Saccharomyces cerevisiae GNA1, an Essential Gene Encoding a Novel Acetyltransferase Involved in UDP-N-acetylglucosamine Synthesis
The Saccharomyces cerevisiae gene,YFL017C, for a putative acetyltransferase was characterized. Disruption of YFL017C was lethal, leading to a morphology similar to those caused by the depletion ofAGM1 or UAP1, the genes encoding phospho-N-acetylglucosamine mutase and UDP-N-acetylglucosamine pyrophos...
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| Veröffentlicht in: | The Journal of biological chemistry 1999-01, Vol.274 (1), p.424-429 |
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| creator | Mio, Toshiyuki Yamada-Okabe, Toshiko Arisawa, Mikio Yamada-Okabe, Hisafumi |
| description | The Saccharomyces cerevisiae gene,YFL017C, for a putative acetyltransferase was characterized. Disruption of YFL017C was lethal, leading to a morphology similar to those caused by the depletion ofAGM1 or UAP1, the genes encoding phospho-N-acetylglucosamine mutase and UDP-N-acetylglucosamine pyrophosphorylase, respectively. This implies the involvement of YFL017C in UDP-N-acetylglucosamine synthesis. The recombinant protein for YFL017C displayed phosphoglucosamine acetyltransferase activities in vitro and utilized glucosamine 6-phosphate as the substrate. When incubated with Agm1p and Uap1p, the Yfl017c protein produced UDP-N-acetylglucosamine from glucosamine 6-phosphate. These results indicate that YFL017C specifies glucosamine-6-phosphate acetyltransferase; therefore, the gene was designated GNA1(glucosamine-6-phosphateacetyltransferase). In addition, whereas bacterial phosphoglucosamine acetyltransferase and UDP-N-acetylglucosamine pyrophosphorylase activities are intrinsic in a single polypeptide, they are encoded by distinct essential genes in yeast. When the sequence of ScGna1p was compared with those of other acetyltransferases, Ile97, Glu98, Val102, Gly112, Leu115, Ile116, Phe142, Tyr143, and Gly147 were found to be highly conserved. When alanine was substituted for these amino acids, the enzyme activity for the substituted Phe142 or Tyr143 enzymes was severely diminished. Although the activity of Y143A was too low to perform kinetics, F142A displayed a significantly increased Km value for acetyl-CoA, suggesting that the Phe142 and Tyr143 residues are essential for the catalysis. |
| doi_str_mv | 10.1074/jbc.274.1.424 |
| format | Article |
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Disruption of YFL017C was lethal, leading to a morphology similar to those caused by the depletion ofAGM1 or UAP1, the genes encoding phospho-N-acetylglucosamine mutase and UDP-N-acetylglucosamine pyrophosphorylase, respectively. This implies the involvement of YFL017C in UDP-N-acetylglucosamine synthesis. The recombinant protein for YFL017C displayed phosphoglucosamine acetyltransferase activities in vitro and utilized glucosamine 6-phosphate as the substrate. When incubated with Agm1p and Uap1p, the Yfl017c protein produced UDP-N-acetylglucosamine from glucosamine 6-phosphate. These results indicate that YFL017C specifies glucosamine-6-phosphate acetyltransferase; therefore, the gene was designated GNA1(glucosamine-6-phosphateacetyltransferase). In addition, whereas bacterial phosphoglucosamine acetyltransferase and UDP-N-acetylglucosamine pyrophosphorylase activities are intrinsic in a single polypeptide, they are encoded by distinct essential genes in yeast. When the sequence of ScGna1p was compared with those of other acetyltransferases, Ile97, Glu98, Val102, Gly112, Leu115, Ile116, Phe142, Tyr143, and Gly147 were found to be highly conserved. When alanine was substituted for these amino acids, the enzyme activity for the substituted Phe142 or Tyr143 enzymes was severely diminished. Although the activity of Y143A was too low to perform kinetics, F142A displayed a significantly increased Km value for acetyl-CoA, suggesting that the Phe142 and Tyr143 residues are essential for the catalysis.