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Starch‐synthase III family encodes a tandem of three starch‐binding domains
Author(s) -
Palopoli Nicolás,
Busi María Victoria,
Fornasari María Silvina,
GomezCasati Diego,
Ugalde Rodolfo,
Parisi Gustavo
Publication year - 2006
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21007
Subject(s) - biochemistry , amino acid , starch , arabidopsis thaliana , tandem repeat , peptide sequence , starch synthase , enzyme , structural similarity , arabidopsis , biology , chemistry , gene , genome , amylopectin , mutant , amylose
The starch‐synthase III (SSIII), with a total of 1025 residues, is one of the enzymes involved in plants starch synthesis. SSIII from Arabidopsis thaliana contains a putative N‐terminal transit peptide followed by a 557‐amino acid SSIII‐specific domain (SSIII‐SD) with three internal repeats and a C‐terminal catalytic domain of 450 amino acids. Here, using computational characterization techniques, we show that each of the three internal repeats encodes a starch‐binding domain (SBD). Although the SSIII from A. thaliana and its close homologous proteins show no detectable sequence similarity with characterized SBD sequences, the amino acid residues known to be involved in starch binding are well conserved. Proteins 2006. © 2006 Wiley‐Liss, Inc.