Document Detail

Aspartate:2-oxoglutarate aminotransferase from Trichomonas vaginalis: comparison with pig heart cytoplasmic enzyme.
MedLine Citation:
PMID:  2876843     Owner:  NLM     Status:  MEDLINE    
The aspartate:2-oxoglutarate aminotransferase from the protozoon Trichomonas vaginalis exists as a mixture of sub-forms of identical Mr and amino acid composition, and of similar catalytic properties. The amino acid composition closely resembles that of aspartate aminotransferase from prokaryotic and vertebrate sources. Some molecular and catalytic properties of the T. vaginalis aspartate aminotransferase are compared with those of the cytoplasmic pig heart enzyme. A major difference is in the ability of the trichomonal enzyme to transaminate aromatic amino acids and 2-oxo acids. A range of inhibitors have been used to compare the active-site regions of the T. vaginalis and cytoplasmic pig heart aspartate aminotransferases.
P N Lowe; A F Rowe
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Comparative biochemistry and physiology. B, Comparative biochemistry     Volume:  85     ISSN:  0305-0491     ISO Abbreviation:  Comp. Biochem. Physiol., B     Publication Date:  1986  
Date Detail:
Created Date:  1986-12-17     Completed Date:  1986-12-17     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2984730R     Medline TA:  Comp Biochem Physiol B     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  93-9     Citation Subset:  IM    
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MeSH Terms
Amino Acids / analysis
Aspartate Aminotransferases / isolation & purification,  metabolism*
Cytoplasm / enzymology
Myocardium / enzymology*
Species Specificity
Swine / metabolism*
Trichomonas vaginalis / enzymology*
Tyrosine Transaminase / metabolism
Reg. No./Substance:
0/Amino Acids; EC Aminotransferases; EC Transaminase

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

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