ATP:guanido phosphotransferase family

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ATP:guanido phosphotransferase catalytic domain
PDB 1sd0 EBI.jpg
structure of arginine kinase c271a mutant
Identifiers
Symbol ATP-gua_Ptrans
Pfam PF00217
Pfam clan CL0286
InterPro IPR022414
PROSITE PDOC00103
SCOP 1crk
SUPERFAMILY 1crk
ATP:guanido phosphotransferase N-terminal domain
PDB 1p50 EBI.jpg
transition state structure of an arginine kinase mutant
Identifiers
Symbol ATP-gua_PtransN
Pfam PF02807
InterPro IPR022413
PROSITE PDOC00103
SCOP 1crk
SUPERFAMILY 1crk

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 phosphogens. The enzymes belonging to this family include:

  • Smc74, a cercaria-specific enzyme from Schistosoma mansoni.[1]

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[edit]

  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. 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. 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. doi:10.1038/381341a0. PMID 8692275. 

This article incorporates text from the public domain Pfam and InterPro IPR022413

This article incorporates text from the public domain Pfam and InterPro IPR022414