EC Number   |
Natural Substrates |
|---|
   1.14.11.7 | L-proline-[collagen] + O2 |
- |
| 1.14.11.7 | more |
isoform P3H2 is responsible for the hydroxylation of collagen IV |
| 1.14.11.7 | more |
the collagen prolyl 3-hydroxylation complex, comprised by cyclophilin B (PPIB), CRTAP and P3H1, catalyzes a specific posttranslational modification of types I, II, and V collagen, and may act as a general chaperone. Collagen 3-hydroxylation complex function, overview |
| 1.14.11.7 | more |
the P3H1-CRTAP-Cyp B complex does not stabilize the collagen triple helix, but does inhibit collgane fibril formation, overview |
| 1.14.11.7 | more |
type IV collagen contains more prolyl 3-hydroxylation sites than any other collagen types |
| 1.14.11.7 | procollagen + 2-oxoglutarate + O2 |
the enzyme catalyzes the synthesis of 3-hydroxyproline in collagen by the hydroxylation of prolyl residues |
| 1.14.11.7 | procollagen L-proline + 2-oxoglutarate + O2 |
P3H1 catalyzes the 3-hydroxylation of specific proline residues in procollagen I |
| 1.14.11.7 | [procollagen]-L-proline + 2-oxoglutarate + O2 |
- |
| 1.14.11.7 | [procollagen]-L-proline + 2-oxoglutarate + O2 |
prolyl 3-hydroxylation in lens capsule, prolyl 3-hydroxylation at Pro602 from alpha1(IV) and Pro197 from alpha2(IV). Pro707 site in alpha1(I) is a tissue-specific substrate unique to P3h2 |
| 1.14.11.7 | [procollagen]-L-proline + 2-oxoglutarate + O2 |
Residue alpha1(I) K930 is 98% hydroxylated and non-glycosylated in both genotypes and alpha1(I)K87 is 92% hydroxylated in wild-type and 93% in Lepre1H662A/H662A |
