User:Kristian Koski/P4H
From Proteopedia
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Chlamydomonas reinhardtii prolyl 4-hydroxylase is a monomeric enzyme which catalyse the hydroxylation of proline residues of the proline-rich cell wall proteins. The structure of Cr-P4H has been determined as apo and in complexed with Zinc and serine-proline rich peptide<ref>pmid 19553701</ref>. | Chlamydomonas reinhardtii prolyl 4-hydroxylase is a monomeric enzyme which catalyse the hydroxylation of proline residues of the proline-rich cell wall proteins. The structure of Cr-P4H has been determined as apo and in complexed with Zinc and serine-proline rich peptide<ref>pmid 19553701</ref>. | ||
| - | == Function ==http://proteopedia.org/wiki/index.php?title=User:Kristian_Koski/P4H&action=edit | + | == Function == |
| + | http://proteopedia.org/wiki/index.php?title=User:Kristian_Koski/P4H&action=edit | ||
Prolyl 4-hydroxylase (P4H) catalyses the hydroxylation of a proline resiue in the collagens . | Prolyl 4-hydroxylase (P4H) catalyses the hydroxylation of a proline resiue in the collagens . | ||
Revision as of 13:36, 28 February 2019
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References
- ↑ Koski MK, Hieta R, Hirsila M, Ronka A, Myllyharju J, Wierenga RK. The crystal structure of an algal prolyl 4-hydroxylase complexed with a proline-rich peptide reveals a novel buried tripeptide binding motif. J Biol Chem. 2009 Sep 11;284(37):25290-301. Epub 2009 Jun 24. PMID:19553701 doi:10.1074/jbc.M109.014050
