English Journal

Functional characterization of the UDP-xylose biosynthesis pathway in Rhodothermus marinus.

Duan XC1, Lu AM, Gu B, Cai ZP, Ma HY, Wei S, Laborda P, Liu L, Voglmeir J.
Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2015 Jun 2. [Epub ahead of print]
UDP-glucuronic acid dehydrogenase (UGD) and UDP-xylose synthase (UXS) are the two enzymes responsible for the biosynthesis of UDP-xylose from UDP-glucose. Several UGDs from bacterial sources, which oxidize UDP-glucose to glucuronic acid, have been found and functionally characterized whereas only fe
PMID 26033773

Stability, redox parameters and electrocatalytic activity of a cytochrome domain from a new subfamily.

Molinas MF1, Benavides L1, Castro MA1, Murgida DH2.
Bioelectrochemistry (Amsterdam, Netherlands).Bioelectrochemistry.2015 May 6;105:25-33. doi: 10.1016/j.bioelechem.2015.05.005. [Epub ahead of print]
We report a spectroscopic, electrochemical and spectroelectrochemical characterization of the soluble cytochrome c domain (Cyt-D) from the Rhodothermus marinus caa3 terminal oxygen reductase and its putative electron donor, a high potential [4Fe-4S] protein (HiPIP). Cyt-D exhibits superior stability
PMID 25978786

Dye-linked D-amino acid dehydrogenase from the thermophilic bacterium Rhodothermus marinus JCM9785: characteristics and role in trans-4-hydroxy-L-proline catabolism.

Satomura T1, Ishikura M, Koyanagi T, Sakuraba H, Ohshima T, Suye S.
Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2015 May;99(10):4265-75. doi: 10.1007/s00253-014-6263-9. Epub 2014 Dec 5.
A gene from the thermophilic Gram-negative bacterium Rhodothermus marinus JCM9785, encoding a dye-linked D-amino acid dehydrogenase homologue, was overexpressed in Escherichia coli, and its product was purified and characterized. The expressed enzyme was a highly thermostable dye-linked D-amino acid
PMID 25472442

Japanese Journal

Immobilization of a Thermostable Cellobiose 2-Epimerase from Rhodothermus marinus JCM9785 and Continuous Production of Epilactose

SATO Hiroki,SABURI Wataru,OJIMA Teruyo [他],TAGUCHI Hidenori,MORI Haruhide,MATSUI Hirokazu
Bioscience, biotechnology, and biochemistry 76(8), 1584-1587, 2012-08-23
NAID 10031066440

Novel low-temperature-active, salt-tolerant and proteases-resistant endo-1,4-β-mannanase from a new Sphingomonas strain(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

Zhou Junpei,Zhang Rui,Gao Yajie [他],Li Junjun,Tang Xianghua,Mu Yuelin,Wang Feng,Li Chao,Dong Yanyan,Huang Zunxi
Journal of bioscience and bioengineering 113(5), 568-574, 2012-05
… A mannanase-coding gene (1191 bp) was cloned and encodes a 396-residue polypeptide (ManAJB13) showing the highest amino acid sequence identities of 56.2% with the putative glycosyl hydrolase (GH) family 26 endo-1,4-β-mannanase from Rhodothermus marinus (YP_004824245), and 44.2% with the identified GH 26 endo-1,4-β-mannanase from Cellvibrio japonicus (2VX5_A). …
NAID 110009456893