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Literature summary for 4.1.3.4 extracted from

  • Narasimhan, C.; Roberts, J.R.; Miziorko, H.M.
    Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl-CoA lyase: testing the function of the active site cysteine by site-directed mutation (1995), Biochemistry, 34, 9930-9935.
    View publication on PubMed
Search for more literature for 4.1.3.4

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Pseudomonas mevalonii

Inhibitors

Inhibitors Comment Organism Structure
2-butynoyl-CoA active-site inhibition, only recombinant wild-type, not C237 mutants, indication of active-site directed mutagenesis Pseudomonas mevalonii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 hydroxymethylglutaryl-CoA wild-type Pseudomonas mevalonii
0.053
-
 hydroxymethylglutaryl-CoA C237A mutant Pseudomonas mevalonii

Organism

Organism UniProt Comment Textmining
Pseudomonas mevalonii
-
 recombinant wild-type enzyme and C237 mutants
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas mevalonii

Reaction

Reaction Comment Organism Reaction ID
(S)-3-Hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate C237 is crucial for catalysis Pseudomonas mevalonii
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0018 0.11 C237 mutants Pseudomonas mevalonii
80
-
 wild-type Pseudomonas mevalonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxy-3-methylglutaryl-CoA
-
 Pseudomonas mevalonii acetoacetate + acetyl-CoA
-
 ?