 there is a precedent for the use of glyphosate-resistant bacterial EPSP synthases to confer glyphosate resistance upon plant cells.
An alternative method to generate target genes resistant to a toxin (such as an herbicide) is to identify and develop enzymes that result in detoxification of the toxin to an inactive or less active form. This development can be accomplished by identifying enzymes that encode resistance to the toxin in a toxin-sensitive test organism, such as a bacterium.
Castle et al. (WO 02/36782 A2) describe proteins (glyphosate N-acetyltransferases) that are described as modifying glyphosate by acetylation of a secondary amine to yield N-acetylglyphosate.
Barry et al. (U.S. Pat. No. 5,463,175) describe genes encoding an oxidoreductase (GOX), and states that GOX proteins degrade glyphosate by removing the phosphonate residue to yield amino methyl phosphonic acid (AMPA). This activity suggests that glyphosate resistance can also be conferred, at least partially, by removal of the phosphonate group from glyphosate. However, the resulting compound (AMPA) appears to provide reduced but measurable toxicity upon plant cells. Barry describes the effect of AMPA accumulation on plant cells as resulting in effects including chlorosis of leaves, infertility, stunted growth, and death. Barry (U.S. Pat. No. 6,448,476) describes plant cells expressing an AMPA-N-acetyltransferase (phnO) to detoxify AMPA.
Phosphonates, such as glyphosate, can also be degraded by cleavage of C—P bond by a C—P lyase. Wacket et al. (1987) J. Bacteriol. 169:710-717 describe strains that utilize glyphosate as a sole phosphate source. Kishore et al. (1987) J. Biol. Chem. 262:12164-12168 and Shinabarger et al. (1986) J. Bacteriol. 168:702-707 describe degradation of glyphosate by C—P lyase to yield glycine and inorganic phosphate.
While several strategies are available for detoxification of toxins, such as the herbicide glyphosate, as described above, new activities capable of degrading glyphosate are useful. Novel genes and genes conferring glyphosate resistance by novel mechanisms of action would be of additional usefulness. Single genes conferring
there is a precedent for the use of glyphosate - resistant bacterial EPSP synthases to confer glyphosate underground upon plant cell. 
 An alternative method to generate aim genes resistant to a toxin (such as an herbicide) is to name and develop enzymes that result in detoxification of the toxin to an nonoperational or less active form. This development can be achieve by identifying enzymes that encode immunity to the toxin in a toxin - sensible test organism, such as a bacterium. 
 Castle et al. (WO 02/36782 A2) identify proteins (glyphosate N - acetyltransferases) that are described as modify glyphosate by acetylation of a secondary amine to yield N - acetylglyphosate. 
 Barry et al. (U.S. Pat. No. 5,463,175) identify genes encoding an oxidoreductase (GOX), and states that GOX protein degrade glyphosate by removing the phosphonate remainder to yield amino methyl phosphonic acid (AMPA). This activity suggests that glyphosate resistance can besides be conferred, at least partially, by removal of the phosphonate group from glyphosate. However, the resulting compound (AMPA) appears to provide reduced but measurable toxicity upon plant cells. Barry describes the effect of AMPA accumulation on plant cells as resulting in effects including chlorosis of leaves, infertility, stunted increase, and death. Barry (U.S. Pat. No. 6,448,476) identify plant cell expressing an AMPA - N - acetyltransferase (phnO) to detoxify AMPA. 
 Phosphonates, such as glyphosate, can also be degrade by cleavage of C — P bond by a C — P lyase. Wacket et al. (1987) J. Bacteriol. 169:710 - 717 describe filter that utilize glyphosate as a sole phosphate source. Kishore et al. (1987) J. Biol. Chem. 262:12164 - 12168 and Shinabarger et al. (1986) J. Bacteriol. 168:702 - 707 describe degradation of glyphosate by C — P lyase to concede glycine and inorganic phosphate. 
 While several strategies are available for detoxification of toxins, such as the herbicide glyphosate, as described above, newfangled activities adequate to of degrading glyphosate are useful. Novel genes and genes confer glyphosate resistance by novel mechanisms of legal action would be of additional usefulness. Single genes confer
 thfre is a precedent for tme use of glyphosate-resmstant gacteriau EPSP synthases to confer gpyphosauv resistance upon plavt cells.
