会员体验
专利管家(专利管理)
工作空间(专利管理)
风险监控(情报监控)
数据分析(专利分析)
侵权分析(诉讼无效)
联系我们
交流群
官方交流:
QQ群: 891211   
微信请扫码    >>>
现在联系顾问~
热词
    • 1. 发明专利
    • New non-naturally occurring variant of glutaryl amidase comprising histidine or glutamate in its substrate binding pocket, binds cephalosporin C (CPC) as substrate and catalyzes conversion of CPC to 7-aminocephalosporanic acid
    • DE10112608A1
    • 2002-09-19
    • DE10112608
    • 2001-03-14
    • KOLLER KLAUS-PETER
    • KOLLER KLAUS-PETERLANGE GUDRUNSAUBER KLAUSFRITZ-WOLF KARINKABSCH WOLFGANG
    • C07D501/28C12N9/80C12N15/55C12P35/00C12N9/14C07D519/06C12P17/18C12P35/06
    • Non-naturally occurring variant of a glutaryl amidase (GA) (I) which binds cephalosporin C (CPC) as a substrate and catalyzes conversion of the CPC to 7-aminocephalosporanic acid (7-ACA), where the variant comprises a histidine or glutamate in the substrate binding pocket that binds the alpha -amino adipyl moiety of the CPC, is new. A non-naturally occurring variant of a glutaryl amidase (GA) (I) which binds cephalosporin C (CPC) as a substrate and catalyzes conversion of the CPC to 7-aminocephalosporanic acid (7-ACA), where the variant comprises a histidine or glutamate in the substrate binding pocket that binds the alpha -amino adipyl moiety of the CPC. (I) comprises a combination of mutations chosen from PheB177His, LeuB24Arg, ArgB57His; PheB177His, LeuB24Arg, ArgB57His, GlnB50Val; PheB177His, LeuB24Arg, ArgB57His, GlnB50Ala; PheB177His, LeuB24Arg, ArgB57His, GlnB50Val, ValB70His; PheB177His, LeuB24Arg, ArgB57His, GlnB50Ala, ValB70His; PheB177His, LeuB24Arg, ArgB57His, GlnB50Val, ValB70His, TyrB153Leu; PheB177His, LeuB24Arg, ArgB57His, GlnB50Ala, ValB70His, TyrB153Leu; PheB177His, ThrB176Asp; PheB177His, ThrB176Asp, TyrA150Ala; PheB177His, ThrB176Asp, LeuB24Arg, ArgB57His; PheB177His, ThrB176Asp, LeuB24Arg, ArgB57His, TyrA150Ala; PheB177His, ThrB176Asp, GlnB50Arg, ArgB57His; PheB177His, ThrB176Asp, GlnB50Arg, ArgB57His, TyrA150Ala; TyrA150Glu; TyrA150Glu, PheB177His; TyrA150Glu, LeuB24Arg, ArgB57His; TyrA150Glu, LeuB24Arg, ArgB57His, PheB177His; TyrA150Glu, GlnB50Arg, ArgB57His; TyrA150Glu, GlnB50Arg, ArgB57His, PheB177His; PheB177His, ThrB176Asp, TyrA150Ala, TyrB33Ser; PheB177His, ThrB176Asp, LeuB24Arg, ArgB57His, TyrA150Ala, TyrB33Ser; PheB177His, ThrB176Asp, GlnB50Arg, ArgB57His, TyrA150Ala, TyrB33Ser; TyrA150Glu, PheB177His, TyrB33Ser; TyrA150Glu, LeuB24Arg, ArgB57His, TyrB33Ser; PheB177His, LeuB24Arg, ArgB57His, TyrB33Ser; and PheB177His, LeuB24Arg, ArgB57His, TyrB33Ser, ValB70His. Independent claims are also included for: (1) a polynucleotide (II) encoding (I); (2) a nucleic acid vector (III) comprising (II); (3) a host cell (IV) comprising (II) operably linked to regulatory control sequence which direct expression of the variant GA in the host cell; (4) production of (I); (5) production of 7-aminocephalosporanic acid; and (6) modifying (M1) a GA enzyme to enhance the CPC acylase activity of the enzyme, which involves by introducing a non-naturally occurring histidine or glutamate amino acid residue in the substrate binding pocket of the enzyme which histidine or glutamate binds the alpha -amino adipyl moiety of a CPC substrate molecule.
