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Comparison of the construction of a 3-D model for human thromboxane synthase using P450cam and BM-3 as templates: implications for the substrate binding pocket

Ruan, K.H.; Milfeld, K.; Kulmacz, R.J.; Wu, K.K.; Protein Eng. 7, 1345-1351 (1994)

Data extracted from this reference:

Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
5.3.99.5
Homo sapiens
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.3.99.5
Prostaglandin H2
i.e. PGH2
3193
Homo sapiens
Thromboxane B2 + 12(L)-hydroxy-5,8,10-heptadecatrienoic acid
-
-
-
-
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
5.3.99.5
heme
comparison of thromboxane A2 synthase model based on the P450BM-3 with another thromboxane A2 synthase model based on the P450cam structure indicates that P450BM-3 is a more suitable template for homology modeling of thromboxane A2 synthase. P450BM-3 and p450cam are hemoprotein domains of cytochrome; hemoprotein
Homo sapiens
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
5.3.99.5
heme
comparison of thromboxane A2 synthase model based on the P450BM-3 with another thromboxane A2 synthase model based on the P450cam structure indicates that P450BM-3 is a more suitable template for homology modeling of thromboxane A2 synthase. P450BM-3 and p450cam are hemoprotein domains of cytochrome; hemoprotein
Homo sapiens
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5.3.99.5
Prostaglandin H2
i.e. PGH2
3193
Homo sapiens
Thromboxane B2 + 12(L)-hydroxy-5,8,10-heptadecatrienoic acid
-
-
-
-