Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum: identification of a likely allosteric domain
Fungal (Penicillium chrysogenum) and yeast (Saccharomyces cerevisiae) ATP sulfurylases were shown to have very similar kinetic and chemical properties except that the fungal enzyme (a) contains a highly reactive Cys residue (SH-1) whose modification results in sigmoidal velocity curves (Renosto, F.,...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-08, Vol.269 (31), p.19777-19786 |
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| creator | Foster, B.A. (University of California, Davis, CA.) Thomas, S.M Mahr, J.A Renosto, F Patel, H.C Segel, I.H |
| description | Fungal (Penicillium chrysogenum) and yeast (Saccharomyces cerevisiae) ATP sulfurylases were shown to have very similar kinetic
and chemical properties except that the fungal enzyme (a) contains a highly reactive Cys residue (SH-1) whose modification
results in sigmoidal velocity curves (Renosto, F., Martin, R. L., and Segel, I. H. (1987) J. Biol. Chem. 262, 16279-16288)
and (b) is allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS), while the yeast enzyme displays neither
of these properties. The fungal enzyme subunit (64.3 kDa, 572 amino acids) is also larger than the yeast enzyme subunit (59.3
kDa, 521 amino acids). To correlate the unique allosteric properties of the fungal enzyme with specific structural features,
we cloned and sequenced the ATP sulfurylase gene (aps) from P. chrysogenum. The yeast and fungal enzymes are homologous over
the first 400 amino acids and contain two regions high in basic residues which are conserved in sulfurylases from Arabidopsis
and the Riftia pachyptila (hydrothermal vent tube worm) chemolithotrophic symbiont. These regions may participate in forming
the binding sites for MgATP2- and SO4(2-). The fungal enzyme has no sites for MgATP2- and SO4(2-). The fungal enzyme has no
significant sequence homology to the yeast enzyme in the C-terminal 172 amino acids. This C-terminal region contains SH-1
(Cys-508) and has homology to MET14 (S. cerevisiae), CYSC (E. coli), and NODQ (Rhizobium meliloti), i.e. adenosine 5'-phosphosulfate
(APS) kinase. The cumulative results suggest that (a) the allosteric PAPS binding site of P. chrysogenum ATP sulfurylase is
located in the C-terminal domain of the protein and (b) that this domain may have evolved from APS kinase. In spite of the
homology, this C-terminal region does not account for the APS kinase activity of P. chrysogenum. Fungal ATP sulfurylase has
no significant homology to (or regulatory properties in common with) CYSD or CYSN, proteins reported to comprise E. coli ATP
sulfurylase (Leyh, T., Vogt, T. F., and Suo, Y. (1992) J. Biol. Chem. 267, 10405-10410). |
| doi_str_mv | 10.1016/S0021-9258(17)32088-4 |
| format | Article |
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and chemical properties except that the fungal enzyme (a) contains a highly reactive Cys residue (SH-1) whose modification
results in sigmoidal velocity curves (Renosto, F., Martin, R. L., and Segel, I. H. (1987) J. Biol. Chem. 262, 16279-16288)
and (b) is allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS), while the yeast enzyme displays neither
of these properties. The fungal enzyme subunit (64.3 kDa, 572 amino acids) is also larger than the yeast enzyme subunit (59.3
kDa, 521 amino acids). To correlate the unique allosteric properties of the fungal enzyme with specific structural features,
we cloned and sequenced the ATP sulfurylase gene (aps) from P. chrysogenum. The yeast and fungal enzymes are homologous over
the first 400 amino acids and contain two regions high in basic residues which are conserved in sulfurylases from Arabidopsis
