يعرض 1 - 20 نتائج من 35 نتيجة بحث عن '"Kantrowitz, E R"', وقت الاستعلام: 0.58s تنقيح النتائج
  1. 1
    Academic Journal
    Mutation of Arg-166 of AlkalinePhosphatase Alters the Thio Effect but Not the Transition State for Phosphoryl Transfer.Implications for the Interpretation of Thio Effects in Reactions of Phosphatases

    المؤلفون: Holtz, K. M., Catrina, I. E., Hengge, Alvan C., Kantrowitz, E. R.

    المصدر: Chemistry and Biochemistry Faculty Publications

    مصطلحات موضوعية: mutation, alkaline, phosphatase, transition state, thio effects, Chemistry

    Relation: https://digitalcommons.usu.edu/chem_facpub/397

    الاتاحة: https://digitalcommons.usu.edu/chem_facpub/397
    https://doi.org/10.1021/bi000899x

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  2. 2
    Academic Journal
    Shared active sites of fructose-1,6-bisphosphatase. Arginine 243 mediates substrate binding and fructose 2,6-bisphosphate inhibition.

    المؤلفون: Giroux, E, Williams, M K, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry ; volume 269, issue 50, page 31404-31409 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(18)31708-3
    https://api.elsevier.com/content/article/PII:S0021925818317083?httpAccept=text/xml
    https://api.elsevier.com/content/article/PII:S0021925818317083?httpAccept=text/plain

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  3. 3
    Academic Journal
    Mutations at histidine 412 alter zinc binding and eliminate transferase activity in Escherichia coli alkaline phosphatase.

    المؤلفون: Ma, L, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry ; volume 269, issue 50, page 31614-31619 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(18)31738-1
    https://api.elsevier.com/content/article/PII:S0021925818317381?httpAccept=text/xml
    https://api.elsevier.com/content/article/PII:S0021925818317381?httpAccept=text/plain

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  4. 4
    Academic Journal
    Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase.

    المؤلفون: Fetler, Luc, Tauc, Patrick, Baker, D. P., Macol, C. P., Kantrowitz, E. R., Vachette, P.

    المساهمون: Synthèse, Structure et Fonction de Molécules Bioactives (SSFMB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie et de Pharmacologie Appliquée (LBPA), École normale supérieure - Cachan (ENS Cachan)-Centre National de la Recherche Scientifique (CNRS), Merkert Chemistry Center, Boston College (BC), Institut de biochimie et biophysique moléculaire et cellulaire (IBBMC), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS)

    المصدر: ISSN: 0961-8368.

    مصطلحات موضوعية: MESH: Adenosine Triphosphate, MESH: Allosteric Regulation, MESH: Amino Acid Substitution, MESH: Aspartate Carbamoyltransferase, MESH: Aspartic Acid, MESH: Escherichia coli, MESH: Phosphonoacetic Acid, MESH: Protein Structure, Quaternary, MESH: Substrate Specificity, MESH: X-Rays, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics

    Relation: info:eu-repo/semantics/altIdentifier/pmid/11967364; hal-00216107; https://hal.science/hal-00216107; PUBMED: 11967364

    الاتاحة: https://hal.science/hal-00216107

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  5. 5
    Academic Journal
    Catalytic-regulatory subunit interactions and allosteric effects in aspartate transcarbamylase.

    المؤلفون: Ladjimi, M M, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry ; volume 262, issue 1, page 312-318 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(19)75928-6
    https://api.elsevier.com/content/article/PII:S0021925819759286?httpAccept=text/xml
    https://api.elsevier.com/content/article/PII:S0021925819759286?httpAccept=text/plain

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  6. 6
    Academic Journal
    Functionally important arginine residues of aspartate transcarbamylase.

    المؤلفون: Kantrowitz, E R, Lipscomb, W N

    المصدر: Journal of Biological Chemistry ; volume 252, issue 9, page 2873-2880 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(17)40444-3
    https://api.elsevier.com/content/article/PII:S0021925817404443?httpAccept=text/xml
    https://api.elsevier.com/content/article/PII:S0021925817404443?httpAccept=text/plain

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  7. 7
    Academic Journal
    Site-directed mutagenesis of a residue located in the regulatory site of Escherichia coli aspartate transcarbamoylase. Involvement of lysine 94 in effector binding and the allosteric mechanism.

    المؤلفون: Zhang, Y, Ladjimi, M M, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry ; volume 263, issue 3, page 1320-1324 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(19)57303-3
    https://api.elsevier.com/content/article/PII:S0021925819573033?httpAccept=text/xml
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  8. 8
    Academic Journal
    Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway.