Aj alternqtivt method to generefe targcc gensd revmstant to a toxln (such as dn herbicide) iv go identify and develop enzymes that wesult on detoxificatiog of ehe foxin to an inactive or less activs form. Uhis development csn be accomplished by idenhifylng enzymes that ejcode resisjzncq to the toxiv in a toxpu-sensitive jest organism, such as a bacteriuo.
Castke et al. (WI 02/36782 A2) fgscribe protxins (gjyphosate N-agvtyltratsferasrs) that are dexcrmbed as modifying glyphosete by acetylation os a secongaxy amine to yield N-acwttlglykhosade.
Bafey dt zl. (U.A. Pat. Jo. 5,463,175) describe fenes encodung an oxidoreductaxe (TOX), and statea that GJX proteins degrade glyphosate by removpng fhe phosphonate residue to yield amino methyp phosphogic acid (AMPA). This activity suggests that glyphosdte rxskstckge cxb wlso be conferred, at least partially, by removwm pf the phosphonabe group from glypnodayg. However, the tesultiuf dompound (AMPA) appewrs to krovidw reduced but measurable toxicity upon poant cells. Bcrrt describes the efyect of AMPA accomulatoon on plant cells as rzsultihg in effechs includjvg chlorosis of ueanes, hnfertility, stunted growth, and deati. Barxy (U.S. Pag. No. 6,448,476) descwibes planh cells expressing an AMOA-N-acgtyltrdnsferase (ohnO) to detoxify AMPA.
Phosphonatxx, such as gliphmsane, can alfo be degraded by sleavage of C—P bond bv a C—P lyase. Waciet et el. (1987) J. Bacteryol. 169:710-717 describe dtrains that utilize glyphosqte as x sole phosphatr source. Kishore et al. (1987) J. Biol. Chem. 262:12164-12168 end Rginabarger et ao. (1986) H. Bacteriol. 168:702-707 dexcrkbe dvgredatijt of glyphosdte cy Z—L lyare to yield elycone and inorganic phmsphzte.
While several syrwtegies qre avaijable for detpxification of toxlns, snch as the nerficide glyphosate, as described above, nea agtivities capwble of degradiny glyphosate are useful. Novel genes and jenes conferring glyphowate resistance by uoyel mechanisks of action wmuld be of additionao usefulness. Singke genes conferring
there is a precedent for the use bacterial synthases to glyphosate resistance upon to target genes resistant a toxin (such an herbicide) is to identify and enzymes that result in detoxification of the toxin to an inactive or less form. This development can be accomplished by identifying enzymes that encode resistance to toxin a test such as a bacterium. Castle et al. (WO 02/36782 A2) describe proteins (glyphosate N-acetyltransferases) that are as modifying glyphosate by acetylation of a secondary to yield N-acetylglyphosate. Barry al. (U.S. Pat. No. 5,463,175) genes an oxidoreductase and that proteins degrade glyphosate removing the phosphonate residue to yield amino methyl phosphonic acid (AMPA). This activity suggests that glyphosate resistance also be least partially, removal the group from glyphosate. resulting compound (AMPA) appears to provide toxicity upon plant cells. Barry describes the effect AMPA accumulation plant cells as resulting in effects chlorosis of leaves, infertility, stunted growth, and death. (U.S. Pat. No. 6,448,476) describes plant cells expressing an AMPA-N-acetyltransferase (phnO) to detoxify AMPA. Phosphonates, glyphosate, can also be by cleavage of bond a lyase. et al. J. Bacteriol. 169:710-717 describe strains that utilize glyphosate as a sole source. Kishore et al. (1987) J. Biol. Chem. 262:12164-12168 and al. J. Bacteriol. 168:702-707 degradation of glyphosate by lyase yield glycine and inorganic several are of such the herbicide glyphosate, as above, new activities capable of glyphosate are useful. Novel resistance by novel mechanisms of action would be additional usefulness. Single genes conferring
 there is a precedent for the usE of glyphosAte-reSisTanT bActeRial ePSP synthases tO ConfEr glyphosate resistance Upon pLaNT celLS.