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.1.424</identifier><identifier>PMID: 9867860</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetyltransferases - chemistry ; Acetyltransferases - genetics ; Acetyltransferases - metabolism ; ACILTRANSFERASA ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; ACYLTRANSFERASE ; ACYLTRANSFERASES ; Amino Acid Sequence ; AMINO ACID SEQUENCES ; Animals ; Base Sequence ; Binding Sites ; BIOLOGICAL DIFFERENCES ; Catalysis ; CHEMICAL COMPOSITION ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; DIFERENCIAS BIOLOGICAS ; DIFFERENCE BIOLOGIQUE ; ENZYMIC ACTIVITY ; GENBANK/AB017626 ; GENBANK/AB017627 ; GENBANK/AB017628 ; GENBANK/AB017629 ; GENE ; GENES ; Glucosamine 6-Phosphate N-Acetyltransferase ; GNA1 GENE ; Humans ; MOLECULAR SEQUENCE DATA ; MUTACION ; Mutagenesis, Site-Directed ; MUTANT ; MUTANTES ; MUTANTS ; MUTATION ; NUCLEOTIDE SEQUENCE ; PHOSPHOGLUCOSAMINE ; PHOSPHOGLUCOSAMINE ACETYLTRANSFERASE ; SACCHAROMYCES ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins ; SECUENCIA NUCLEOTIDICA ; Sequence Homology, Amino Acid ; SEQUENCE NUCLEOTIDIQUE ; SPECIES DIFFERENCES ; STRUCTURAL GENES ; TARGETED MUTAGENESIS ; Uridine Diphosphate N-Acetylglucosamine - biosynthesis</subject><ispartof>The Journal of biological chemistry, 1999-01, Vol.274 (1), p.424-429</ispartof><rights>1999 © 1999 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-ac3b8d09669d13b6da2896bec6fbc5dd5cbc2c4a7c78609d1e842f8f8228ad353</citedby><cites>FETCH-LOGICAL-c454t-ac3b8d09669d13b6da2896bec6fbc5dd5cbc2c4a7c78609d1e842f8f8228ad353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9867860$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mio, Toshiyuki</creatorcontrib><creatorcontrib>Yamada-Okabe, Toshiko</creatorcontrib><creatorcontrib>Arisawa, Mikio</creatorcontrib><creatorcontrib>Yamada-Okabe, Hisafumi</creatorcontrib><title>Saccharomyces cerevisiae GNA1, an Essential Gene Encoding a Novel Acetyltransferase Involved in UDP-N-acetylglucosamine Synthesis</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The Saccharomyces cerevisiae gene,YFL017C, for a putative acetyltransferase was characterized. Disruption of YFL017C was lethal, leading to a morphology similar to those caused by the depletion ofAGM1 or UAP1, the genes encoding phospho-N-acetylglucosamine mutase and UDP-N-acetylglucosamine pyrophosphorylase, respectively. This implies the involvement of YFL017C in UDP-N-acetylglucosamine synthesis. The recombinant protein for YFL017C displayed phosphoglucosamine acetyltransferase activities in vitro and utilized glucosamine 6-phosphate as the substrate. When incubated with Agm1p and Uap1p, the Yfl017c protein produced UDP-N-acetylglucosamine from glucosamine 6-phosphate. These results indicate that YFL017C specifies glucosamine-6-phosphate acetyltransferase; therefore, the gene was designated GNA1(glucosamine-6-phosphateacetyltransferase). In addition, whereas bacterial phosphoglucosamine acetyltransferase and UDP-N-acetylglucosamine pyrophosphorylase activities are intrinsic in a single polypeptide, they are encoded by distinct essential genes in yeast. When the sequence of ScGna1p was compared with those of other acetyltransferases, Ile97, Glu98, Val102, Gly112, Leu115, Ile116, Phe142, Tyr143, and Gly147 were found to be highly conserved. When alanine was substituted for these amino acids, the enzyme activity for the substituted Phe142 or Tyr143 enzymes was severely diminished. Although the activity of Y143A was too low to perform kinetics, F142A displayed a significantly increased Km value for acetyl-CoA, suggesting that the Phe142 and Tyr143 residues are essential for the catalysis.