Nucleotide sequence of the melA gene, coding for α-galactosidase in Escherichia coli K-12
Melibiose uptake and hydrolysis in E.coli is performed by the MelB and MelA proteins, respectively. We report the cloning and sequencing of the melA gene. The nucleotide sequence data showed that melA codes for a 450 amino acid long protein with a molecular weight of 50.6 kd. The sequence data also...
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| Veröffentlicht in: | Nucleic acids research 1987-03, Vol.15 (5), p.2213-2220 |
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| container_title | Nucleic acids research |
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| creator | Liljestoüm, Pirkko L. Liljestrom, Peter |
| description | Melibiose uptake and hydrolysis in E.coli is performed by the MelB and MelA proteins, respectively. We report the cloning and sequencing of the melA gene. The nucleotide sequence data showed that melA codes for a 450 amino acid long protein with a molecular weight of 50.6 kd. The sequence data also supported the assumption that the mel locus forms an operon with melA in proximal position. A comparison of MelA with alpha-galactosidase proteins from yeast and human origin showed that these proteins have only limited homology, the yeast and human proteins being more related. However, regions common to all three proteins were found indicating sequences that might comprise the active site of alpha-galactosidase. |
| doi_str_mv | 10.1093/nar/15.5.2213 |
| format | Article |
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We report the cloning and sequencing of the melA gene. The nucleotide sequence data showed that melA codes for a 450 amino acid long protein with a molecular weight of 50.6 kd. The sequence data also supported the assumption that the mel locus forms an operon with melA in proximal position. A comparison of MelA with alpha-galactosidase proteins from yeast and human origin showed that these proteins have only limited homology, the yeast and human proteins being more related. However, regions common to all three proteins were found indicating sequences that might comprise the active site of alpha-galactosidase.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/15.5.2213</identifier><identifier>PMID: 3031590</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>alpha-Galactosidase - genetics ; Amino Acid Sequence ; Bacteriology ; Base Sequence ; Biological and medical sciences ; Cloning, Molecular ; Codon ; DNA Restriction Enzymes ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Fundamental and applied biological sciences. 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We report the cloning and sequencing of the melA gene. The nucleotide sequence data showed that melA codes for a 450 amino acid long protein with a molecular weight of 50.6 kd. The sequence data also supported the assumption that the mel locus forms an operon with melA in proximal position. A comparison of MelA with alpha-galactosidase proteins from yeast and human origin showed that these proteins have only limited homology, the yeast and human proteins being more related. However, regions common to all three proteins were found indicating sequences that might comprise the active site of alpha-galactosidase.</description><subject>alpha-Galactosidase - genetics</subject><subject>Amino Acid Sequence</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>Codon</subject><subject>DNA Restriction Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactosidases - genetics</subject><subject>Genes</subject><subject>Genes, Bacterial</subject><subject>Genetic Complementation Test</subject><subject>Genetics</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0c9uVCEUBnBiNHVaXbo0YWFc9U6BA9zLwkXT1D9poxvduCEM9zCDYaDCHRMfyxfpM3mbTiZ2VVcsvt8hcD5CXnG25MzAWXb1jKulWgrB4QlZcNCik0aLp2TBgKmOMzk8J8et_WCMS67kETkCBlwZtiDfP-98wjLFEWnDnzvMHmkJdNog3WI6p2vMeEp9GWNe01Aqvf3TrV1yfiotjq4hjZleNr_BGv0mupmmSK86Ll6QZ8Glhi_35wn59v7y68XH7vrLh08X59edlwBTF3phmGPouV4pNnomR2-MGVDgoAfQwbARgAtg2okgBjmi0rByvhdh5MzDCXl3f-_NbrXF0WOeqkv2psatq79tcdE-THLc2HX5ZUEyLYZ5_u1-vpZ5AW2y29g8puQyll2zfS-1Fv8BudEg9NA_DpUA0JrPsLuHvpbWKobDqzmzd-3aud2ZW2Xv2p3963-_etD7Ouf8zT53zbsUqss-tgPrpewVKPgLt2-tRA</recordid><startdate>19870311</startdate><enddate>19870311</enddate><creator>Liljestoüm, Pirkko L.</creator><creator>Liljestrom, Peter</creator><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>M7N</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19870311</creationdate><title>Nucleotide sequence of the melA gene, coding for α-galactosidase in Escherichia coli K-12</title><author>Liljestoüm, Pirkko L. ; Liljestrom, Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c433t-f7290a0ec16b50dc04dc9998e2e86836f90d3312306a2f284de563bac72fd10c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>alpha-Galactosidase - genetics</topic><topic>Amino Acid Sequence</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>Codon</topic><topic>DNA Restriction Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactosidases - genetics</topic><topic>Genes</topic><topic>Genes, Bacterial</topic><topic>Genetic Complementation Test</topic><topic>Genetics</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liljestoüm, Pirkko L.</creatorcontrib><creatorcontrib>Liljestrom, Peter</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liljestoüm, Pirkko L.</au><au>Liljestrom, Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nucleotide sequence of the melA gene, coding for α-galactosidase in Escherichia coli K-12</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>1987-03-11</date><risdate>1987</risdate><volume>15</volume><issue>5</issue><spage>2213</spage><epage>2220</epage><pages>2213-2220</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>Melibiose uptake and hydrolysis in E.coli is performed by the MelB and MelA proteins, respectively. We report the cloning and sequencing of the melA gene. The nucleotide sequence data showed that melA codes for a 450 amino acid long protein with a molecular weight of 50.6 kd. The sequence data also supported the assumption that the mel locus forms an operon with melA in proximal position. A comparison of MelA with alpha-galactosidase proteins from yeast and human origin showed that these proteins have only limited homology, the yeast and human proteins being more related. However, regions common to all three proteins were found indicating sequences that might comprise the active site of alpha-galactosidase.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>3031590</pmid><doi>10.1093/nar/15.5.2213</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Nucleic acids research, 1987-03, Vol.15 (5), p.2213-2220 |
| issn | 0305-1048 1362-4962 |
| language | eng |
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| source | MEDLINE; Oxford University Press Journals Digital Archive Legacy; PubMed Central |
| subjects | alpha-Galactosidase - genetics Amino Acid Sequence Bacteriology Base Sequence Biological and medical sciences Cloning, Molecular Codon DNA Restriction Enzymes Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Galactosidases - genetics Genes Genes, Bacterial Genetic Complementation Test Genetics Microbiology Molecular Weight |
| title | Nucleotide sequence of the melA gene, coding for α-galactosidase in Escherichia coli K-12 |
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