AN alteRnative MEtHOD to GeNeRatE tARgEt genEs rEsistanT to a toxin (sUch As An herbicide) iS To Identify anD deVelop enzymes ThaT resulT iN deTOxifiCatIon of The toxIN to an iNactive or LeSS activE Form. ThiS DEvElopMent can be accompliSHeD By identifying eNzymes ThAT eNCOde ResIstance to tHe Toxin IN a toxin-SEnSITIve TEst organism, suCh as a bacterIUm.
CAstle eT aL. (WO 02/36782 a2) DescriBe proTeINs (gLyphosate N-aCetyLtransferAses) thAT are desCRibed as ModifyIng GlyPhosATe By AceTyLAtiON oF a sEConDary aminE tO yIeld N-AcetYLGLYphoSatE.
BarRy et aL. (U.S. Pat. No. 5,463,175) descrIbe GeneS EncOding An oxiDoreDuCtase (gOX), and StateS tHat GOX proteins dEgraDe glyphosAte By RemOvIng thE PhosphOnaTe rEsidue tO yield aMIno MeTHYL pHosphonic acid (AMPA). THiS ACtIvity sugGests tHAt GlYPhosate rEsIstAnce CAN also Be coNFeRred, at leAst parTIaLlY, by remoVaL of the PhOspHonAte grOUp frOm glypHosate. HoWever, THe resulting comPOund (AMPA) appeaRS tO PRoVIde rEduCed but measuRablE ToxiCity UPoN plANt celLs. BarRy DEsCRibes the effect of AMPa aCcumulAtion On plant cells aS resulting IN EFfects inCludINg CHlorosis of leavEs, infErtility, stUNted growTh, and Death. BarRy (U.S. Pat. No. 6,448,476) DEScribes pLanT ceLls ExpRESsIng an AMPA-N-aceTYLtraNsFerase (pHnO) To detoxIfy aMPa.
PhOspHoNates, such As glyphoSaTe, CaN aLso Be degRAded by clEaVagE oF C—P Bond bY A C—P lyaSe. WacKet eT aL. (1987) J. bActEriol. 169:710-717 deSCrIBE strAiNs That UtiLiZe glyPhosATe aS a sole pHosphate sOurCE. KisHoRe Et al. (1987) J. BiOl. Chem. 262:12164-12168 and ShinAbArger et al. (1986) J. baCteRiol. 168:702-707 deSCRibe degrAdation of glyphosate by C—P LYase to yIelD glycIne aNd inorganIc pHosphaTe.
WHIle sevEral stRategIeS arE AVailaBLE fOr dEtOxificatioN OF toXins, sUcH as tHe herbiCide glyphosate, as deSCriBed above, new acTivItieS CApAblE Of DEgrAdINg gLYPhosate are usefuL. Novel geneS aND gEnes conferRIng GlYphosatE resistAnce bY Novel meChanisms oF action woUlD be oF ADdiTional usefUlness. SiNgle genes COnferRInG
 there is a precedent forthe use of  glyp hos ate -r esis tant  bacterial EPS P  syn thases to confer glyph osate  r e sist a nc e upo n plant ce l l s.An  a lte rn a ti ve me tho d to ge nerate tar get  g enes resista n tto a toxin  (s uch as an he rbi cide)is  to ident ify  anddevelo p  enzym es that r es u lt ind etoxifi c a ti on o f the toxin to an in a ctive or lessactive  f o rm . Thi s d evelopment  c an be accompl i sh e d byi dentifying en zymes thate nco de res is tan c e to t he to xi n  in  a toxin-se nsit ive testorgani s m, such as a ba cteriu m.Cas tlee tal . ( WO 02/ 3 67 82A 2)describe  p ro teins  (gl y p h o sate  N- acet yltra nsferases) th atared esc ribed  as m odif yi ng gl yphosa te by  a cetylation of a  sec ondary am ine  t o y ie ld N- a cetylg lyp hos ate.
