Primary structure and tetrahydropteroylglutamate binding site of rabbit liver cytosolic 5,10-methenyltetrahydrofolate synthetase
The primary sequence of 5,10-methenyltetrahydrofolate synthetase from rabbit liver was determined by amino acid sequencing of the purified enzyme. The enzyme contains 201 amino acid residues with a predicted mass of 22,779 Da. The enzyme is located in the cytosolic fraction of liver homogenates. Car...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-07, Vol.269 (28), p.18429-18433 |
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| container_title | The Journal of biological chemistry |
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| creator | MARAS, B STOVER, P VALIANTE, S BARRA, D SCHIRCH, V |
| description | The primary sequence of 5,10-methenyltetrahydrofolate synthetase from rabbit liver was determined by amino acid sequencing
of the purified enzyme. The enzyme contains 201 amino acid residues with a predicted mass of 22,779 Da. The enzyme is located
in the cytosolic fraction of liver homogenates. Carbodiimide-activated 5-formyltetrahydropteroylmonoglutamate and the pentaglutamate
form of the substrate both irreversibly inactivate the enzyme by forming a covalent bond to Lys-18. Non-activated 5-formyltetrahydropteroylpentaglutamate
protected against this inactivation. Substrate specificity studies showed that increasing the number of glutamate residues
from zero to five on 5-formyltetrahydropteroate results in a 2 order of magnitude increase in the affinity of the substrate
for the enzyme but only a 3-fold increase in the value of Vmax. |
| doi_str_mv | 10.1016/S0021-9258(17)32326-8 |
| format | Article |
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of the purified enzyme. The enzyme contains 201 amino acid residues with a predicted mass of 22,779 Da. The enzyme is located
in the cytosolic fraction of liver homogenates. Carbodiimide-activated 5-formyltetrahydropteroylmonoglutamate and the pentaglutamate
form of the substrate both irreversibly inactivate the enzyme by forming a covalent bond to Lys-18. Non-activated 5-formyltetrahydropteroylpentaglutamate
protected against this inactivation. Substrate specificity studies showed that increasing the number of glutamate residues
from zero to five on 5-formyltetrahydropteroate results in a 2 order of magnitude increase in the affinity of the substrate
for the enzyme but only a 3-fold increase in the value of Vmax.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)32326-8</identifier><identifier>PMID: 8034591</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Binding Sites ; Biological and medical sciences ; Carbon-Nitrogen Ligases ; Cyanogen Bromide ; Cytosol - enzymology ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; L-Lactate Dehydrogenase - metabolism ; Ligases - chemistry ; Ligases - isolation & purification ; Ligases - metabolism ; Liver - enzymology ; Mass Spectrometry ; Miscellaneous ; Mitochondria, Liver - enzymology ; Molecular Sequence Data ; Peptide Fragments - chemistry ; Peptide Fragments - isolation & purification ; Rabbits ; Substrate Specificity ; Succinate Cytochrome c Oxidoreductase - metabolism ; Tetrahydrofolates - metabolism ; Trypsin</subject><ispartof>The Journal of biological chemistry, 1994-07, Vol.269 (28), p.18429-18433</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-92089c3c5408fea1650aca7e3323aa8de946f241fec004394381660e1c61620e3</citedby><cites>FETCH-LOGICAL-c409t-92089c3c5408fea1650aca7e3323aa8de946f241fec004394381660e1c61620e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4235063$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8034591$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MARAS, B</creatorcontrib><creatorcontrib>STOVER, P</creatorcontrib><creatorcontrib>VALIANTE, S</creatorcontrib><creatorcontrib>BARRA, D</creatorcontrib><creatorcontrib>SCHIRCH, V</creatorcontrib><title>Primary structure and tetrahydropteroylglutamate binding site of rabbit liver cytosolic 5,10-methenyltetrahydrofolate synthetase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The primary sequence of 5,10-methenyltetrahydrofolate synthetase from rabbit liver was determined by amino acid sequencing
of the purified enzyme. The enzyme contains 201 amino acid residues with a predicted mass of 22,779 Da. The enzyme is located
in the cytosolic fraction of liver homogenates. Carbodiimide-activated 5-formyltetrahydropteroylmonoglutamate and the pentaglutamate
form of the substrate both irreversibly inactivate the enzyme by forming a covalent bond to Lys-18. Non-activated 5-formyltetrahydropteroylpentaglutamate
protected against this inactivation. Substrate specificity studies showed that increasing the number of glutamate residues
from zero to five on 5-formyltetrahydropteroate results in a 2 order of magnitude increase in the affinity of the substrate
