Literature DB >> 2089377

Tomato and Aspergillus niger pectinesterases. Correlation of differences in existing reports: large species variations.

O Markovic1, H Jörnvall.   

Abstract

Existing reports on the enzyme tomato pectinesterase differ in alignments of two internal segments and in many single-residue replacements. The alignment from cDNA data, with a 317-residue mature protein, is correct, but protein analyses also show at least 18 single-residue replacements, suggesting the presence of many native or (less likely) cloning-derived microheterogeneities. Purification of Aspergillus niger pectinesterase and N-terminal sequence analysis of this enzyme reveal a different structure and indicate an extensive protein divergence.

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Year:  1990        PMID: 2089377

Source DB:  PubMed          Journal:  Protein Seq Data Anal        ISSN: 0931-9506


  4 in total

1.  Modification of tomato and Aspergillus niger pectinesterases with diethyl pyrocarbonate.

Authors:  O Markovic; J Stovícková; H Jörnvall
Journal:  J Protein Chem       Date:  1996-02

2.  Molecular characterisation of cDNA clones representing pectin esterase isozymes from tomato.

Authors:  L N Hall; C R Bird; S Picton; G A Tucker; G B Seymour; D Grierson
Journal:  Plant Mol Biol       Date:  1994-05       Impact factor: 4.076

3.  Disulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active site segments.

Authors:  O Markovic; H Jörnvall
Journal:  Protein Sci       Date:  1992-10       Impact factor: 6.725

4.  Mapping the polysaccharide degradation potential of Aspergillus niger.

Authors:  Mikael R Andersen; Malene Giese; Ronald P de Vries; Jens Nielsen
Journal:  BMC Genomics       Date:  2012-07-16       Impact factor: 3.969

  4 in total

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