Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.4.1.5 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 6.4.1.5

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information GCCase shows sigmoidal kinetic behavior for geranoyl-CoA and bicarbonate but shows Michaelis-Menten kinetics for 3-methylcrotonyl-CoA and the cosubstrate ATP. The apparent K0.5 values of GCCase are 8.8 microM and 1.2 microM for geranoyl-CoA and bicarbonate, respectively Pseudomonas aeruginosa
0.01
-
 ATP pH 8.5, 37°C Pseudomonas aeruginosa
0.014
-
 3-methylcrotonyl-CoA pH 8.5, 37°C Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63000
-
 x * 74000, biotinylated subunit AtuF, x * 63000, subunit AtuC Pseudomonas aeruginosa
74000
-
 x * 74000, biotinylated subunit AtuF, x * 63000, subunit AtuC Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas aeruginosa the enzymatic properties suggest that geranoyl-CoA carboxylase may substitute for 3-methylcrotonyl-CoA carboxylase in leucine catabolism and that both enzymes play important roles in the leucine and acyclic terpene catabolic pathways ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
reconstitution of functional enzyme after coexpression and copurification of the subunit genes AtuC and AtuF Pseudomonas aeruginosa

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of functional enzyme after coexpression and copurification of the subunit genes AtuC and AtuF Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-methylcrotonyl-CoA + HCO3- geranoyl-CoA is preferred over 3-methylcrotonyl-CoA as substrate Pseudomonas aeruginosa ADP + phosphate + 3-methylglutaconyl-CoA
-
 ?
ATP + geranoyl-CoA + HCO3- geranoyl-CoA is preferred over 3-methylcrotonyl-CoA as substrate Pseudomonas aeruginosa ADP + phosphate + 3-(4-methylpent-3-en-1-yl)pent-2-enedioyl-CoA
-
 ?
additional information the enzymatic properties suggest that geranoyl-CoA carboxylase may substitute for 3-methylcrotonyl-CoA carboxylase in leucine catabolism and that both enzymes play important roles in the leucine and acyclic terpene catabolic pathways Pseudomonas aeruginosa ?
-
 ?

Subunits

Subunits Comment Organism
? x * 74000, biotinylated subunit AtuF, x * 63000, subunit AtuC Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Pseudomonas aeruginosa