NDLI: Redox and metal-regulated oligomeric state for human porphobilinogen synthase activation

Content Provider	Springer Nature Link
Author	Sawada, N. Nagahara, N. Arisaka, F. Mitsuoka, K. Minami, M.
Copyright Year	2010
Abstract	The oligomeric state of human porphobilinogen synthase (PBGS) [EC.4.2.1.24] is homooctamer, which consists of conformationally heterogenous subunits in the tertiary structure under air-saturated conditions. When PBGS is activated by reducing agent with zinc ion, a reservoir zinc ion coordinated by Cys223 is transferred in the active center to be coordinated by Cys122, Cys124, and Cys132 (Sawada et al. in J Biol Inorg Chem 10:199–207, 2005). The latter zinc ion serves as an electrophilic catalysis. In this study, we investigated a conformational change associated with the PBGS activation by reducing agent and zinc ion using analytical ultracentrifugation, negative staining electron microscopy, native PAGE, and enzyme activity staining. The results are in good agreement with our notion that the main component of PBGS is octamer with a few percent of hexamer and that the octamer changes spatial subunit arrangement upon reduction and further addition of zinc ion, accompanying decrease in f/f 0. It is concluded that redox-regulated PBGS activation via cleavage of disulfide bonds among Cys122, Cys124, and Cys132 and coordination with zinc ion is closely linked to change in the oligomeric state.
Starting Page	173
Ending Page	180
Page Count	8
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	41
Issue Number	1
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2010-03-31
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Analytical ultracentrifugation Conformational change Enzyme activity regulation Negative staining electron microscopy Porphobilinogen synthase Proteomics Life Sciences Analytical Chemistry Biochemistry Neurobiology Biochemical Engineering
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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