Abstract：
:The open reading frame PA3859 of Pseudomonas aeruginosa encodes an intracellular carboxylesterase belonging to a group of microbial enzymes (EC 3.1.1.1) that catalyze the hydrolysis of aliphatic and aromatic esters with a broad substrate specificity. With few exceptions, for this class of enzymes, belonging to the α/β-hydrolase fold superfamily, very little information is available regarding their biochemical activity and in vivo function. The X-ray crystal structure of recombinant PA3859 has been determined for two crystal forms (space groups P2(1) and P2(1)2(1)2). The kinetic properties of the enzyme were studied using p-nitrophenyl esters as substrates and data fitted to a surface dilution mixed micelle kinetic model. Enzymatic assays and computational docking simulations, pinpointed the enzyme's preference for esters of palmitic and/or stearic acids and provided insights into the enzyme-substrate favorable binding modes.
journal_name
Biochimiejournal_title
Biochimieauthors
Pesaresi A,Lamba Ddoi
10.1016/j.biochi.2010.09.001subject
Has Abstractpub_date
2010-12-01 00:00:00pages
1787-92issue
12eissn
0300-9084issn
1638-6183pii
S0300-9084(10)00317-2journal_volume
92pub_type
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