Tomato and Aspergillus niger pectinesterases. Correlation of differences in existing reports: large species variations.
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.
Markovic
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O
Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden.
Jörnvall
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H
D000595:Amino Acid Sequence; D001234:Aspergillus niger / Q000201:enzymology* / Q000235:genetics; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000235:genetics*; D004247:DNA / Q000737:chemistry; D014644:Genetic Variation; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology* / Q000235:genetics; D012091:Repetitive Sequences, Nucleic Acid; D012689:Sequence Homology, Nucleic Acid
D004247:DNA; D002265:Carboxylic Ester Hydrolases; C022323:pectinesterase