Gm. Rossolini et al., BACTERIAL NONSPECIFIC ACID PHOSPHOHYDROLASES - PHYSIOLOGY, EVOLUTION AND USE AS TOOLS IN MICROBIAL BIOTECHNOLOGY, Cellular and molecular life sciences, 54(8), 1998, pp. 833-850
Bacterial nonspecific acid phosphohydrolases (NSAPs) are secreted enzy
mes, produced as soluble periplasmic proteins or as membrane-bound lip
oproteins, that are usually able to dephosphorylate a broad array of s
tructurally unrelated substrates and exhibit optimal catalytic activit
y at-acidic to neutral pH values. Bacterial NSAPs are monomeric or oli
gomeric proteins containing polypeptide components with an M-r of 25-3
0 kDa. On the basis of amino acid sequence relatedness, three differen
t molecular families of NSAPs can be distinguished, indicated as molec
ular class A, B and C, respectively. Members of each class share some
common biophysical and functional features, but may also exhibit funct
ional differences. NSAPs have been detected in several microbial taxa,
and enzymes of different classes can be produced by the same bacteria
l species. Structural and phyletic relationships exist among the vario
us bacterial NSAPs and some other bacterial and eucaryotic phosphohydr
olases. Current knowledge on bacterial NSAPs is reviewed, together wit
h analytical tools that may be useful for their characterization. An o
verview is also presented concerning the use of bacterial NSAPs in bio
technology.