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RESEARCH PRODUCT
Chapter 17: The cholinesterases: a discussion of some unanswered questions
Victor P. Whittakersubject
chemistry.chemical_classificationbiologyActive siteSubstrate (chemistry)AcetylcholinesteraseIsozymeSynapsechemistry.chemical_compoundmedicine.anatomical_structureEnzymeBiochemistrychemistrybiology.proteinmedicineBasal laminaButyrylcholinesterasedescription
Publisher Summary During the past three decades, a vast body of specificity and kinetic data relating to the cholinesterases has accumulated, which must now be explained by the extremely interesting new sequence and X-ray crystallographic results presented by MassouliC et al. As this chapter shows, the cholinesterases are remarkable among enzymes in having a broad specificity embracing both charged and uncharged substrates but with a clearly expressed preference, at any rate in the aliphatic series, for the acylcholine configuration: a classical example of the principle of complementariness between substrate and active site as the basis for enzyme action. It is well known that AChE exists in multiple forms in which up to two or more dimeric, catalytically active, globular heads are attached to glycolipid-containing or collagen-like tails that serve to anchor the enzyme to the plasma membrane or the basal lamina, respectively. Junctional AChE may be contributed both by the presynaptic nerve terminal and the target (nerve or muscle) cell; the proportion of AChE and the forms of it delivered by the pre- and post-synaptic components varies in different types of synapse and during development.
year | journal | country | edition | language |
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1993-01-01 |