Biochemical Characterization and Mass Spectrometric Disulfide Bond Mapping of Periplasmic α-Amylase MalS of Escherichia coli *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 272, Issue: 35, Page: 22125-22133
1997
- 36Citations
- 39Captures
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Metrics Details
- Citations36
- Citation Indexes36
- 36
- CrossRef30
- Captures39
- Readers39
- 39
Article Description
Periplasmic α-amylase of Escherichia coli, the malS gene product, hydrolyzes linear maltodextrins. The purified enzyme exhibited a K m of 49 μ m and a V max of 0.36 μmol of p -nitrophenylhexaoside hydrolyzed per min per mg of protein. Amylase activity was optimal at pH 8 and was dependent on divalent cations such as Ca 2+. MalS exhibited altered migration on SDS-polyacrylamide gel electrophoresis under nonreducing conditions. Analytical ultracentrifugation and electrospray mass spectrometry indicated that MalS is monomeric. The four cysteine residues are involved in intramolecular disulfide bonds. To map disulfide bonds, MalS was proteolytically digested. The resulting peptides were separated by reverse phase-high performance liquid chromatography, and matrix-assisted laser desorption/ionization mass spectrometry analysis indicated the presence of two disulfide bonds, i.e. Cys 40–58 and Cys 104–520. The disulfide bond at Cys 40–58 is located in an N-terminal extension of about 160 amino acids which has no homology to other amylases but to the proposed peptide binding domain of GroEL, the Hsp60 of E. coli. The N-terminal extension is linked to the C-terminal amylase domain via disulfide bond Cys 104–520. Reduction of disulfide bonds by dithiothreitol treatment led to aggregation suggesting that the N terminus of MalS may represent an internal chaperone domain.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819656711; http://dx.doi.org/10.1074/jbc.272.35.22125; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0030771489&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9268356; https://linkinghub.elsevier.com/retrieve/pii/S0021925819656711; https://dx.doi.org/10.1074/jbc.272.35.22125
Elsevier BV
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