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ALKALINE PHOSPHATASE MUTANT H331QALKALINE PHOSPHATASE MUTANT H331Q
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedUsing a mutant version of E. coli alkaline phosphatase, we succeeded in trapping and determining the structure of the phospho-enzyme intermediate. The X-ray structure also revealed the catalytic water molecule, bound to one of the active site zinc ions, positioned ideally for the apical attack necessary for the hydrolysis of the intermediate. Trapping and visualization of a covalent enzyme-phosphate intermediate.,Murphy JE, Stec B, Ma L, Kantrowitz ER Nat Struct Biol. 1997 Aug;4(8):618-22. PMID:9253408[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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