{"id":1040,"date":"2017-10-27T16:45:50","date_gmt":"2017-10-27T16:45:50","guid":{"rendered":"https:\/\/courses.lumenlearning.com\/suny-nutrition\/?post_type=chapter&#038;p=1040"},"modified":"2017-11-14T17:50:42","modified_gmt":"2017-11-14T17:50:42","slug":"12-81-zinc-functions","status":"publish","type":"chapter","link":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/chapter\/12-81-zinc-functions\/","title":{"raw":"12.81 Zinc Functions","rendered":"12.81 Zinc Functions"},"content":{"raw":"<div class=\"__UNKNOWN__\">\r\n\r\nZinc is a cofactor for up to 300 enzymes in the body<sup>1<\/sup>. Enzymes that use zinc as a cofactor are known as metalloenzymes.\r\n\r\nZinc is a cofactor for the antioxidant enzyme superoxide dismutase that converts superoxide to hydrogen peroxide, as shown below.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"1139\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164324\/1000000000000473000002F5A403A9C6.png\" alt=\"\" width=\"1139\" height=\"757\" \/> Figure 12.811 Superoxide dismutase uses zinc as a cofactor[\/caption]\r\n\r\n<\/div>\r\nAlcohol dehydrogenase uses 4 zincs per enzyme. Its role in ethanol metabolism is shown below<sup>2<\/sup>.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"1157\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164327\/1000000000000485000002BC92E7E74A.png\" alt=\"\" width=\"1157\" height=\"700\" \/> Figure 12.812 Ethanol metabolism<sup>3,4<\/sup>[\/caption]\r\n\r\n<\/div>\r\nDelta-aminolevulinic acid dehydratase (ALA dehydrogenase), which is involved in heme synthesis, uses 8 zincs\/enzyme to form porphobilinogen, as shown below<sup>2<\/sup>.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"584\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164329\/10000000000002480000013E2A766B8C.png\" alt=\"\" width=\"584\" height=\"318\" \/> Figure 12.813 ALA dehydrogenase requires zinc in the heme synthesis pathway<sup>5<\/sup>[\/caption]\r\n\r\n<\/div>\r\nThe enzyme that cleaves the extra glutamates from folate so that it can be taken up into the enterocyte is a metalloenzyme2. The cleavage of folate is shown in the figure below.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"1157\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164331\/1000000000000485000002865A4D04FD.png\" alt=\"\" width=\"1157\" height=\"646\" \/> Figure 12.814 The absorption of folate and folic acid[\/caption]\r\n\r\n<\/div>\r\nOther notable metalloenzymes include DNA and RNA polymerase<sup>2<\/sup>.\r\n\r\nZinc is also important for the formation of zinc fingers in proteins. Zinc fingers help proteins bind to DNA2.\r\n<div>\r\n\r\n[caption id=\"\" align=\"aligncenter\" width=\"800\"]<img src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164333\/1000000000000320000002555905FFA8.png\" alt=\"\" width=\"800\" height=\"597\" \/> Figure 12.815 Structure of a zinc finger, zinc is the green atom bound in the center<sup>6<\/sup>[\/caption]\r\n\r\n<\/div>\r\nZinc is also important for growth, immune function, and reproduction<sup>2<\/sup>.\r\n\r\nA recent Cochrane review concluded that when taken within 24 hours of the onset of symptoms, that zinc lozenges or syrup results in a significant decrease in the duration and severity of common cold symptoms<sup>7<\/sup>. Thus, commonly used zinc lozenges may be an effective way to combat the common cold. However, large amounts of zinc consumption can be problematic for copper and ultimately iron levels in the body, as described in the copper section.\r\n\r\n<b>References &amp; Links<\/b>\r\n\r\n1. Byrd-Bredbenner C, Moe G, Beshgetoor D, Berning J. (2009) Wardlaw's perspectives in nutrition. New York, NY: McGraw-Hill.