Literature DB >> 1369144

Cloning and heterologous expression of a novel arylmalonate decarboxylase gene from Alcaligenes bronchisepticus KU 1201.

K Miyamoto1, H Ohta.   

Abstract

We have cloned and sequenced a DNA fragment that encodes the arylmalonate decarboxylase (AM-Dase) gene from Alcaligenes bronchisepticus KU 1201. The AMDase gene consists of an open reading frame of 720 nucleotides, which specifies a 240-amino-acid protein of relative molecular mass (M(r)) 24734. The M(r) deduced from the AMDase gene is in good agreement with that of the AMDase isolated from A. bronchisepticus. No TATA or TTGA sequence was observed within the cloned DNA fragment, but the fragment was expressed in Escherichia coli by the lac promoter of pUC19. The enzyme produced in E. coli has the same M(r) and the same enzyme activity as that purified from A. bronchisepticus. Comparison of the DNA sequence and the deduced amino acid sequence of AMDase with available DNA and amino acid sequence data bases revealed that there are no significant sequence homologies.

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Year:  1992        PMID: 1369144     DOI: 10.1007/bf00174474

Source DB:  PubMed          Journal:  Appl Microbiol Biotechnol        ISSN: 0175-7598            Impact factor:   4.813


  4 in total

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  4 in total
  2 in total

1.  Crystallization and preliminary X-ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticus.

Authors:  Masayoshi Nakasako; Rika Obata; Ryosuke Okubo; Shyuichi Nakayama; Kenji Miyamoto; Hiromichi Ohta
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2008-06-11

2.  Enzymatic enantioselective decarboxylative protonation of heteroaryl malonates.

Authors:  Ross Lewin; Mark Goodall; Mark L Thompson; James Leigh; Michael Breuer; Kai Baldenius; Jason Micklefield
Journal:  Chemistry       Date:  2015-03-12       Impact factor: 5.236

  2 in total

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