</description><subject>Acetyltransferases - chemistry</subject><subject>Acetyltransferases - genetics</subject><subject>Acetyltransferases - metabolism</subject><subject>ACILTRANSFERASA</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>ACYLTRANSFERASE</subject><subject>ACYLTRANSFERASES</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACID SEQUENCES</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>BIOLOGICAL DIFFERENCES</subject><subject>Catalysis</subject><subject>CHEMICAL COMPOSITION</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>DIFERENCIAS BIOLOGICAS</subject><subject>DIFFERENCE BIOLOGIQUE</subject><subject>ENZYMIC ACTIVITY</subject><subject>GENBANK/AB017626</subject><subject>GENBANK/AB017627</subject><subject>GENBANK/AB017628</subject><subject>GENBANK/AB017629</subject><subject>GENE</subject><subject>GENES</subject><subject>Glucosamine 6-Phosphate N-Acetyltransferase</subject><subject>GNA1 GENE</subject><subject>Humans</subject><subject>MOLECULAR SEQUENCE DATA</subject><subject>MUTACION</subject><subject>Mutagenesis, Site-Directed</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>MUTANTS</subject><subject>MUTATION</subject><subject>NUCLEOTIDE SEQUENCE</subject><subject>PHOSPHOGLUCOSAMINE</subject><subject>PHOSPHOGLUCOSAMINE ACETYLTRANSFERASE</subject><subject>SACCHAROMYCES</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>SECUENCIA NUCLEOTIDICA</subject><subject>Sequence Homology, Amino Acid</subject><subject>SEQUENCE NUCLEOTIDIQUE</subject><subject>SPECIES DIFFERENCES</subject><subject>STRUCTURAL GENES</subject><subject>TARGETED MUTAGENESIS</subject><subject>Uridine Diphosphate N-Acetylglucosamine - biosynthesis</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kL1vEzEYhy0EKmlhZEQyC1Mv2L4v3xiVECpVASlEYrN8r99LXN3Zxb4cysh_jkMiJvDi4ffokf0Q8oazOWd18eGxhbmoizmfF6J4RmacyTzLS_79OZkxJnjWiFK-JNcxPrJ0ioZfkatGVrWs2Iz82miAvQ5-OAJGChhwstFqpKv1gt9S7egyRnSj1T1doUO6dOCNdTuq6dpP2NMF4Hjsx6Bd7DDoiPTeTb6f0FDr6Pbj12yd6T_Mrj-Aj3qwSbM5unGP0cZX5EWn-4ivL_cN2X5afrv7nD18Wd3fLR4yKMpiTIa8lYY1VdUYnreV0UI2VYtQdS2UxpTQgoBC13D6WGJQFqKTnRRCapOX-Q15f_Y-Bf_jgHFUg42Afa8d-kNUvOZC1FwmMDuDEHyMATv1FOygw1Fxpk7JVUquUnLFVUqe-LcX8aEd0PylL43T_u687-1u_9MGVK31sMfhX45Oe6V3wUa13fCmaRhnVXNy1OcdU6HJYlARLDpAk3wwKuPtf173GxQKpWA</recordid><startdate>19990101</startdate><enddate>19990101</enddate><creator>Mio, Toshiyuki</creator><creator>Yamada-Okabe, Toshiko</creator><creator>Arisawa, Mikio</creator><creator>Yamada-Okabe, Hisafumi</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19990101</creationdate><title>Saccharomyces cerevisiae GNA1, an Essential Gene Encoding a Novel Acetyltransferase Involved in UDP-N-acetylglucosamine Synthesis</title><author>Mio, Toshiyuki ; Yamada-Okabe, Toshiko ; Arisawa, Mikio ; Yamada-Okabe, Hisafumi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-ac3b8d09669d13b6da2896bec6fbc5dd5cbc2c4a7c78609d1e842f8f8228ad353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Acetyltransferases - chemistry</topic><topic>Acetyltransferases - genetics</topic><topic>Acetyltransferases - metabolism</topic><topic>ACILTRANSFERASA</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>ACYLTRANSFERASE</topic><topic>ACYLTRANSFERASES</topic><topic>Amino Acid Sequence</topic><topic>AMINO ACID SEQUENCES</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>BIOLOGICAL DIFFERENCES</topic><topic>Catalysis</topic><topic>CHEMICAL COMPOSITION</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>DIFERENCIAS BIOLOGICAS</topic><topic>DIFFERENCE BIOLOGIQUE</topic><topic>ENZYMIC ACTIVITY</topic><topic>GENBANK/AB017626</topic><topic>GENBANK/AB017627</topic><topic>GENBANK/AB017628</topic><topic>GENBANK/AB017629</topic><topic>GENE</topic><topic>GENES</topic><topic>Glucosamine 6-Phosphate N-Acetyltransferase</topic><topic>GNA1 GENE</topic><topic>Humans</topic><topic>MOLECULAR SEQUENCE DATA</topic><topic>MUTACION</topic><topic>Mutagenesis, Site-Directed</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>MUTANTS</topic><topic>MUTATION</topic><topic>NUCLEOTIDE SEQUENCE</topic><topic>PHOSPHOGLUCOSAMINE</topic><topic>PHOSPHOGLUCOSAMINE ACETYLTRANSFERASE</topic><topic>SACCHAROMYCES</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>SECUENCIA NUCLEOTIDICA</topic><topic>Sequence Homology, Amino Acid</topic><topic>SEQUENCE