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Archives of Microbiology

, Volume 169, Issue 4, pp 322–332 | Cite as

The genes lmbB1 and lmbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of l-tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A

  • Dietmar Neusser
  • Heike Schmidt
  • Jaroslav Spizèk
  • Jitka Novotnà
  • Ursula Peschke
  • Stefan Kaschabeck
  • Pavel Tichy
  • W. Piepersberg
Original paper

Abstract

The genes lmbA,B1,B2 in the lincomycin A production gene cluster of Streptomyces lincolnensis were shown to form a common transcription unit with the promoter located directly upstream of lmbA. The proteins LmbB1 (mol. mass, 18 kDa) and LmbB2 (mol. mass 34 kDa), when over-produced together in Escherichia coli, brought about enzyme activities for the specific conversion of both l-tyrosine and l-3,4-dihydroxyphenylalanine (l-DOPA) to a yellow-colored product. The LmbB1 protein alone catalyzed the conversion of l-DOPA, but not of l-tyrosine. The purified LmbB1 protein showed a K m for l-DOPA of 258.3 μM. The l-tyrosine converting activity could not been demonstrated in vitro. The preliminary interpretation of these data suggests that the protein LmbB1 is an l-DOPA extradiol-cleaving 2,3-dioxygenase and that the protein LmbB2, either alone or in accord with LmbB1, represents an l-tyrosine 3-hydroxylase. This sequence of putative oxidation reactions on l-tyrosine seems to represent a new pathway different from the ones catalyzed by mammalian l-tyrosine hydroxylases or the wide-spread tyrosinases. The protein LmbA seemed not to be involved in this process. The labile, yellow-colored product from l-DOPA could not be converted to a picolinic acid derivative [3-(2-carboxy-5-pyridyl)alanine] in the presence of ammonia. Therefore, it probably is not a derivative of a cis,cis-3-hydroxymuconic acid semialdehyde; instead, its speculative structure represents a heterocyclic precursor of the propylhygric acid moiety of lincomycin A.

Key words Antibiotic biosynthesis Lincomycin Streptomyces lincolnensis Oxidases Propylhygric acid 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • Dietmar Neusser
    • 1
  • Heike Schmidt
    • 1
  • Jaroslav Spizèk
    • 2
  • Jitka Novotnà
    • 2
  • Ursula Peschke
    • 1
  • Stefan Kaschabeck
    • 1
  • Pavel Tichy
    • 2
  • W. Piepersberg
    • 1
  1. 1.Bergische Universitat GH, Mikrobiologie-FB 9, Gaussstrasse 20, D-42097 Wuppertal, Germany Tel. +49-202-439-2521; Fax +49-202-439-2698 e-mail: piepersb@uni-wuppertal.deDE
  2. 2.Institute of Microbiology, Czech Academy of Sciences, Videnska 1083, 142 20 Prague 4, Czech RepublicXX

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