Discovery of β-1,4-d-Mannosyl-N-acetyl-d-glucosamine Phosphorylase Involved in the Metabolism of N-Glycans

Nihira, Takanori; Suzuki, Érika; Kitaoka, Motomitsu; Nishimoto, Mamoru; Ohtsubo, Ken’ichi; Nakai, Hiroyuki

doi:10.1074/jbc.m113.469080

Cited by 78 publications

(84 citation statements)

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“…Several recent studies targeted N-glycan metabolization by human intestinal bacteria, which might be linked with inflammatory bowel diseases. These studies revealed that N-glycan metabolization involves both glycoside hydrolases and phosphorylases (Renzi et al, 2011;Ladevèze et al, 2013;Nihira et al, 2013).…”

Section: Ramp1 and Ramp2 Act On β-D-manp-(1→4)-d-glcpmentioning

confidence: 99%

“…campestris (Dupoiron et al, 2015). (B) Human high mannose (HMNG) and complex N-glycan (CNG) degradation by Gram-negative bacteria such as Bacteroides fragilis NCTC 9343 (Ladevèze et al, 2013;Nihira et al, 2013). (C1) Fungal N-glycan degradation by a Gram-negative bacterium such as Bacteroides thetaiotaomicron VPI-5482 (Cuskin et al, 2015b).…”

Section: Ramp1 and Ramp2 Act On β-D-manp-(1→4)-d-glcpmentioning

confidence: 99%

“…mannoside phosphorylase specific to the disaccharide β-d-Manp-1,4-d-GlcpNAc, a N-glycan core motif (gene ID: AAO76140). The analysis of the surrounding genes present in its PUL revealed the presence of four GH92, GH20, GH33 and GH18 glycoside hydrolases assigned to α-mannosidase, β-N -acetylhexosaminidase, exo-α-sialidase, and endo-β-N -acetylglucosaminidase activities, which would act synergistically to break down host N-glycans completely (Nihira et al, 2013). In addition, this gene cluster encodes a major facilitator superfamily transporter, a protein of unknown function, an outer membrane lipoprotein and a TonB-dependent oligosaccharide transporter.…”

Section: Ramp1 and Ramp2 Act On β-D-manp-(1→4)-d-glcpmentioning

confidence: 99%

“…In addition, this gene cluster encodes a major facilitator superfamily transporter, a protein of unknown function, an outer membrane lipoprotein and a TonB-dependent oligosaccharide transporter. Based on these elements, Nihira et al (2013) developed a model of N-glycan metabolization (Fig. 4B).…”

Section: Ramp1 and Ramp2 Act On β-D-manp-(1→4)-d-glcpmentioning

confidence: 99%

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Mannoside recognition and degradation by bacteria

et al. 2016

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Mannosides constitute a vast group of glycans widely distributed in nature. Produced by almost all organisms, these carbohydrates are involved in numerous cellular processes, such as cell structuration, protein maturation and signalling, mediation of protein-protein interactions and cell recognition. The ubiquitous presence of mannosides in the environment means they are a reliable source of carbon and energy for bacteria, which have developed complex strategies to harvest them. This review focuses on the various mannosides that can be found in nature and details their structure. It underlines their involvement in cellular interactions and finally describes the latest discoveries regarding the catalytic machinery and metabolic pathways that bacteria have developed to metabolize them.

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Section: Ramp1 and Ramp2 Act On β-D-manp-(1→4)-d-glcpmentioning

confidence: 99%

Section: Ramp1 and Ramp2 Act On β-D-manp-(1→4)-d-glcpmentioning

confidence: 99%

Section: Ramp1 and Ramp2 Act On β-D-manp-(1→4)-d-glcpmentioning

confidence: 99%

Section: Ramp1 and Ramp2 Act On β-D-manp-(1→4)-d-glcpmentioning

confidence: 99%

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Mannoside recognition and degradation by bacteria

