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ATP:guanido phosphotransferase family

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ATP:guanido phosphotransferase catalytic domain
structure of arginine kinase c271a mutant
Identifiers
SymbolATP-gua_Ptrans
PfamPF00217
Pfam clanCL0286
InterProIPR022414
PROSITEPDOC00103
SCOP21crk / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
ATP:guanido phosphotransferase N-terminal domain
transition state structure of an arginine kinase mutant
Identifiers
SymbolATP-gua_PtransN
PfamPF02807
InterProIPR022413
PROSITEPDOC00103
SCOP21crk / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the ATP:guanido phosphotransferase family is a family of structurally and functionally related enzymes,[1][2] that reversibly catalyse the transfer of phosphate between ATP and various phosphagens. The enzymes belonging to this family include:

Creatine kinase plays an important role in energy metabolism of vertebrates. There are at least four different, but very closely related, forms of CK. Two isozymes, M (muscle) and B (brain), are cytosolic, while the other two are mitochondrial. In sea urchins there is a flagellar isozyme, which consists of the triplication of a CK-domain. A cysteine residue is implicated in the catalytic activity of these enzymes and the region around this active site residue is highly conserved.

ATP:guanido phosphotransferases contain a C-terminal catalytic domain which consists of a duplication where the common core consists of two beta-alpha-beta2-alpha repeats.[5] The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain.[5] They also contain an N-terminal domain which has an all-alpha fold consisting of an irregular array of 6 short helices.[5]

References

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  1. ^ a b Stein LD, Harn DA, David JR (April 1990). "A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni has a novel duplicated structure". J. Biol. Chem. 265 (12): 6582–8. doi:10.1016/S0021-9258(19)39187-2. PMID 2324092.
  2. ^ Strong SJ, Ellington WR (January 1995). "Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues". Biochim. Biophys. Acta. 1246 (2): 197–200. doi:10.1016/0167-4838(94)00218-6. PMID 7819288.
  3. ^ Bessman SP, Carpenter CL (1985). "The creatine-creatine phosphate energy shuttle". Annu. Rev. Biochem. 54: 831–62. doi:10.1146/annurev.bi.54.070185.004151. PMID 3896131.
  4. ^ Haas RC, Strauss AW (April 1990). "Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isoenzymes". J. Biol. Chem. 265 (12): 6921–7. doi:10.1016/S0021-9258(19)39237-3. PMID 2324105.
  5. ^ a b c Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W (May 1996). "Structure of mitochondrial creatine kinase". Nature. 381 (6580): 341–5. Bibcode:1996Natur.381..341F. doi:10.1038/381341a0. PMID 8692275. S2CID 4254253.
This article incorporates text from the public domain Pfam and InterPro: IPR022413
This article incorporates text from the public domain Pfam and InterPro: IPR022414