Renin Inhibits N-Acetyl-d-Glucosamine 2-Epimerase (Renin-Binding Protein)

Takahashi, Saori; Kumagai, Masanori; Shindo, Sho; Saito, Kyuichi; Kawamura, Yukio

doi:10.1093/oxfordjournals.jbchem.a022846

Cited by 27 publications

(25 citation statements)

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“…The nanE gene product is annotated in the NCTC genome project as having homology to the porcine RnBP, a polypeptide first characterized by its ability to tightly bind and inactivate the peptidase renin (20,34). RnBPs from human and porcine kidney have been shown to possess N-acetylglucosamine 2-epimerase activity (18,28,30). We tested for this activity in extracts of the wild-type ADB77 and RC201 (⌬nanE) using manNAc and ATP as described in Materials and Methods.…”

Section: Resultsmentioning

confidence: 99%

Sialic Acid ( N -Acetyl Neuraminic Acid) Utilization by Bacteroides fragilis Requires a Novel N -Acetyl Mannosamine Epimerase

et al. 2009

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We characterized the nanLET operon in Bacteroides fragilis, whose products are required for the utilization of the sialic acid N-acetyl neuraminic acid (NANA) as a carbon and energy source. The first gene of the operon is nanL, which codes for an aldolase that cleaves NANA into N-acetyl mannosamine (manNAc) and pyruvate. The next gene, nanE, codes for a manNAc/N-acetylglucosamine (NAG) epimerase, which, intriguingly, possesses more similarity to eukaryotic renin binding proteins than to other bacterial NanE epimerase proteins. Unphosphorylated manNAc is the substrate of NanE, while ATP is a cofactor in the epimerase reaction. The third gene of the operon is nanT, which shows similarity to the major transporter facilitator superfamily and is most likely to be a NANA transporter. Deletion of any of these genes eliminates the ability of B. fragilis to grow on NANA. Although B. fragilis does not normally grow with manNAc as the sole carbon source, we isolated a B. fragilis mutant strain that can grow on this substrate, likely due to a mutation in a NAG transporter; both manNAc transport and NAG transport are affected in this strain. Deletion of the nanE epimerase gene or the rokA hexokinase gene, whose product phosphorylates NAG, in the manNAc-enabled strain abolishes growth on manNAc. Thus, B. fragilis possesses a new pathway of NANA utilization, which we show is also found in other Bacteroides species.Many bacteria have the ability to release sialic acids from complex glycoproteins and oligosaccharides present in the media or on cell surfaces at sites of colonization or infection. To use the released sialic acids as a rich source of carbon and nitrogen for growth, bacteria must have the ability to transport these compounds into the cell and convert the nine carbon sugars into intermediates that enter the central glycolytic pathways. The utilization of N-acetyl neuraminic acid (NANA), one of the sialic acids, has been well studied in Escherichia coli (36, 37), Haemophilus spp. (1, 35), and Clostridium spp. (38), to name a few.In many microorganisms, the genes for NANA utilization are arranged in an operon that may be regulated by a repressor protein, termed NanR. A comprehensive review of the organization and composition of several prokaryotic operons involved in NANA utilization has been published (36). Many of these operons share common components, including a transport gene for NANA (nanT), a gene encoding an aldolase (nanA) that splits NANA into pyruvate and N-acetyl mannosamine (manNAc), a gene encoding a kinase activity (nanK) that phosphorylates manNAc to form manNAc 6-P and, finally, an epimerase gene (nanE) whose product converts manNAc 6-P to N-acetylglucosamine 6-P (NAG 6-P). NAG 6-P then enters the common pathway of aminosugar utilization (21). For a schematic of the NANA utilization pathway in E. coli, the current paradigm of prokaryotic NANA utilization, see Fig. 7A.Bacteroides fragilis possesses a neuraminidase activity, which can liberate free NANA from complex glycoproteins and oligosaccharides. Go...

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Section: Resultsmentioning

confidence: 99%

Sialic Acid ( N -Acetyl Neuraminic Acid) Utilization by Bacteroides fragilis Requires a Novel N -Acetyl Mannosamine Epimerase

et al. 2009

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“…The hydrolysis of the IQF substrate at the Leu-Val or Leu-Leu bond was spectrophotometrically determined. 7,12) The reaction mixture contained 39 ml of 50 mM sodium phosphate buffer, pH 6.5, 0.1 M NaCl, 0.02% NaN 3 , 0.02% Tween 20, 1 ml of 1 mM IQF substrate solution in DMSO, 5 ml of 5 mg/ml of rh-or porcine renin solution, and 5 ml of inhibitor solution in a total volume of 50 ml. The reaction mixture was incubated at 37 C for 30 min, and the reaction was terminated by adding 0.2 ml of 0.1 M triethanolamine, pH 9.5.…”

Section: Methodsmentioning

confidence: 99%

Isolation of Human Renin Inhibitor from Soybean: Soyasaponin I Is the Novel Human Renin Inhibitor in Soybean

Takahashi

Hori

Shinbo³

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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“…It is noteworthy that as RnBP/NAGE inhibits renin activity, so too renin inhibits NAGE activity (69). Therefore, it is possible that renin taken up into RnBP/NAGE-expressing cells might regulate NAGE activity.…”

Section: Rnbp Has N-acyl-glucosamine 2-epimerase Activitymentioning

confidence: 99%

Physiological Relevance of Renin/Prorenin Binding and Uptake

Catanzaro

2005

Hypertens Res

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Renin Inhibits N-Acetyl-d-Glucosamine 2-Epimerase (Renin-Binding Protein)

Cited by 27 publications

References 0 publications

Sialic Acid ( N -Acetyl Neuraminic Acid) Utilization by Bacteroides fragilis Requires a Novel N -Acetyl Mannosamine Epimerase

Sialic Acid ( N -Acetyl Neuraminic Acid) Utilization by Bacteroides fragilis Requires a Novel N -Acetyl Mannosamine Epimerase

Isolation of Human Renin Inhibitor from Soybean: Soyasaponin I Is the Novel Human Renin Inhibitor in Soybean

Physiological Relevance of Renin/Prorenin Binding and Uptake

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