Open AccessProstatic acid phosphatase: structural aspects of inhibition by L-(+)-tartrate ions.
Author(s) -
L Lovelace,
K Lewiński,
C G Jakob,
R Kuciel,
W Ostrowski,
L Lebioda
Publication year - 1997
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1997_4369
Subject(s) - tartrate , chemistry , acid phosphatase , ligand (biochemistry) , prostatic acid phosphatase , phosphatase , chirality (physics) , biochemistry , ion , stereochemistry , enzyme , organic chemistry , physics , receptor , chiral symmetry breaking , quantum mechanics , nambu–jona lasinio model , quark
The crystal structure of the complex between rat-prostatic acid phosphatase (PAP) and L-(+)-tartrate (Lindqvist et al., J. Biol. Chem., 1993, 268, 20744-20746) contains the model of the ligand with incorrect chirality. We report here the correct model and discuss the relation between this model and the model of the inhibitory complexes between PAP and oxy-anions.