Menu
Home
People
Places
Arts
History
Plants & Animals
Science
Life & Culture
Technology
Reference.org
Pyruvate, phosphate dikinase
open-in-new
<h2 id="nomenclature">Nomenclature</h2> <p>The <a href="/facts/List_of_enzymes/w2RP6EwU">systematic name</a> of this enzyme class is ATP:pyruvate, phosphate phosphotransferase. Other names in common use include pyruvate, orthophosphate dikinase, pyruvate-phosphate dikinase (phosphorylating), pyruvate phosphate dikinase, pyruvate-inorganic phosphate dikinase, pyruvate-phosphate dikinase, pyruvate-phosphate ligase, pyruvic-phosphate dikinase, pyruvic-phosphate ligase, pyruvate, Pi dikinase, and PPDK. </p> <h2 id="reaction-mechanism">Reaction mechanism</h2> <p>PPDK catalyses the conversion of <a href="/facts/Pyruvate/qJTgl4J9">pyruvate</a> to <a href="/facts/Phosphoenolpyruvate/CeUbr30F">phosphoenolpyruvate</a> (PEP), consuming 1 molecule of <a href="/facts/Adenosine_triphosphate/nB9bwgcU">ATP</a>, and producing one molecule of <a href="/facts/Adenosine_monophosphate/D9Ryfqad">AMP</a> in the process. The <a href="/facts/Reaction_mechanism/9lanyVuy">mechanism</a> consists of 3 reversible reactions:<a class="footnote-ref" id="fnref:2" href="#fn:2"><sup>2</sup></a> </p> <ol><li>The enzyme PPDK binds to ATP, to produce AMP and a <a href="/facts/Phosphorylation/LXUEEeIL">diphosphorylated</a> PPDK.</li> <li>The diphosphorylated PPDK binds to <a href="/facts/Inorganic_phosphate/FDGVCxUG">inorganic phosphate</a>, producing <a href="/facts/Diphosphate/L9FPEkhF">diphosphate</a> and (mono)phosphorylated PPDK.</li> <li>Phosphorylated PPDK binds to pyruvate, producing phosphoenolpyruvate, and regenerating PPDK.</li></ol> <p>The reaction is similar to the reaction catalysed by <a href="/facts/Pyruvate_kinase/Str5huU6">pyruvate kinase</a>, which also converts pyruvate to PEP.<a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> However, pyruvate kinase catalyses an <a href="/facts/Irreversible_reaction/V3Afejgb">irreversible reaction</a>, and does not consume ATP. By contrast, PPDK catalyses a reversible reaction, and consumes 1 molecule of ATP for each molecule of pyruvate converted. </p><p>Currently, the details of each mechanistic step is unknown<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> </p> <h2 id="structure">Structure</h2> <p>In its active form, PPDK is a <a href="/facts/Homotetramer/bpk1VucR">homotetramer</a> with <a href="/facts/Protein_subunit/HhuET9UP">subunits</a> about 95 <a href="/facts/KDa/IMATU3vf">kDa</a><a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> </p><p>There are two different reaction centres about 45 <a href="/facts/Angstrom/T5mjdd97">Angstroms</a> apart, in which different <a href="/facts/Enzyme_substrate/6MnaV19h">substrates</a> bind.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> The <a href="/facts/Nucleotide/pQKEwlJI">nucleotide</a> (ATP) <a href="/facts/Binding_site/gd9r9Rw7">binding site</a> is on the <a href="/facts/N-terminus/yKYpuaBJ">N-terminus</a>, has 240 <a href="/facts/Amino_acids/WDxYwBny">amino acids</a>, and a characteristic <a href="/facts/ATP-grasp/6696qYKW">ATP-grasp</a>. The pyruvate/PEP binding site is on the <a href="/facts/C-terminus/ws4scHgT">C-terminus</a>, has 340 amino acids, and an α/β-barrel fold. There is also a central domain, which contains <a href="/facts/Histidine/le7781NF">His</a>455, the primary <a href="/facts/Amino_acid/WDxYwBny">residue</a> responsible for catalysis. His455 is the phosphoryl acceptor or donor residue.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> The structure of the enzyme suggests that the His455 arm undergoes a <a href="/facts/Swivel/CuQCCBww">swivelling</a> motion to shuttle a phosphoryl group between the two reaction centres.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> During this swivelling, the central domain <a href="/facts/Rotation/yChkz49x">rotates</a> at least 92 degrees, and <a href="/facts/Translation_(geometry)/KlpWmnfX">translates</a> 0.5 Angstroms.