The Mg insertion step in chlorophyll biosynthesis
A developing chloroplast preparation obtained from greening cucumber cotyledons is able to bring about the synthesis of Mg-protoporphyrin-IX and/or Mg-protoporphyrin-IX monomethyl ester. l-glutamate, δ-aminolevulinic acid, and protoporphyrin-IX can serve as precursors for Mg-protoporphyrin synthesis...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1979-01, Vol.192 (2), p.592-598 |
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creator | Castelfranco, Paul A. Weinstein, Jon D. Schwarcz, Stephen Pardo, Anthony D. Wezelman, Barbara E. |
description | A developing chloroplast preparation obtained from greening cucumber cotyledons is able to bring about the synthesis of Mg-protoporphyrin-IX and/or Mg-protoporphyrin-IX monomethyl ester.
l-glutamate, δ-aminolevulinic acid, and protoporphyrin-IX can serve as precursors for Mg-protoporphyrin synthesis. However, when δ-aminolevulinic acid or protoporpyrin are used, no Mg-protoporphyrin is formed unless
l-glutamate is also added. Mg-Protoporphyrin synthesis with δ-aminolevulinic acid plus
l-glutamate, or proto-porphyrin plus
l-glutamate, is much more active than with
l-glutamate alone. Therefore, it is apparent that
l-glutamate plays a role in the Mg chelation step in chloroplasts. α-Keto-glutarate can replace
l-glutamate in this role; glutamine cannot. ATP is also required for Mg chelation. The role of
l-glutamate in the Mg insertion step is not yet understood, except that
l-glutamate itself does not need to be converted to porphyrins in this process, because Mg-protoporphyrin can be synthesized from protoporphyrin and
l-glutamate even in the presence of the δ-aminolevulinic acid dehydratase inhibitor, levulinate. |
doi_str_mv | 10.1016/0003-9861(79)90130-9 |
format | Article |
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l-glutamate, δ-aminolevulinic acid, and protoporphyrin-IX can serve as precursors for Mg-protoporphyrin synthesis. However, when δ-aminolevulinic acid or protoporpyrin are used, no Mg-protoporphyrin is formed unless
l-glutamate is also added. Mg-Protoporphyrin synthesis with δ-aminolevulinic acid plus
l-glutamate, or proto-porphyrin plus
l-glutamate, is much more active than with
l-glutamate alone. Therefore, it is apparent that
l-glutamate plays a role in the Mg chelation step in chloroplasts. α-Keto-glutarate can replace
l-glutamate in this role; glutamine cannot. ATP is also required for Mg chelation. The role of
l-glutamate in the Mg insertion step is not yet understood, except that
l-glutamate itself does not need to be converted to porphyrins in this process, because Mg-protoporphyrin can be synthesized from protoporphyrin and
l-glutamate even in the presence of the δ-aminolevulinic acid dehydratase inhibitor, levulinate.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(79)90130-9</identifier><identifier>PMID: 434841</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Aminolevulinic Acid - metabolism ; Chlorophyll - biosynthesis ; Chloroplasts - metabolism ; cucumbers ; Glutamates - metabolism ; Kinetics ; magnesium ; Magnesium - metabolism ; Plants ; Porphyrins - metabolism ; Protoporphyrins - metabolism ; Spectrometry, Fluorescence</subject><ispartof>Archives of biochemistry and biophysics, 1979-01, Vol.192 (2), p.592-598</ispartof><rights>1979</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c403t-914c999d5bdb8a16459dec9da9b549e1bbcd5726d5a464ea1c7f81452aaf52ab3</citedby><cites>FETCH-LOGICAL-c403t-914c999d5bdb8a16459dec9da9b549e1bbcd5726d5a464ea1c7f81452aaf52ab3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(79)90130-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/434841$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Castelfranco, Paul A.</creatorcontrib><creatorcontrib>Weinstein, Jon D.</creatorcontrib><creatorcontrib>Schwarcz, Stephen</creatorcontrib><creatorcontrib>Pardo, Anthony D.</creatorcontrib><creatorcontrib>Wezelman, Barbara E.</creatorcontrib><creatorcontrib>West Indies Univ. St. Augustine (Trinidad and Tobago). Dept. of Soil Science</creatorcontrib><title>The Mg insertion step in chlorophyll biosynthesis</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>A developing chloroplast preparation obtained from greening cucumber cotyledons is able to bring about the synthesis of Mg-protoporphyrin-IX and/or Mg-protoporphyrin-IX monomethyl ester.
