH + H+
(-)-enantiomer, reverse reaction: 3.3fold higher activity than with (-)-3-dehydroquinate
-
-
r
L-quinate + 3-acetylpyridine adenine dinucleotide
67% of the activity with NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + ?
-
-
-
?
L-quinate + 3-acetylpyridine adenine dinucleotide
67% of the activity with NAD+
654384
Rhodococcus rhodochrous N75
3-dehydroquinate + ?
-
-
-
?
L-quinate + beta-NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity
654384
Rhodococcus rhodochrous
3-dehydroquinate + beta-NADH + H+
(-)-enantiomer, reverse reaction: lower activity than with t-4,c-5-dihydroxy-3-oxocyclohexane-c-1-carboxylate or 4-hydroxy-3-oxocyclohexane-c-1-carboxylate
-
-
r
L-quinate + beta-NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity
654384
Rhodococcus rhodochrous N75
3-dehydroquinate + beta-NADH + H+
(-)-enantiomer, reverse reaction: lower activity than with t-4,c-5-dihydroxy-3-oxocyclohexane-c-1-carboxylate or 4-hydroxy-3-oxocyclohexane-c-1-carboxylate
-
-
r
L-quinate + NADP+
0.3% of the activity with NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + NADPH + H+
-
-
-
?
L-quinate + nicotinamide 1,N6-ethenoadenine dinucleotide
69% of the activity with NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + ?
-
-
-
?
L-quinate + nicotinamide hypoxanthine dinucleotide
1.3fold higher activity than with NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + ?
-
-
-
?
L-quinate + oxidized nicotinamide 1,N6-ethanoadenine dinucleotide
69% activity compared to NAD+
654384
Rhodococcus rhodochrous
3-dehydroquinate + reduced nicotinamide 1,N6-ethanoadenine dinucleotide
-
-
-
r
additional information
initial enzyme of the hydroaromatic pathway
654384
Rhodococcus rhodochrous
?
-
-
-
?
additional information
substrate specificity, enzyme is highly stereospecific with regard to hydroaromatic substrates, oxidizing only the axial hydroxyl group at C-3 of (-)-enantiomer of quinate, shikimate, dihydroshikimate and t-3,t-4-dihydroxycyclohexane-c-1-carboxylate, enzyme shows activity with several NAD+ analogues, reverse reaction: not 4-hydroxy-3-oxocyclohex-4-ene-c-1-carboxylate, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
654384
Rhodococcus rhodochrous
?
-
-
-
?
additional information
initial enzyme of the hydroaromatic pathway
654384
Rhodococcus rhodochrous N75
?
-
-
-
?
additional information
substrate specificity, enzyme is highly stereospecific with regard to hydroaromatic substrates, oxidizing only the axial hydroxyl group at C-3 of (-)-enantiomer of quinate, shikimate, dihydroshikimate and t-3,t-4-dihydroxycyclohexane-c-1-carboxylate, enzyme shows activity with several NAD+ analogues, reverse reaction: not 4-hydroxy-3-oxocyclohex-4-ene-c-1-carboxylate, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
654384
Rhodococcus rhodochrous N75
?
-
-
-
?
shikimate + NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, a single enzyme with both quinate and shikimate dehydrogenase activity, 72% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous
3-dehydroshikimate + NADH + H+
(-)-enantiomer, reverse reaction: 15% of the activity with (-)-3-dehydroquinate
-
-
r
t-3,t-4-dihydroxycyclohexane-c-1-carboxylate + NAD+
highly stereospecific with regard to hydroaromatic substrates, oxidizes only the axial hydroxyl group at C-3 of the (-)-enantiomer, 44% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous
4-hydroxy-3-oxocyclohexane-c-1-carboxylate + NADH + H+
(-)-isomer, reverse reaction: 2.2fold higher activity than with (-)-3-dehydroquinate
-
-
r
t-3-hydroxy-4-oxocyclohexane-c-1-carboxylate + NAD+
6% of the activity with (-)-quinate
654384
Rhodococcus rhodochrous
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 31500, SDS-PAGE
Rhodococcus rhodochrous
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
45
-
t1/2: 1.85 min
Rhodococcus rhodochrous
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
reduction reaction, assay at
Rhodococcus rhodochrous
10
-
oxidation reaction, quinate or shikimate as substrates, 50 mM glycine-KOH
Rhodococcus rhodochrous
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7
8.5
the rate of activity decreases more rapidly, maximal 25% at pH 7.5, at pH values from 8.5 to 7 when shikimate rather than quinate is used as substrate
Rhodococcus rhodochrous
Other publictions for EC 1.1.1.282
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740881
Garcia
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1
2
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5
-
-
-
3
-
-
-
1
-
7
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-
3
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1
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1
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5
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