and the Riftia pachyptila (hydrothermal vent tube worm) chemolithotrophic symbiont. These regions may participate in forming
the binding sites for MgATP2- and SO4(2-). The fungal enzyme has no sites for MgATP2- and SO4(2-). The fungal enzyme has no
significant sequence homology to the yeast enzyme in the C-terminal 172 amino acids. This C-terminal region contains SH-1
(Cys-508) and has homology to MET14 (S. cerevisiae), CYSC (E. coli), and NODQ (Rhizobium meliloti), i.e. adenosine 5'-phosphosulfate
(APS) kinase. The cumulative results suggest that (a) the allosteric PAPS binding site of P. chrysogenum ATP sulfurylase is
located in the C-terminal domain of the protein and (b) that this domain may have evolved from APS kinase. In spite of the
homology, this C-terminal region does not account for the APS kinase activity of P. chrysogenum. Fungal ATP sulfurylase has
no significant homology to (or regulatory properties in common with) CYSD or CYSN, proteins reported to comprise E. coli ATP
sulfurylase (Leyh, T., Vogt, T. F., and Suo, Y. (1992) J. Biol. Chem. 267, 10405-10410).</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)32088-4</identifier><identifier>PMID: 8051058</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; ADENOSINA ; ADENOSINE ; Allosteric Site ; Amino Acid Sequence ; AMINO ACID SEQUENCES ; Analytical, structural and metabolic biochemistry ; APS GENE ; Base Sequence ; BINDING SITES ; Biological and medical sciences ; BIOLOGICAL DIFFERENCES ; CHEMICAL COMPOSITION ; Cloning, Molecular ; COMPARISONS ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; DERIVATIVES ; DIFERENCIAS BIOLOGICAS ; DIFFERENCE BIOLOGIQUE ; DNA, Fungal ; Enzymes and enzyme inhibitors ; ENZYMIC ACTIVITY ; Fundamental and applied biological sciences. Psychology ; GENBANK/U07353 ; GENE ; GENES ; Guanosine Triphosphate - metabolism ; INTRONS ; KINASES ; Kinetics ; MOLECULAR SEQUENCE DATA ; NUCLEOTIDE SEQUENCE ; PENICILLIUM CHRYSOGENUM ; Penicillium chrysogenum - enzymology ; Penicillium chrysogenum - genetics ; REGULATORY SEQUENCES ; SACCHAROMYCES CEREVISIAE ; SECUENCIA NUCLEOTIDICA ; Sequence Homology, Amino Acid ; SEQUENCE NUCLEOTIDIQUE ; SPECIES DIFFERENCES ; STRUCTURAL GENES ; Sulfate Adenylyltransferase - antagonists & inhibitors ; Sulfate Adenylyltransferase - genetics ; Sulfate Adenylyltransferase - metabolism ; TRANSFERASAS ; TRANSFERASE ; TRANSFERASES</subject><ispartof>The Journal of biological chemistry, 1994-08, Vol.269 (31), p.19777-19786</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c431t-6a3102e8ffd855ffa2512f2230e5f05d9efb7fb0ca7499f6b1cc9351c73e79313</citedby><cites>FETCH-LOGICAL-c431t-6a3102e8ffd855ffa2512f2230e5f05d9efb7fb0ca7499f6b1cc9351c73e79313</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4246493$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8051058$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Foster, B.A. (University of California, Davis, CA.)</creatorcontrib><creatorcontrib>Thomas, S.M</creatorcontrib><creatorcontrib>Mahr, J.A</creatorcontrib><creatorcontrib>Renosto, F</creatorcontrib><creatorcontrib>Patel, H.C</creatorcontrib><creatorcontrib>Segel, I.H</creatorcontrib><title>Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum: identification of a likely allosteric domain</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Fungal (Penicillium chrysogenum) and yeast (Saccharomyces cerevisiae) ATP sulfurylases were shown to have very similar kinetic
and chemical properties except that the fungal enzyme (a) contains a highly reactive Cys residue (SH-1) whose modification
results in sigmoidal velocity curves (Renosto, F., Martin, R. L., and Segel, I. H. (1987) J. Biol. Chem. 262, 16279-16288)
