Sequence homology and structure predictions of the creatine kinase isoenzymes

Mühlebach, S. M.; Groß, Martin; Wirz, T.; Wallimann, Theo; Perriard, J.-C.; Wyss, Markus

doi:10.1007/bf01267958

Cited by 157 publications

(101 citation statements)

References 85 publications

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“…There is approximately 98% homology in MM-CK and 95% homology in BB-CK across species. The intraspecies homology between MM-CK and BB-CK is approximately 80%, which although less than interspecies homology within isoform is still extremely high (40). Interestingly there is sequence divergence between MM and BB-CK in the carboxyl-terminal of the enzyme.…”

Section: Discussionmentioning

confidence: 90%

“…The phylogenetic tree of CK reveals gene duplication events that resulted in the multiple isoforms expressed today in cellular systems of all vertebrates and most invertebrates. Based on sequence homology there are distant evolutionary connections between CK and other guanidino kinases such as arginine kinase, the major guanidino kinase found in invertebrates (40). Conservation of guanidino kinases indicates an important role in cellular energetics for this class of enzyme.…”

Section: Discussionmentioning

confidence: 99%

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Functional Equivalence of Creatine Kinase Isoforms in Mouse Skeletal Muscle

Roman¹,

Wieringa²,

Koretsky³

1997

Journal of Biological Chemistry

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Creatine kinase (CK) is a highly conserved enzyme abundant in skeletal muscle that has a key role in high energy phosphate metabolism. The localization of the muscle isoenzyme of CK (MM-CK) to the M line and the sarcoplasmic reticulum of myofibrils has been suggested to be important for proper force development in skeletal muscle. The importance of this subcellular compartmentation has not been directly tested in vivo. To test the role of myofibrilar localization of CK, the consequences of a complete CK isoform switch from MM-CK to the brain (BB-CK) isoform, which does not localize to the M line, was studied in transgenic mouse skeletal muscle. In MM-CK knockout mice there are large contractile defects. When MM-CK was replaced by BB-CK, the aberrant contractile phenotypes seen in MM-CK knockout mice were returned to normal despite the lack of myofibrillar localization. These results indicate that CK compartmentation to the myofibril of skeletal muscle is not essential for contractile function and that there is functional equivalence of creatine kinase isoforms in supporting cellular energy metabolism.

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Section: Discussionmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Functional Equivalence of Creatine Kinase Isoforms in Mouse Skeletal Muscle

Roman¹,

Wieringa²,

Koretsky³

1997

Journal of Biological Chemistry

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“…Analysis of the deduced amino acid sequences of the three carp muscle subisoforms revealed 83-87% identity with human and other species' creatine kinase muscle isoenzyme (Table I). In mammals and birds, the amino acid identities within each isoenzyme class range from 88 to 99% (24). Evidently, a higher degree of homology can be observed between the B-and the M-CKs (77-82%), while the homology between the cytosolic and the mitochondrial CK isoforms is lower (60 -65%) ( Table I) (24).…”

Section: Amino Acid Primary Structure Of Carp M1-ck M2-ck and M3-ckmentioning

confidence: 99%

Cloning, Characterization, and Expression in Escherichia coli of Three Creatine Kinase Muscle Isoenzyme cDNAs from Carp (Cyprinus carpio)Striated Muscle

Sun¹,

Hui²,

Wu³

1998

Journal of Biological Chemistry

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In vertebrates, the creatine kinase isoenzyme family consists of four types of isoforms: cytosolic muscle type (M-CK), cytosolic brain type (B-CK), mitochondrial ubiquitous, acidic type (Miu-CK), and mitochondrial sarcomeric, basic type (Mis-CK). Until recently, the existence of more than one subisoform of CK isoenzyme has been demonstrated only in fishes by starch gel electrophoresis. We report herein the isolation of three full-length cDNAs that correspond to three closely related creatine kinase M-CK genes from common carp (Cyprinus carpio), designated the M1-CK, M2-CK, and M3-CK genes. Using oligonucleotide probes that correspond to the same region but with the most variable sequences, different restricted genomic hybridization patterns have been obtained. These Southern blot results indicate that the three cDNAs come from different genes. Northern blot analysis using probes that correspond to the 3-untranslated regions further show that all three subisoforms are expressed specifically in carp muscle. The deduced amino acid sequences of these three subisoforms of carp M-CK show about 85% identity to mammalian M-CK isoenzyme. Finally, the three cDNAs have been expressed in Escherichia coli with a molecular mass of approximately 43,000 Da, and these recombinant proteins exhibit creatine kinase activity. All of these data suggest that the M-CK isoenzymes have at least three subisoforms in carp.All living organisms require energy to survive and carry out the many tasks that characterize biological activity. Cellular energy demand and supply are generally balanced and tightly regulated for economic and efficient energy use. The enzyme creatine kinase (CK 1 ; EC 2.7.3.2) plays a key role in the energy metabolism of cells that have fluctuating energy requirements (for a review, see Ref.

