1zxx

<table><tr><td colspan='2'>[[1zxx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermobacterium_bulgaricum"_orla-jensen_1919 "thermobacterium bulgaricum" orla-jensen 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZXX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pfkA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1585 "Thermobacterium bulgaricum" Orla-Jensen 1919])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] </span></td></tr>

[[https://www.uniprot.org/uniprot/PFKA_LACDE PFKA_LACDE]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_00339]<ref>PMID:1828763</ref>

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== Publication Abstract from PubMed ==

Phosphofructokinase from Lactobacillus delbrueckii subspecies bulgaricus (LbPFK) has been reported to be a nonallosteric analogue of phosphofructokinase from Escherichia coli at pH 8.2 [Le Bras et al. (1991) Eur. J. Biochem. 198, 683-687]. A reexamination of the kinetics of this enzyme shows LbPFK to have limited binding affinity toward the allosteric ligands, MgADP and PEP, with dissociation constants of approximately 20 mM for both. Their allosteric effects are observed only at high concentrations of these ligands, with both exhibiting inhibitory effects on substrate binding. No pH dependence was observed for the binding and the influence of MgADP and PEP on the enzyme. To attempt to explain these results, the crystal structure of LbPFK was solved using molecular replacement to 1.86 A resolution. A comparative study of the LbPFK structure with that of phosphofructokinases from E. coli (EcPFK) and Bacillus stearothermophilus (BsPFK) reveals a structure with conserved fold and substrate binding site. The effector binding site, however, shows many differences that could explain the observed decreases in binding affinity for MgADP and PEP in LbPFK as compared to the other two enzymes.

Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus.,Paricharttanakul NM, Ye S, Menefee AL, Javid-Majd F, Sacchettini JC, Reinhart GD Biochemistry. 2005 Nov 22;44(46):15280-6. PMID:16285731<ref>PMID:16285731</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1zxx" style="background-color:#fffaf0;"></div>

[[Category: Thermobacterium bulgaricum orla-jensen 1919]]

[[Category: 6-phosphofructokinase]]

[[Category: Javid-Majd, F]]

[[Category: Menefee, A L]]

[[Category: Paricharttanakul, N M]]

[[Category: Reinhart, G D]]

[[Category: Sacchettini, J C]]

[[Category: Ye, S]]

[[Category: Transferase]]