for the enzyme but only a 3-fold increase in the value of Vmax.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Carbon-Nitrogen Ligases</subject><subject>Cyanogen Bromide</subject><subject>Cytosol - enzymology</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>L-Lactate Dehydrogenase - metabolism</subject><subject>Ligases - chemistry</subject><subject>Ligases - isolation & purification</subject><subject>Ligases - metabolism</subject><subject>Liver - enzymology</subject><subject>Mass Spectrometry</subject><subject>Miscellaneous</subject><subject>Mitochondria, Liver - enzymology</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - isolation & purification</subject><subject>Rabbits</subject><subject>Substrate Specificity</subject><subject>Succinate Cytochrome c Oxidoreductase - metabolism</subject><subject>Tetrahydrofolates - metabolism</subject><subject>Trypsin</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>eNpFkF-L1DAUxYMo6-zqR1jog4iC1fyf5FEWXYUFBRV8C2l6O42kzZikSt_86GZ2htm8XMI591zOD6Frgt8STOS7bxhT0moq1Cuyfc0oo7JVj9CGYMVaJsjPx2hztjxFlzn_wvVxTS7QhcKMC0026N_X5Ceb1iaXtLiyJGjs3DcFSrLj2qe4L5DiGnZhKXayBZrOz72fd0329ROHJtmu86UJ_g-kxq0l5hi8a8QbgtsJygjzGh7ihhgOIXmdq1JshmfoyWBDhueneYV-fPzw_eZTe_fl9vPN-7vWcaxLLYGVdswJjtUAlkiBrbNbYLW4taoHzeVAORnA1Y5Mc6aIlBiIk0RSDOwKvTzm7lP8vUAuZvLZQQh2hrhks5VCEU1ENYqj0aWYc4LB7I-IDMHmQN7ckzcHrIZszT15o-re9enA0k3Qn7dOqKv-4qTb7GwYkp2dz2cbp0xgyR5so9-Nf30C0_noRpgMldrQelJxqtl_He-aTg</recordid><startdate>19940715</startdate><enddate>19940715</enddate><creator>MARAS, B</creator><creator>STOVER, P</creator><creator>VALIANTE, S</creator><creator>BARRA, D</creator><creator>SCHIRCH, V</creator><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>19940715</creationdate><title>Primary structure and tetrahydropteroylglutamate binding site of rabbit liver cytosolic 5,10-methenyltetrahydrofolate synthetase</title><author>MARAS, B ; STOVER, P ; VALIANTE, S ; BARRA, D ; SCHIRCH, V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-92089c3c5408fea1650aca7e3323aa8de946f241fec004394381660e1c61620e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Carbon-Nitrogen Ligases</topic><topic>Cyanogen Bromide</topic><topic>Cytosol - enzymology</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>L-Lactate Dehydrogenase - metabolism</topic><topic>Ligases - chemistry</topic><topic>Ligases - isolation & purification</topic><topic>Ligases - metabolism</topic><topic>Liver - enzymology</topic><topic>Mass Spectrometry</topic><topic>Miscellaneous</topic><topic>Mitochondria, Liver - enzymology</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - isolation & purification</topic><topic>Rabbits</topic><topic>Substrate Specificity</topic><topic>Succinate Cytochrome c Oxidoreductase - metabolism</topic><topic>Tetrahydrofolates - metabolism</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MARAS, B</creatorcontrib><creatorcontrib>STOVER, P</creatorcontrib><creatorcontrib>VALIANTE, S</creatorcontrib><creatorcontrib>BARRA, D</creatorcontrib><creatorcontrib>SCHIRCH, V</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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MARAS, B</au><au>STOVER, P</au><au>VALIANTE, S</au><au>BARRA, D</au><au>SCHIRCH, V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Primary structure and tetrahydropteroylglutamate binding site of rabbit liver cytosolic 5,10-methenyltetrahydrofolate synthetase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-07-15</date><risdate>1994</risdate><volume>269</volume><issue>28</issue><spage>18429</spage><epage>18433</epage><pages>18429-18433</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The primary sequence of 5,10-methenyltetrahydrofolate synthetase from rabbit liver was determined by amino acid sequencing
of the purified enzyme. The enzyme contains 201 amino acid residues with a predicted mass of 22,779 Da. The enzyme is located
in the cytosolic fraction of liver homogenates. Carbodiimide-activated 5-formyltetrahydropteroylmonoglutamate and the pentaglutamate
form of the substrate both irreversibly inactivate the enzyme by forming a covalent bond to Lys-18. Non-activated 5-formyltetrahydropteroylpentaglutamate
protected against this inactivation. Substrate specificity studies showed that increasing the number of glutamate residues
from zero to five on 5-formyltetrahydropteroate results in a 2 order of magnitude increase in the affinity of the substrate
for the enzyme but only a 3-fold increase in the value of Vmax.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8034591</pmid><doi>10.1016/S0021-9258(17)32326-8</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1994-07, Vol.269 (28), p.18429-18433 |
| 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 | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Binding Sites Biological and medical sciences Carbon-Nitrogen Ligases Cyanogen Bromide Cytosol - enzymology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology L-Lactate Dehydrogenase - metabolism Ligases - chemistry Ligases - isolation & purification Ligases - metabolism Liver - enzymology Mass Spectrometry Miscellaneous Mitochondria, Liver - enzymology Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - isolation & purification Rabbits Substrate Specificity Succinate Cytochrome c Oxidoreductase - metabolism Tetrahydrofolates - metabolism Trypsin |
| title | Primary structure and tetrahydropteroylglutamate binding site of rabbit liver cytosolic 5,10-methenyltetrahydrofolate synthetase |
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