A New α-Amylase from Reticulitermes speratus KMT1

Park, Han-Saem; Ham, Youngseok; Ahn, Hee-Hoon; Shin, Keum; Kim, Yeong-Suk; Kim, Tae‐Jong

doi:10.5658/wood.2014.42.2.149

Cited by 2 publications

(3 citation statements)

References 15 publications

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“…A putative chitinase gene was selected using transcriptomic analysis from previous studies (Park et al, 2014) aimed at elucidating its biological function.…”

Section: Chitinase Genes Of R Speratus Kmt001mentioning

confidence: 99%

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A New Putative Chitinase from Reticulitermes speratus KMT001

Ham¹,

Park²,

Kim³

et al. 2019

Journal of the Korean Wood Science and Technology

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Termites are pests that cause serious economic and cultural damage by digesting wood cellulose. Termites are arthropods and have an epidermis surrounded by a chitin layer. To maintain a healthy epidermis, termites have chitinase (β -1,4-poly-N-acetyl glucosamidinase, EC 3.2.1.14), an enzyme that hydrolyzes the β-1,4 bond of chitin. In this study, the amino acid sequence of the gene, which is presumed to be termite chitinolytic enzyme (NCBI accession no. KC477099), was obtained from a transcriptomic analysis of Reticulitermes speratus KMT001 in Bukhan Mountain, Korea. An NCBI protein BLAST search confirmed that the protein is a glycoside hydrolase family 18 (GH18). The highest homology value found was 47%, with a chitinase from Araneus ventricosus. Phylogenetic analysis indicated that the KC477099 protein has the same origins as those of arthropods but has a very low similarity with other arthropod chitinases, resulting in separation at an early stage of evolution. The KC477099 protein contains two conserved motifs, which encode the general enzymatic characteristics of the GH18 group. The amino acid sequences Asp 156 -Trp 157 -Glu 158 , which play an important role in the enzymatic activity of the GH18 group, were also present. This study suggests that the termite KC477099 protein is a new type of chitinase, which is evolutionarily distant from other insect chitinases.

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“…A putative chitinase gene was selected using transcriptomic analysis from previous studies (Park et al, 2014) aimed at elucidating its biological function.…”

Section: Chitinase Genes Of R Speratus Kmt001mentioning

confidence: 99%

“…A previous transcriptomic analysis of R. speratus KMT001 using the GS FLX System (Park et al, 2014) provided sequence information for the expressed mRNA.…”

Section: Putative Chitinases Of R Speratus Kmt001mentioning

confidence: 99%

A New Putative Chitinase from Reticulitermes speratus KMT001

Ham¹,

Park²,

Kim³

et al. 2019

Journal of the Korean Wood Science and Technology

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“…Inoue et al (1997) found that R. serratus has both cellulase in their saliva whereas there is virtually no xylanase activity. Park et al (2014) found that R. serratus produces α-amylase which is commonly found in insect salivary glands (Cohen, 2004) and has been found in the saliva of other termite genera (Hewitt et al, 1974;La Fage & Nutting, 1978). Thus, if Reticulitermes foragers are detecting polysaccharides salivary fluid then starch should be detectable to the termites whereas xylan would not be detectable.…”

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confidence: 99%