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

BRENDA support

Literature summary for 6.4.1.4 extracted from

  • Sloane, V.; Waldrop, G.L.
    Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: Evidence for cooperativity in biotin carboxylase (2004), J. Biol. Chem., 279, 15772-15778.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
M169K mutant with lack of carboxylation activity Escherichia coli
R338Q mutant with lack of carboxylation activity Escherichia coli
R338S mutant with lack of carboxylation activity Escherichia coli
R385S human mutant leading to methylcrotonylglycinuria Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.081
-
ATP
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + acetyl-CoA + HCO3- Escherichia coli
-
ADP + malonyl-CoA + phosphate
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetyl-CoA + HCO3-
-
Escherichia coli ADP + malonyl-CoA + phosphate
-
r

Subunits

Subunits Comment Organism
homodimer alphabeta Escherichia coli

Synonyms

Synonyms Comment Organism
MCC
-
Escherichia coli