NUCLEOTIDIQUE</topic><topic>SPECIES DIFFERENCES</topic><topic>STRUCTURAL GENES</topic><topic>TARGETED MUTAGENESIS</topic><topic>Uridine Diphosphate N-Acetylglucosamine - biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mio, Toshiyuki</creatorcontrib><creatorcontrib>Yamada-Okabe, Toshiko</creatorcontrib><creatorcontrib>Arisawa, Mikio</creatorcontrib><creatorcontrib>Yamada-Okabe, Hisafumi</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mio, Toshiyuki</au><au>Yamada-Okabe, Toshiko</au><au>Arisawa, Mikio</au><au>Yamada-Okabe, Hisafumi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Saccharomyces cerevisiae GNA1, an Essential Gene Encoding a Novel Acetyltransferase Involved in UDP-N-acetylglucosamine Synthesis</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-01-01</date><risdate>1999</risdate><volume>274</volume><issue>1</issue><spage>424</spage><epage>429</epage><pages>424-429</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The Saccharomyces cerevisiae gene,YFL017C, for a putative acetyltransferase was characterized. Disruption of YFL017C was lethal, leading to a morphology similar to those caused by the depletion ofAGM1 or UAP1, the genes encoding phospho-N-acetylglucosamine mutase and UDP-N-acetylglucosamine pyrophosphorylase, respectively. This implies the involvement of YFL017C in UDP-N-acetylglucosamine synthesis. The recombinant protein for YFL017C displayed phosphoglucosamine acetyltransferase activities in vitro and utilized glucosamine 6-phosphate as the substrate. When incubated with Agm1p and Uap1p, the Yfl017c protein produced UDP-N-acetylglucosamine from glucosamine 6-phosphate. These results indicate that YFL017C specifies glucosamine-6-phosphate acetyltransferase; therefore, the gene was designated GNA1(glucosamine-6-phosphateacetyltransferase). In addition, whereas bacterial phosphoglucosamine acetyltransferase and UDP-N-acetylglucosamine pyrophosphorylase activities are intrinsic in a single polypeptide, they are encoded by distinct essential genes in yeast. When the sequence of ScGna1p was compared with those of other acetyltransferases, Ile97, Glu98, Val102, Gly112, Leu115, Ile116, Phe142, Tyr143, and Gly147 were found to be highly conserved. When alanine was substituted for these amino acids, the enzyme activity for the substituted Phe142 or Tyr143 enzymes was severely diminished. Although the activity of Y143A was too low to perform kinetics, F142A displayed a significantly increased Km value for acetyl-CoA, suggesting that the Phe142 and Tyr143 residues are essential for the catalysis.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9867860</pmid><doi>10.1074/jbc.274.1.424</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1999-01, Vol.274 (1), p.424-429 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acetyltransferases - chemistry Acetyltransferases - genetics Acetyltransferases - metabolism ACILTRANSFERASA ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ACYLTRANSFERASE ACYLTRANSFERASES Amino Acid Sequence AMINO ACID SEQUENCES Animals Base Sequence Binding Sites BIOLOGICAL DIFFERENCES Catalysis CHEMICAL COMPOSITION COMPOSICION QUIMICA COMPOSITION CHIMIQUE DIFERENCIAS BIOLOGICAS DIFFERENCE BIOLOGIQUE ENZYMIC ACTIVITY GENBANK/AB017626 GENBANK/AB017627 GENBANK/AB017628 GENBANK/AB017629 GENE GENES Glucosamine 6-Phosphate N-Acetyltransferase GNA1 GENE Humans MOLECULAR SEQUENCE DATA MUTACION Mutagenesis, Site-Directed MUTANT MUTANTES MUTANTS MUTATION NUCLEOTIDE SEQUENCE PHOSPHOGLUCOSAMINE PHOSPHOGLUCOSAMINE ACETYLTRANSFERASE SACCHAROMYCES SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins SECUENCIA NUCLEOTIDICA Sequence Homology, Amino Acid SEQUENCE NUCLEOTIDIQUE SPECIES DIFFERENCES STRUCTURAL GENES TARGETED MUTAGENESIS Uridine Diphosphate N-Acetylglucosamine - biosynthesis |
| title | Saccharomyces cerevisiae GNA1, an Essential Gene Encoding a Novel Acetyltransferase Involved in UDP-N-acetylglucosamine Synthesis |
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