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3g7q

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    Comparing version 16:30, 14 May 2015 by cawprice with version 14:52, 18 May 2015 by cawprice.
    {{ template.Protein{ leadContact:"", title:"Crystal structure of valine-pyruvate aminotransferase AvtA (NP_462565.1) from Salmonella typhimurium LT2 at 1.80 A resolution. To be published",site:'JCSG', status:'In PDB', date:"2009-02-10", targetid:"391498", pdbid:"3g7q", source:"Salmonella typhimurium lt2", relatedPDBs:[], refids:"NP_462565.1, 3.40.640.10, 325186", molwt:"46582.42", residues:"416", isopoint:"5.74", sequence:"mtfslfgdkftrhsgitrlmedlndglrtpgaimlgggnpahipamqdyfqtlltdmvesgkaadalcn ydgpqgktallnalavllretlgwdiepqnialtngsqsaffylfnlfagrradgstkkvlfplapeyi gyadsgleddlfvsarpniellpegqfkyhvdfehlhigeetgmicvsrptnptgnvitdeelmkldrl anqhniplvidnaygvpfpgiifsearplwnpniilcmslsklglpgsrcgiiiandktitaianmngi islapggmgpammcemikrndllrlsetvikpfyyqrvqqtiaiirrylseerclihkpegaiflwlwf kdlpittellyqrlkargvlmvpghyffpgldkpwphthqcmrmnyvpepdkieagvkilaeeierawreg", method:"XRAY", numchains:"1", resolution:"1.80", rfree:"0.19577", mattcoeff:"2.94", rfactor:"0.17797", waters:"280", solcontent:"58.23", ligands:"", metals:"", model:"False", uniprot:"Q8ZL86", pubmed:"" } }}

    ...

    StAvtA enzymaticStAvtAenzymatic activity followed Michaelis-Menten kinetics in both the forward and reverse directions. The Km for L-alanine was 2.2 mM and the kcat was 3.8 s-1; the Km for 3-methyl-2-oxobutanoate was 0.010 mM and the kcat was 19 s-1 (Figure 2, panels A and B).  These values are similar to published parameters for the VPATs from Psychrobacter arcticus (3IF2; alanine Km = 4.4 mM, kcat = 77.8 s-1; 3-methyl-2-oxobutanoate Km = 0.28 mM, kcat = 46.3 s-1; 100 mM Tris pH 8, 125 µM PLP, 0.28 mM NADH, 4 U/mL LDH, and 54 nM 3IF2)5 and Brevibacterium flavum ATCC 14067 (alanine Km = 1.5 mM; 3-methyl-2-oxobutanoate Km = 0.23 mM)6. The StAvtA Km for L-valine was 0.65 mM and the kcat was 0.0014 s-1 (Figure 2, panel C), indicating that valine may have a higher affinity than alanine but the overall turnover is much slower.

    ...


    Version from 16:30, 14 May 2015

    This revision modified by cawprice (Ban)
    {{ template.Protein{ leadContact:"", title:"Crystal structure of valine-pyruvate aminotransferase AvtA (NP_462565.1) from Salmonella typhimurium LT2 at 1.80 A resolution. To be published",site:'JCSG', status:'In PDB', date:"2009-02-10", targetid:"391498", pdbid:"3g7q", source:"Salmonella typhimurium lt2", relatedPDBs:[], refids:"NP_462565.1, 3.40.640.10, 325186", molwt:"46582.42", residues:"416", isopoint:"5.74", sequence:"mtfslfgdkftrhsgitrlmedlndglrtpgaimlgggnpahipamqdyfqtlltdmvesgkaadalcn ydgpqgktallnalavllretlgwdiepqnialtngsqsaffylfnlfagrradgstkkvlfplapeyi gyadsgleddlfvsarpniellpegqfkyhvdfehlhigeetgmicvsrptnptgnvitdeelmkldrl anqhniplvidnaygvpfpgiifsearplwnpniilcmslsklglpgsrcgiiiandktitaianmngi islapggmgpammcemikrndllrlsetvikpfyyqrvqqtiaiirrylseerclihkpegaiflwlwf kdlpittellyqrlkargvlmvpghyffpgldkpwphthqcmrmnyvpepdkieagvkilaeeierawreg", method:"XRAY", numchains:"1", resolution:"1.80", rfree:"0.19577", mattcoeff:"2.94", rfactor:"0.17797", waters:"280", solcontent:"58.23", ligands:"", metals:"", model:"False", uniprot:"Q8ZL86", pubmed:"" } }}

    ...

