Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase (Q27643647)

1

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Sowmya Sampath

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Jerry Coll-Rodriguez

3

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Jack Schmidt

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Kallol Ray

5

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David W Rodgers

Journal of Biological Chemistry

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language of work or name

English

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publication date

30 March 2007

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published in

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volume

282

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issue

13

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page(s)

9722-32

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cites work

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The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation

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Metalloendopeptidase EC 3.4.24.15 is necessary for Alzheimer's amyloid-beta peptide degradation

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Structure of neurolysin reveals a deep channel that limits substrate access

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Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization

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Thimet oligopeptidase specificity: evidence of preferential cleavage near the C-terminus and product inhibition from kinetic analysis of peptide hydrolysis

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Mapping sequence differences between thimet oligopeptidase and neurolysin implicates key residues in substrate recognition

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