    • 3. 发明专利
    • New non-naturally occurring variant of glutaryl amidase comprising histidine or glutamate in its substrate binding pocket, binds cephalosporin C (CPC) as substrate and catalyzes conversion of CPC to 7-aminocephalosporanic acid
    • DE10148723A1
    • 2003-04-10
    • DE10148723
    • 2001-10-02
    • KOLLER KLAUS-PETER
    • KOLLER KLAUS-PETERLANGE GUDRUNSAUBER KLAUSFRITZ-WOLF KARIN
    • C07D501/02C12N9/80C12N15/55C12P35/00C12N9/86
    • Non-naturally occurring variant of a glutaryl amidase (GA) (I) which binds cephalosporin C (CPC) as a substrate and catalyzes conversion of the CPC to 7-aminocephalosporanic acid (7-ACA), where the variant comprises a histidine or glutamate in the substrate binding pocket that binds the alpha -amino adipyl moiety of the CPC, is new. A non-naturally occurring variant of a glutaryl amidase (GA) (I) which binds cephalosporin C (CPC) as a substrate and catalyzes conversion of the CPC to 7-aminocephalosporanic acid (7-ACA), where the variant comprises a histidine or glutamate in the substrate binding pocket that binds the alpha -amino adipyl moiety of the CPC. (I) comprises a combination of mutations chosen from PheB177His, LeuB24Arg, ArgB57His; PheB177His, LeuB24Arg, ArgB57His, GlnB50Val; PheB177His, LeuB24Arg, ArgB57His, GlnB50Ala; PheB177His, LeuB24Arg, ArgB57His, GlnB50Val, ValB70His; PheB177His, LeuB24Arg, ArgB57His, GlnB50Ala, ValB70His; PheB177His, LeuB24Arg, ArgB57His, GlnB50Val, ValB70His, TyrB153Leu; PheB177His, LeuB24Arg, ArgB57His, GlnB50Ala, ValB70His, TyrB153Leu; PheB177His, ThrB176Asp; PheB177His, ThrB176Asp, TyrA150Ala; PheB177His, ThrB176Asp, LeuB24Arg, ArgB57His; PheB177His, ThrB176Asp, LeuB24Arg, ArgB57His, TyrA150Ala; PheB177His, ThrB176Asp, GlnB50Arg, ArgB57His; PheB177His, ThrB176Asp, GlnB50Arg, ArgB57His, TyrA150Ala; TyrA150Glu; TyrA150Glu, PheB177His; TyrA150Glu, LeuB24Arg, ArgB57His; TyrA150Glu, LeuB24Arg, ArgB57His, PheB177His; TyrA150Glu, GlnB50Arg, ArgB57His; TyrA150Glu, GlnB50Arg, ArgB57His, PheB177His; PheB177His, ThrB176Asp, TyrA150Ala, TyrB33Ser; PheB177His, ThrB176Asp, LeuB24Arg, ArgB57His, TyrA150Ala, TyrB33Ser; PheB177His, ThrB176Asp, GlnB50Arg, ArgB57His, TyrA150Ala, TyrB33Ser; TyrA150Glu, PheB177His, TyrB33Ser; TyrA150Glu, LeuB24Arg, ArgB57His, TyrB33Ser; PheB177His, LeuB24Arg, ArgB57His, TyrB33Ser; and PheB177His, LeuB24Arg, ArgB57His, TyrB33Ser, ValB70His. Independent claims are also included for: (1) a polynucleotide (II) encoding (I); (2) a nucleic acid vector (III) comprising (II); (3) a host cell (IV) comprising (II) operably linked to regulatory control sequence which direct expression of the variant GA in the host cell; (4) production of (I); (5) production of 7-aminocephalosporanic acid; and (6) modifying (M1) a GA enzyme to enhance the CPC acylase activity of the enzyme, which involves by introducing a non-naturally occurring histidine or glutamate amino acid residue in the substrate binding pocket of the enzyme which histidine or glutamate binds the alpha -amino adipyl moiety of a CPC substrate molecule.
