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Literature summary for 6.4.1.4 extracted from

  • Diez, T.A.; Wurtele, E.S.; Nikolau, B.J.
    Purification and characterization of 3-methylcrotonyl-coenzyme-A carboxylase from leaves of Zea mays (1994), Arch. Biochem. Biophys., 310, 64-75.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
(E)-2-methyl-2-butenoyl-CoA weak Zea mays
acetoacetyl-CoA
-
Zea mays
ATP
-
Zea mays
butanoyl-CoA weak Zea mays
isobutanoyl-CoA weak Zea mays
Li+ slight inhibition Zea mays
n-hexanoyl-CoA weak Zea mays
Na+ slight inhibition Zea mays
p-hydroxymercuribenzoate
-
Zea mays
pentanoyl-CoA weak Zea mays
Phenylglyoxal 3-methylcrotonoyl-CoA or ATP protects Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
3-methylcrotonoyl-CoA
-
Zea mays
0.02
-
ATP
-
Zea mays
0.11
-
crotonoyl-CoA
-
Zea mays
0.8
-
HCO3-
-
Zea mays

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates with 57% of the efficiency relative to Mg2+ Zea mays
Cs+ monovalent cations activate, K+, Cs+, Rb+ or NH4+ Zea mays
K+ monovalent cations activate, K+, Cs+, Rb+ or NH4+ Zea mays
Mg2+ maximal activity at 2 mM Mg2+, at ATP concentrations 0.025 mM, 0.05 mM or 1 mM Zea mays
Mg2+ divalent cation required, Mg2+ is the best activator Zea mays
Mn2+ activates with 77% of the efficiency relative to Mg2+ Zea mays
NH4+ monovalent cations activate, K+, Cs+, Rb+ or NH4+ Zea mays
Rb+ monovalent cations activate, K+, Cs+, Rb+ or NH4+. Maximal activity obtained with Rb+ Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58500
-
6 * 58500 + 6 * 80000, SDS-PAGE Zea mays
80000
-
6 * 58500 + 6 * 80000, SDS-PAGE Zea mays
835000
-
PAGE, gel filtration Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Zea mays

Reaction

Reaction Comment Organism Reaction ID
ATP + 3-methylcrotonoyl-CoA + HCO3- + H+ = ADP + phosphate + 3-methylglutaconyl-CoA ATP and HCO3- bind sequentially to the enzyme. ATP and 3-methylcrotonoyl-CoA bind in ping-pong fashion Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.206
-
-
Zea mays

Storage Stability

Storage Stability Organism
-20°C, for at least 3 months without loss of activity Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-methylcrotonoyl-CoA + HCO3-
-
Zea mays ADP + phosphate + 3-methylglutaconyl-CoA
-
?
ATP + acetoacetyl-CoA + HCO3- acetoacetyl-CoA inhibits, no activity as substrate Zea mays ?
-
?
ATP + crotonoyl-CoA + HCO3-
-
Zea mays ?
-
?

Subunits

Subunits Comment Organism
dodecamer 6 * 58500 + 6 * 80000, SDS-PAGE Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Zea mays

pH Range

pH Minimum pH Maximum Comment Organism
6.8 10.1 6.8: more than 70% of maximal activity, 9.5: more than 70% of maximal activity, 10.1: 33% of maximal activity Zea mays