\r\n\r\n2. Gropper SS, Smith JL, Groff JL. (2008) Advanced nutrition and human metabolism. Belmont, CA: Wadsworth Publishing.\r\n\r\n3. http:\/\/en.wikipedia.org\/wiki\/File:Ethanol_flat_structure.png\r\n\r\n4. https:\/\/en.wikipedia.org\/wiki\/Acetaldehyde#\/media\/File:Acetaldehyde-2D-flat.svg\r\n\r\n5. http:\/\/en.wikipedia.org\/wiki\/File:Heme_synthesis.png\r\n\r\n6. http:\/\/en.wikipedia.org\/wiki\/File:Zinc_finger_rendered.png\r\n\r\n7. Singh M, Das RR. (2011) Zinc for the common cold (Review). The Cochrane Collaboration.\r\n\r\n<\/div>","rendered":"<div class=\"__UNKNOWN__\">\n<p>Zinc is a cofactor for up to 300 enzymes in the body<sup>1<\/sup>. Enzymes that use zinc as a cofactor are known as metalloenzymes.<\/p>\n<p>Zinc is a cofactor for the antioxidant enzyme superoxide dismutase that converts superoxide to hydrogen peroxide, as shown below.<\/p>\n<div>\n<div style=\"width: 1149px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164324\/1000000000000473000002F5A403A9C6.png\" alt=\"\" width=\"1139\" height=\"757\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.811 Superoxide dismutase uses zinc as a cofactor<\/p>\n<\/div>\n<\/div>\n<p>Alcohol dehydrogenase uses 4 zincs per enzyme. Its role in ethanol metabolism is shown below<sup>2<\/sup>.<\/p>\n<div>\n<div style=\"width: 1167px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164327\/1000000000000485000002BC92E7E74A.png\" alt=\"\" width=\"1157\" height=\"700\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.812 Ethanol metabolism<sup>3,4<\/sup><\/p>\n<\/div>\n<\/div>\n<p>Delta-aminolevulinic acid dehydratase (ALA dehydrogenase), which is involved in heme synthesis, uses 8 zincs\/enzyme to form porphobilinogen, as shown below<sup>2<\/sup>.<\/p>\n<div>\n<div style=\"width: 594px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164329\/10000000000002480000013E2A766B8C.png\" alt=\"\" width=\"584\" height=\"318\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.813 ALA dehydrogenase requires zinc in the heme synthesis pathway<sup>5<\/sup><\/p>\n<\/div>\n<\/div>\n<p>The enzyme that cleaves the extra glutamates from folate so that it can be taken up into the enterocyte is a metalloenzyme2. The cleavage of folate is shown in the figure below.<\/p>\n<div>\n<div style=\"width: 1167px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164331\/1000000000000485000002865A4D04FD.png\" alt=\"\" width=\"1157\" height=\"646\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.814 The absorption of folate and folic acid<\/p>\n<\/div>\n<\/div>\n<p>Other notable metalloenzymes include DNA and RNA polymerase<sup>2<\/sup>.<\/p>\n<p>Zinc is also important for the formation of zinc fingers in proteins. Zinc fingers help proteins bind to DNA2.<\/p>\n<div>\n<div style=\"width: 810px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" decoding=\"async\" src=\"https:\/\/s3-us-west-2.amazonaws.com\/courses-images\/wp-content\/uploads\/sites\/2569\/2017\/10\/27164333\/1000000000000320000002555905FFA8.png\" alt=\"\" width=\"800\" height=\"597\" \/><\/p>\n<p class=\"wp-caption-text\">Figure 12.815 Structure of a zinc finger, zinc is the green atom bound in the center<sup>6<\/sup><\/p>\n<\/div>\n<\/div>\n<p>Zinc is also important for growth, immune function, and reproduction<sup>2<\/sup>.<\/p>\n<p>A recent Cochrane review concluded that when taken within 24 hours of the onset of symptoms, that zinc lozenges or syrup results in a significant decrease in the duration and severity of common cold symptoms<sup>7<\/sup>. Thus, commonly used zinc lozenges may be an effective way to combat the common cold. However, large amounts of zinc consumption can be problematic for copper and ultimately iron levels in the body, as described in the copper section.