Distinct Roles of beta-Galactosidase Paralogues of the Rumen Bacterium Mannheimia succiniciproducens

Cited 5 time in webofscience Cited 0 time in scopus
  • Hit : 439
  • Download : 0
DC FieldValueLanguage
dc.contributor.authorLee, Eun-Gyeongko
dc.contributor.authorKim, Seonghunko
dc.contributor.authorOh, Doo-Byoungko
dc.contributor.authorLee, Sang Yupko
dc.contributor.authorKwon, Ohsukko
dc.date.accessioned2013-03-11T00:38:39Z-
dc.date.available2013-03-11T00:38:39Z-
dc.date.created2012-03-07-
dc.date.created2012-03-07-
dc.date.created2012-03-07-
dc.date.created2012-03-07-
dc.date.issued2012-01-
dc.identifier.citationJOURNAL OF BACTERIOLOGY, v.194, no.2, pp.426 - 436-
dc.identifier.issn0021-9193-
dc.identifier.urihttp://hdl.handle.net/10203/97822-
dc.description.abstractMannheimia succiniciproducens, a rumen bacterium belonging to the family Pasteurellaceae, has two putative beta-galactosidase genes, bgaA and bgaB, encoding polypeptides whose deduced amino acid sequences share 56% identity with each other and show approximately 30% identity to the Escherichia coli gene for LacZ. The M. succiniciproducens bgaA (MsbgaA) gene-deletion mutant was not able to grow on lactose as the sole carbon source, suggesting its essential role in lactose metabolism, whereas the MsbgaB gene-deletion mutant did not show any growth defect on a lactose medium. Furthermore, the expression of the MsbgaA gene was induced by the addition of lactose in the growth medium, whereas the MsbgaB gene was constitutively expressed independently of a carbon source. Biochemical characterization of the recombinant proteins revealed that MsBgaA is more efficient than MsBgaB in hydrolyzing o-nitrophenyl-beta-D-galactopyranoside and p-nitrophenyl-beta-D-galactopyranoside. MsBgaA was highly specific for the hydrolysis of lactose, with a catalytic efficiency of 46.9 s(-1) mM(-1). However, MsBgaB was more efficient for the hydrolysis of lactulose than lactose, and the catalytic efficiency was 10.0 s(-1) mM(-1). Taken together, our results suggest that the beta-galactosidase paralogues of M. succiniciproducens BgaA and BgaB play a critical role in lactose metabolism and in an unknown but likely specific function for rumen bacteria, respectively.-
dc.languageEnglish-
dc.publisherAMER SOC MICROBIOLOGY-
dc.titleDistinct Roles of beta-Galactosidase Paralogues of the Rumen Bacterium Mannheimia succiniciproducens-
dc.typeArticle-
dc.identifier.wosid000298677400025-
dc.identifier.scopusid2-s2.0-84862942747-
dc.type.rimsART-
dc.citation.volume194-
dc.citation.issue2-
dc.citation.beginningpage426-
dc.citation.endingpage436-
dc.citation.publicationnameJOURNAL OF BACTERIOLOGY-
dc.identifier.doi10.1128/JB.05911-11-
dc.contributor.localauthorLee, Sang Yup-
dc.contributor.nonIdAuthorLee, Eun-Gyeong-
dc.contributor.nonIdAuthorKim, Seonghun-
dc.contributor.nonIdAuthorOh, Doo-Byoung-
dc.contributor.nonIdAuthorKwon, Ohsuk-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusMICROBIAL-PRODUCTION-
dc.subject.keywordPlusBOVINE RUMEN-
dc.subject.keywordPlusACID-
dc.subject.keywordPlusGENE-
dc.subject.keywordPlusLACTOSE-
dc.subject.keywordPlusSYSTEM-
dc.subject.keywordPlusIMMOBILIZATION-
dc.subject.keywordPlusPURIFICATION-
dc.subject.keywordPlusDEGRADATION-
Appears in Collection
CBE-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 5 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0