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Rational Design of α-Keto Triglyceride Analogues as Inhibitors for Staphylococcus hyicus Lipase

Autor: Jan-Willem F. A. Simons, Ruud C. Cox, Maarten R. Egmond, Hubertus M. Verheij

Publikováno v: Biochemistry. 38:6346-6351

We have synthesized a series of alpha-keto triglyceride analogues as inhibitors for the lipase from Staphylococcus hyicus (SHL). Hydrolysis at positions 1 and 2 was prevented by replacement of the ester bonds by nonhydrolyzable ether, carbamoyl, or a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40f35251e9ec178ef0cc31f83daed815
https://doi.org/10.1021/bi982498b

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Incorporation of an unnatural amino acid in the active site of porcine pancreatic phospholipase A2. Substitution of histidine by l,2,4-triazole-3-alanine yields an enzyme with high activity at acidic pH

Autor: Bert van den Berg, Hubertus M. Verheij, Sigrid H.W. Beiboer, Ruud C. Cox, Niek Dekker

Publikováno v: "Protein Engineering, Design and Selection". 9:345-352

The effect of the substitution of the active site histidine 48 by the unnatural 1,2,4-triazole-3-alanine (TAA) amino acid analogue in porcine pancreas phospholipase A2 (PLA2) was studied. TAA was introduced biosynthetically using a his-auxotrophic Es

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::56fdac2bcef123ee476872df9716e2d1
https://doi.org/10.1093/protein/9.4.345

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An Extended Binding Pocket Determines the Polar Head Group Specificity of Porcine Pancreatic Phospholipase A2

Autor: Hubertus M. Verheij, Sigrid H.W. Beiboer, Peet A. Franken, Ruud C. Cox

Publikováno v: European Journal of Biochemistry. 231:747-753

Porcine pancreatic phospholipase A2 (PLA2) was studied by site-directed mutagenesis. Arg53 and/or Lys56 were replaced by a methionine (R53M or K56M, respectively) in combination with the Tyr69-->Phe (Y69F) substitution. These substitutions improved t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d374534f08960b32773419c79fd7e1d2
https://doi.org/10.1111/j.1432-1033.1995.0747d.x

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Cutinase from Fusarium solani pisi Hydrolyzing Triglyceride Analogs. Effect of Acyl Chain Length and Position in the Substrate Molecule on Activity and Enantioselectivity

Autor: G.H. de Haas, J. De Vlieg, Bart C. Koops, H. T. W. M. Van Der Hijden, Maarten Robert Egmond, Hubertus M. Verheij, Ruud C. Cox, M. L. M. Mannesse

Publikováno v: Biochemistry. 34:6400-6407

Triglyceride analogues were synthesized in which one of the primary acyl ester functions has been replaced by an alkyl group and the secondary acyl ester bond has been replaced by an acyl amino bond. The chain length at either position was varied, an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98649888a11d3dfbbd5afe4d7bdf60bf
https://doi.org/10.1021/bi00019a020

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Competitive inhibition of lipolytic enzymes. X. Further delineation of the active site of pancreatic phospholipases A2 from pig, ox and horse by comparing the inhibitory power of a number of (R)-2-acylamino phospholipid analogues

Autor: Ruud C. Cox, R. Dijkman, G.H. de Haas, L.H. van den Berg, Hubertus M. Verheij

Publikováno v: Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1212:50-58

Two series of (R)-phospholipid analogues, each containing a n-propyl group at the C-1 position and various acylamino functions at the C-2 position have been synthesized and their inhibitory properties towards three mammalian pancreatic phospholipases

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edbc8f67220c083aa7d08fd1cd12409b
https://doi.org/10.1016/0005-2760(94)90188-0

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Identification of a calcium binding site in Staphylococcus hyicus lipase: generation of calcium-independent variants

Autor: Muriel D. van Kampen, Ruud C. Cox, Cristina M. Alves dos Santos, Jan-Willem F. A. Simons, Iban Ubarretxena-Belandia, Hubertus M. Verheij, Maarten R. Egmond

Publikováno v: Biochemistry. 38(1)

In this study we have identified the presence of a high-affinity binding site for calcium in the lipase from Staphylococcus hyicus. By means of isothermal titration calorimetry we showed that the enzyme binds one calcium per molecule of enzyme with a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fed5dee4f3c510a896e8d4a59eb3f9e9
https://pubmed.ncbi.nlm.nih.gov/9890877

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