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> </p><p>Studies of <a href="/facts/Crystal_structures/bJ4bCeHd">crystal structures</a> of PPDK show that the central domain is located in different proximity to the two other domains depending on the source of the enzyme.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> In <a href="/facts/Maize/lJ6c5xMH">maize</a>, it is closer to the C-terminal, while in <i><a href="/facts/Clostridium/HRXJyYCn">Clostridium symbiosum</a></i>, it is closer to the N-terminal. </p><p>Research has shown that the PPDK binding mechanisms are similar to that of <a href="/facts/D-alanine%E2%80%94D-alanine_ligase/PgX6ksNy">D-Ala-D-Ala ligase</a> and <a href="/facts/Pyruvate_kinase/Str5huU6">pyruvate kinase</a>.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> In particular, PPDK is very similar to pyruvate kinase, which also catalyses the conversion of pyruvate to phosphoenolpyruvate; however, it does so without a phosphorylated-enzyme intermediate.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> Though their amino acid sequences are different, residues key to catalysis are preserved in both enzymes. <a href="/facts/Point_mutation/q30PEGFd">Point-mutagenesis</a> experiments have shown that catalytic residues include <a href="/facts/Arginine/y49Hdf1e">Arg</a>561, <a href="/facts/Arginine/y49Hdf1e">Arg</a>617, <a href="/facts/Glutamic_acid/7oXbNcvu">Glu</a>745, <a href="/facts/Asparagine/KYIft5Jd">Asn</a>768, and <a href="/facts/Cysteine/kbqvUm6d">Cys</a>831 (numbering relative to the <i>C, symbiosum</i> protein, <a href="/facts/Protein_Data_Bank/oUhq4ABD">PDB</a>: <a href="https://www.rcsb.org/structure/1KBL">1KBL</a>, <a href="https://www.rcsb.org/structure/1KC7">1KC7</a>).<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> </p> Protein domain infoboxes<table><tbody><tr><td></td><td></td><td></td></tr></tbody></table> <h2 id="biological-function-and-evolution">Biological function and evolution</h2> <p>PPDK is used in the <a href="/facts/C4_carbon_fixation/2dLTxsae">C4 pathway</a>, to improve the efficiency of <a href="/facts/Carbon_dioxide/xGzpppEp">carbon dioxide</a> fixation.<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> In environments where there is a lot of light, the rate of <a href="/facts/Photosynthesis/TMV7w693">photosynthesis</a> in plants is <a href="/facts/Limiting_factor/IYufWHvx">limited</a> by the rate of carbon dioxide (CO2) uptake. This can be improved by using a series of chemical reactions to transport CO2 from <a href="/facts/Mesophyll_tissue/1m6wCNTg">mesophyll</a> cells (which are located on the outside of a leaf) to <a href="/facts/Bundle_sheath/m2x5jxoa">bundle sheath</a> cells (which are located inside the cells). PPDK converts pyruvate to PEP, which reacts with CO2 to produce <a href="/facts/Oxaloacetate/ojLoQw81">oxaloacetate</a>. When CO2 is released in the bundle sheath cells, pyruvate is regenerated, and the cycle continues.<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> </p><p>Though the reaction catalysed by PPDK is reversible, PEP is favoured as the product in biological conditions. This is due to the <a href="/facts/Base_(chemistry)/M9wA7qeM">basic</a> <a href="/facts/PH/RnSv8D7y">pH</a> in the <a href="/facts/Stroma_(fluid)/AYwQHKSm">stroma</a>, where the reaction occurs, as well as high concentrations of <a href="/facts/Adenylate_kinase/XVLmsCUa">adenylate kinase</a> and <a href="/facts/Pyrophosphatase/Cmw4WzmI">pyrophosphatase</a>. Because these two enzymes catalyse <a href="/facts/Exergonic/2kPJobE7">exergonic</a> reactions involving AMP, and disphosphate, respectively, they drive the PPDK-catalysed reaction forward.<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> Because PPDK consumes ATP, the C4 pathway is unfavourable for plants in environments with little access to light, as they are unable to produce large quantities of ATP.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a> </p><p>PPDK is highly abundant in C4 leaves, comprising up to 10% of total <a href="/facts/Protein/Jxmagu3E">protein</a>.