    المؤلفون: Nowlan, S F, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry ; volume 260, issue 27, page 14712-14716 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(17)38630-1
    https://api.elsevier.com/content/article/PII:S0021925817386301?httpAccept=text/xml
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  9. 9
    Academic Journal
    The Importance of the Link Between Glu204 of the Catalytic Chain and Arg130 of the Regulatory Chain for the Homotropic and Heterotropic Properties of Escherichia coli Aspartate Transcarbamoylase

    المؤلفون: Stebbins, J W, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry ; volume 264, issue 25, page 14860-14864 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(18)63780-9
    https://api.elsevier.com/content/article/PII:S0021925818637809?httpAccept=text/xml
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  10. 10
    Academic Journal
    Site-specific Mutation of Tyr240 → Phe in the Catalytic Chain of Escherichia coli Aspartate Transcarbamylase

    المؤلفون: Hsuanyu, Y, Wedler, F C, Kantrowitz, E R, Middleton, S A

    المصدر: Journal of Biological Chemistry ; volume 264, issue 29, page 17259-17265 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(18)71486-5
    https://api.elsevier.com/content/article/PII:S0021925818714865?httpAccept=text/xml
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  11. 11
    Academic Journal
    An essential residue at the active site of aspartate transcarbamylase.

    المؤلفون: Kantrowitz, E R, Lipscomb, W N

    المصدر: Journal of Biological Chemistry ; volume 251, issue 9, page 2688-2695 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(17)33542-1
    https://api.elsevier.com/content/article/PII:S0021925817335421?httpAccept=text/xml
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  12. 12
    Academic Journal
    Regulatory Behavior of Escherichia coli Aspartate Transcarbamylase Altered by Site-specific Mutation of Tyr240 → Phe in the Catalytic Chain

    المؤلفون: Wedler, F C, Hsuanyu, Y C, Kantrowitz, E R, Middleton, S A

    المصدر: Journal of Biological Chemistry ; volume 264, issue 29, page 17266-17274 ; ISSN 0021-9258

    الاتاحة: http://dx.doi.org/10.1016/s0021-9258(18)71487-7
    https://api.elsevier.com/content/article/PII:S0021925818714877?httpAccept=text/xml
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  13. 13
    Periodical
    The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase.

    المؤلفون: Sakash, J B, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry; September 2000, Vol. 275 Issue: 37 p28701-7, 7p

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  14. 14
    Periodical
    Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase.

    المؤلفون: Sakash, J B, Chan, R S, Tsuruta, H, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry; January 2000, Vol. 275 Issue: 2 p752-8, 7p

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  15. 15
    Periodical
    A model of the transition state in the alkaline phosphatase reaction.

    المؤلفون: Holtz, K M, Stec, B, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry; March 1999, Vol. 274 Issue: 13 p8351-4, 4p

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  16. 16
    Periodical
    Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase.

    المؤلفون: Middleton, S A, Kantrowitz, E R

    المصدر: Proceedings of the National Academy of Sciences of the United States of America; August 1986, Vol. 83 Issue: 16 p5866-5870, 5p

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  17. 17
    Periodical
    Regulatory Behavior of Escherichia coliAspartate Transcarbamylase Altered by Site-specific Mutation of Tyr240→ Phe in the Catalytic Chain

    المؤلفون: Wedler, F C, Hsuanyu, Y C, Kantrowitz, E R, Middleton, S A

    المصدر: Journal of Biological Chemistry; October 1989, Vol. 264 Issue: 29 p17266-17274, 9p

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  18. 18
    Periodical
    Site-specific Mutation of Tyr240→ Phe in the Catalytic Chain of Escherichia coliAspartate Transcarbamylase

    المؤلفون: Hsuanyu, Y, Wedler, F C, Kantrowitz, E R, Middleton, S A

    المصدر: Journal of Biological Chemistry; October 1989, Vol. 264 Issue: 29 p17259-17265, 7p

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  19. 19
    Periodical
    Engineered complementation in Escherichia coli aspartate transcarbamoylase. Heterotropic regulation by quaternary structure stabilization.

    المؤلفون: Aucoin, J M, Pishko, E J, Baker, D P, Kantrowitz, E R

    المصدر: Journal of Biological Chemistry; November 1996, Vol. 271 Issue: 47 p29865-9, 5p

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  20. 20
    Periodical
    The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain.

    المؤلفون: Newton, C J, Kantrowitz, E R

    المصدر: Proceedings of the National Academy of Sciences of the United States of America; March 1990, Vol. 87 Issue: 6 p2309-2313, 5p

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