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Literature summary for 1.1.1.282 extracted from

  • Bruce, N.C.; Cain, R.B.
    Hydroaromatic metabolism in Rhodococcus rhodochrous: purification and characterization of its NAD-dependent quinate dehydrogenase (1990), Arch. Microbiol., 154, 179-186.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment 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] Comment Organism
31500
-
1 * 31500, SDS-PAGE Rhodococcus rhodochrous
44000
-
gel filtration Rhodococcus rhodochrous

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rhodococcus rhodochrous initial enzyme of the hydroaromatic pathway ?
-
?
additional information Rhodococcus rhodochrous N75 initial enzyme of the hydroaromatic pathway ?
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus rhodochrous
-
-
-
Rhodococcus rhodochrous N75
-
-
-

Purification (Commentary)

Purification (Comment) Organism
188fold Rhodococcus rhodochrous

Reaction

Reaction Comment 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 [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
additional information
-
-
Rhodococcus rhodochrous

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 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 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+ Rhodococcus rhodochrous 3-dehydroquinate + ?
-
?
L-quinate + 3-acetylpyridine adenine dinucleotide 67% of the activity with NAD+ 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 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 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+ Rhodococcus rhodochrous 3-dehydroquinate + NADPH + H+
-
?
L-quinate + nicotinamide 1,N6-ethenoadenine dinucleotide 69% of the activity with NAD+ Rhodococcus rhodochrous 3-dehydroquinate + ?
-
?
L-quinate + nicotinamide hypoxanthine dinucleotide 1.3fold higher activity than with NAD+ Rhodococcus rhodochrous 3-dehydroquinate + ?
-
?
L-quinate + oxidized nicotinamide 1,N6-ethanoadenine dinucleotide 69% activity compared to NAD+ Rhodococcus rhodochrous 3-dehydroquinate + reduced nicotinamide 1,N6-ethanoadenine dinucleotide
-
r
additional information initial enzyme of the hydroaromatic pathway 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 Rhodococcus rhodochrous ?
-
?
additional information initial enzyme of the hydroaromatic pathway 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 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 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 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 Rhodococcus rhodochrous ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 31500, SDS-PAGE Rhodococcus rhodochrous

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
45
-
t1/2: 1.85 min Rhodococcus rhodochrous

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment 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 Comment 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 Comment 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