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Literature summary for 6.3.4.14 extracted from

  • Bordelon, T.; Nilsson Lill, S.; Waldrop, G.
    The utility of molecular dynamics simulations for understanding site-directed mutagenesis of glycine residues in biotin carboxylase (2009), Proteins Struct. Funct. Bioinform., 74, 808-819.
    View publication on PubMed
Search for more literature for 6.3.4.14

Crystallization (Commentary)

Crystallization (Comment) Organism
in absence and presence of ATP. Upon ATP binding, the central B-domain closes. Residues G165 and G166 play a role in ATP binding Escherichia coli

Protein Variants

Protein Variants Comment Organism
G165V the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold Escherichia coli
G165V/G166V the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold Escherichia coli
G166V the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.5
-
 HCO3- mutant G165V/G166V, pH 8.0, 25°C Escherichia coli
0.8
-
 HCO3- mutant G166V, pH 8.0, 25°C Escherichia coli
1.7
-
 HCO3- mutant G165V, pH 8.0, 25°C Escherichia coli
3.3
-
 ATP mutant G165V, pH 8.0, 25°C Escherichia coli
3.4
-
 ATP mutant G166V, pH 8.0, 25°C Escherichia coli
3.8
-
 ATP mutant G165V/G166V, pH 8.0, 25°C Escherichia coli
186
-
 biotin mutant G166V, pH 8.0, 25°C Escherichia coli
256
-
 biotin mutant G165V, pH 8.0, 25°C Escherichia coli
321
-
 biotin mutant G165V/G166V, pH 8.0, 25°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + HCO3-
-
 Escherichia coli ADP + phosphate + carboxybiotin
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0016
-
 HCO3- mutant G165V/G166V, pH 8.0, 25°C Escherichia coli
0.0016
-
 HCO3- mutant G166V, pH 8.0, 25°C Escherichia coli
0.0025
-
 HCO3- mutant G165V, pH 8.0, 25°C Escherichia coli
0.0037
-
 biotin mutant G166V, pH 8.0, 25°C Escherichia coli
0.005
-
 biotin mutant G165V, pH 8.0, 25°C Escherichia coli
0.007
-
 biotin mutant G165V/G166V, pH 8.0, 25°C Escherichia coli