and (b) is allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS), while the yeast enzyme displays neither
of these properties. The fungal enzyme subunit (64.3 kDa, 572 amino acids) is also larger than the yeast enzyme subunit (59.3
kDa, 521 amino acids). To correlate the unique allosteric properties of the fungal enzyme with specific structural features,
we cloned and sequenced the ATP sulfurylase gene (aps) from P. chrysogenum. The yeast and fungal enzymes are homologous over
the first 400 amino acids and contain two regions high in basic residues which are conserved in sulfurylases from Arabidopsis
and the Riftia pachyptila (hydrothermal vent tube worm) chemolithotrophic symbiont. These regions may participate in forming
the binding sites for MgATP2- and SO4(2-). The fungal enzyme has no sites for MgATP2- and SO4(2-). The fungal enzyme has no
significant sequence homology to the yeast enzyme in the C-terminal 172 amino acids. This C-terminal region contains SH-1
(Cys-508) and has homology to MET14 (S. cerevisiae), CYSC (E. coli), and NODQ (Rhizobium meliloti), i.e. adenosine 5'-phosphosulfate
(APS) kinase. The cumulative results suggest that (a) the allosteric PAPS binding site of P. chrysogenum ATP sulfurylase is
located in the C-terminal domain of the protein and (b) that this domain may have evolved from APS kinase. In spite of the
homology, this C-terminal region does not account for the APS kinase activity of P. chrysogenum. Fungal ATP sulfurylase has
no significant homology to (or regulatory properties in common with) CYSD or CYSN, proteins reported to comprise E. coli ATP
sulfurylase (Leyh, T., Vogt, T. F., and Suo, Y. (1992) J. Biol. Chem. 267, 10405-10410).</description><subject>3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>ADENOSINA</subject><subject>ADENOSINE</subject><subject>Allosteric Site</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACID SEQUENCES</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>APS GENE</subject><subject>Base Sequence</subject><subject>BINDING SITES</subject><subject>Biological and medical sciences</subject><subject>BIOLOGICAL DIFFERENCES</subject><subject>CHEMICAL COMPOSITION</subject><subject>Cloning, Molecular</subject><subject>COMPARISONS</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>DERIVATIVES</subject><subject>DIFERENCIAS BIOLOGICAS</subject><subject>DIFFERENCE BIOLOGIQUE</subject><subject>DNA, Fungal</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ENZYMIC ACTIVITY</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENBANK/U07353</subject><subject>GENE</subject><subject>GENES</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>INTRONS</subject><subject>KINASES</subject><subject>Kinetics</subject><subject>MOLECULAR SEQUENCE DATA</subject><subject>NUCLEOTIDE SEQUENCE</subject><subject>PENICILLIUM CHRYSOGENUM</subject><subject>Penicillium chrysogenum - enzymology</subject><subject>Penicillium chrysogenum - genetics</subject><subject>REGULATORY SEQUENCES</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>SECUENCIA NUCLEOTIDICA</subject><subject>Sequence Homology, Amino Acid</subject><subject>SEQUENCE NUCLEOTIDIQUE</subject><subject>SPECIES DIFFERENCES</subject><subject>STRUCTURAL GENES</subject><subject>Sulfate Adenylyltransferase - antagonists & inhibitors</subject><subject>Sulfate Adenylyltransferase - genetics</subject><subject>Sulfate Adenylyltransferase - metabolism</subject><subject>TRANSFERASAS</subject><subject>TRANSFERASE</subject><subject>TRANSFERASES</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkF1rHCEUhqW0pNu0PyHgRSntxbQeHUftXVj6BYEGkkDvxHF019bRVGco--87kywbbw5ynvcczoPQBZCPQKD7dEMIhUZRLt-D-MAokbJpn6ENEMkaxuHXc7Q5IS_Rq1p_k-W1Cs7QmSQcCJcbNG1jTiHtsEkDru7v7JJdv9njy9trXOfo53KIpjrsSx7xtUvBhhjDPGK7L4eady7N42ccBpem4IM1U8hpzRscwx8XD9jEmOvkSrB4yKMJ6TV64U2s7s2xnqO7r19ut9-bq5_ffmwvrxrbMpiazjAg1EnvB8m594ZyoJ5SRhz3hA_K-V74nlgjWqV814O1arncCuaEYsDO0bvHufclL5fVSY-hWhejSS7PVYuuYyD5CvJH0JZca3Fe35cwmnLQQPRqWz_Y1qtKDUI_2Nbtkrs4Lpj70Q2n1FHv0n977JtqTfTFLHbrCWtp27WKPWH7sNv_C8XpPmS7d6OmndIMNCghxNM2b7I2u7JMursBpQThggnO_gOX3p4F</recordid><startdate>19940805</startdate><enddate>19940805</enddate><creator>Foster, B.A. (University of California, Davis, CA.)</creator><creator>Thomas, S.M</creator><creator>Mahr, J.A</creator><creator>Renosto, F</creator><creator>Patel, H.C</creator><creator>Segel, I.H</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</scope><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>7X8</scope></search><sort><creationdate>19940805</creationdate><title>Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum: identification of a likely allosteric domain</title><author>Foster, B.A. (University of California, Davis, CA.) ; Thomas, S.M ; Mahr, J.A ; Renosto, F ; Patel, H.C ; Segel, I.H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-6a3102e8ffd855ffa2512f2230e5f05d9efb7fb0ca7499f6b1cc9351c73e79313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>ADENOSINA</topic><topic>ADENOSINE</topic><topic>Allosteric Site</topic><topic>Amino Acid Sequence</topic><topic>AMINO ACID SEQUENCES</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>APS GENE</topic><topic>Base Sequence</topic><topic>BINDING SITES</topic><topic>Biological and medical sciences</topic><topic>BIOLOGICAL DIFFERENCES</topic><topic>CHEMICAL COMPOSITION</topic><topic>Cloning, Molecular</topic><topic>COMPARISONS</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>DERIVATIVES</topic><topic>DIFERENCIAS BIOLOGICAS</topic><topic>DIFFERENCE BIOLOGIQUE</topic><topic>DNA, Fungal</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ENZYMIC ACTIVITY</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENBANK/U07353</topic><topic>GENE</topic><topic>GENES</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>INTRONS</topic><topic>KINASES</topic><topic>Kinetics</topic><topic>MOLECULAR SEQUENCE DATA</topic><topic>NUCLEOTIDE SEQUENCE</topic><topic>PENICILLIUM CHRYSOGENUM</topic><topic>Penicillium chrysogenum - enzymology</topic><topic>Penicillium chrysogenum - genetics</topic><topic>REGULATORY SEQUENCES</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>SECUENCIA NUCLEOTIDICA</topic><topic>Sequence Homology, Amino Acid</topic><topic>SEQUENCE NUCLEOTIDIQUE</topic><topic>SPECIES DIFFERENCES</topic><topic>STRUCTURAL GENES</topic><topic>Sulfate Adenylyltransferase - antagonists & inhibitors</topic><topic>Sulfate Adenylyltransferase - genetics</topic><topic>Sulfate Adenylyltransferase - metabolism</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>TRANSFERASES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Foster, B.A. (University of California, Davis, CA.)</creatorcontrib><creatorcontrib>Thomas, S.M</creatorcontrib><creatorcontrib>Mahr, J.A</creatorcontrib><creatorcontrib>Renosto, F</creatorcontrib><creatorcontrib>Patel, H.C</creatorcontrib><creatorcontrib>Segel, I.H</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Foster, B.A. (University of California, Davis, CA.)</au><au>Thomas, S.M</au><au>Mahr, J.A</au><au>Renosto, F</au><au>Patel, H.C</au><au>Segel, I.H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum: identification of a likely allosteric domain</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-08-05</date><risdate>1994</risdate><volume>269</volume><issue>31</issue><spage>19777</spage><epage>19786</epage><pages>19777-19786</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Fungal (Penicillium chrysogenum) and yeast (Saccharomyces cerevisiae) ATP sulfurylases were shown to have very similar kinetic
