Cloned (Comment) | Organism |
---|---|
BCMO gene, DNA and mino acid sequence determination and analysis, expression in Escherichia coli strain ER2566 | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
K108F | site-directed mutagenesis, the mutant shows highly decreased affinity for substrates with ionone rings at both ends, such as alpha-carotene, beta-carotene, and beta-cryptoxanthin, and a 7.2fold increased Km for beta-carotene compared to the wild-type enzyme. But the mutation has little effect on the affinity of the enzyme for substrates with one ionone ring and one open-chain end, such as beta-apo-4'-carotenal and beta-apo-8'-carotenal | Homo sapiens |
K108L | site-directed mutagenesis, the mutant shows highly decreased affinity for substrates with ionone rings at both ends, such as alpha-carotene, beta-carotene, and beta-cryptoxanthin, and a 2.9fold increased Km for beta-carotene compared to the wild-type enzyme. But the mutation has little effect on the affinity of the enzyme for substrates with one ionone ring and one open-chain end, such as beta-apo-4'-carotenal and beta-apo-8'-carotenal | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics of wild-type enzyme and mutants K108L and K108F with beta-carotene and beta-apo-8'-carotenal, overview | Homo sapiens | |
0.03 | - |
beta-carotene | pH 8.0, 37°C, recombinant wild-type enzyme | Homo sapiens | |
0.088 | - |
beta-carotene | pH 8.0, 37°C, recombinant mutant K108L | Homo sapiens | |
0.215 | - |
beta-carotene | pH 8.0, 37°C, recombinant mutant K108F | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-carotene + O2 | Homo sapiens | - |
2 retinal | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9HAY6 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli by affinity and anion exchange chromatography | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-carotene + O2 | - |
Homo sapiens | 2 retinal | - |
? | |
beta-carotene + O2 | substrate binding structure, overview | Homo sapiens | 2 retinal | - |
? | |
beta-cryptoxanthin + O2 | - |
Homo sapiens | ? | - |
? | |
additional information | BCMO is also active with alpha-carotene, beta-apo-8'-carotenal, and beta-apo-4'-carotenal. The hydrophobicity of residue 108 specifically affects the affinity of beta-carotene 15,15'-monooxygenase for substrates with two ionone rings. Residue 108 may be related to the indirect interaction with the second ionone ring of the substrates with two ionone rings, comparison with apo-carotenoid 15,15'-oxygenase, EC 1.14.99.41, overview | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | BCMO three-dimensional structure, with entrance of active tunnel and the hydrophobic patch, including Pro101, Cys102, Ile105, Phe106, Lys108, Leu258, Thr262, and Tyr264, modelling, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
BCMO | - |
Homo sapiens |
beta-carotene 15,15-monooxygenase | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0395 | - |
beta-carotene | pH 8.0, 37°C, recombinant mutant K108L | Homo sapiens | |
0.04 | - |
beta-carotene | pH 8.0, 37°C, recombinant mutant K108F | Homo sapiens | |
0.046 | - |
beta-carotene | pH 8.0, 37°C, recombinant wild-type enzyme | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Homo sapiens |