Advertisement

Complete amino acid sequence of α-acetolactate decarboxylase from Bacillus brevis

  • IB Svendsen
  • Birger Rostgaard Jensen
  • Martin Ottesen
Article

Abstract

The complete amino acid sequence of acetolactate decarboxylase (EC 4.1.1.5) from Bacillus brevis has been determined by sequencing of the intact enzyme and of peptides obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease and trypsin, respectively. Determination of the C-terminal part was made by treatment with carboxypeptidases Y and M II. The enzyme has a molecular weight of 29.093 and consists of 260 amino acid residues arranged in a single peptide chain without disulphide bonds.

Keywords

Beer maturation 

Abbreviations

ALDC

acetolactate decarboxylase

CPD-MII

carboxypeptidase II from malt

CPD-Y

carboxypeptidase Y from yeast

TFA

trifluoro acetic acid

References

  1. 1.
    Diderichsen, B., U. Wedsted, L. Hedegaard, B.R. Jensen & C. Sjøholm: Cloning of an unusual exoenzyme: α-acetolactate decarboxylase from Bacillus brevis. (To be published)Google Scholar
  2. 2.
    Garnier, J., D.J. Osguthorpe &B. Robson: Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97–120 (1978)PubMedCrossRefGoogle Scholar
  3. 3.
    Godtfredsen, S.E. &M. Ottesen: Maturation of beer with α-acetolactate decarboxylase. Carlsberg Res. Commun 47, 93–102 (1982)CrossRefGoogle Scholar
  4. 4.
    Godtfredsen, S.E., H. Lorck &P. Sigsgaard: On the occurrence of α-acetolactate decarboxylases among microorganisms. Carlsberg Res. Commun. 48, 239–247 (1983)Google Scholar
  5. 5.
    Godtfredsen, S.E., A.M. Rasmussen, M. Ottesen, P. Rafn &N. Peitersen: Occurrence of α-acetolactate decarboxylases among lactic acid bacteria and their utilization for maturation of beer. Appl. Microbiol. Biotechnol. 20, 23–28 (1984)CrossRefGoogle Scholar
  6. 6.
    Jensen, B.R., I. Svendsen &M. Ottesen: Isolation and characterization of an α-acetolactate decarboxylase useful for accelerated beer maturation. Proc. Congr.-Eur. Brew. Conv. 21, 545–552 (1987)Google Scholar
  7. 7.
    Laursen, R.A. &F.H. Westheimer: The activite site of acetoacetate decarboxylase. J. Amer. Chem. Soc. 88, 3426–3430 (1966)CrossRefGoogle Scholar
  8. 8.
    Lederer, F., S.M. Coutts, R.A. Laursen &F.H. Westheimer: Acetoacetate decarboxylase. Subunits and properties. Biochemistry 5, 823–833 (1966)PubMedCrossRefGoogle Scholar
  9. 9.
    Sonf, H., T. Fujii, K. Kondo, F. Shimizu, J. Tanaka &I. Takashi: Nucleotide sequence and expression of the enterobacter aerogenes alpha-acetolactate decarboxylase gene in brewer's yeast. Appl. Environ. Microbiol. 54, 38–42 (1988)Google Scholar

Copyright information

© Carlsberg Laboratory 1989

Authors and Affiliations

  • IB Svendsen
    • 1
  • Birger Rostgaard Jensen
    • 2
  • Martin Ottesen
    • 1
  1. 1.Carlsberg LaboratoryDepartment of ChemistryCopenhagen Valby
  2. 2.Novo Industry A/SBagsvaerd

Personalised recommendations