Comparison of Enzymatic and Antifungal Properties between Family 18 and 19 Chitinases from<i>S. coelicolor</i>A3(2)

Kawase, Tomokazu; Yokokawa, Shinya; Saito, Akihiro; Fujii, Takeshi; Nikaidou, Naoki; Miyashita, Kiyotaka; Watanabe, Takeshi

doi:10.1271/bbb.70.988

Cited by 123 publications

(108 citation statements)

References 29 publications

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“…3). The major hydrolysis products from (GlcNAc) 6 were (GlcNAc) 4 , (GlcNAc) 3 , and (GlcNAc) 2 , and those from (GlcNAc) 5 were mainly (GlcNAc) 3 and (GlcNAc) 2 . A small amount of (GlcNAc) 3 , (GlcNAc) 2 , and GlcNAc were detected during (GlcNAc) 4 hydrolysis by EaChiA.…”

Section: Resultsmentioning

confidence: 99%

“…HPLC analysis of the hydrolysis products of (GlcNAc) n by EaChiA. Notes: S, Standards (GlcNAc) [1][2][3][4][5][6] ; (A) hydrolysis products of (GlcNAc) 6 ; (B) hydrolysis products of (GlcNAc) 5 ; (C) hydrolysis products of (GlcNAc) 4 . I to VI indicate (GlcNAc) [1][2][3][4][5][6] ; α and β indicate the α-and β-anomer, respectively.…”

Section: Antifungal Activity Of Eachiamentioning

confidence: 99%

“…Notes: S, Standards (GlcNAc) [1][2][3][4][5][6] ; (A) hydrolysis products of (GlcNAc) 6 ; (B) hydrolysis products of (GlcNAc) 5 ; (C) hydrolysis products of (GlcNAc) 4 . I to VI indicate (GlcNAc) [1][2][3][4][5][6] ; α and β indicate the α-and β-anomer, respectively. Standard (GlcNAc) [1][2][3][4][5][6] and the reaction mixtures were analyzed by HPLC on a TSKgel amide-80 column as described in Materials and Methods.…”

Section: Antifungal Activity Of Eachiamentioning

confidence: 99%

“…I to VI indicate (GlcNAc) [1][2][3][4][5][6] ; α and β indicate the α-and β-anomer, respectively. Standard (GlcNAc) [1][2][3][4][5][6] and the reaction mixtures were analyzed by HPLC on a TSKgel amide-80 column as described in Materials and Methods. Notes: Samples to be tested were placed in wells in 10 μL of distilled water.…”

Section: Antifungal Activity Of Eachiamentioning

confidence: 99%

“…However, GH-19 chitinases have been found mainly in seed plants 1,2) and rarely in bacteria. 3) Independent of the CAZy classification, plant chitinases are divided into five classes 1,4,5) and two subclasses 6,7) based on their amino acid sequences and domain architectures: class I chitinases, consisting of an N-terminal chitin-binding domain and a catalytic domain; class II chitinases, which have only a catalytic domain homologous to that of class I chitinases; class IV chitinases, which share homology with class I chitinases, but are smaller as a result of one deletion in the chitin-binding domain and four deletions of loop regions in the catalytic domain; and class II-L chitinases, which are a low molecular weight subclass of class II due to some deletion(s) of the loop region(s). 8) Class III, IIIb, and V chitinases share a DxDxE motif around the catalytic cleft and a (β/α) 8 barrel structure, but share very little homology (10-15%).…”

mentioning

confidence: 99%

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Purification, cDNA cloning, and characterization of LysM-containing plant chitinase from horsetail (Equisetum arvense)

Inamine

Onaga

Ohnuma

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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Chitinase-A (EaChiA), molecular mass 36 kDa, was purified from the vegetative stems of a horsetail (Equisetum arvense) using a series of column chromatography. The N-terminal amino acid sequence of EaChiA was similar to the lysin motif (LysM). A cDNA encoding EaChiA was cloned by rapid amplification of cDNA ends and polymerase chain reaction. It consisted of 1320 nucleotides and encoded an open reading frame of 361 amino acid residues. The deduced amino acid sequence indicated that EaChiA is composed of a N-terminal LysM domain and a C-terminal plant class IIIb chitinase catalytic domain, belonging to the glycoside hydrolase family 18, linked by proline-rich regions. EaChiA has strong chitin-binding activity, however, no antifungal activity. This is the first report of a chitinase from Equisetopsida, a class of fern plants, and the second report of a LysM-containing chitinase from a plant.

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