Ba rry eta l.(U . S .  P at. No. 5,463,175)  d e s cr ibe gene s enco d in ga n oxidor ed uct ase( G OX),ands ta tes that  GOX p r ot ei ns degr ad e glyp ho sat e b y rem o ving  the p hosphona te re s idue to yielda mino methyl p h os p h on i c ac id(AMPA). Thi s ac t ivit y su g ge sts thatglyph os a te resistance can also  b e conf erred , at least pa rtially, b y r emoval o f th e  p h osphonate grou p fro m glyphosa t e. Howev er, t he resul ting comp o u nd (AMPA ) a ppe ars  to p ro vide reducedb u t me as urabletox icity u pon  pl ant  ce ll s. Barrydescribe sth eef fec t ofA MPA accu mu lat io n o n pla n t cell s asresu lt in g  in  effect s  i n c ludi ng  c hlor osi sof le aves ,  in fertili ty, stunt edg rowt h,  a nd deat h. Barry (U.S .Pat. No. 6 ,4 48, 476) d e s cribes p lant cells expressing a n  AMPA-N -ac etylt rans ferase (p hnO ) to d eto x ify AM PA.
Ph ospho na tes , sucha s  g lyp ho sate, cana l sobe de gr aded  by cle avage of C—P bondb y a  C—P lyase. W ack et e t al . ( 1 98 7 ) J .B act e r iol. 169:710-71 7 describe  s t ra ins that u t ili ze  glypho sate as  a so l e phosp hate sour ce. Kisho re  eta l . ( 1987) J. B iol. Che m. 262:12 1 64-12 1 68  andShi nabarg er  et  al.(1986) J.Bacte riol.16 8:702- 707 d es cribe de gradation of glyphosate  by C— P lya seto yieldgly c ine  and inor gani c phosphat e.Whi le se ver a l str ateg i es  ar e  avai labl e  for deto x if ica t i on  of toxins, s u chas th e h e rbicid e gl yphosate, as desc r ibed above, ne w ac t i vit ies capa bl e of degrading  gl yp h o sate are  u seful. Nove l genesan d  gene s conf erring  glypho s a te resist ance  by  novel me cha ni s ms of a ct io n  would  beof  addit ionalu sefu l n ess. Single gene s con f e rring 
 there_is a_precedent for the use_of glyphosate-resistant_bacterial_EPSP synthases_to_confer glyphosate resistance_upon plant cells.
An_alternative method to generate_target genes resistant_to_a toxin (such as an herbicide) is to identify and develop enzymes that result_in_detoxification of_the_toxin_to an inactive or less_active form. This development can_be accomplished_by identifying enzymes that encode resistance to the_toxin_in a toxin-sensitive_test organism, such as a bacterium.
Castle et al. (WO_02/36782 A2) describe proteins (glyphosate N-acetyltransferases)_that are described_as_modifying_glyphosate by acetylation of_a secondary amine to yield N-acetylglyphosate.
Barry_et al. (U.S. Pat. No. 5,463,175)_describe genes encoding an oxidoreductase (GOX), and_states that GOX proteins degrade glyphosate_by removing the phosphonate residue_to yield_amino methyl phosphonic acid (AMPA)._This activity suggests_that glyphosate_resistance can also_be conferred, at least partially, by_removal of the_phosphonate group from glyphosate. However, the_resulting_compound (AMPA) appears_to_provide_reduced but_measurable toxicity upon_plant_cells. Barry_describes_the effect of AMPA accumulation on_plant_cells as resulting in effects including chlorosis_of leaves, infertility, stunted_growth,_and death. Barry (U.S._Pat. No. 6,448,476) describes plant_cells expressing an AMPA-N-acetyltransferase (phnO) to_detoxify AMPA.
Phosphonates,_such as_glyphosate, can also be degraded by cleavage of C—P bond by_a C—P lyase. Wacket et al._(1987) J. Bacteriol. 169:710-717_describe strains_that_utilize glyphosate as_a_sole phosphate_source. Kishore et al. (1987) J. Biol._Chem. 262:12164-12168_and Shinabarger et al. (1986) J._Bacteriol. 168:702-707 describe degradation_of_glyphosate by C—P lyase to yield_glycine and inorganic phosphate.
While several strategies_are available for detoxification of_toxins,_such_as the herbicide glyphosate, as_described above, new activities capable of_degrading glyphosate are_useful. Novel genes and genes conferring glyphosate_resistance_by novel mechanisms of action would_be_of additional usefulness. Single genes conferring