<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a> Research has shown that the enzyme is about 96% identical in different <a href="/facts/Species/oDg6b96r">species</a> of plants. <a href="/facts/Hybrid_(biology)/pzVJ54xU">Hybridization</a> experiments revealed that the genetic differences correlate with the extent to which the plants perform the C4 pathway – the uncommon sequences exist in plants which also display C3 characteristics.<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> PPDK is also found in small quantities in C3 plants. Evolutionary history suggests that it once had a role in <a href="/facts/Glycolysis/a5ApxLoG">glycolysis</a> like the similar <a href="/facts/Pyruvate_kinase/Str5huU6">pyruvate kinase</a>, and eventually <a href="/facts/Evolution/Hj0qAaBk">evolved</a> into the C4 pathway.<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> </p><p>Besides plants, PPDK is also found in the parasitic ameoba <i><a href="/facts/Entamoeba_histolytica/lMPf2xDp">Entamoeba histolytica</a></i> (<a href="https://www.uniprot.org/uniprot/P37213">P37213</a>) and the bacteria <i>Clostridium symbiosum</i> (<a href="https://www.uniprot.org/uniprot/P22983">P22983</a>; as well as other bacteria).<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a> In those two organisms PPDK functions similarly to (and sometimes in place of) pyruvate kinase, catalyzing the reaction in the ATP-producing direction as a part of glycolysis. Inhibitors for the <i>Entamoeba</i> PPDK have been proposed as <a href="/facts/Amebicide/YyzJWPCr">amebicides</a> against this organism.<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a> </p> <h2 id="regulation">Regulation</h2> <p>Plant PPDK is regulated by the <a href="/facts/(Pyruvate,_phosphate_dikinase)-phosphate_phosphotransferase/Y8rz9pD6">pyruvate, phosphate dikinase regulatory protein</a> (PDRP).<a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> When levels of light are high, PDRP dephosphorylates <a href="/facts/Threonine/7zffFQ6W">Thr</a>456 on PPDK using <a href="/facts/Adenosine_monophosphate/D9Ryfqad">AMP</a>, thus activating the enzyme.<a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a> PDRP deactivates PPDK by phosphorylating the same <a href="/facts/Threonine/7zffFQ6W">threonine</a> <a href="/facts/Amino_acid/WDxYwBny">residue</a>, using <a href="/facts/Diphosphate/L9FPEkhF">diphosphate</a>. PDRP is a unique <a href="/facts/Regulation/eFR0l2x9">regulator</a> because it catalyses both activation and deactivation of PPDK, through two different mechanisms.<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a> </p><p>Research on <a href="/facts/Maize/lJ6c5xMH">maize</a> PPDK suggests that <a href="/facts/Intron/LS6YdBEK">introns</a>, <a href="/facts/Terminator_(genetics)/mdR46gBa">terminator sequences</a>, and perhaps other enhancer sequences, act cooperatively to increase the level of functional and stable <a href="/facts/Messenger_RNA/oUL6qxQn">mRNA</a>. PPDK <a href="/facts/CDNA/P2nWeY4T">cDNA</a> was expressed only slightly in transgenic <a href="/facts/Rice/wvL1hBCz">rice</a>, compared to intact DNA which saw significant expression.<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a> </p> <h2 id="structural-studies">Structural studies</h2> <p>As of early 2018, 14 <a href="/facts/Tertiary_structure/VaN6MEYh">structures</a> have been solved for this class of enzymes, with <a href="/facts/Protein_Data_Bank/oUhq4ABD">PDB</a> accession codes <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1DIK">1DIK</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1GGO">1GGO</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1H6Z">1H6Z</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1JDE">1JDE</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1KBL">1KBL</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1KC7">1KC7</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1VBG">1VBG</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1VBH">1VBH</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=2DIK">2DIK</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=2FM4">2FM4</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=5JVJ">5JVJ</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=5JVL">5JVL</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=5JVN">5JVN</a>, <a href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=5LU4">5LU4</a>. </p> <h2 id="further-reading">Further reading</h2> <ul><li>Hatch MD, Slack CR (January 1968). