Loading…
Effect of arginine modifying reagents on pigeon liver fatty acid synthetase: evidence for the presence of essential arginine residues at the beta-ketoacyl reductase and enoyl-CoA reductase domain
Pigeon liver fatty acid synthetase was inactivated by arginine modifying reagent, phenylglyoxal and 2,3-butanedione. The inactivation of overall fatty acid synthetase was accompanied by the loss of beta-ketoacyl reductase and enoyl-CoA reductase activity. The inactivation followed a pseudo-first ord...
Saved in:
Published in: | Indian journal of biochemistry & biophysics 2000-02, Vol.37 (1), p.28-33 |
---|---|
Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | |
---|---|
cites | |
container_end_page | 33 |
container_issue | 1 |
container_start_page | 28 |
container_title | Indian journal of biochemistry & biophysics |
container_volume | 37 |
creator | Mukherjee, S Katiyar, S S |
description | Pigeon liver fatty acid synthetase was inactivated by arginine modifying reagent, phenylglyoxal and 2,3-butanedione. The inactivation of overall fatty acid synthetase was accompanied by the loss of beta-ketoacyl reductase and enoyl-CoA reductase activity. The inactivation followed a pseudo-first order kinetics and sum of the second order rate constants for the two reductase reactions equaled that for the synthetase reaction. Inactivation of all three activities was prevented by NADPH or its analogs 2',5'-ADP and 2'-AMP but not by the corresponding nucleotides containing the 5'-phosphate. These results suggest that binding of NADPH to fatty acid synthetase involves specific interaction of the 2'-phosphate with the guanidino group of arginine residues at the active site of the two reductases. pH-Dependent inactivation by phenylglyoxal indicated that a group with a pka 7.5 is involved in the loss of enzyme activity. Stoichiometric results showed that 4 out of 164 arginine residues per enzyme molecule were essential for the enzyme activity. |
format | article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_72256183</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>72256183</sourcerecordid><originalsourceid>FETCH-LOGICAL-p207t-8aff64d80ee871275e72ac591e373f71ed86d0f8f50cdf16b00bcdec934151043</originalsourceid><addsrcrecordid>eNpNkMFOwzAQRHMA0VL4BbQnbpHspElcblVVoFIlLnCOHHsdDIkdbKdSvo8fw5QiOO1qZvR2NWfJnOSEpjQjbJZcev9GSFkWWXGRzChZsXxJyTz53CqFIoBVwF2rjTYIvZVaTdq04JC3aIIHa2DQLcbR6QM6UDyECbjQEvxkwisG7vEO8KAlGoGgrIOowuDQH4XIRx_XoHn3dym6Wo7ogYdjvImc9B2D5WLqoitH8Q0GbiSgsVOXbuz6ny5tz7W5Ss4V7zxen-YiebnfPm8e0_3Tw26z3qdDRqqQMq5UuZSMILKKZlWBVcZFsaKYV7mqKEpWSqKYKoiQipYNIY2QKFaxqYKSZb5Ibn-4g7Mf8etQ99oL7Dpu0I6-rrKsKCnLY_DmFBybHmU9ON1zN9W_tedfR1SCuw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>72256183</pqid></control><display><type>article</type><title>Effect of arginine modifying reagents on pigeon liver fatty acid synthetase: evidence for the presence of essential arginine residues at the beta-ketoacyl reductase and enoyl-CoA reductase domain</title><source>Free Full-Text Journals in Chemistry</source><creator>Mukherjee, S ; Katiyar, S S</creator><creatorcontrib>Mukherjee, S ; Katiyar, S S</creatorcontrib><description>Pigeon liver fatty acid synthetase was inactivated by arginine modifying reagent, phenylglyoxal and 2,3-butanedione. The inactivation of overall fatty acid synthetase was accompanied by the loss of beta-ketoacyl reductase and enoyl-CoA reductase activity. The inactivation followed a pseudo-first order kinetics and sum of the second order rate constants for the two reductase reactions equaled that for the synthetase reaction. Inactivation of all three activities was prevented by NADPH or its analogs 2',5'-ADP and 2'-AMP but not by the corresponding nucleotides containing the 5'-phosphate. These results suggest that binding of NADPH to fatty acid synthetase involves specific interaction of the 2'-phosphate with the guanidino group of arginine residues at the active site of the two reductases. pH-Dependent inactivation by phenylglyoxal indicated that a group with a pka 7.5 is involved in the loss of enzyme activity. Stoichiometric results showed that 4 out of 164 arginine residues per enzyme molecule were essential for the enzyme activity.