Hydrolasen für Synthese und Hydrolyse von biologisch aktiven reinen Enantiomersubstanzen

• 2-10.018D
  

  Andre Rieks: Stereospezifität und chirale Erkennung von Enzymen: Optimierung der Enantioselektivität von Penicillinamidase durch Variation der Reaktionsparameter und der Primärstruktur, TUHH, 1997

• 2-10.025D
  

  Karsten Lummer: Inter- und intramolekulare enzymatisch katalysierte Reaktionen am Beispiel der Penicillinamidase, TUHH 2000

• 2-10.129V
  

  V.Kasche, B.Galunsky, A.Nurk, E.Piotraschke, A.Rieks (1996) The dependency of the stereoselectivity of penicillin amidase-enzymes with R-specific S1- and S-specific S1¿-subsites on temperature and primary structure Biotechnol. Lett. 18, 455-460

• V-06.035V
  

  Tishinov, K., Stambolieva, N., Petrova, S., Galunsky, B., B.,  Nedkov, P., (2009)  Purification and characterization of the sunflower seed (Helianthus annuus L.) major aminopeptidase. Acta Physiol Plant  31, 199-205.

• 2-10.134V
  

  Z. Mincheva, N. Stambolieva, K. Petrova, and B. Galunsky (1996) Penicillin amidase-catalysed preparative synthesis of cephem 7-(2-benzoxazolon-3-yl-acetamido)-desacetoxycephalosporanic acid using a nonspecific polyethyleneglycol-modified acyl donor Biotechnol. Tech. 10, 727-730

• 2-10.137V
  

  B.Galunsky, Z.Ignatova, V.Kasche (1997) Temperature effects on S1- and S1`-enantioselectivity of a-chymotrypsin. Biochem. Biophys. Acta 1343, 130-138

• 2-10.138V
  

  Z.Ignatova, S.Stoeva, B.Galunsky, C.Hörnle, A.Nurk, E.Piotraschke, W.Voelter, V.Kasche (1998) Proteolytic processing of penicillin amidases from Alcaligenes faecalis cloned in E.coli yields several active forms Biotechnol. Lett. 20, 977-982

• 2-10.148V
  

  K. Lummer, A. Rieks, B. Galunsky, V. Kasche (1999) pH dependence of penicillin amidase enantioselectivity for charged substrates Biochim. Biophys. Acta 1433, 327-334

• 2-10.162V
  

  N. Stambolieva, Z. Mincheva, B.Galunsky (1998) Kinetic comparison of penicillin amidase catalysed transfer of nonspecific and specific acyl moieties to 7-aminodeacetoxycephalosporanic acid Biocatal. Biotransform. 16, 225-232

• 2-10.167V
  

  B. Galunsky, K. Lummer, V. Kasche (2000) Comparative study of substrate- and stereospecificity of penicillin G amidases from different sources and hybrid enzymes Chem. Montl. 131, 623-632

• 2-10.187V
  

  B. Galunsky, V. Kasche (2002) Determination of the enantioselectivity for kinetically controlled condensations catalysed by amidases and peptidases. Adv.Synth.Catal. 344, 1115-1119

• 2-10.192V
  

  V. Kasche, B. Galunsky, Z. Ignatova (2003) Fragments of pro-peptide activate mature penicillin amidase of Alkaligenes faecalis. Eur. J. Biochem. 270, 4721-4728

• 2-10.001P
  

  Kasche, V., Ignatova, Z., Galunsky, B. (2004) Gentechnisch veränderte Penicillinamidase und Verfahren zu ihrer Herstellung. DE 102 51 747 A1, 19.05.2004.

• 2-10.194V
  

  Bozhinova, D., Galunsky, B., Yueping, G., Franzreb, M., Köster, R., & Kasche, V. (2004) Evaluation of magnetic polymer micro-beads as carriers of for immobilised biocatalysts for selective and stereoselective transformations. Biotechnol. Lett. 26, 343-350.

• 2-10.195V
  

  Guncheva, M., Ivanov, I., Galunsky, B., Stambolieva, N., Kaneti, J. (2004) Kinetic studies and molecular modelling attribute a crucial role in the specificity and stereoselectivity of penicillin acylase to the pair ArgA145-ArgB263. Eur. J. Biochem. 271, 2272-2279.

• V-06.041V
  

  Zhiryakova, D., Ivanov, I., Ilieva, S., Guncheva, M., Galunsky, B., Stambolieva, N. (2009) Are Ntn-Hydrolases Indeed with a Single-Amino-Acid Catalytic Centre? Supporting Amino Acid Residues at the Active Site of Penicillin G Acylase. FEBS J 276, 2589-2598.

• V-06.042V
  

  Tishinov, K., Stambolieva, N., Nedkov, P., Galunsky, B. (2009) Sunflower seed aminopeptidase-catalyzed hydrolysis of Phe-Xaa dipeptides. Exploring the S₁¿ specificity of the enzyme.  J. Mol.Catal.B: Enzym. 59, 106-110.

• V-06.061V
  

  Tishinov, K., Stambolieva, N., Petrova, S., Galunsky, B., Nedkov, P.  Purification and characterization of the sunflower seed (Helianthus annuus L.) major aminopeptidase. Acta Physiol Plant 31 (2009) 199-205

• V-06.062V
  

  Tishinov, K., Stambolieva, N., Nedkov, P., Galunsky, B.  Sunflower seed aminopeptidase-catalyzed hydrolysis of Phe-Xaa dipeptides. Exploring the S₁¿ specificity of the enzyme.  J Plant Biochem Biotechnol 18 (2009) 237-239

• V-06.063V
  

  Ruslan Yuryev, Volker Kasche, Zoya Ignatova and Boris Galunsky Improved A. faecalispenicillin amidase mutant retains the thermodynamic and pH stability of the wild type enzyme. The Protein Journal (2010) DOI 10.1007/s10930-010-9238-4

• V-06.001V
  

  Siwek, M., Galunsky, B., Niemeyer, B. (2005) Isolation of selenium organic species from Antarctic krill after enzymatic hydrolysis. Anal. Bioanal. Chem. 381, 737-741.

• V-06.033V
  

  Siwek, M., Noubar, A.B., Bergmann, J., Niemeyer, B., Galunsky, B. (2006) Enhancement of enzymatic digestion of Antarctic krill and successive extraction of selenium organic compounds by ultrasound treatment. Anal. Bioanal. Chem. 384, 244-249.

Stichwörter

• enantioselectivity
• kinetic resolution
• kinetically controlled synthesis
• penicillin amidase
• proteolitic enzymes
• stereoselectivity