    • 6. 发明专利
    • New non-naturally occurring variant of glutaryl amidase comprising histidine or glutamate in its substrate binding pocket, binds cephalosporin C (CPC) as substrate and catalyzes conversion of CPC to 7-aminocephalosporanic acid
    • DE10153389A1
    • 2003-05-15
    • DE10153389
    • 2001-10-31
    • KOLLER KLAUS-PETER
    • KOLLER KLAUS-PETERLANGE GUDRUNSAUBER KLAUSFRITZ-WOLF KARINKABSCH WOLFGANG
    • C12N9/80C12N15/55C12P35/00
    • Non-naturally occurring variant of a glutaryl amidase (GA) (I) which binds cephalosporin C (CPC) as a substrate and catalyzes conversion of the CPC to 7-aminocephalosporanic acid (7-ACA), where the variant comprises a histidine or glutamate in the substrate binding pocket that binds the alpha -amino adipyl moiety of the CPC, is new. A non-naturally occurring variant of a glutaryl amidase (GA) (I) which binds cephalosporin C (CPC) as a substrate and catalyzes conversion of the CPC to 7-aminocephalosporanic acid (7-ACA), where the variant comprises a histidine or glutamate in the substrate binding pocket that binds the alpha -amino adipyl moiety of the CPC. (I) comprises a combination of mutations chosen from PheB177His, LeuB24Arg, ArgB57His; PheB177His, LeuB24Arg, ArgB57His, GlnB50Val; PheB177His, LeuB24Arg, ArgB57His, GlnB50Ala; PheB177His, LeuB24Arg, ArgB57His, GlnB50Val, ValB70His; PheB177His, LeuB24Arg, ArgB57His, GlnB50Ala, ValB70His; PheB177His, LeuB24Arg, ArgB57His, GlnB50Val, ValB70His, TyrB153Leu; PheB177His, LeuB24Arg, ArgB57His, GlnB50Ala, ValB70His, TyrB153Leu; PheB177His, ThrB176Asp; PheB177His, ThrB176Asp, TyrA150Ala; PheB177His, ThrB176Asp, LeuB24Arg, ArgB57His; PheB177His, ThrB176Asp, LeuB24Arg, ArgB57His, TyrA150Ala; PheB177His, ThrB176Asp, GlnB50Arg, ArgB57His; PheB177His, ThrB176Asp, GlnB50Arg, ArgB57His, TyrA150Ala; TyrA150Glu; TyrA150Glu, PheB177His; TyrA150Glu, LeuB24Arg, ArgB57His; TyrA150Glu, LeuB24Arg, ArgB57His, PheB177His; TyrA150Glu, GlnB50Arg, ArgB57His; TyrA150Glu, GlnB50Arg, ArgB57His, PheB177His; PheB177His, ThrB176Asp, TyrA150Ala, TyrB33Ser; PheB177His, ThrB176Asp, LeuB24Arg, ArgB57His, TyrA150Ala, TyrB33Ser; PheB177His, ThrB176Asp, GlnB50Arg, ArgB57His, TyrA150Ala, TyrB33Ser; TyrA150Glu, PheB177His, TyrB33Ser; TyrA150Glu, LeuB24Arg, ArgB57His, TyrB33Ser; PheB177His, LeuB24Arg, ArgB57His, TyrB33Ser; and PheB177His, LeuB24Arg, ArgB57His, TyrB33Ser, ValB70His. Independent claims are also included for: (1) a polynucleotide (II) encoding (I); (2) a nucleic acid vector (III) comprising (II); (3) a host cell (IV) comprising (II) operably linked to regulatory control sequence which direct expression of the variant GA in the host cell; (4) production of (I); (5) production of 7-aminocephalosporanic acid; and (6) modifying (M1) a GA enzyme to enhance the CPC acylase activity of the enzyme, which involves by introducing a non-naturally occurring histidine or glutamate amino acid residue in the substrate binding pocket of the enzyme which histidine or glutamate binds the alpha -amino adipyl moiety of a CPC substrate molecule.