</description><identifier>ISSN: 0301-1208</identifier><identifier>PMID: 10983410</identifier><language>eng</language><publisher>India</publisher><subject>Animals ; Arginine - chemistry ; Columbidae ; Fatty Acid Synthases - antagonists & inhibitors ; Fatty Acid Synthases - chemistry ; Fatty Acid Synthases - metabolism ; Kinetics ; Liver - enzymology ; Protein Structure, Tertiary</subject><ispartof>Indian journal of biochemistry & biophysics, 2000-02, Vol.37 (1), p.28-33</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10983410$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mukherjee, S</creatorcontrib><creatorcontrib>Katiyar, S S</creatorcontrib><title>Effect of arginine modifying reagents on pigeon liver fatty acid synthetase: evidence for the presence of essential arginine residues at the beta-ketoacyl reductase and enoyl-CoA reductase domain</title><title>Indian journal of biochemistry & biophysics</title><addtitle>Indian J Biochem Biophys</addtitle><description>Pigeon liver fatty acid synthetase was inactivated by arginine modifying reagent, phenylglyoxal and 2,3-butanedione. The inactivation of overall fatty acid synthetase was accompanied by the loss of beta-ketoacyl reductase and enoyl-CoA reductase activity. The inactivation followed a pseudo-first order kinetics and sum of the second order rate constants for the two reductase reactions equaled that for the synthetase reaction. Inactivation of all three activities was prevented by NADPH or its analogs 2',5'-ADP and 2'-AMP but not by the corresponding nucleotides containing the 5'-phosphate. These results suggest that binding of NADPH to fatty acid synthetase involves specific interaction of the 2'-phosphate with the guanidino group of arginine residues at the active site of the two reductases. pH-Dependent inactivation by phenylglyoxal indicated that a group with a pka 7.5 is involved in the loss of enzyme activity. Stoichiometric results showed that 4 out of 164 arginine residues per enzyme molecule were essential for the enzyme activity.</description><subject>Animals</subject><subject>Arginine - chemistry</subject><subject>Columbidae</subject><subject>Fatty Acid Synthases - antagonists & inhibitors</subject><subject>Fatty Acid Synthases - chemistry</subject><subject>Fatty Acid Synthases - metabolism</subject><subject>Kinetics</subject><subject>Liver - enzymology</subject><subject>Protein Structure, Tertiary</subject><issn>0301-1208</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNpNkMFOwzAQRHMA0VL4BbQnbpHspElcblVVoFIlLnCOHHsdDIkdbKdSvo8fw5QiOO1qZvR2NWfJnOSEpjQjbJZcev9GSFkWWXGRzChZsXxJyTz53CqFIoBVwF2rjTYIvZVaTdq04JC3aIIHa2DQLcbR6QM6UDyECbjQEvxkwisG7vEO8KAlGoGgrIOowuDQH4XIRx_XoHn3dym6Wo7ogYdjvImc9B2D5WLqoitH8Q0GbiSgsVOXbuz6ny5tz7W5Ss4V7zxen-YiebnfPm8e0_3Tw26z3qdDRqqQMq5UuZSMILKKZlWBVcZFsaKYV7mqKEpWSqKYKoiQipYNIY2QKFaxqYKSZb5Ibn-4g7Mf8etQ99oL7Dpu0I6-rrKsKCnLY_DmFBybHmU9ON1zN9W_tedfR1SCuw</recordid><startdate>200002</startdate><enddate>200002</enddate><creator>Mukherjee, S</creator><creator>Katiyar, S S</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>200002</creationdate><title>Effect of arginine modifying reagents on pigeon liver fatty acid synthetase: evidence for the presence of essential arginine residues at the beta-ketoacyl reductase and enoyl-CoA reductase domain</title><author>Mukherjee, S ; Katiyar, S S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p207t-8aff64d80ee871275e72ac591e373f71ed86d0f8f50cdf16b00bcdec934151043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Arginine - chemistry</topic><topic>Columbidae</topic><topic>Fatty Acid Synthases - antagonists & inhibitors</topic><topic>Fatty Acid Synthases - chemistry</topic><topic>Fatty Acid Synthases - metabolism</topic><topic>Kinetics</topic><topic>Liver - enzymology</topic><topic>Protein Structure, Tertiary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mukherjee, S</creatorcontrib><creatorcontrib>Katiyar, S S</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Indian journal of biochemistry & biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mukherjee, S</au><au>Katiyar, S S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of arginine modifying reagents on pigeon liver fatty acid synthetase: evidence for the presence of essential arginine residues at the beta-ketoacyl reductase and enoyl-CoA reductase domain</atitle><jtitle>Indian journal of biochemistry & biophysics</jtitle><addtitle>Indian J Biochem Biophys</addtitle><date>2000-02</date><risdate>2000</risdate><volume>37</volume><issue>1</issue><spage>28</spage><epage>33</epage><pages>28-33</pages><issn>0301-1208</issn><abstract>Pigeon liver fatty acid synthetase was inactivated by arginine modifying reagent, phenylglyoxal and 2,3-butanedione. The inactivation of overall fatty acid synthetase was accompanied by the loss of beta-ketoacyl reductase and enoyl-CoA reductase activity. The inactivation followed a pseudo-first order kinetics and sum of the second order rate constants for the two reductase reactions equaled that for the synthetase reaction. Inactivation of all three activities was prevented by NADPH or its analogs 2',5'-ADP and 2'-AMP but not by the corresponding nucleotides containing the 5'-phosphate. These results suggest that binding of NADPH to fatty acid synthetase involves specific interaction of the 2'-phosphate with the guanidino group of arginine residues at the active site of the two reductases. pH-Dependent inactivation by phenylglyoxal indicated that a group with a pka 7.5 is involved in the loss of enzyme activity. Stoichiometric results showed that 4 out of 164 arginine residues per enzyme molecule were essential for the enzyme activity.</abstract><cop>India</cop><pmid>10983410</pmid><tpages>6</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0301-1208 |
ispartof | Indian journal of biochemistry & biophysics, 2000-02, Vol.37 (1), p.28-33 |
issn | 0301-1208 |
language | eng |
recordid | cdi_proquest_miscellaneous_72256183 |
source | Free Full-Text Journals in Chemistry |
subjects | Animals Arginine - chemistry Columbidae Fatty Acid Synthases - antagonists & inhibitors Fatty Acid Synthases - chemistry Fatty Acid Synthases - metabolism Kinetics Liver - enzymology Protein Structure, Tertiary |
title | Effect of arginine modifying reagents on pigeon liver fatty acid synthetase: evidence for the presence of essential arginine residues at the beta-ketoacyl reductase and enoyl-CoA reductase domain |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T22%3A22%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Effect%20of%20arginine%20modifying%20reagents%20on%20pigeon%20liver%20fatty%20acid%20synthetase:%20evidence%20for%20the%20presence%20of%20essential%20arginine%20residues%20at%20the%20beta-ketoacyl%20reductase%20and%20enoyl-CoA%20reductase%20domain&rft.jtitle=Indian%20journal%20of%20biochemistry%20&%20biophysics&rft.au=Mukherjee,%20S&rft.date=2000-02&rft.volume=37&rft.issue=1&rft.spage=28&rft.epage=33&rft.pages=28-33&rft.issn=0301-1208&rft_id=info:doi/&rft_dat=%3Cproquest_pubme%3E72256183%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-p207t-8aff64d80ee871275e72ac591e373f71ed86d0f8f50cdf16b00bcdec934151043%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=72256183&rft_id=info:pmid/10983410&rfr_iscdi=true |