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Literature summary for 6.4.1.4 extracted from

  • Aguilar, J.A.; Diaz-Perez, C.; Diaz-Perez, A.L.; Rodriguez-Zavala, J.S.; Nikolau, B.J.; Campos-Garcia, J.
    Substrate specificity of the 3-methylcrotonyl coenzyme A (CoA) and geranyl-CoA carboxylases from Pseudomonas aeruginosa (2008), J. Bacteriol., 190, 4888-4893.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.4.1.4

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged MCCase in Escherichia coli strain BL21 Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information MCCase activity shows sigmoidal kinetics for all the substrates and non-Michaelis-Menten kinetics, overview Pseudomonas aeruginosa
0.0008
-
 HCO3- pH 8.0, 30°C, recombinant methylcrotonyl-CoA carboxylase Pseudomonas aeruginosa
0.0098
-
 3-methylcrotonoyl-CoA pH 8.0, 30°C, recombinant methylcrotonyl-CoA carboxylase Pseudomonas aeruginosa
0.01
-
 ATP pH 8.0, 30°C, recombinant geranyl-CoA carboxylase Pseudomonas aeruginosa
0.013
-
 ATP pH 8.0, 30°C, recombinant methylcrotonyl-CoA carboxylase Pseudomonas aeruginosa
0.014
-
 3-methylcrotonoyl-CoA pH 8.0, 30°C, recombinant geranyl-CoA carboxylase Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 3-methylcrotonoyl-CoA + HCO3- Pseudomonas aeruginosa
-
 ADP + phosphate + 3-methylglutaconyl-CoA
-
 ?
additional information Pseudomonas aeruginosa geranyl-CoA carboxylase, GCCase, may substitute for MCCase in leucine catabolism, both the MCCase and GCCase enzymes play important roles in the leucine and acyclic terpene catabolic pathways, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged MCCase from Escherichia coli strain BL21 by avidin affinity chromatography Pseudomonas aeruginosa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-methylcrotonoyl-CoA + HCO3-
-
 Pseudomonas aeruginosa ADP + phosphate + 3-methylglutaconyl-CoA
-
 ?
ATP + 3-methylcrotonoyl-CoA + HCO3- substrate of MCCase, EC 6.4.1.4, and GCCAse, EC 6.4.1.5 Pseudomonas aeruginosa ADP + phosphate + 3-methylglutaconyl-CoA
-
 ?
additional information geranyl-CoA carboxylase, GCCase, may substitute for MCCase in leucine catabolism, both the MCCase and GCCase enzymes play important roles in the leucine and acyclic terpene catabolic pathways, overview Pseudomonas aeruginosa ?
-
 ?
additional information MCCase shows no activity with geranyl-CoA, while the geranyl-CoA carboxylase, EC 6.4.1.5, is also active with 3-methylcrotonoyl-CoA in addition to the preferred substrate geranyl-CoA Pseudomonas aeruginosa ?
-
 ?

Synonyms

Synonyms Comment Organism
3-methylcrotonyl coenzyme A carboxylase
-
 Pseudomonas aeruginosa
MC-CoA carboxylase
-
 Pseudomonas aeruginosa
MCCase
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 native and recombinant enzyme Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 native and recombinant enzyme Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Pseudomonas aeruginosa