Document Detail


Occurrence of D-amino acids in a few archaea and dehydrogenase activities in hyperthermophile Pyrobaculum islandicum.
MedLine Citation:
PMID:  10561548     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The contents of D-enantiomers of serine, alanine, proline, glutamate (glutamine) and aspartate (asparagine) were examined in the membrane fractions, soluble proteins and free amino acids from some species of archaea, Pyrobaculum islandicum, Methanosarcina barkeri and Halobacterium salinarium. Around 2% (D/D+L) of D-aspartate was found in the membrane fractions. In the soluble proteins, the D-amino acid content was higher in P. islandicum than that in the other archaeal cells: the concentrations in P. islandicum were 3 and 4% for D-serine and D-aspartate, respectively. High concentrations of free D-amino acids were found in P. islandicum and H. salinarium; the concentrations of D-serine (12-13%), D-aspartate (4-7%) and D-proline (3-4%) were higher than those of D-alanine and D-glutamate. This result showed a resemblance between these archaea and not bacterial, but eukaryotic cells. The presence of D-amino acids was confirmed by their digestion with D-amino acid oxidase and D-aspartate oxidase. The occurrence of D-amino acids was also confirmed by the presence of activities catalyzing catabolism of D-amino acids in the P. islandicum homogenate, as measured by 2-oxo acid formation. The catalytic activities oxidizing D-alanine, D-aspartate and D-serine at 90 degrees C were considerably high. Under anaerobic conditions, dehydrogenase activities of the homogenate were 69, 84 and 30% of the above oxidase activities toward D-alanine, D-aspartate and D-serine, respectively. Comparable or higher dehydrogenase activities were also detected with these D-amino acids as substrate by the reduction of 2, 6-dichlorophenolindophenol. No D-amino acid oxidase activity was detected in the homogenates of M. barkeri and H. salinarium.
Authors:
Y Nagata; K Tanaka; T Iida; Y Kera; R Yamada; Y Nakajima; T Fujiwara; Y Fukumori; T Yamanaka; Y Koga; S Tsuji; K Kawaguchi-Nagata
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1435     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1999 Nov 
Date Detail:
Created Date:  2000-01-11     Completed Date:  2000-01-11     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  160-6     Citation Subset:  IM    
Affiliation:
Department of Life Science, Himeji Institute of Technology, Himeji, Hyogo, Japan. nagata@sci.himeji-tech.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Archaea / chemistry*
Membrane Proteins / chemistry
Oxidation-Reduction
Oxidoreductases / analysis
Thermoproteaceae / enzymology*
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Membrane Proteins; EC 1.-/Oxidoreductases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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