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The amino acid sequence of a type I copper protein with an unusual serine‐ and hydroxyproline‐rich C‐terminal domain isolated from cucumber peelings
Author(s) -
Mann Karlheinz,
Schäfer Wolfram,
Thoenes Ulrich,
Messerschmidt Albrecht,
Mehrabian Zara,
Nalbandyan Robert
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81475-2
Subject(s) - amino acid , serine , hydroxyproline , peptide sequence , biochemistry , chemistry , residue (chemistry) , enzyme , gene
We have determined the amino acid sequence of a small copper protein isolated from cucumber peelings. This cupredoxin contains 137 amino acids including a pyroglutamate as the first residue. The N‐terminal 110 amino acid‐long domain shows 30–37% identity to 2 other cupredoxins, stellacyanin and cucumber basic blue protein. A unique feature of this protein is a 27 amino acid‐long, C‐terminal domain rich in 4‐hydroxyproline and serine and resembling certain plant cell wall proteins. The prolines in this domain are hydroxylated to a different extent depending on the surrounding sequence.