l-glutamate, δ-aminolevulinic acid, and protoporphyrin-IX can serve as precursors for Mg-protoporphyrin synthesis. However, when δ-aminolevulinic acid or protoporpyrin are used, no Mg-protoporphyrin is formed unless
l-glutamate is also added. Mg-Protoporphyrin synthesis with δ-aminolevulinic acid plus
l-glutamate, or proto-porphyrin plus
l-glutamate, is much more active than with
l-glutamate alone. Therefore, it is apparent that
l-glutamate plays a role in the Mg chelation step in chloroplasts. α-Keto-glutarate can replace
l-glutamate in this role; glutamine cannot. ATP is also required for Mg chelation. The role of
l-glutamate in the Mg insertion step is not yet understood, except that
l-glutamate itself does not need to be converted to porphyrins in this process, because Mg-protoporphyrin can be synthesized from protoporphyrin and
l-glutamate even in the presence of the δ-aminolevulinic acid dehydratase inhibitor, levulinate.</description><subject>Aminolevulinic Acid - metabolism</subject><subject>Chlorophyll - biosynthesis</subject><subject>Chloroplasts - metabolism</subject><subject>cucumbers</subject><subject>Glutamates - metabolism</subject><subject>Kinetics</subject><subject>magnesium</subject><subject>Magnesium - metabolism</subject><subject>Plants</subject><subject>Porphyrins - metabolism</subject><subject>Protoporphyrins - metabolism</subject><subject>Spectrometry, Fluorescence</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEFL5DAUx4Oo66j7DUR7EvfQNa9J2r6LIKKu4LKH1XNIk1cn0mnGpCPMt7djxYvg5YXH-_3_hB9jR8B_A4fynHMucqxLOKvwF3IQPMctNgOOZc5FLbfZ7BPZY_spPXMOIMviB9uVQtYSZgwe5pT9fcp8nygOPvRZGmg5rpmddyGG5XzddVnjQ1r3w5yST4dspzVdop8f7wF7vLl-uPqT3_-7vbu6vM-t5GLIEaRFRKca19QGSqnQkUVnsFESCZrGOlUVpVNGlpIM2KqtQarCmHYcjThgp1PvMoaXFaVBL3yy1HWmp7BKupJKKFmqEZQTaGNIKVKrl9EvTFxr4HojSm8s6I0FXaF-F6VxjB199K-aBbnP0GRmPJ9M59YEbZ6iT_rxf7HJgqhrVYiROP5KANacSxT4XnExATRqevUUdbKeekvOR7KDdsF__8U3MUSJDw</recordid><startdate>19790101</startdate><enddate>19790101</enddate><creator>Castelfranco, Paul A.</creator><creator>Weinstein, Jon D.</creator><creator>Schwarcz, Stephen</creator><creator>Pardo, Anthony D.</creator><creator>Wezelman, Barbara E.</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>19790101</creationdate><title>The Mg insertion step in chlorophyll biosynthesis</title><author>Castelfranco, Paul A. ; Weinstein, Jon D. ; Schwarcz, Stephen ; Pardo, Anthony D. ; Wezelman, Barbara E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c403t-914c999d5bdb8a16459dec9da9b549e1bbcd5726d5a464ea1c7f81452aaf52ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Aminolevulinic Acid - metabolism</topic><topic>Chlorophyll - biosynthesis</topic><topic>Chloroplasts - metabolism</topic><topic>cucumbers</topic><topic>Glutamates - metabolism</topic><topic>Kinetics</topic><topic>magnesium</topic><topic>Magnesium - metabolism</topic><topic>Plants</topic><topic>Porphyrins - metabolism</topic><topic>Protoporphyrins - metabolism</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Castelfranco, Paul A.</creatorcontrib><creatorcontrib>Weinstein, Jon D.</creatorcontrib><creatorcontrib>Schwarcz, Stephen</creatorcontrib><creatorcontrib>Pardo, Anthony D.</creatorcontrib><creatorcontrib>Wezelman, Barbara E.</creatorcontrib><creatorcontrib>West Indies Univ. St. Augustine (Trinidad and Tobago). Dept. of Soil Science</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Castelfranco, Paul A.</au><au>Weinstein, Jon D.</au><au>Schwarcz, Stephen</au><au>Pardo, Anthony D.</au><au>Wezelman, Barbara E.</au><aucorp>West Indies Univ. St. Augustine (Trinidad and Tobago). Dept. of Soil Science</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Mg insertion step in chlorophyll biosynthesis</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1979-01-01</date><risdate>1979</risdate><volume>192</volume><issue>2</issue><spage>592</spage><epage>598</epage><pages>592-598</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>A developing chloroplast preparation obtained from greening cucumber cotyledons is able to bring about the synthesis of Mg-protoporphyrin-IX and/or Mg-protoporphyrin-IX monomethyl ester.
l-glutamate, δ-aminolevulinic acid, and protoporphyrin-IX can serve as precursors for Mg-protoporphyrin synthesis. However, when δ-aminolevulinic acid or protoporpyrin are used, no Mg-protoporphyrin is formed unless
l-glutamate is also added. Mg-Protoporphyrin synthesis with δ-aminolevulinic acid plus
l-glutamate, or proto-porphyrin plus
l-glutamate, is much more active than with
l-glutamate alone. Therefore, it is apparent that
l-glutamate plays a role in the Mg chelation step in chloroplasts. α-Keto-glutarate can replace
l-glutamate in this role; glutamine cannot. ATP is also required for Mg chelation. The role of
l-glutamate in the Mg insertion step is not yet understood, except that
l-glutamate itself does not need to be converted to porphyrins in this process, because Mg-protoporphyrin can be synthesized from protoporphyrin and
l-glutamate even in the presence of the δ-aminolevulinic acid dehydratase inhibitor, levulinate.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>434841</pmid><doi>10.1016/0003-9861(79)90130-9</doi><tpages>7</tpages></addata></record> |
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source | MEDLINE; Elsevier ScienceDirect Journals Complete |
subjects | Aminolevulinic Acid - metabolism Chlorophyll - biosynthesis Chloroplasts - metabolism cucumbers Glutamates - metabolism Kinetics magnesium Magnesium - metabolism Plants Porphyrins - metabolism Protoporphyrins - metabolism Spectrometry, Fluorescence |
title | The Mg insertion step in chlorophyll biosynthesis |
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