Chemisty and Biological Activity
Chemical Formula
C44H69NO12
Chemical Name
[3S- [3R*[E(1S*,3S*,4S*)],4S*,5R*,8S*,9E,12R*,14R*,15S*,16R*,18S*,19S*,26aR*]]- 5,6,8,11,12,13,14,15,16,17,18,19,24,25,26,26a-hexadecahydro-5, 19- dihydroxy-3- [2-(4-hydroxy-3-methoxycyclohexyl) -1-methylethenyl]-14, 16- dimethoxy-4,10,12,18-tetramethyl-8-(2-propenyl)-15, 19-epoxy-3H-pyrido[2,1- c][1,4] oxaazacyclotricosine-1,7,20, 21(4H,23H)-tetrone, monohydrate
Chemical Structure
Molecular Weight
804.018 g/mol
Physical State
Solid
Melting Point
126 oC
Water Solubility
Insoluble
Isoelectric Point
Not Available
Organisms Affected
Humans and other mammals
Phase 1 Metabolising Enzyme (1-st Step of Metabolism)
CYP3A4
Primary Drug Target
| Name | FK506-binding protein 1A | | Gene Name | FKBP1A | | Synonyms | EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase; PPIase; Rotamase; 12 kDa FKBP; FKBP-12; Immunophilin FKBP12 | | General Function | Posttranslational modification, protein turnover, chaperones | | Specific Function | May play a role in modulation of ryanodine receptor isoform-1 (RYR-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. There are four molecules of FKBP12 per skeletal muscle RYR. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | | Reaction | peptidylproline (omega=180) = peptidylproline (omega=0) |
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