Characteristics of a new enantioselective thermostable dipeptidase from Brevibacillus borstelensis BCS-1 and its application to synthesis of a D-amino-acid-containing dipeptide

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dc.contributor.authorDae Heoun Baek-
dc.contributor.authorJae Jun Song-
dc.contributor.authorSeok Joon Kwon-
dc.contributor.authorC Park-
dc.contributor.authorC M Jung-
dc.contributor.authorM H Sung-
dc.date.accessioned2017-04-19T09:00:50Z-
dc.date.available2017-04-19T09:00:50Z-
dc.date.issued2004-
dc.identifier.issn0099-2240-
dc.identifier.uri10.1128/AEM.70.3.1570-1575.2004ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6415-
dc.description.abstractA new thermostable dipeptidase gene was cloned from the thermophile Brevibacillus borstelensis BCS-1 by genetic complementation of the D-Glu auxotroph Escherichia coli WM335 on a plate containing D-Ala-D-Glu. Nucleotide sequence analysis revealed that the gene included an open reading frame coding for a 307-amino-acid sequence with an Mr of 35,000. The deduced amino acid sequence of the dipeptidase exhibited 52% similarity with the dipeptidase from Listeria monocytogenes. The enzyme was purified to homogeneity from recombinant E. coli WM335 harboring the dipeptidase gene from B. borstelensis BCS-1. Investigation of the enantioselectivity (E) to the P 1 and P1′ site of Ala-Ala revealed that the ratio of the specificity constant (kcat/Km) for L-enantioselectivity to the P1 site of Ala-Ala was 23.4 ± 2.2 [E = (kcat/Km)L,D/(kcat/K m)D,D], while the D-enantioselectivity to the P 1′ site of Ala-Ala was 16.4 ± 0.5 [E = (k cat/Km)L,D/(kcat/Km) L.L] at 55°C. The enzyme was stable up to 55°C, and the optimal pH and temperature were 8.5 and 65°C, respectively. The enzyme was able to hydrolyze L-Asp-D-Ala, L-Asp-D-AlaOMe, Z-D-Ala-D-AlaOBzl, and Z-L-Asp-D-AlaOBzl, yet it could not hydrolyze D-Ala-L-Asp, D-Ala-L-Ala, D-AlaNH2, and L-AlaNH2. The enzyme also exhibited >-lactamase activity similar to that of a human renal dipeptidase. The dipeptidase successfully synthesized the precursor of the dipeptide sweetener Z-L-Asp-D-AlaOBzl.-
dc.publisherAmer Soc Microb-
dc.titleCharacteristics of a new enantioselective thermostable dipeptidase from Brevibacillus borstelensis BCS-1 and its application to synthesis of a D-amino-acid-containing dipeptide-
dc.title.alternativeCharacteristics of a new enantioselective thermostable dipeptidase from Brevibacillus borstelensis BCS-1 and its application to synthesis of a D-amino-acid-containing dipeptide-
dc.typeArticle-
dc.citation.titleApplied and Environmental Microbiology-
dc.citation.number3-
dc.citation.endPage1575-
dc.citation.startPage1570-
dc.citation.volume70-
dc.contributor.affiliatedAuthorDae Heoun Baek-
dc.contributor.affiliatedAuthorJae Jun Song-
dc.contributor.affiliatedAuthorSeok Joon Kwon-
dc.contributor.alternativeName백대헌-
dc.contributor.alternativeName송재준-
dc.contributor.alternativeName권석준-
dc.contributor.alternativeName박청-
dc.contributor.alternativeName정창민-
dc.contributor.alternativeName성문희-
dc.identifier.bibliographicCitationApplied and Environmental Microbiology, vol. 70, no. 3, pp. 1570-1575-
dc.identifier.doi10.1128/AEM.70.3.1570-1575.2004-
dc.description.journalClassY-
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Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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