{"search_session":{},"preferences":{"l":"en","queryLanguage":"en"},"patentId":"086-048-459-743-151","frontPageModel":{"patentViewModel":{"ref":{"entityRefType":"PATENT","entityRefId":"086-048-459-743-151"},"entityMetadata":{"linkedIds":{"empty":true},"tags":[],"collections":[{"id":11813,"type":"PATENT","title":"University of Aberdeen Patent Portfolio","description":"","access":"OPEN_ACCESS","displayAvatar":true,"attested":false,"itemCount":27926,"tags":[],"user":{"id":91044780,"username":"Cambialens","firstName":"","lastName":"","created":"2015-05-04T00:55:26.000Z","displayName":"Cambialens","preferences":"{\"usage\":\"public\",\"beta\":false}","accountType":"PERSONAL","isOauthOnly":false},"notes":[{"id":8443,"type":"COLLECTION","user":{"id":91044780,"username":"Cambialens","firstName":"","lastName":"","created":"2015-05-04T00:55:26.000Z","displayName":"Cambialens","preferences":"{\"usage\":\"public\",\"beta\":false}","accountType":"PERSONAL","isOauthOnly":false},"text":"
Search Applicants and Owners separately: univ* aberdeen. Select more for logical variants. Add to collection. Select all patents in the collection and expand by simple families. Add to collection. Total patents: 1658
Search Applicants and Owners separately: univ* aberdeen. Select more for logical variants. Add to collection. Select all patents in the collection and expand by simple families. Add to collection. Total patents: 1658
(A) providing a reaction mixture comprising \n\n(1) (a) an acyl carrier moiety or (b) enzymes and precursors sufficient to generate the acyl carrier moiety;\n(2) a bacterial enzymatic pathway comprising at least two consecutively acting enzymes selected from the group consisting of: \n\n(a) malonyl-CoA:ACP transacylase,\n(b) β-ketoacyl-ACP synthase III,\n(c) NADPH-dependent β-ketoacyl-ACP reductase,\n(d) β-hydroxyacyl-ACP dehydrase, and\n(e) enoyl-ACP reductase; and\n(3) first substrates and cofactors required for activity of the enzymes;\n
(B) contacting the reaction mixture with a bioactive agent;\n
(C) conducting a high throughput measurement of the activity of the enzymatic pathway; and\n
(D) determining if the contacting alters the activity of the enzymatic pathway."],"number":1,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein the bacterial enzymatic pathway comprises at least three consecutively acting enzymes selected from:\n
(a) malonyl-CoA:ACP transacylase,\n
(b) β-ketoacyl-ACP synthase III,\n
(c) NADPH-dependent β-ketoacyl-ACP reductase,\n
(d) β-hydroxyacyl-ACP dehydrase, and\n
(e) enoyl-ACP reductase."],"number":2,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein the bacterial enzymatic pathway comprises at least four consecutively acting enzymes selected from:\n
(a) malonyl-CoA:ACP transacylase,\n
(b) β-ketoacyl-ACP synthase III,\n
(c) NADPH-dependent β-ketoacyl-ACP reductase,\n
(d) β-hydroxyacyl-ACP dehydrase, and\n
(e) enoyl-ACP reductase."],"number":3,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein the bacterial enzymatic pathway comprises at least five consecutively acting enzymes selected from:\n
(a) malonyl-CoA:ACP transacylase,\n
(b) β-ketoacyl-ACP synthase III,\n
(c) NADPH-dependent β-ketoacyl-ACP reductase,\n
(d) β-hydroxyacyl-ACP dehydrase, and\n
(e) enoyl-ACP reductase."],"number":4,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein the high throughput measurement measures the activity of enoyl-ACP reductase."],"number":5,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein the high throughput measurement comprises:\n
(1) photometrically measuring consumption of NADH; or\n
(2) providing [3H]NADH as a cofactor to the enzymatic pathway and capturing a radioactive product on a support that provides a scintillant."],"number":6,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, further comprising: providing intermediate substrates in a reacting step, wherein the intermediate substrates are not derived from said first substrates and are provided in an amount adapted to maintain such intermediate substrates at a concentration at least approaching the Km of a respective enzyme that acts on the substrate during an assay timeframe."],"number":7,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 7, further comprising: selecting at least one of the enzymes from a corresponding enzyme produced by