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1198479">"A new enzyme for the interconversion of pyruvate and phosphopyruvate and its role in the C4 dicarboxylic acid pathway of photosynthesis"</a>. <i>The Biochemical Journal</i>. 106 (1): 141–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1042%2Fbj1060141">10.1042/bj1060141</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1198479">1198479</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/4305612">4305612</a>.</li> <li>Reeves RE (June 1968). <a href="https://doi.org/10.1016%2FS0021-9258%2818%2993395-8">"A new enzyme with the glycolytic function of pyruvate kinase"</a>. <i>The Journal of Biological Chemistry</i>. 243 (11): 3202–4. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0021-9258%2818%2993395-8">10.1016/S0021-9258(18)93395-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/4297474">4297474</a>.</li> <li>Reeves RE (November 1971). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1178089">"Pyruvate,phosphate dikinase from Bacteroides symbiosus"</a>. <i>The Biochemical Journal</i>. 125 (2): 531–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1042%2Fbj1250531">10.1042/bj1250531</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1178089">1178089</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/5144757">5144757</a>.</li> <li>Reeves RE, Menzies RA, Hsu DS (October 1968). <a href="https://doi.org/10.1016%2FS0021-9258%2818%2991972-1">"The pyruvate-phosphate dikinase reaction. The fate of phosphate and the equilibrium"</a>. <i>The Journal of Biological Chemistry</i>. 243 (20): 5486–91. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0021-9258%2818%2991972-1">10.1016/S0021-9258(18)91972-1</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/4302788">4302788</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Pocalyko DJ, Carroll LJ, Martin BM, Babbitt PC, Dunaway-Mariano D (December 1990). "Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs". Biochemistry. 29 (48): 10757–65. doi:10.1021/bi00500a006. PMID 2176881. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Evans HJ, Wood HG (December 1968). "The mechanism of the pyruvate, phosphate dikinase reaction". Proceedings of the National Academy of Sciences of the United States of America. 61 (4): 1448–53. Bibcode:1968PNAS...61.1448E. doi:10.1073/pnas.61.4.1448. PMC 225276. PMID 4303480. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC225276" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC225276</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, et al. (January 2002). "Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis". Biochemistry. 41 (3): 780–7. doi:10.1021/bi011799+. PMID 11790099. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, et al. (January 2002). "Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis". Biochemistry. 41 (3): 780–7. doi:10.1021/bi011799+. PMID 11790099. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Chastain CJ, Failing CJ, Manandhar L, Zimmerman MA, Lakner MM, Nguyen TH (May 2011). "Functional evolution of C(4) pyruvate, orthophosphate dikinase". Journal of Experimental Botany. 62 (9): 3083–91. doi:10.1093/jxb/err058. PMID 21414960. <a href="https://doi.org/10.1093%2Fjxb%2Ferr058" target="_blank">https://doi.org/10.1093%2Fjxb%2Ferr058</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Herzberg O, Chen CC, Kapadia G, McGuire M, Carroll LJ, Noh SJ, Dunaway-Mariano D (April 1996). "Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites". Proceedings of the National Academy of Sciences of the United States of America. 