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Literature summary for 1.1.1.88 extracted from

  • Darnay, B.G.; Wang, Y.; Rodwell, V.W.
    Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (1992), J. Biol. Chem., 267, 15064-15070.
    View publication on PubMed
Search for more literature for 1.1.1.88

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 Pseudomonas mevalonii

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type and mutants, H381A, H381N, H381K, H381Q, 3 A resolution Pseudomonas mevalonii

Protein Variants

Protein Variants Comment Organism
H381A 6% of wild-type activity Pseudomonas mevalonii
H381K 45% of wild-type activity at pH 11 Pseudomonas mevalonii
H381N 16% of wild-type activity Pseudomonas mevalonii
H381Q 23% of wild-type activity Pseudomonas mevalonii

General Stability

General Stability Organism
diethyl polycarbonate causes loss of activity Pseudomonas mevalonii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03
-
 CoASH H381A mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
0.05
-
 CoASH wild-type enzyme, oxidative acylation of mevalonate Pseudomonas mevalonii
0.11
-
 CoASH H381Q mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
0.14
-
 NAD+ H381A mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
0.2
-
 CoASH H381N mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
0.22
-
 NAD+ wild-type enzyme, oxidative acylation of mevalonate Pseudomonas mevalonii
0.27
-
 (R,S)-mevalonate H381A mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
0.45
-
 (R,S)-mevalonate wild-type enzyme, oxidative acylation of mevalonate Pseudomonas mevalonii
0.5
-
 CoASH H381K mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
0.62
-
 NAD+ H381Q mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
0.71
-
 (R,S)-mevalonate H381Q mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
0.75
-
 (R,S)-mevalonate H381K mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
0.81
-
 NAD+ H381N mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
1.23
-
 NAD+ H381K mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
3.7
-
 (R,S)-mevalonate H381N mutant, oxidative acylation of mevalonate Pseudomonas mevalonii

Organism

Organism UniProt Comment Textmining
Pseudomonas mevalonii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas mevalonii

Renatured (Commentary)

Renatured (Comment) Organism
after inactivation with diethyl polycarbonate addition of hydroxylamine restores 50% of activity Pseudomonas mevalonii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.011
-
 H381A-mutant, mevalonate acylation Pseudomonas mevalonii
0.029
-
 H381N-mutant, mevalonate acylation Pseudomonas mevalonii
0.041
-
 H381Q-mutant, mevalonate acylation Pseudomonas mevalonii
0.091
-
 H381K-mutant, mevalonate acylation Pseudomonas mevalonii
18
-
 mevalonate acylation pH 8.1 Pseudomonas mevalonii
20.3
-
 mevalonate acylation pH 11 Pseudomonas mevalonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-mevalonate + CoA + 2 NAD+
-
 Pseudomonas mevalonii (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
-
 ?
3-hydroxy-3-methylglutaryl-CoA + NADH + H+
-
 Pseudomonas mevalonii mevalonate + CoA + NAD+
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 oxidative acylation of mevalonate Pseudomonas mevalonii
9.5
-
 H381N mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
10
-
 H381A mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
10.5
-
 H381Q mutant, oxidative acylation of mevalonate Pseudomonas mevalonii
11
-
 H381K mutant, oxidative acylation of mevalonate Pseudomonas mevalonii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Pseudomonas mevalonii
NADH reverse reaction Pseudomonas mevalonii