| Literature DB >> 3828494 |
Abstract
The nucleotide sequence of a 1.46 kb cDNA, selected from a human liver library by the expression of fumarase antigenic determinants, was determined using the dideoxy chain termination method. The cDNA contained an open reading frame extending from the extreme 5'-base and coding for a protein with 468 amino acids. This protein, with the exception of an N-terminal methionine, was identified as mitochondrial fumarase. The protein showed a high degree of identity of structure with the fumarase from Bacillus subtilis (56.6%) and a fumarase from Escherichia coli (product of the fumC gene, 59.3%), and a lower degree of identity with the aspartase of E. coli (37.2%).Entities:
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Year: 1986 PMID: 3828494 DOI: 10.1007/bf01116247
Source DB: PubMed Journal: Biosci Rep ISSN: 0144-8463 Impact factor: 3.840