Staphylococcus aureous, Haemophilus influenzae or Streptococcus pneumoniae. "],"number":8,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 8, further comprising: providing as the enoyl-ACP reductase a NADH-specific enoyl-ACP reductase."],"number":9,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 9, further comprising: providing to the reacting step NADPH in a constant amount such that the NADH consumption by enoyl-ACP reductase (FabI) can be quantitated accurately and without interference, or an amount effective to reduce NADH consumption by more NADPH-dependent enzymes."],"number":10,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 10, further comprising: providing to the reacting step an NADPH regenerating enzyme system."],"number":11,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 8, further comprising: providing as the β-ketoacyl-ACP synthase III a β-ketoacyl-ACP synthase III derived from E. coli or H. influenzae. "],"number":12,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein\n
the malonyl-CoA:ACP transacylase is derived from Streptococcus or Staphylococcus,\n
the β-ketoacyl-ACP synthase III is derived from Streptococcus, Staphylococcus or Escherichia,\n
the NADPH-dependent β-ketoacyl-ACP reductase is derived from Streptococcus or Staphylococcus,\n
the β-hydroxyacyl-ACP dehydrase is derived from Streptococcus or Staphylococcus, and\n
the enoyl-ACP reductase is derived from Staphylococcus or Escherichia."],"number":13,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, wherein the NADPH-dependent β-ketoacyl-ACP reductase is derived from Streptococcus, Staphylococcus or Pseudomonas. "],"number":14,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, further comprising: β-ketoacyl-ACP synthase II as part of the enzymatic pathway."],"number":15,"annotation":false,"title":false,"claim":true},{"lines":["The method of claim 1, further comprising: when a bioactive agent affecting the enzymatic pathway is identified, applying one or more deconvolution assays for determining which enzymes in the enzyme pathway are affected, said deconvolution assays comprising contacting the identified bioactive agent with (i) an enzyme in the enzymatic pathway or (ii) two or more, but less than all, enzymes acting sequentially in the enzymatic pathway."],"number":16,"annotation":false,"title":false,"claim":true},{"lines":["A screening method for biological agents affecting fatty acid biosynthesis:\n
(A) providing a reaction mixture comprising \n\n(1) (a) an acyl carrier moiety or (b) enzymes and precursors sufficient to generate the acyl carrier moiety;\n(2) a bacterial enzymatic pathway comprising at least two consecutively acting enzymes selected from: \n\n(a) malonyl-CoA:ACP transacylase,\n(b) β-ketoacyl-ACP synthase III,\n(c) NADPH-dependent β-ketoacyl-ACP reductase,\n(d) β-hydroxyacyl-ACP dehydrase, and\n(e) enoyl-ACP reductase; and\n(3) first substrates and cofactors required for activity of the enzymes;\n
(B) contacting the reaction mixture with a bioactive agent;\n
(C) conducting a high throughput measurement of the activity of the enzymatic pathway;\n
and determining if the contacting alters the activity of the enzymatic pathway, wherein at least one of the following applies: \n"],"number":17,"annotation":false,"title":false,"claim":true}]}},"filters":{"npl":[],"notNpl":[],"applicant":[],"notApplicant":[],"inventor":[],"notInventor":[],"owner":[],"notOwner":[],"tags":[],"dates":[],"types":[],"notTypes":[],"j":[],"notJ":[],"fj":[],"notFj":[],"classIpcr":[],"notClassIpcr":[],"classNat":[],"notClassNat":[],"classCpc":[],"notClassCpc":[],"so":[],"notSo":[],"sat":[]},"sequenceFilters":{"s":"SEQIDNO","d":"ASCENDING","p":0,"n":10,"sp":[],"si":[],"len":[],"t":[],"loc":[]}}(1) the enoyl-ACP reductase is a NADH-specific enoyl-ACP reductase; or\n(2) the β-ketoacyl-ACP synthase III is a β-ketoacyl-ACP synthase III derived from E. coli or H. influenzae; or\n(3) NADPH is provided to the reacting step in a constant amount such that the NADH consumption by enoyl-ACP reductase (FabI) can be quantitated accurately and without interference, or an amount effective to reduce NADH consumption by more NADPH-dependent enzymes; or\n(4) the NADPH-dependent β-ketoacyl-ACP reductase is derived from Streptococci, Staphylococci or Pseudomonas.\n