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Gerard H. de Haas

Affiliations: 
Utrecht University, Utrecht, Netherlands 
Area:
biochemistry
Website:
http://profs.library.uu.nl/index.php/profrec/getprofdata/766/5/11/0
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"Gerard de Haas"
Mean distance: 10.37
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Parents

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Laurens L.M. van Deenen grad student 1963 Utrecht
 (Glycerophosphatides, their chemical syntheses and application in lipid biochemistry)

Children

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Maria C.E. van Dam-Mieras grad student 1976 Utrecht
Oscar P. Kuipers grad student 1990 Utrecht

Collaborators

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Publications

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Lang DA, Mannesse ML, de Haas GH, et al. (1998) Structural basis of the chiral selectivity of Pseudomonas cepacia lipase. European Journal of Biochemistry / Febs. 254: 333-40
Mannesse ML, de Haas GH, van der Hijden HT, et al. (1997) Chiral preference of cutinase in the reaction with phosphonate inhibitors. Biochemical Society Transactions. 25: 165-70
Longhi S, Mannesse M, Verheij HM, et al. (1997) Crystal structure of cutinase covalently inhibited by a triglyceride analogue. Protein Science : a Publication of the Protein Society. 6: 275-86
Mannesse ML, Cox RC, Koops BC, et al. (1995) Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity. Biochemistry. 34: 6400-7
Boots JW, van Dongen WD, Verheij HM, et al. (1995) Identification of the active site histidine in Staphylococcus hyicus lipase using chemical modification and mass spectrometry. Biochimica Et Biophysica Acta. 1248: 27-34
van den Berg B, Tessari M, Boelens R, et al. (1995) Solution structure of porcine pancreatic phospholipase A2 complexed with micelles and a competitive inhibitor. Journal of Biomolecular Nmr. 5: 110-21
van den Berg B, Tessari M, Boelens R, et al. (1995) NMR structures of phospholipase A2 reveal conformational changes during interfacial activation. Nature Structural Biology. 2: 402-6
De Haas GH, Dijkman R, Boots JW, et al. (1995) Competitive inhibition of lipolytic enzymes. XI. Estimation of the interfacial dissociation constants of porcine pancreatic phospholipase A2 for substrate and inhibitor in the absence of detergents. Biochimica Et Biophysica Acta. 1257: 87-95
van den Berg B, Tessari M, de Haas GH, et al. (1995) Solution structure of porcine pancreatic phospholipase A2. The Embo Journal. 14: 4123-31
Mannesse ML, Boots JW, Dijkman R, et al. (1995) Phosphonate analogues of triacylglycerols are potent inhibitors of lipase. Biochimica Et Biophysica Acta. 1259: 56-64
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