Literature DB >> 3728214

Histamine (HIS) degradation in microorganisms: imidazole ring splitting and formation of imidazolyl ethanol (IMET) and imidazolyl acetic acid (IMAC) in mycobacteria.

Z Tarnok, I Tarnok.   

Abstract

Mycobacterium smegmatis SN 46, isolated from a fatal human oesophagus infection, is able to degrade HIS by imidazole ring splitting. In this respect, SN 46 is unique under the bacteria strains tested. Some other mycobacteria (M. diernhoferi, M. fortuitum, M. chelonei etc.) oxidize HIS to IMET and IMAC without further change. Cell-free extracts of SN 46 transform HIS to IMET and IMAC, while ring splitting enzymes are not detectable. IMAC and IMET were identified by combined gas-liquid chromatography and mass-spectrometry. At present, the possibility of HIS degradation by SN 46 via imidazolyl acetaldehyde (according to the pathway in vertebrates) can not be excluded.

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Year:  1986        PMID: 3728214     DOI: 10.1007/bf01987975

Source DB:  PubMed          Journal:  Agents Actions        ISSN: 0065-4299


  4 in total

1.  A METABOLITE OF HISTAMINE: 4(5)-IMIDAZOYL-ETHANE-2-OL.

Authors:  T NAKAJIMA; I SANO
Journal:  Biochim Biophys Acta       Date:  1964-02-10

2.  Biochemical background of some enzymatic tests used for the differentiation of mycobacteria.

Authors:  I Tarnok; E Röhrscheidt
Journal:  Tubercle       Date:  1976-06

3.  Metabolism of 14C-histamine in domestic animals. I. Goat.

Authors:  K A Eliassen
Journal:  Acta Physiol Scand       Date:  1969 May-Jun

4.  Presence and measurement of methylimidazoleacetic acids in brain and body fluids.

Authors:  J K Khandelwal; L B Hough; B Pazhenchevsky; A M Morrishow; J P Green
Journal:  J Biol Chem       Date:  1982-11-10       Impact factor: 5.157

  4 in total

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