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Literature summary for 3.2.1.41 extracted from

  • Fujita, N.; Toyosawa, Y.; Utsumi, Y.; Higuchi, T.; Hanashiro, I.; Ikegami, A.; Akuzawa, S.; Yoshida, M.; Mori, A.; Inomata, K.; Itoh, R.; Miyao, A.; Hirochika, H.; Satoh, H.; Nakamura, Y.
    Characterization of pullulanase (PUL)-deficient mutants of rice (Oryza sativa L.) and the function of PUL on starch biosynthesis in the developing rice endosperm (2009), J. Exp. Bot., 60, 1009-1023.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information investigation of the function of pullulanase in starch biosynthesis using the mutant lines e10-/- and i16-/- containing the Tos17 insertion at exon 10 and intron 16 of the OsPUL gene, respectively, and EM1003, a product of N-methyl-N-nitrosourea mutagenesis, which mutated from C to T at 1266 bp before the start codon. Reduction of pullulanase activity has no effects on the other enzymes involved in starch biosynthesis. Short chains with a degree of polymerizytion below 14 are increased in the mutants compared with wild-type. The alpha-glucan composition and the structure of the starch components of the mutants is essentially the same, although the average chain length of the B2,3 chains of amylopectin in the mutants is about 3 residues longer than that of wild-type. Pullulanase fucntion may partially overlap with that of isoamylase 1 Oryza sativa

Organism

Organism UniProt Comment Textmining
Oryza sativa
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Source Tissue

Source Tissue Comment Organism Textmining