1998
DOI: 10.1016/s0378-1119(97)00590-8
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The gene encoding dipeptidyl aminopeptidase BI from Pseudomonas sp. WO24: cloning, sequencing and expression in Escherichia coli

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Cited by 6 publications
(7 citation statements)
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“…3) showed a clear (57% height of the origin peak) noncrystallographic twofold axis, indicating that the number of molecules in the asymmetric unit of the DAP BII crystal would be an even number. This observation is consistent with the dimeric nature of DAP BII (Ogasawara et al, 1998) and indicates that the number of molecules in the asymmetric unit of the DAP BII crystal must be two. A search for heavy-atom derivatives intended for phasing by multiple isomorphous replacement and preparation of selenomethioninesubstituted DAP BII using LeMaster medium (Hendrickson et al, 1990) Stereographic projection of the self-rotation function in spherical polar angles at = 180 for the DAP BII crystal.…”
Section: X-ray Analysessupporting
confidence: 82%
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“…3) showed a clear (57% height of the origin peak) noncrystallographic twofold axis, indicating that the number of molecules in the asymmetric unit of the DAP BII crystal would be an even number. This observation is consistent with the dimeric nature of DAP BII (Ogasawara et al, 1998) and indicates that the number of molecules in the asymmetric unit of the DAP BII crystal must be two. A search for heavy-atom derivatives intended for phasing by multiple isomorphous replacement and preparation of selenomethioninesubstituted DAP BII using LeMaster medium (Hendrickson et al, 1990) Stereographic projection of the self-rotation function in spherical polar angles at = 180 for the DAP BII crystal.…”
Section: X-ray Analysessupporting
confidence: 82%
“…The hydrolytic activities of recombinant DAP BII for synthetic substrates were 3.4 AE 0.1 mmol min À1 mg À1 (U mg À1 ) and 10 AE 0.2 U mg À1 for Gly-Phe-pNA and Ala-Ala-pNA, respectively, which were compar- able to those of native DAP BII (3.3 AE 0.1 and 9.5 AE 0.2 U mg À1 for Gly-Phe-pNA and Ala-Ala-pNA, respectively). The recombinant enzyme was equally stable to the native enzyme at temperatures below 293 K for 30 min (Ogasawara et al, 1998).…”
Section: Resultsmentioning
confidence: 99%
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“…DAPs are present in all organisms, from bacteria to mammals, and the enzyme contributes to several important physiological functions such as the absorption of nutrients, immunity and the ability of pathogens to invade host cells151617. DAP BI18 and DAP IV19 show amino acid sequence homology and similar substrate specificity to enzymes that belong to the peptidase family S920 in clan SC, such as oligopeptidase B and DPP IV. In contrast, no homologs have been identified for DAP BII and DAP BIII.…”
mentioning
confidence: 99%