Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase.
Crystals of acylpeptide hydrolase suitable for structure determination have been obtained. This enzyme removes the N-terminal formyl or acetyl group together with the first amino acid residue from N-terminal blocked peptides including bioactive peptides. One set of crystals, which diffract to 2.2 A, are in space group P2 with cell dimensions a = 118.6 A, b = 82.3 A, c = 182.1 A, beta = 91.6 degrees. The search for suitable heavy-atom derivatives is underway.
Feese
M
M
Institute of Molecular Biology, University of Oregon, Eugene 97403.
Scaloni
A
A
Jones
W M
WM
Manning
J M
JM
Remington
S J
SJ
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry*; D003460:Crystallization; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D010447:Peptide Hydrolases; D000626:Aminopeptidases; C038220:acylaminoacyl-peptidase