Prolyl 3-hydroxylase 2 is an enzyme that in humans is encoded by the gene P3H2 (formally LEPREL1).[5][6] This enzyme is involved in the assembly of collagen.[6] Pathogenic mutations in the gene are associated with severe nearsightedness (myopia) and cataracts.[6]
Function
As their names suggests, the Prolyl 3-hydroxylase 2 and its relatives Prolyl 3-hydroxylase 1 and 3 function as collagen prolyl 3-hydroxylases.[6] This means they act on the amino acid, proline, located in collagen precursor proteins, and attaches a hydroxyl at the 3-position, converting the proline into 3-hydroxyproline.[7] This seems to function to help the corresponding collagen fibrils bind together and align properly.[8]
P3H2 differs from P3H1 in a number of important ways. It is primarily expressed in basement membrane-rich tissues (P3H1 is primarily in fibrillar collagens rich tissues).[8] It is also able to act on type IV collagen (especially COL4A1),[7] unlike P3H1.[8] Both enzymes are able to act on Type I collagen (and COL1A1),[7] but they tend to modify the prolines at different positions.[8] P3H2 also appears to function on its own, while P3H1 forms a complex with two other proteins (CRTAP and CypB).[8]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000090530 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038168 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Jarnum S, Kjellman C, Darabi A, Nilsson I, Edvardsen K, Aman P (Apr 2004). "LEPREL1, a novel ER and Golgi resident member of the Leprecan family". Biochem Biophys Res Commun. 317 (2): 342–51. doi:10.1016/j.bbrc.2004.03.060. PMID 15063763.
- 1 2 3 4 "P3H2 prolyl 3-hydroxylase 2 [ Homo sapiens (human) ]". National Library of Medicine. Retrieved 2026-07-30.
- 1 2 3 "Q8IVL5 · P3H2_HUMAN". uniprot.org. UniProt consortium. Retrieved 2026-08-13.
- 1 2 3 4 5 Gjaltema RA, Bank RA (2017-01-02). "Molecular insights into prolyl and lysyl hydroxylation of fibrillar collagens in health and disease". Critical reviews in biochemistry and molecular biology. 52 (1): 74–95. doi:10.1080/10409238.2016.1269716. ISSN 1040-9238.
