An endo-(1→3)-β-d-glucanase from the scallop Chlamys albidus: catalytic properties, cDNA cloning and secondary-structure characterization

Kovalchuk, Svetlana N.; Bakunina, I. Yu.; Burtseva, Yulia; Emelyanenko, V. I.; Kim, Natalia Yu.; Guzev, Konstantin V.; Kozhemyako, Valery B.; Rasskazov, V. A.; Zvyagintseva, T. N.

doi:10.1016/j.carres.2008.10.028

Cited by 24 publications

(17 citation statements)

References 31 publications

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“…2, marked in green) and 2 arginine residues and 1 histidine residue (Fig. 2, marked in blue) that help to modify the pKa of the catalytic glutamate residues (Genta et al, 2009;Kovalchuk et al, 2009;Song et al, 2010;Zakharenko et al, 2011). The predicted tertiary structure, produced from homology modelling of the putative amino acid sequences, had a β-jelly roll motif, which is also typical of family 16 glycosyl hydrolases (Genta et al, 2009) (Fig.…”

Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 98%

“…2, marked in yellow) and the correct catalytic and binding residues to be a catalytically active β-1,3-glucanase (Juncosa et al, 1994;Henrissat and Davies, 1997;Genta et al, 2009;Kovalchuk et al, 2009;Song et al, 2010). Both sequences contained features that are characteristic of glycosyl hydrolase family 16 enzymes, in particular the amino acid sequence "Glu-Ile-Asp-Ile-Val-Glu" (Fig.…”

Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 99%

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A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

Linton

Cameron

Gray

et al. 2015

Gene

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To identify the gene responsible for the production of a β-1,3-glucanase (laminarinase) within crustacea, a glycosyl hydrolase family 16 (GHF16) gene was sequenced from the midgut glands of the gecarcinid land crab, Gecarcoidea natalis and the freshwater crayfish, Cherax destructor. An open reading frame of 1098 bp for G. natalis and 1095 bp for C. destructor was sequenced from cDNA. For G. natalis and C. destructor respectively, this encoded putative proteins of 365 and 364 amino acids with molecular masses of 41.4 and 41.5 kDa. mRNA for an identical GHF16 protein was also expressed in the haemolymph of C. destructor. These putative proteins contained binding and catalytic domains that are characteristic of a β-1,3-glucanase from glycosyl hydrolase family 16. The amino acid sequences of two short 8-9 amino acid residue peptides from a previously purified β-1,3-glucanase from G. natalis matched exactly that of the putative protein sequence. This plus the molecular masses of the putative proteins matching that of the purified proteins strongly suggests that the sequences obtained encode for a catalytically active β-1,3-glucanase. A glycosyl hydrolase family 16 cDNA was also partially sequenced from the midgut glands of other amphibious (Mictyris platycheles and Paragrapsus laevis) and terrestrial decapod species (Coenobita rugosus, Coenobita perlatus, Coenobita brevimanus and Birgus latro) to confirm that the gene is widely expressed within this group. There are three possible hypothesised functions and thus evolutionary routes for the β-1,3-glucanase: 1) a digestive enzyme which hydrolyses β-1,3-glucans, 2) an enzyme which cleaves β-1,3-glycosidic bonds within cell walls to release cell contents or 3) an immune protein which can hydrolyse the cell walls of potentially pathogenic micro-organisms.

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Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 98%

Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 99%

A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

Linton

Cameron

Gray

et al. 2015

Gene

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“…These marine molluscan enzymes are also called laminarinase since they can efficiently hydrolyze the -1,3-linkage of laminarin from brown seaweeds (Sova et al, 1970b;Privalova and Elyakova, 1978;Lépagnol-Descamps et al, 1998;Kumagai et al, 2008). Primary structures of molluscan -1,3-glucanases have been reported in the surf clam and scallop enzymes (Kozhemyako et al, 2004;Kovalchuk et al, 2006;Kovalchuk et al, 2009). According to the hydrophobic cluster analysis of the primary structure (CAZy http://www.cazy.org/), these bivalve -1,3-glucanases have been classified under the glycosyl hydrolase family16 (GHF16).…”