and chemical properties except that the fungal enzyme (a) contains a highly reactive Cys residue (SH-1) whose modification
results in sigmoidal velocity curves (Renosto, F., Martin, R. L., and Segel, I. H. (1987) J. Biol. Chem. 262, 16279-16288)
and (b) is allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS), while the yeast enzyme displays neither
of these properties. The fungal enzyme subunit (64.3 kDa, 572 amino acids) is also larger than the yeast enzyme subunit (59.3
kDa, 521 amino acids). To correlate the unique allosteric properties of the fungal enzyme with specific structural features,
we cloned and sequenced the ATP sulfurylase gene (aps) from P. chrysogenum. The yeast and fungal enzymes are homologous over
the first 400 amino acids and contain two regions high in basic residues which are conserved in sulfurylases from Arabidopsis
and the Riftia pachyptila (hydrothermal vent tube worm) chemolithotrophic symbiont. These regions may participate in forming
the binding sites for MgATP2- and SO4(2-). The fungal enzyme has no sites for MgATP2- and SO4(2-). The fungal enzyme has no
significant sequence homology to the yeast enzyme in the C-terminal 172 amino acids. This C-terminal region contains SH-1
(Cys-508) and has homology to MET14 (S. cerevisiae), CYSC (E. coli), and NODQ (Rhizobium meliloti), i.e. adenosine 5'-phosphosulfate
(APS) kinase. The cumulative results suggest that (a) the allosteric PAPS binding site of P. chrysogenum ATP sulfurylase is
located in the C-terminal domain of the protein and (b) that this domain may have evolved from APS kinase. In spite of the
homology, this C-terminal region does not account for the APS kinase activity of P. chrysogenum. Fungal ATP sulfurylase has
no significant homology to (or regulatory properties in common with) CYSD or CYSN, proteins reported to comprise E. coli ATP
sulfurylase (Leyh, T., Vogt, T. F., and Suo, Y. (1992) J. Biol. Chem. 267, 10405-10410).</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8051058</pmid><doi>10.1016/S0021-9258(17)32088-4</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | The Journal of biological chemistry, 1994-08, Vol.269 (31), p.19777-19786 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76631851 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ADENOSINA ADENOSINE Allosteric Site Amino Acid Sequence AMINO ACID SEQUENCES Analytical, structural and metabolic biochemistry APS GENE Base Sequence BINDING SITES Biological and medical sciences BIOLOGICAL DIFFERENCES CHEMICAL COMPOSITION Cloning, Molecular COMPARISONS COMPOSICION QUIMICA COMPOSITION CHIMIQUE DERIVATIVES DIFERENCIAS BIOLOGICAS DIFFERENCE BIOLOGIQUE DNA, Fungal Enzymes and enzyme inhibitors ENZYMIC ACTIVITY Fundamental and applied biological sciences. Psychology GENBANK/U07353 GENE GENES Guanosine Triphosphate - metabolism INTRONS KINASES Kinetics MOLECULAR SEQUENCE DATA NUCLEOTIDE SEQUENCE PENICILLIUM CHRYSOGENUM Penicillium chrysogenum - enzymology Penicillium chrysogenum - genetics REGULATORY SEQUENCES SACCHAROMYCES CEREVISIAE SECUENCIA NUCLEOTIDICA Sequence Homology, Amino Acid SEQUENCE NUCLEOTIDIQUE SPECIES DIFFERENCES STRUCTURAL GENES Sulfate Adenylyltransferase - antagonists & inhibitors Sulfate Adenylyltransferase - genetics Sulfate Adenylyltransferase - metabolism TRANSFERASAS TRANSFERASE TRANSFERASES |
| title | Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum: identification of a likely allosteric domain |
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