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NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism

✍ Scribed by Kim, Y.; Cunningham, M. A.; Mire, J.; Tesar, C.; Sacchettini, J.; Joachimiak, A.

Book ID
120069781
Publisher
The Federation of American Societies for Experimental Biology
Year
2013
Tongue
English
Weight
396 KB
Volume
27
Category
Article
ISSN
0892-6638

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## Abstract Based on the high‐resolution X‐ray crystallographic structure of phospholipase C from __Bacillus cereus__, the orientation of the phosphatidylcholine substrate in the active site of the enzyme is proposed. The proposal is based on extensive calculations using the GRID program and molecu