Secretion of an acid phosphatase (SapM) by Mycobacterium tuberculosis that is similar to eukaryotic acid phosphatases.
Mycobacterium tuberculosis secretes a large number of polypeptides with broad biological and immunological functions. We describe here the characterization of a 28-kDa acid phosphatase of M. tuberculosis (SapM) localized to the culture filtrate. The mature protein demonstrated biochemical characteristics similar to those of the bacterial nonspecific acid phosphatases. However, SapM yielded significant sequence homology to fungal acid phosphatases and not those of bacteria. Thus, SapM may represent a new class of bacterial nonspecific acid phosphatases.
Saleh
M T
MT
Department of Microbiology, Colorado State University, Fort Collins, Colorado 80523-1677, USA.
Belisle
J T
JT
D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D004791:Enzyme Inhibitors; D005057:Eukaryotic Cells / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D013347:Subcellular Fractions; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D000135:Acid Phosphatase