The amino acid sequence of the constitutive flavodoxin from the red alga Chondrus crispus was determined from the analyses of peptide fragments derived by enzymic digestions of the carboxymethylated protein. This is the first sequence reported for a flavodoxin from a eukaryote. The protein is composed of 173 amino acid residues and is a member of the longer-chain group of flavodoxins. The extent of sequence homology to the three other flavodoxins in the group for which sequences are available is in the range 36-39%, with the most strongly conserved regions being those implicated in binding of the FMN, the redox-active prosthetic group. Nevertheless, Chondrus crispus flavodoxin stands apart in a number of respects, in particular the possession of an unusually high content of proline, with these residues distributed more or less regularly along the peptide chain.
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November 1989
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Research Article|
November 01 1989
The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus
S Wakabayashi;
S Wakabayashi
*Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560, Japan.
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T Kimura;
T Kimura
*Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560, Japan.
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K Fukuyama;
K Fukuyama
*Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560, Japan.
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H Matsubara;
H Matsubara
*Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560, Japan.
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L J Rogers
L J Rogers
†Department of Biochemistry, University College of Wales, Aberystwyth, Dyfed SY23 3DD, Wales, U.K.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1989 London: The Biochemical Society
1989
Biochem J (1989) 263 (3): 981–984.
Citation
S Wakabayashi, T Kimura, K Fukuyama, H Matsubara, L J Rogers; The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus. Biochem J 1 November 1989; 263 (3): 981–984. doi: https://doi.org/10.1042/bj2630981
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