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Literature summary for 1.1.1.34 extracted from

  • Bischoff, K.M.; Rodwell, V.W.
    3-Hydroxy-3-methylglutaryl-coenzyme A reductase of Haloferax volcanii: role of histidine 398 and attenuation of activity by introduction of negative charge at position 404 (1997), Protein Sci., 6, 156-161.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.34

Protein Variants

Protein Variants Comment Organism
H398Q low activity for catalysis of reductive deacylation of (S)-3-hydroxy-3-methylglutaryl-CoA or oxidative acylation of mevaldehyde, but readily catalyzed mevaldehyde reduction Haloferax volcanii
additional information mutant forms of the 403 residue Haloferax volcanii enzyme are constructed to model phosphorylation and infer whether attenuated activity involves interaction with His398. Chimeric Haloferax volcanii-hamster enzymes constructed in an effort to create an active, phosphorylatable chimeric enzyme are inactive or not phosphorylated. Asp is added at position 404 to mimic the introduction of negative charge that would accompany phosphorylation. Enzyme 404D/H398Q was inactive for reductive deacylation of (S)-3-hydroxy-3-methylglutaryl-CoA or oxidative acylation of mevaldehyde, but catalyzed reaction mevaldehyde reduction at 35% the wild-type rate. These observations are consistent with the model that attenuation of catalytic activity results from an ionic interaction between the imidazolium cation of His 398 and the carboxylate anion of Asp404 Haloferax volcanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.031
-
 (R)-mevaldehyde pH 7.3, 37°C, second step of the reaction, mutant enzyme 404N with Asp is added at position 404 Haloferax volcanii
0.032
-
 (R)-mevaldehyde pH 7.3, 37°C, second step of the reaction, wild-type enzyme Haloferax volcanii
0.06
-
 (S)-3-hydroxy-3-methylglutaryl-CoA pH 7.3, 37°C, first step of the reaction, wild-type enzyme Haloferax volcanii
0.066
-
 NADPH pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, wild-type enzyme Haloferax volcanii
0.068
-
 NADPH pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme 404D with Asp is added at position 404 Haloferax volcanii
0.068
-
 NADPH pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404 Haloferax volcanii
0.072
-
 NADPH pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme 404N with Asp is added at position 404 Haloferax volcanii
0.077
-
 (S)-3-hydroxy-3-methylglutaryl-CoA pH 7.3, 37°C, first step of the reaction, mutant enzyme 404N with Asp is added at position 404 Haloferax volcanii
0.083
-
 (S)-3-hydroxy-3-methylglutaryl-CoA pH 7.3, 37°C, first step of the reaction, mutant enzyme 404D with Asp is added at position 404 Haloferax volcanii
0.083
-
 (S)-3-hydroxy-3-methylglutaryl-CoA pH 7.3, 37°C, first step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404 Haloferax volcanii
0.084
-
 (R)-mevaldehyde pH 7.3, 37°C, second step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404 Haloferax volcanii
0.1
-
 (R)-mevaldehyde pH 7.3, 37°C, second step of the reaction, mutant enzyme H398Q Haloferax volcanii
0.177
-
 NADPH pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme H398Q Haloferax volcanii
0.2
-
 (S)-3-hydroxy-3-methylglutaryl-CoA pH 7.3, 37°C, first step of the reaction, mutant enzyme H398Q Haloferax volcanii
0.55
-
 NADPH pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, wild-type enzyme Haloferax volcanii
2.1
-
 NADPH pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404 Haloferax volcanii
3
-
 NADPH pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, mutant enzyme H398Q Haloferax volcanii
4.2
-
 NADPH pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, mutant enzyme 404N with Asp is added at position 404 Haloferax volcanii

Organism

Organism UniProt Comment Textmining
Haloferax volcanii Q59468
-
-
Haloferax volcanii DSM 3757 Q59468
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-mevaldehyde + NADPH + H+ second step of the reaction Haloferax volcanii (R)-mevalonate + NADP+
-
 ?
(R)-mevaldehyde + NADPH + H+ second step of the reaction Haloferax volcanii DSM 3757 (R)-mevalonate + NADP+
-
 ?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ overall reaction Haloferax volcanii (R)-mevalonate + CoA + 2 NADP+
-
 ?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ overall reaction Haloferax volcanii DSM 3757 (R)-mevalonate + CoA + 2 NADP+
-
 ?

Synonyms

Synonyms Comment Organism
3-hydroxy-3-methylglutaryl-coenzyme A reductase
-
 Haloferax volcanii
HMG-CoA reductase
-
 Haloferax volcanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Haloferax volcanii