Sandbox Reserved 431: Difference between revisions

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==Additional Features==
==Additional Features==


This molecule has a heme which is bound to iron, which, combined with its structural conformation, allows for hydroxylation with the attached substrate.  This molecule carries out important functions and is not species or sex specific.
Cytochrome P45 has a central iron-bound heme, which, combined with its structural conformation, allows for hydroxylation with the attached substrate.  Cytochrome P450 has specific vitamin D 25-hydroxylase activity, which does not function properly when a person has rickets.  Rickets is caused when a person lacks sufficient vitamin D in their system, which is often caused by a vitamin D-25 hydroxylation defect.  Leu99Pro is an evolutionarily conserved mutation in the beta helix which contributes to the hydroxylation defect.  Leu99 does not inhibit substrate binding; however, Leu99Pro disturbs hydrogen binding around the heme and interferes with the helix steric properties, causing protein instability.  When Leu99 does not have the proline mutation, its carboxyl group forms hydrogen bonds with Arg445 which are both located around the central heme.




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