Purification and characterization of a calf thymus protein active on lipid metabolism

1989 ◽  
Vol 21 (9) ◽  
pp. 1009-1014 ◽  
Author(s):  
Paolo Mondola ◽  
Mariarosaria Santillo ◽  
Franco Santangelo ◽  
Carlo Caporale ◽  
Anna Belfiore ◽  
...  
1980 ◽  
Vol 255 (10) ◽  
pp. 4535-4538
Author(s):  
H.C. Schröder ◽  
R.K. Zahn ◽  
K. Dose ◽  
W.E. Müller

2008 ◽  
Vol 25 (3) ◽  
pp. 475-480 ◽  
Author(s):  
Jing Quan ◽  
Yan-Qian Chai ◽  
Christopher J. Branford-White ◽  
Li-Min Zhu

2007 ◽  
Vol 189 (11) ◽  
pp. 4153-4160 ◽  
Author(s):  
Sarah K. Parker ◽  
Kathryn M. Curtin ◽  
Michael L. Vasil

ABSTRACT We describe mycobacterial phospholipase A activity (MPLA) and, using reverse genetics, have associated this activity with putative mycobacterial cutinase. PLAs, which hydrolyze fatty acids on phospholipids, play a significant role in human inflammatory states and disease pathogenesis. In prokaryotes, the recognition of their role in virulence is more recent. Cutinases are serine esterases whose primary substrate is cutin, the waxy exterior layer of plants. Mycobacterium tuberculosis has maintained seven putative cutinases, though it should not encounter cutin; we demonstrate that known cutinases and MPLA cleave phospholipids in a PLA-type manner and also hydrolyze Tween. We analyzed cutinase motifs in mycobacteria and found the motif very prevalent. All mycobacteria tested had MPLA activity. These studies suggest an alternative use for putative cutinases by the M. tuberculosis group that is likely related to MPLA activity and lipid metabolism.


1981 ◽  
Vol 89 (1) ◽  
pp. 143-152 ◽  
Author(s):  
Michitoshi NAKAMURA ◽  
Yoshiyuki SAKAKI ◽  
Nobuko WATANABE ◽  
Yasuyuki TAKAGI

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