Crystallization and preliminary x-ray diffraction studies of guanidinoacetate methyltransferase from rat liver.
Guanidinoacetate methyltransferase is the enzyme which catalyzes the last step of creatine biosynthesis. The enzyme is found ubiquitously and in abundance in the livers of all vertebrates. Recombinant rat-liver guanidinoacetate methyltransferase has been crystallized with guanidinoacetate and S-adenosylhomocysteine. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 54.8, b = 162.5, c = 56.1 A, beta = 96.8 (1) degrees at 93 K, and typically diffract beyond 2.8 A.
Komoto
J
J
Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66045-0045, USA.
Huang
Y
Y
Hu
Y
Y
Takata
Y
Y
Konishi
K
K
Ogawa
H
H
Gomi
T
T
Fujioka
M
M
Takusagawa
F
F
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D005998:Glycine / Q000031:analogs & derivatives; D050937:Guanidinoacetate N-Methyltransferase; D008099:Liver / Q000201:enzymology; D008780:Methyltransferases / Q000737:chemistry*; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry; D012435:S-Adenosylhomocysteine / Q000737:chemistry
D011994:Recombinant Proteins; D012435:S-Adenosylhomocysteine; D008780:Methyltransferases; C494506:GAMT protein, human; C494508:Gamt protein, rat; D050937:Guanidinoacetate N-Methyltransferase; C004946:glycocyamine; D005998:Glycine