93 (7): 2652–7. Bibcode:1996PNAS...93.2652H. doi:10.1073/pnas.93.7.2652. PMC 39685. PMID 8610096. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC39685" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC39685</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, et al. (January 2002). "Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis". Biochemistry. 41 (3): 780–7. doi:10.1021/bi011799+. PMID 11790099. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Lim K, Read RJ, Chen CC, Tempczyk A, Wei M, Ye D, et al. (December 2007). "Swiveling domain mechanism in pyruvate phosphate dikinase". Biochemistry. 46 (51): 14845–53. CiteSeerX 10.1.1.421.2653. doi:10.1021/bi701848w. PMID 18052212. <a href="/wiki/CiteSeerX_(identifier)" target="_blank">/wiki/CiteSeerX_(identifier)</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Nakanishi T, Nakatsu T, Matsuoka M, Sakata K, Kato H (February 2005). "Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion". Biochemistry. 44 (4): 1136–44. doi:10.1021/bi0484522. PMID 15667207. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Nakanishi T, Nakatsu T, Matsuoka M, Sakata K, Kato H (February 2005). "Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion". Biochemistry. 44 (4): 1136–44. doi:10.1021/bi0484522. PMID 15667207. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Herzberg O, Chen CC, Kapadia G, McGuire M, Carroll LJ, Noh SJ, Dunaway-Mariano D (April 1996). "Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites". Proceedings of the National Academy of Sciences of the United States of America. 93 (7): 2652–7. Bibcode:1996PNAS...93.2652H. doi:10.1073/pnas.93.7.2652. PMC 39685. PMID 8610096. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC39685" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC39685</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> <li id="fn:12"><p>Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, et al. (January 2002). "Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis". Biochemistry. 41 (3): 780–7. doi:10.1021/bi011799+. PMID 11790099. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li> <li id="fn:13"><p>Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, et al. (January 2002). "Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis". Biochemistry. 41 (3): 780–7. doi:10.1021/bi011799+. PMID 11790099. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:13" class="footnote-back-ref">↩</a></p></li> <li id="fn:14"><p>Berg J, Tymoczko J, Stryer L (2012). "The Calvin Cycle and the Pentose Phosphate Pathway". Biochemistry (7th ed.). New York: W.H Freeman. pp. 599–600. ISBN 9780716787242. <a href="9780716787242" target="_blank">9780716787242</a> <a href="#fnref:14" class="footnote-back-ref">↩</a></p></li> <li id="fn:15"><p>Berg J, Tymoczko J, Stryer L (2012). "The Calvin Cycle and the Pentose Phosphate Pathway". Biochemistry (7th ed.). New York: W.H Freeman. pp. 599–600. ISBN 9780716787242. <a href="9780716787242" target="_blank">9780716787242</a> <a href="#fnref:15" class="footnote-back-ref">↩</a></p></li> <li id="fn:16"><p>Chastain C (2010). "Structure, Function, and Post-Translational Regulation of C4 Pyruvate Orthophosphate Dikinase". In Raghavendra A (ed.). C4 Photosynthesis and Related CO2 Concentrating Mechanisms. Springer. pp. 301–305. ISBN 9789048194063. <a href="9789048194063" target="_blank">9789048194063</a> <a href="#fnref:16" class="footnote-back-ref">↩</a></p></li> <li id="fn:17"><p>Berg J, Tymoczko J, Stryer L (2012). "The Calvin Cycle and the Pentose Phosphate Pathway". Biochemistry (7th ed.). New York: W.H Freeman. pp. 599–600. ISBN 9780716787242. <a href="9780716787242" target="_blank">9780716787242</a> <a href="#fnref:17" class="footnote-back-ref">↩</a></p></li> <li id="fn:18"><p>Chastain CJ, Fries JP, Vogel JA, Randklev CL, Vossen AP, Dittmer SK, et al. (April 2002). "Pyruvate,orthophosphate dikinase in leaves and chloroplasts of C(3) plants undergoes light-/dark-induced reversible phosphorylation". Plant Physiology. 