<\/p>\n<p><b>References &amp; Links<\/b><\/p>\n<p>1. Byrd-Bredbenner C, Moe G, Beshgetoor D, Berning J. (2009) Wardlaw&#8217;s perspectives in nutrition. New York, NY: McGraw-Hill.<\/p>\n<p>2. Gropper SS, Smith JL, Groff JL. (2008) Advanced nutrition and human metabolism. Belmont, CA: Wadsworth Publishing.<\/p>\n<p>3. http:\/\/en.wikipedia.org\/wiki\/File:Ethanol_flat_structure.png<\/p>\n<p>4. https:\/\/en.wikipedia.org\/wiki\/Acetaldehyde#\/media\/File:Acetaldehyde-2D-flat.svg<\/p>\n<p>5. http:\/\/en.wikipedia.org\/wiki\/File:Heme_synthesis.png<\/p>\n<p>6. http:\/\/en.wikipedia.org\/wiki\/File:Zinc_finger_rendered.png<\/p>\n<p>7. Singh M, Das RR. (2011) Zinc for the common cold (Review). The Cochrane Collaboration.<\/p>\n<\/div>\n\n\t\t\t <section class=\"citations-section\" role=\"contentinfo\">\n\t\t\t <h3>Candela Citations<\/h3>\n\t\t\t\t\t <div>\n\t\t\t\t\t\t <div id=\"citation-list-1040\">\n\t\t\t\t\t\t\t <div class=\"licensing\"><div class=\"license-attribution-dropdown-subheading\">CC licensed content, Shared previously<\/div><ul class=\"citation-list\"><li>Kansas State University Human Nutrition Flexbook. <strong>Authored by<\/strong>: Brian Lindshield. <strong>Provided by<\/strong>: Kansas State University. <strong>Located at<\/strong>: <a target=\"_blank\" href=\"http:\/\/goo.gl\/vOAnR\">http:\/\/goo.gl\/vOAnR<\/a>. <strong>License<\/strong>: <em><a target=\"_blank\" rel=\"license\" href=\"https:\/\/creativecommons.org\/licenses\/by\/4.0\/\">CC BY: Attribution<\/a><\/em><\/li><\/ul><\/div>\n\t\t\t\t\t\t <\/div>\n\t\t\t\t\t <\/div>\n\t\t\t <\/section>","protected":false},"author":5759,"menu_order":32,"template":"","meta":{"_candela_citation":"[{\"type\":\"cc\",\"description\":\"Kansas State University Human Nutrition Flexbook\",\"author\":\"Brian Lindshield\",\"organization\":\"Kansas State University\",\"url\":\"goo.gl\/vOAnR\",\"project\":\"\",\"license\":\"cc-by\",\"license_terms\":\"\"}]","CANDELA_OUTCOMES_GUID":"","pb_show_title":"on","pb_short_title":"","pb_subtitle":"","pb_authors":[],"pb_section_license":""},"chapter-type":[],"contributor":[],"license":[],"class_list":["post-1040","chapter","type-chapter","status-publish","hentry"],"part":883,"_links":{"self":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters\/1040","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters"}],"about":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/types\/chapter"}],"author":[{"embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/users\/5759"}],"version-history":[{"count":4,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters\/1040\/revisions"}],"predecessor-version":[{"id":1851,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters\/1040\/revisions\/1851"}],"part":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/parts\/883"}],"metadata":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapters\/1040\/metadata\/"}],"wp:attachment":[{"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/media?parent=1040"}],"wp:term":[{"taxonomy":"chapter-type","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/pressbooks\/v2\/chapter-type?post=1040"},{"taxonomy":"contributor","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/contributor?post=1040"},{"taxonomy":"license","embeddable":true,"href":"https:\/\/courses.lumenlearning.com\/atd-herkimer-nutrition\/wp-json\/wp\/v2\/license?post=1040"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}