Sandbox Reserved 349: Difference between revisions
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Although PBGD appears to have hydrogen bonding capabilities between two identical PBGD units, at physiological pH, these interactions account for a dimer interface of approximately 5% while average dimer interface between subunits is 16%<ref name="Raj">PMID: 19207107</ref>. Therefore, it is generally assumed that this protein is active naturally as a monomeric enzyme, while the crystalline form is a homo-dimeric structure of two identical PBGD subunits<ref name="Raj">PMID: 19207107</ref>. | Although PBGD appears to have hydrogen bonding capabilities between two identical PBGD units, at physiological pH, these interactions account for a dimer interface of approximately 5% while average dimer interface between subunits is 16%<ref name="Raj">PMID: 19207107</ref>. Therefore, it is generally assumed that this protein is active naturally as a monomeric enzyme, while the crystalline form is a homo-dimeric structure of two identical PBGD subunits<ref name="Raj">PMID: 19207107</ref>. | ||
==Function== | ==Function== | ||
===Sub1=== | |||
:This mechanism on the formation of hydroxymethylbilane by porphobilinogen deaminase is modelled based on the research of Lander ''et al.''1992<ref name="Lander">PMID: 1150073</ref>. | :This mechanism on the formation of hydroxymethylbilane by porphobilinogen deaminase is modelled based on the research of Lander ''et al.''1992<ref name="Lander">PMID: 1150073</ref>. | ||
==Importance of hPBGD== | ==Importance of hPBGD== | ||
