DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Eun-Gyeong | ko |
dc.contributor.author | Kim, Seonghun | ko |
dc.contributor.author | Oh, Doo-Byoung | ko |
dc.contributor.author | Lee, Sang Yup | ko |
dc.contributor.author | Kwon, Ohsuk | ko |
dc.date.accessioned | 2013-03-11T00:38:39Z | - |
dc.date.available | 2013-03-11T00:38:39Z | - |
dc.date.created | 2012-03-07 | - |
dc.date.created | 2012-03-07 | - |
dc.date.created | 2012-03-07 | - |
dc.date.created | 2012-03-07 | - |
dc.date.issued | 2012-01 | - |
dc.identifier.citation | JOURNAL OF BACTERIOLOGY, v.194, no.2, pp.426 - 436 | - |
dc.identifier.issn | 0021-9193 | - |
dc.identifier.uri | http://hdl.handle.net/10203/97822 | - |
dc.description.abstract | Mannheimia 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.language | English | - |
dc.publisher | AMER SOC MICROBIOLOGY | - |
dc.title | Distinct Roles of beta-Galactosidase Paralogues of the Rumen Bacterium Mannheimia succiniciproducens | - |
dc.type | Article | - |
dc.identifier.wosid | 000298677400025 | - |
dc.identifier.scopusid | 2-s2.0-84862942747 | - |
dc.type.rims | ART | - |
dc.citation.volume | 194 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 426 | - |
dc.citation.endingpage | 436 | - |
dc.citation.publicationname | JOURNAL OF BACTERIOLOGY | - |
dc.identifier.doi | 10.1128/JB.05911-11 | - |
dc.contributor.localauthor | Lee, Sang Yup | - |
dc.contributor.nonIdAuthor | Lee, Eun-Gyeong | - |
dc.contributor.nonIdAuthor | Kim, Seonghun | - |
dc.contributor.nonIdAuthor | Oh, Doo-Byoung | - |
dc.contributor.nonIdAuthor | Kwon, Ohsuk | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | MICROBIAL-PRODUCTION | - |
dc.subject.keywordPlus | BOVINE RUMEN | - |
dc.subject.keywordPlus | ACID | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | LACTOSE | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | IMMOBILIZATION | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | DEGRADATION | - |
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