The Complete Amino Acid Sequence and Enzymatic Properties of an i-Type Lysozyme Isolated from the Common Orient Clam (<i>Meretrix lusoria</i>)

Kuwano, Yuko; Yoneda, Kazunari; Kawaguchi, Yuya; Araki, Nobuhito; Araki, Toshimitsu

doi:10.1271/bbb.130534

Cited by 10 publications

(7 citation statements)

References 48 publications

(62 reference statements)

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“…3.1. Crystal structure Details of the purification of MLL have been reported in Kuwano et al (2013) and the determined amino-acid sequence of MLL is shown in Fig. 1 together with that of VPL (UniProt accession No.…”

Section: Resultsmentioning

confidence: 99%

“…One of the M. lusoria lysozyme isozymes (MLL-B) was purified according to the method described by Kuwano et al (2013). Namely, the samples were homogenized in 2% acetic acid and centrifuged (5000g, 20 min, 277 K).…”

Section: Purification Of Lysozymementioning

confidence: 99%

“…This dimeric structure suppresses the activity of VPL at low concentrations of NaCl, and gel-filtration analysis of VPL provided empirical evidence of dimer formation at low ionic strength (Goto et al, 2007). However, the enzymatic activities of MLL were not affected by the ionic strength (Kuwano et al, 2013). We therefore compared the residues at the interface of the dimer in VPL with those of MLL (Fig.…”

Section: Figurementioning

confidence: 99%

“…We compared the structure of MLL with those of HEL and VPL. The results revealed that MLL has a largely similar structure to VPL, but that the location of the side chain of the second catalytic residue is different and amino-acid substitutions at the dimer-formation interface of VPL may be responsible for the lack of salt-dependent activation of MLL (Kuwano et al, 2013).…”

Section: Introductionmentioning

confidence: 98%

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The tertiary structure of an i-type lysozyme isolated from the common orient clam (Meretrix lusoria)

et al. 2013

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To evaluate the structure-function relationships of invertebrate lysozymes, a new invertebrate-type (i-type) lysozyme was isolated from the common orient clam (Meretrix lusoria) and the tertiary structure of this enzyme was determined. Comparison of the tertiary structure of this enzyme with those of chicken and Venerupi philippinarum lysozymes revealed that the location of the side chain of the second catalytic residue, an aspartic acid, and the N-acetylglucosamine trimer bound at subsites A-C were different. Furthermore, the amino acid electrostatically interacting with Asp30 in V. philippinarum lysozyme, Lys108, was substituted by Gly in M. lusoria lysozyme and no other possible amino acid that could contribute to this interaction was found in M. lusoria lysozyme. It therefore seems that the substitutions of the amino acids at the interface of the V. philippinarum lysozyme dimer are likely to change the oligomeric state of the M. lusoria lysozyme.

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Section: Resultsmentioning

confidence: 99%

Section: Purification Of Lysozymementioning

confidence: 99%

Section: Figurementioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

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The tertiary structure of an i-type lysozyme isolated from the common orient clam (Meretrix lusoria)

et al. 2013

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“…The first i‐type lysozyme was isolated from the echinoderm starfish Asterias rubens and was assigned to a new class because the N‐terminal sequence had no similarity to the lysozymes known at the time (Jollès & Jollès, ). Similar i‐type lysozymes were later isolated from the sea cucumber Stichopus japonicus (Cong et al ., ), the sponge Suberites domuncula (Thakur et al ., ) and several bivalves including the Iceland scallop Chlamys islandica (Nilsen et al ., ), the blue mussel Mytilus edulis (Olsen et al ., ), the eastern oyster Crassostrea virginica (Xue et al ., ), the Asiatic hard clam Meretrix meretrix (Yue et al ., ) and the common orient clam Meretrix lusoria (Kuwano et al ., ). All of these enzymes were shown to possess muramidase activity.…”

Section: Introductionmentioning

confidence: 97%

Expression and characterization of a recombinant i‐type lysozyme from the harlequin ladybird beetle Harmonia axyridis

Beckert

Wiesner

Schmidtberg

et al. 2016

Insect Molecular Biology

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Lysozymes are enzymes that destroy bacterial cell walls by hydrolysing the polysaccharide component of peptidoglycan. In insects, there are two classes of lysozymes, the c-type with muramidase activity and the i-type whose prototypical members from annelids and molluscs possess both muramidase and isopeptidase activities. Many insect genes encoding c-type and i-type lysozymes have been identified during genome and transcriptome analyses, but only c-type lysozymes have been functionally characterized at the protein level. Here we produced one of five i-type lysozymes represented in the immunity-related transcriptome of the invasive harlequin ladybird beetle Harmonia axyridis as recombinant protein. This was the only one containing the serine and histidine residues that are thought to be required for isopeptidase activity. This i-type lysozyme was recombinantly expressed in the yeast Pichia pastoris, but the purified protein was inactive in both muramidase and isopeptidase assays. Transcription and immunofluorescence analysis revealed that this i-type lysozyme is produced in the fat body but is not inducible by immune challenge. These data suggest that i-type lysozymes in insects may have acquired novel and as yet undetermined functions in the course of evolution.

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Complete Amino Acid Sequence of a Copper/Zinc-Superoxide Dismutase from Ginger Rhizome

et al. 2017

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Superoxide dismutase (SOD) is an antioxidant enzyme protecting cells from oxidative stress. Ginger (Zingiber officinale) is known for its antioxidant properties, however, there are no data on SODs from ginger rhizomes. In this study, we purified SOD from the rhizome of Z. officinale (Zo-SOD) and determined its complete amino acid sequence using N terminal sequencing, amino acid analysis, and de novo sequencing by tandem mass spectrometry. Zo-SOD consists of 151 amino acids with two signature Cu/Zn-SOD motifs and has high similarity to other plant Cu/Zn-SODs. Multiple sequence alignment showed that Cu/Zn-binding residues and cysteines forming a disulfide bond, which are highly conserved in Cu/Zn-SODs, are also present in Zo-SOD. Phylogenetic analysis revealed that plant Cu/Zn-SODs clustered into distinct chloroplastic, cytoplasmic, and intermediate groups. Among them, only chloroplastic enzymes carried amino acid substitutions in the region functionally important for enzymatic activity, suggesting that chloroplastic SODs may have a function distinct from those of SODs localized in other subcellular compartments. The nucleotide sequence of the Zo-SOD coding region was obtained by reverse-translation, and the gene was synthesized, cloned, and expressed. The recombinant Zo-SOD demonstrated pH stability in the range of 5-10, which is similar to other reported Cu/Zn-SODs, and thermal stability in the range of 10-60 °C, which is higher than that for most plant Cu/Zn-SODs but lower compared to the enzyme from a Z. officinale relative Curcuma aromatica.

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The Complete Amino Acid Sequence and Enzymatic Properties of an i-Type Lysozyme Isolated from the Common Orient Clam (Meretrix lusoria)

Cited by 10 publications

References 48 publications

The tertiary structure of an i-type lysozyme isolated from the common orient clam (Meretrix lusoria)

The tertiary structure of an i-type lysozyme isolated from the common orient clam (Meretrix lusoria)

Expression and characterization of a recombinant i‐type lysozyme from the harlequin ladybird beetle Harmonia axyridis

Complete Amino Acid Sequence of a Copper/Zinc-Superoxide Dismutase from Ginger Rhizome

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