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“…No evidence was found for derivatization in either F307-K318 or R319-K357. Arg-291 corresponds to Arg-287 in the octameric mitochondrial CK, which is one of seven arginines found at the ATP binding site (3), and is invariant (32). Interestingly, the rabbit muscle CK mutant R291Q is inactive, and the R291K mutant has approximately 1% activity (C.L.B.…”

Section: Resultsmentioning

confidence: 99%

“…4) and 1:2 for the 4ϩ charge state. This shift restricts the second reactive site to Arg-129, Arg-131, or Arg-134, all of which are invariant in all CK isoforms (32). The 3ϩ ions of the oncederivatized G116-K137 peptide were accumulated (33,34) in the FTMS trap for 10 cycles by using selective stored waveform inverse FT (SWIFT) (25) waveforms and quadrupolar axialization (33)(34)(35)(36), but sustained off-resonance irradiationcollisionally activated dissociation (SORI-CAD) (Ϫ1.1 kHz, Ϸ3 V pp ) of these (22,23) gave only P122-I136 as the smallest fragment ion containing the phenylglyoxal; higher collision energies and infrared multiphoton dissociation (37) produced no other identifiable fragments.…”

Section: Resultsmentioning

confidence: 99%

Creatine kinase: Essential arginine residues at the nucleotide binding site identified by chemical modification and high-resolution tandem mass spectrometry

Wood

Guan

Borders

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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Phenylglyoxal is an arginine-specific reagent that inactivates creatine kinase (CK). Previous results suggest that modification of the dimeric enzyme at a single arginine residue per subunit causes complete inactivation accompanied by the loss of nucleotide binding; the actual site of modification was not identified. Here, high-resolution tandem mass spectrometry (MS͞MS) was used to identify three phenylglyoxal-modified Arg residues in monomeric rabbit muscle CK. Electrospray ionizaton Fourier-transform MS of the phenylglyoxal-modified CK that had lost Ϸ80% activity identified three species: unmodified, once-modified (؉116 Da), and twice-modified (؉232 Da) enzyme in a ratio of approximately 1:4:1. MS͞MS restricts the derivatized sites to P122-P212 and P283-V332, whereas MS of Lys-C digestions revealed two modified peptides, A266-K297 and G116-K137. The only Arg in A266-K297 is Arg-291 (invariant), whereas MS͞MS of modified G116-K137 shows that two of the three sites Arg-129, Arg-131, or Arg-134 (all invariant) can contain the modification. The recently reported x-ray crystal structure for the octameric chicken mitochondrial CK indicates that its nucleotide triphosphate-binding site indeed contains the equivalent of R291, R129, and R131 reported here to be at the active site of rabbit muscle CK.Creatine kinase (CK, EC 2.7.3.2) plays a key role in energy metabolism in cells by catalyzing the reversible transfer of a phosphoryl group from phosphocreatine to MgADP to form creatine and MgATP. Mechanistic studies of CK have been made more difficult by the microheterogeneity found in enzyme preparations (1); mass spectrometry (MS) recently has shown (2) that deamidation is a major cause of this. Microheterogeneity also has been an obstacle to obtaining x-ray crystal structures for dimeric cytosolic (muscle, brain, or muscle-brain heterodimer) isoforms (1, 2), although recently have succeeded in obtaining a 3.0 Å x-ray crystal structure for the octameric chicken mitochondrial CK. Several studies have been done to identify the roles of amino acid residues involved in substrate binding and catalysis in CK.

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Sequence homology and structure predictions of the creatine kinase isoenzymes

Cited by 157 publications

References 85 publications

Functional Equivalence of Creatine Kinase Isoforms in Mouse Skeletal Muscle

Functional Equivalence of Creatine Kinase Isoforms in Mouse Skeletal Muscle

Cloning, Characterization, and Expression in Escherichia coli of Three Creatine Kinase Muscle Isoenzyme cDNAs from Carp (Cyprinus carpio)Striated Muscle

Creatine kinase: Essential arginine residues at the nucleotide binding site identified by chemical modification and high-resolution tandem mass spectrometry

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