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

BRENDA support

Literature summary extracted from

  • Yamamoto, K.; Uchida, E.; Urushino, N.; Sakaki, T.; Kagawa, N.; Sawada, N.; Kamakura, M.; Kato, S.; Inouye, K.; Yamada, S.
    Identification of the amino acid residue of CYP27B1 responsible for binding of 25-hydroxyvitamin D3 whose mutation causes vitamin D-dependent rickets type 1 (2005), J. Biol. Chem., 280, 30511-30516.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.18 expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.18 Q65A site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme Mus musculus
1.14.15.18 Q65E site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme Mus musculus
1.14.15.18 Q65H site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme Mus musculus
1.14.15.18 Q65L site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme Mus musculus
1.14.15.18 Q65N site-directed mutagenesis, three-dimensional structure analysis and comparison to the wild-type enzyme Mus musculus
1.14.15.18 S408A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, three-dimensional structure analysis and comparison to the wild-type enzyme Mus musculus
1.14.15.18 S408I site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, three-dimensional structure analysis and comparison to the wild-type enzyme Mus musculus
1.14.15.18 S408T site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, three-dimensional structure analysis and comparison to the wild-type enzyme Mus musculus
1.14.15.18 S408V site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, three-dimensional structure analysis and comparison to the wild-type enzyme Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.15.18 0.00013
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408T Mus musculus
1.14.15.18 0.00018
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408I Mus musculus
1.14.15.18 0.00024
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408A Mus musculus
1.14.15.18 0.00028
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant wild-type enzyme Mus musculus
1.14.15.18 0.00052
-
 1alpha-hydroxyvitamin D pH 7.4, 37°C, recombinant wild-type enzyme Mus musculus
1.14.15.18 0.00054
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408V Mus musculus
1.14.15.18 0.00066
-
 1alpha-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408V Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.15.18 25-hydroxyvitamin D + NADPH + O2 Mus musculus deficiency of the enzyme, due to mutation of residues Q65 and T409, in substrate binding causes vitamin D-dependent rickets type 1, overview 1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.18 Mus musculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.18 1alpha-hydroxyvitamin D + NADPH + O2
-
 Mus musculus 1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
 ?
1.14.15.18 25-hydroxyvitamin D + NADPH + O2 deficiency of the enzyme, due to mutation of residues Q65 and T409, in substrate binding causes vitamin D-dependent rickets type 1, overview Mus musculus 1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
 ?
1.14.15.18 25-hydroxyvitamin D + NADPH + O2 binding of 25-hydroxyvitamin D3 in a structural pocket involving residues Q65, S408, and T409, molecular modeling and substrate docking Mus musculus 1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.15.18 More three-dimensional structure analysis of wild-type and mutant enzymes, molecular modeling and substrate docking, overview Mus musculus

Synonyms

EC Number Synonyms Comment Organism
1.14.15.18 CYP27B1
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.15.18 37
-
 assay at Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.15.18 0.0004
-
 1alpha-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408V Mus musculus
1.14.15.18 0.0008
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408I Mus musculus
1.14.15.18 0.006
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408A Mus musculus
1.14.15.18 0.01
-
 1alpha-hydroxyvitamin D pH 7.4, 37°C, recombinant wild-type enzyme Mus musculus
1.14.15.18 0.013
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408V Mus musculus
1.14.15.18 0.098
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant mutant S408T Mus musculus
1.14.15.18 0.385
-
 25-hydroxyvitamin D pH 7.4, 37°C, recombinant wild-type enzyme Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.15.18 7.4
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.18 NADPH
-
 Mus musculus