et al. 2016

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“…S1) [5]. GH130_1 contains two 4-O-b-D-mannosyl-D-glucose phosphorylases (EC 2.4.1.281) from Bacteroides fragilis (MGP, locus tag BF0772) [6], and Ruminococcus albus (RaMP1, Rumal_0852) [7], and GH130_2 consists of enzymes with relatively relaxed specificities: b-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319) from R. albus (RaMP2, Rumal_0099) [7], 1,4-b-mannosyl-Nacetylglucosamine phosphorylase (EC 2.4.1.320) from Bacteroides thetaiotaomicron (BT1033) [8], and b-D-mannopyranosyl-1,4-N,N'-diacetylchitobiose phosphorylase (EC 2.4.1.-) from the human gut bacterial metagenome (UhgbMP) [5]. These enzymes are involved in the bacterial utilization of mannans or N-linked glycans.…”

Section: Introductionmentioning

confidence: 99%

Characterization and crystal structure determination of β‐1,2‐mannobiose phosphorylase from Listeria innocua

et al. 2015

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Edited by Judit OvádiKeywords: b-1,2-Mannobiose phosphorylase Glycoside hydrolase family 130 Oligosaccharide synthesis Substrate specificity Structure-function relationship Enzyme-substrate interaction a b s t r a c t Glycoside hydrolase family 130 consists of phosphorylases and hydrolases for b-mannosides. Here, we characterized b-1,2-mannobiose phosphorylase from Listeria innocua (Lin0857) and determined its crystal structures complexed with b-1,2-linked mannooligosaccharides. b-1,2-Mannotriose was bound in a U-shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, and a significant open-close loop displacement was observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size. A structural basis for substrate recognition and phosphorolysis was provided.

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Structural insights into the difference in substrate recognition of two mannoside phosphorylases from two GH130 subfamilies

Saburi

Odaka

et al. 2016

FEBS Letters

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Edited by Judit Ov adiIn Ruminococcus albus, 4-O-b-D-mannosyl-D-glucose phosphorylase (RaMP1) and b-(1,4)-mannooligosaccharide phosphorylase (RaMP2) belong to two subfamilies of glycoside hydrolase family 130. The two enzymes phosphorolyze b-mannosidic linkages at the nonreducing ends of their substrates, and have substantially diverse substrate specificity. The differences in their mechanism of substrate binding have not yet been fully clarified. In the present study, we report the crystal structures of RaMP1 with/without 4-O-b-D-mannosyl-Dglucose and RaMP2 with/without b-(1?4)-mannobiose. The structures of the two enzymes differ at the +1 subsite of the substrate-binding pocket. Three loops are proposed to determine the different substrate specificities. One of these loops is contributed from the adjacent molecule of the oligomer structure. In RaMP1, His245 of loop 3 forms a hydrogen-bond network with the substrate through a water molecule, and is indispensible for substrate binding.Keywords: 4-O-b-D-mannosyl-D-glucose phosphorylase; glycoside hydrolase family 130; hydrogen bond-network; substrate recognition; X-ray crystallography; b-1,4-mannooligosaccharide phosphorylase Highlights• Reveals the structures of RaMP1 and RaMP2, and their complexes with substrates.• Structural insight into substrate recognition of RaMP1 and RaMP2 is discussed.• RaMP1 is the first GH130 enzyme exhibiting as a homotrimer in its native state.• Three loops are important in substrate recognition at the +1 subsite in RaMP1 and RaMP2.• A hydrogen-bond network in RaMP1 is considered to be important for substrate binding.

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Discovery of β-1,4-d-Mannosyl-N-acetyl-d-glucosamine Phosphorylase Involved in the Metabolism of N-Glycans

Cited by 78 publications

References 40 publications

Mannoside recognition and degradation by bacteria

Mannoside recognition and degradation by bacteria

Characterization and crystal structure determination of β‐1,2‐mannobiose phosphorylase from Listeria innocua

Structural insights into the difference in substrate recognition of two mannoside phosphorylases from two GH130 subfamilies

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