128 (4): 1368–78. doi:10.1104/pp.010806. PMC 154264. PMID 11950985. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154264" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154264</a> <a href="#fnref:18" class="footnote-back-ref">↩</a></p></li> <li id="fn:19"><p>Rosche E, Streubel M, Westhoff P (October 1994). "Primary structure of the photosynthetic pyruvate orthophosphate dikinase of the C3 plant Flaveria pringlei and expression analysis of pyruvate orthophosphate dikinase sequences in C3, C3-C4 and C4 Flaveria species". Plant Molecular Biology. 26 (2): 763–9. doi:10.1007/bf00013761. PMID 7948930. S2CID 23276817. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:19" class="footnote-back-ref">↩</a></p></li> <li id="fn:20"><p>Chastain CJ, Fries JP, Vogel JA, Randklev CL, Vossen AP, Dittmer SK, et al. (April 2002). "Pyruvate,orthophosphate dikinase in leaves and chloroplasts of C(3) plants undergoes light-/dark-induced reversible phosphorylation". Plant Physiology. 128 (4): 1368–78. doi:10.1104/pp.010806. PMC 154264. PMID 11950985. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154264" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154264</a> <a href="#fnref:20" class="footnote-back-ref">↩</a></p></li> <li id="fn:21"><p>UniProt 50%-90% clusters: From Clostridium PPDK <a href="/wiki/UniProt" target="_blank">/wiki/UniProt</a> <a href="#fnref:21" class="footnote-back-ref">↩</a></p></li> <li id="fn:22"><p>Stephen P, Vijayan R, Bhat A, Subbarao N, Bamezai RN (September 2008). "Molecular modeling on pyruvate phosphate dikinase of Entamoeba histolytica and in silico virtual screening for novel inhibitors". Journal of Computer-Aided Molecular Design. 22 (9): 647–60. Bibcode:2008JCAMD..22..647S. doi:10.1007/s10822-007-9130-2. PMID 17710553. S2CID 25026913. <a href="/wiki/Bibcode_(identifier)" target="_blank">/wiki/Bibcode_(identifier)</a> <a href="#fnref:22" class="footnote-back-ref">↩</a></p></li> <li id="fn:23"><p>Chastain CJ, Failing CJ, Manandhar L, Zimmerman MA, Lakner MM, Nguyen TH (May 2011). "Functional evolution of C(4) pyruvate, orthophosphate dikinase". Journal of Experimental Botany. 62 (9): 3083–91. doi:10.1093/jxb/err058. PMID 21414960. <a href="https://doi.org/10.1093%2Fjxb%2Ferr058" target="_blank">https://doi.org/10.1093%2Fjxb%2Ferr058</a> <a href="#fnref:23" class="footnote-back-ref">↩</a></p></li> <li id="fn:24"><p>Chastain CJ, Fries JP, Vogel JA, Randklev CL, Vossen AP, Dittmer SK, et al. (April 2002). "Pyruvate,orthophosphate dikinase in leaves and chloroplasts of C(3) plants undergoes light-/dark-induced reversible phosphorylation". Plant Physiology. 128 (4): 1368–78. doi:10.1104/pp.010806. PMC 154264. PMID 11950985. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154264" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154264</a> <a href="#fnref:24" class="footnote-back-ref">↩</a></p></li> <li id="fn:25"><p>Chastain CJ, Fries JP, Vogel JA, Randklev CL, Vossen AP, Dittmer SK, et al. (April 2002). "Pyruvate,orthophosphate dikinase in leaves and chloroplasts of C(3) plants undergoes light-/dark-induced reversible phosphorylation". Plant Physiology. 128 (4): 1368–78. doi:10.1104/pp.010806. PMC 154264. PMID 11950985. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154264" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC154264</a> <a href="#fnref:25" class="footnote-back-ref">↩</a></p></li> <li id="fn:26"><p>Fukayama H, Tsuchida H, Agarie S, Nomura M, Onodera H, Ono K, et al. (November 2001). "Significant accumulation of C(4)-specific pyruvate, orthophosphate dikinase in a C(3) plant, rice". Plant Physiology. 127 (3): 1136–46. doi:10.1104/pp.010641. PMC 129282. PMID 11706193. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC129282" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC129282</a> <a href="#fnref:26" class="footnote-back-ref">↩</a></p></li> </ol>