Nucleotide and deduced amino acid sequences of mutanase-like genes from Paenibacillus isolates: Proposal of a new family of glycoside hydrolases

Hakamada, Yoshihiro; Sumitomo, Nobuyuki; Ogawa, Akinori; Kawano, Takako; Saeki, Katsuhisa; Ozaki, Katsuya; Ito, Susumu; Kobayashi, Tohru

doi:10.1016/j.biochi.2007.09.018

Cited by 16 publications

(18 citation statements)

References 23 publications

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“…KSM-M126. 9) In addition, these mutanases has similar molecular masses. The deduced molecular mass of the mutanase of NA1123 and MuC1 of KSM-M126 were 115399 and 119514, respectively.…”

Section: Discussionmentioning

confidence: 99%

“…The feature of signal sequence of the present enzyme (Arg 2 , Arg 4 , Lys 6 and Pro 30 ) is resemble to that of the mutanase from Paenibacillus strain KSM-M35 (Lys 6 , Lys 8 , Lys 11 and Pro 30 ). 9) The N-terminal and C-terminal regions of the mutanase MuC1 are divided by proline-threonine repeat linker. The proposed function of proline-threonine sequence is considered as the linker or hinge between these domains.…”

Section: Discussionmentioning

confidence: 99%

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Cloning and Expression of the Mutanase Gene of Paenibacillus humicus from Fermented Food

Tsumori

Kawauti

Shimamura

et al. 2010

JOURNAL OF HEALTH SCIENCE

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There has been much interest in mutanases, α-1,3-glucanases, as they have the potential for preventive agents in the oral cavity. Mutanases have been reported in some bacteria and fungi but remain a relatively uncharacterized family of enzymes. We screened bacterial mutanase in fermented food for the application of the enzyme to preventive medicine. Immersed solutions of fermented soybeans, natto, on mutan-containing agar plates exhibited mutanhydrolyzing activity after incubation. We isolated a microorganism that hydrolyzed mutan from the fermented soybeans and named it Paenibacillus humicus strain NA1123. The gene for the mutanase was cloned, and the nucleotide sequence of the gene consisted of 3441-bp open reading frame that encoded a predicted 1146-amino acid polypeptide including a 33-amino acid signaling peptide. The predicted molecular mass of the matured enzyme was 115399. The protein is composed of an N-terminal domain and a C-terminal domain, that are connected by a sequence composed of proline and threonine repeats. The deduced amino acid sequence of the present enzyme showed similarity to that of the mutanase MuC1 of strain KSM-M126 and the mutanase MuE of strain KSM-M318 of Paenibacillus sp. with 77.2% and 73.5% identity, respectively. We con- * To whom correspondence should be addressed: Department of Preventive Medicine and Public Health, National Defense Medical College, 3-2 Namiki, Tokorozawa 359-8513, Japan. Tel.: +81-4-2995-1563; Fax: +81-4-2996-5195; E-mail: yamakami@ndmc.ac.jp firmed that the recombinant mutanase exhibited mutan hydrolyzing activity.

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“…KSM-M126. 9) In addition, these mutanases has similar molecular masses. The deduced molecular mass of the mutanase of NA1123 and MuC1 of KSM-M126 were 115399 and 119514, respectively.…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Cloning and Expression of the Mutanase Gene of Paenibacillus humicus from Fermented Food

Tsumori

Kawauti

Shimamura

et al. 2010

JOURNAL OF HEALTH SCIENCE

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“…15) A biochemical study of mutanase RM indicated that the N-terminal region, corresponding to DS1 and CB6, exhibited -1,3-glucan binding activity and enhanced degrading activity as to biofilms from Streptococcus mutans, 16) but no functions of individual domains, DS1 and CB6, have been investigated in it. In this study, we determined in detail the role of each N-terminal domain, containing DS1, CB6, DS2, and UCD, of Alg-KA by characterizing the domain deletion enzymes, and confirmed their relevance to cell-wall lysis.…”

Section: Discussionmentioning

confidence: 99%

“…strain KSM-126 with identities of approximately 80%, 48.3%, and 46.7% respectively. 15) Hakamada et al compared the amino acid sequences of these -1,3-glucanases with those of other enzymes in databases, and reported that these enzymes included an N-terminal discoidin domain (DS1), a carbohydrate binding module family 6 (CB6), threonine and proline repeats (TPs), a second discoidin domain (DS2), an uncharacterized conserved domain (UCD), and a Cterminal catalytic domain. 15) This indicates that Agl-KA can be classified as a type 87 enzyme that has a domain structure similar to that of Paenibacillus enzymes (Fig.…”

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confidence: 99%

“…This was the first study of an -1,3-glucan binding domain among type 87 enzymes. Although the N-terminal region of mutanase RM1 contains DS1 and CB6 domains according to the domain classification reported by Hakamada et al, 15) it remains unclear whether DS1 and CB6 can bind to -1,3-glucan independently, or can bind only in combination. Moreover, the functions of DS2 and UCD, which are located downstream of DS1 and CB6, have not been clearly established, particularly DS2, which shows high sequence similarity to DS1.…”

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confidence: 99%

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Domain Structure and Function of α-1,3-Glucanase fromBacillus circulansKA-304, an Enzyme Essential for Degrading Basidiomycete Cell Walls

Suyotha

Yano

Takagi

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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α-1,3-Glucanase: present situation and prospect of research

Suyotha

Yano

Wakayama

2016

World J Microbiol Biotechnol

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α-1,3-Glucanases hydrolyze α-1,3-glucan which is an insoluble linear α-1,3-linked homopolymer of glucose and these enzymes are classified into two families of glycoside hydrolases on the basis of amino acid sequence similarity; type-71 α-1,3-glucanases found in fungi and type-87 enzymes in bacteria. α-1,3-Glucan (also called 'mutan') is a major component of dental plaque formed by oral Streptococci and has important physiological roles in various fungal species, including as a component of cell walls, an endogenous carbon source for sexual development, and a virulent factor. Considering these backgrounds, α-1,3-glucanases have been investigated from the perspectives of applications to dental care and development of cell-wall lytic enzymes. Compared with information regarding other glycoside hydrolases such as amylases, cellulases, chitinases, and β-glucanases, there is limited biochemical and structural information available regarding α-1,3-glucanase. Further research on α-1,3-glucanases on enzyme application to dental care and biological control of pathogenic fungi is expected. In this mini-review, we briefly describe how α-1,3-glucanases are categorized and characterized and present our study findings regarding α-1,3-glucanase from Bacillus circulans KA-304. Furthermore, we briefly discuss potential future applications of α-1,3-glucanases.

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Nucleotide and deduced amino acid sequences of mutanase-like genes from Paenibacillus isolates: Proposal of a new family of glycoside hydrolases

Cited by 16 publications

References 23 publications

Cloning and Expression of the Mutanase Gene of Paenibacillus humicus from Fermented Food

Cloning and Expression of the Mutanase Gene of Paenibacillus humicus from Fermented Food

Domain Structure and Function of α-1,3-Glucanase fromBacillus circulansKA-304, an Enzyme Essential for Degrading Basidiomycete Cell Walls

α-1,3-Glucanase: present situation and prospect of research

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