Essentiality of tetramer formation of Cellulomonas parahominis L-ribose isomerase involved in novel L-ribose metabolic pathway

Verfasser / Beitragende:
[Yuji Terami, Hiromi Yoshida, Keiko Uechi, Kenji Morimoto, Goro Takata, Shigehiro Kamitori]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/15(2015-08-01), 6303-6313
Format:
Artikel (online)
ID: 60550671X
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024 7 0 |a 10.1007/s00253-015-6417-4  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-015-6417-4 
245 0 0 |a Essentiality of tetramer formation of Cellulomonas parahominis L-ribose isomerase involved in novel L-ribose metabolic pathway  |h [Elektronische Daten]  |c [Yuji Terami, Hiromi Yoshida, Keiko Uechi, Kenji Morimoto, Goro Takata, Shigehiro Kamitori] 
520 3 |a L-Ribose isomerase from Cellulomonas parahominis MB426 (CpL-RI) can catalyze the isomerization between L-ribose and L-ribulose, which are non-abundant in nature and called rare sugars. CpL-RI has a broad substrate specificity and can catalyze the isomerization between D-lyxose and D-xylulose, D-talose and D-tagatose, L-allose and L-psicose, L-gulose and L-sorbose, and D-mannose and D-fructose. To elucidate the molecular basis underlying the substrate recognition mechanism of CpL-RI, the crystal structures of CpL-RI alone and in complexes with L-ribose, L-allose, and L-psicose were determined. The structure of CpL-RI was very similar to that of L-ribose isomerase from Acinetobacter sp. strain DL-28, previously determined by us. CpL-RI had a cupin-type β-barrel structure, and the catalytic site was detected between two large β-sheets with a bound metal ion. The bound substrates coordinated to the metal ion, and Glu113 and Glu204 were shown to act as acid/base catalysts in the catalytic reaction via a cis-enediol intermediate. Glu211 and Arg243 were found to be responsible for the recognition of substrates with various configurations at 4- and 5-positions of sugar. CpL-RI formed a homo-tetramer in crystals, and the catalytic site independently consisted of residues within a subunit, suggesting that the catalytic site acted independently. Crystal structure and site-direct mutagenesis analyses showed that the tetramer structure is essential for the enzyme activity and that each subunit of CpL-RI could be structurally stabilized by intermolecular contacts with other subunits. The results of growth complementation assays suggest that CpL-RI is involved in a novel metabolic pathway using L-ribose as a carbon source. 
540 |a Springer-Verlag Berlin Heidelberg, 2015 
690 7 |a Crystal structure  |2 nationallicence 
690 7 |a Cupin-type β-barrel  |2 nationallicence 
690 7 |a Rare sugar  |2 nationallicence 
690 7 |a L-Ribose isomerase  |2 nationallicence 
700 1 |a Terami  |D Yuji  |u Rare Sugar Research Center and Faculty of Agriculture, Kagawa University, 2393, Ikenobe, Miki-cho, Kita-gun, 761-0795, Kagawa, Japan  |4 aut 
700 1 |a Yoshida  |D Hiromi  |u Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1, Ikenobe, Miki-cho, Kita-gun, 761-0793, Kagawa, Japan  |4 aut 
700 1 |a Uechi  |D Keiko  |u Rare Sugar Research Center and Faculty of Agriculture, Kagawa University, 2393, Ikenobe, Miki-cho, Kita-gun, 761-0795, Kagawa, Japan  |4 aut 
700 1 |a Morimoto  |D Kenji  |u Rare Sugar Research Center and Faculty of Agriculture, Kagawa University, 2393, Ikenobe, Miki-cho, Kita-gun, 761-0795, Kagawa, Japan  |4 aut 
700 1 |a Takata  |D Goro  |u Rare Sugar Research Center and Faculty of Agriculture, Kagawa University, 2393, Ikenobe, Miki-cho, Kita-gun, 761-0795, Kagawa, Japan  |4 aut 
700 1 |a Kamitori  |D Shigehiro  |u Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1, Ikenobe, Miki-cho, Kita-gun, 761-0793, Kagawa, Japan  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/15(2015-08-01), 6303-6313  |x 0175-7598  |q 99:15<6303  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-015-6417-4  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00253-015-6417-4  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Terami  |D Yuji  |u Rare Sugar Research Center and Faculty of Agriculture, Kagawa University, 2393, Ikenobe, Miki-cho, Kita-gun, 761-0795, Kagawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Yoshida  |D Hiromi  |u Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1, Ikenobe, Miki-cho, Kita-gun, 761-0793, Kagawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Uechi  |D Keiko  |u Rare Sugar Research Center and Faculty of Agriculture, Kagawa University, 2393, Ikenobe, Miki-cho, Kita-gun, 761-0795, Kagawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Morimoto  |D Kenji  |u Rare Sugar Research Center and Faculty of Agriculture, Kagawa University, 2393, Ikenobe, Miki-cho, Kita-gun, 761-0795, Kagawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Takata  |D Goro  |u Rare Sugar Research Center and Faculty of Agriculture, Kagawa University, 2393, Ikenobe, Miki-cho, Kita-gun, 761-0795, Kagawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Kamitori  |D Shigehiro  |u Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1, Ikenobe, Miki-cho, Kita-gun, 761-0793, Kagawa, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/15(2015-08-01), 6303-6313  |x 0175-7598  |q 99:15<6303  |1 2015  |2 99  |o 253