ISSN:
1573-4919
Keywords:
active site
;
catalytic mechanism
;
creatine kinase
;
high-energy phosphate transport
;
membrane binding
;
metabolic channeling
;
mitochondrial energetics
;
octamer/dimer equilibrium
;
X-ray structure
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Abstract Mitochondrial creatine kinase (Mi-CK) is a central enzyme in energy metabolism of tissues with high and fluctuating energy requirements. In this review, recent progress in the functional and structural characterization of Mi-CK is summarized with special emphasis on the solved X-ray structure of chicken Mib-CK octamer (Fritz-Wolf et al., Nature 381, 341-345, 1996). The new results are discussed in a historical context and related to the characteristics of CK isoforms as known from a large number of biophysical and biochemical studies. Finally, two hypothetical functional aspects of the Mi-CK structure are proposed: (i) putative membrane binding motifs at the top and bottom faces of the octamer and (ii) a possible functional role of the central 20 Å channel.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1006851330913
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