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<p>72.78.91.171: </p> <hr /> <div>{{enzyme<br /> | Name = pantoate-beta-alanine ligase<br /> | EC_number = 6.3.2.1<br /> | CAS_number = 9023-49-8<br /> | IUBMB_EC_number = 6/3/2/1<br /> | GO_code = 0004592<br /> | image = <br /> | width = <br /> | caption = <br /> }}<br /> In [[enzymology]], a '''pantoate-beta-alanine ligase''' ({{EC number|6.3.2.1}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]<br /> <br /> :ATP + (R)-pantoate + beta-alanine &lt;math&gt;\rightleftharpoons&lt;/math&gt; AMP + diphosphate + (R)-pantothenate<br /> <br /> The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]], [[(R)-pantoate]], and [[beta-alanine]], whereas its 3 [[product (chemistry)|products]] are [[adenosine monophosphate|AMP]], [[diphosphate]], and [[(R)-pantothenate]].<br /> <br /> This enzyme belongs to the family of [[ligase]]s, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is '''(R)-pantoate:beta-alanine ligase (AMP-forming)'''. Other names in common use include '''pantothenate synthetase''', '''pantoate activating enzyme''', '''pantoic-activating enzyme''', and '''D-pantoate:beta-alanine ligase (AMP-forming)'''. This enzyme participates in [[beta-alanine metabolism]] and [[pantothenate and CoA biosynthesis]].<br /> <br /> ==Structural studies==<br /> <br /> As of late 2007, 15 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1IHO}}, {{PDB link|1MOP}}, {{PDB link|1N2B}}, {{PDB link|1N2E}}, {{PDB link|1N2G}}, {{PDB link|1N2H}}, {{PDB link|1N2I}}, {{PDB link|1N2J}}, {{PDB link|1N2O}}, {{PDB link|1UFV}}, {{PDB link|1V8F}}, {{PDB link|2A7X}}, {{PDB link|2A84}}, {{PDB link|2A86}}, and {{PDB link|2A88}}.<br /> <br /> ==References==<br /> {{reflist|1}}<br /> * {{cite journal | author = GINOZA HS, ALTENBERN RA | year = 1955 | title = The pantothenate-synthesizing enzyme in cell-free extracts of Brucella abortus, strain 19 | journal = Arch. Biochem. | volume = 56 | pages = 537&amp;ndash;41 | pmid = 14377603 | doi = 10.1016/0003-9861(55)90273-3 | issue = 2 }}<br /> * {{cite journal | author = MAAS WK | year = 1952 | title = Pantothenate studies. III. Description of the extracted pantothenate-synthesizing enzyme of Escherichia coli | journal = J. Biol. Chem. | volume = 198 | pages = 23&amp;ndash;32 | pmid = 12999714 | issue = 1 }}<br /> * {{cite journal | author = Maas WK | year = 1956 | title = Mechanism of the enzymatic synthesis of pantothenate from beta-alanine and pantoate | journal = Fed. Proc. | volume = 15 | pages = 305&amp;ndash;306 }}<br /> <br /> {{DEFAULTSORT:Pantoate-beta-alanine ligase}}<br /> [[Category:EC 6.3.2]]<br /> [[Category:Enzymes of known structure]]<br /> <br /> <br /> {{ligase-stub}}</div>

72.78.91.171