    StAvtAenzymatic activity followed Michaelis-Menten kinetics in both the forward and reverse directions. The Km for L-alanine was 2.2 mM and the kcat was 3.8 s-1; the Km for 3-methyl-2-oxobutanoate was 0.010 mM and the kcat was 19 s-1 (Figure 2, panels A and B).  These values are similar to published parameters for the VPATs from Psychrobacter arcticus (3IF2; alanine Km = 4.4 mM, kcat = 77.8 s-1; 3-methyl-2-oxobutanoate Km = 0.28 mM, kcat = 46.3 s-1; 100 mM Tris pH 8, 125 µM PLP, 0.28 mM NADH, 4 U/mL LDH, and 54 nM 3IF2)5 and Brevibacterium flavum ATCC 14067 (alanine Km = 1.5 mM; 3-methyl-2-oxobutanoate Km = 0.23 mM)6. The StAvtA Km for L-valine was 0.65 mM and the kcat was 0.0014 s-1 (Figure 2, panel C), indicating that valine may have a higher affinity than alanine but the overall turnover is much slower.

    ...


    Version as of 14:52, 18 May 2015

    This revision modified by cawprice (Ban)
    {{ template.Protein{ leadContact:"", title:"Crystal structure of valine-pyruvate aminotransferase AvtA (NP_462565.1) from Salmonella typhimurium LT2 at 1.80 A resolution. To be published",site:'JCSG', status:'In PDB', date:"2009-02-10", targetid:"391498", pdbid:"3g7q", source:"Salmonella typhimurium lt2", relatedPDBs:[], refids:"NP_462565.1, 3.40.640.10, 325186", molwt:"46582.42", residues:"416", isopoint:"5.74", sequence:"mtfslfgdkftrhsgitrlmedlndglrtpgaimlgggnpahipamqdyfqtlltdmvesgkaadalcn ydgpqgktallnalavllretlgwdiepqnialtngsqsaffylfnlfagrradgstkkvlfplapeyi gyadsgleddlfvsarpniellpegqfkyhvdfehlhigeetgmicvsrptnptgnvitdeelmkldrl anqhniplvidnaygvpfpgiifsearplwnpniilcmslsklglpgsrcgiiiandktitaianmngi islapggmgpammcemikrndllrlsetvikpfyyqrvqqtiaiirrylseerclihkpegaiflwlwf kdlpittellyqrlkargvlmvpghyffpgldkpwphthqcmrmnyvpepdkieagvkilaeeierawreg", method:"XRAY", numchains:"1", resolution:"1.80", rfree:"0.19577", mattcoeff:"2.94", rfactor:"0.17797", waters:"280", solcontent:"58.23", ligands:"", metals:"", model:"False", uniprot:"Q8ZL86", pubmed:"" } }}

    ...

    StAvtA enzymatic activity followed Michaelis-Menten kinetics in both the forward and reverse directions. The Km for L-alanine was 2.2 mM and the kcat was 3.8 s-1; the Km for 3-methyl-2-oxobutanoate was 0.010 mM and the kcat was 19 s-1 (Figure 2, panels A and B).  These values are similar to published parameters for the VPATs from Psychrobacter arcticus (3IF2; alanine Km = 4.4 mM, kcat = 77.8 s-1; 3-methyl-2-oxobutanoate Km = 0.28 mM, kcat = 46.3 s-1; 100 mM Tris pH 8, 125 µM PLP, 0.28 mM NADH, 4 U/mL LDH, and 54 nM 3IF2)5 and Brevibacterium flavum ATCC 14067 (alanine Km = 1.5 mM; 3-methyl-2-oxobutanoate Km = 0.23 mM)6. The StAvtA Km for L-valine was 0.65 mM and the kcat was 0.0014 s-1 (Figure 2, panel C), indicating that valine may have a higher affinity than alanine but the overall turnover is much slower.

    ...


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