Abstract:
:Creatine kinases (CK) play a prominent role in cell energy distribution through an energy shuttle between mitochondria and other organelles. Human brain CK was cloned and overexpressed in COS-7 cells. We then deleted His-65 and/or Pro-66 situated near the center of a flexible loop as shown by X-ray crystallography on mitochondrial and cytosolic CK. The DeltaH65 mutant had nearly the same affinity for its substrates as wild isoenzyme, but its stability was very low. Unlike DeltaH65, DeltaH65P66 had a eightfold decreased affinity for creatine phosphate and was unable to dephosphorylate cyclocreatine phosphate. Our results demonstrate that, despite an overall similar shape of the proteins, this loop accounts for some subtle differences in isoenzyme functions.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Mourad-Terzian T,Steghens JP,Min KL,Collombel C,Bozon Ddoi
10.1016/s0014-5793(00)01614-8keywords:
subject
Has Abstractpub_date
2000-06-09 00:00:00pages
22-6issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(00)01614-8journal_volume
475pub_type
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