Section: Introductionmentioning

confidence: 99%

Enzymatic properties and the primary structure of a β-1,3-glucanase from the digestive fluid of the Pacific abalone Haliotis discus hannai

Kumagai

Ojima

2009

Comparative Biochemistry and Physiology Part B: Biochemistry an

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A -1,3-glucanase (EC 3.2.1.6) with a molecular mass of 33 kDa was isolated from the digestive fluid of the Pacific abalone Haliotis discus hannai by ammonium sulfate fractionation followed by conventional column chromatography. This enzyme, named HdLam33 in the present study, degraded laminarin and laminarioligosaccharides to laminaribiose and glucose with the optimal temperature and pH at 50 o C and 6.0, respectively.

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“…AkLam33 appeared to be the first exolytic β-1,3-glucanase from marine invertebrates since all β-1,3-glucanases so far purified from marine invertebrates have been characterized as endolytic enzymes (Sova et al, 1970;Lépagnol-Descamps et al, 1998;Kovalchuk et al, 2006;Kumagai et al, 2008;Pesentseva et al, 2008;Zhu et al, 2008;Kumagai and Ojima, 2009;Kovalchuk et al, 2009). Besides AkLam33, exolytic β-1,3-glucanases have been reported on bacteria, yeast, insect, and a terrestrial snail (Marshall and Grand, 1975;Sánchez et al, 1982;Kulminskaya et al, 2001;Hrmova and Fincher, 1998;Igarashi et al, 2003;Genta et al, 2007); however, these enzymes were classified under GHF 3, 5, 17, and 55 (Klebl and Tanner, 1989;Chambers et al, 1993;Hrmova et al, 1996;Sakamoto et al, 2005;Ishida et al, 2009;Ooi et al, 2009).…”

Section: General Properties Of Aklam36 and Aklam33mentioning

confidence: 99%

“…Endolytic β-1,3-glucanases from marine invertebrates have been reported on sea cucumber, surf clam, scallop, and abalone (Sova et al, 1970;Kovalchuk et al, 2006;Zhu et al, 2008;Kumagai et al, 2008;Kumagai et al, 2009;Kumagai and Ojima, 2009;Kovalchuk et al, 2009). These enzymes seem to act as the digestive enzymes that degrade β-1,3-glucans in dietary algae providing laminarioligosaccharides.…”

Section: Physiological Significance Of Aklam33 and Aklam36mentioning

confidence: 99%

Isolation and characterization of two types of β-1,3-glucanases from the common sea hare Aplysia kurodai

Kumagai

Ojima

2010

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Two types of β-1,3-glucanases, AkLam36 and AkLam33 with the molecular masses of 36 kDa and 33 kDa, respectively, were isolated from the digestive fluid of the common sea hare Aplysia kurodai. AkLam36 was regarded as an endolytic enzyme (EC 3.2.1.6) degrading laminarin and laminarioligosaccharides to laminaritriose, laminaribiose, and glucose, while AkLam33 was regarded as an exolytic enzyme (EC 3.2.1.58) directly producing glucose from polymer laminarin. AkLam36 showed higher activity toward β-1,3-glucans with a few β-1,6-linked glucose branches such as Laminaria digitata laminarin (LLam) than highly branched β-1,3-glucans such as Eisenia bicyclis laminarin (ELam). AkLam33 showed moderate activity toward both ELam and LLam and high activity toward smaller substrates such as laminaritetraose and laminaritriose.Although both enzymes did not degrade laminaribiose as a sole substrate, they were capable of degrading it via transglycosylation reaction with laminaritriose. The N-terminal amino-acid sequences of AkLam36 and AkLam33 indicated that both enzymes belong to the glycosyl hydrolase family 16 like other molluscan β-1,3-glucanases.3

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An endo-(1→3)-β-d-glucanase from the scallop Chlamys albidus: catalytic properties, cDNA cloning and secondary-structure characterization

Cited by 24 publications

References 31 publications

A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

Enzymatic properties and the primary structure of a β-1,3-glucanase from the digestive fluid of the Pacific abalone Haliotis discus hannai

Isolation and characterization of two types of β-1,3-glucanases from the common sea hare Aplysia kurodai

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