An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes

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Standard

An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes. / Singh, Ranjitha; Singh, Raushan; Kim, In Won; Sigdel, Sujan; Kalia, Vipin C.; Kang, Yun Chan; Lee, Jung Kul.

I: Enzyme and Microbial Technology, Bind 72, 01.05.2015, s. 56-64.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Singh, R, Singh, R, Kim, IW, Sigdel, S, Kalia, VC, Kang, YC & Lee, JK 2015, 'An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes', Enzyme and Microbial Technology, bind 72, s. 56-64. https://doi.org/10.1016/j.enzmictec.2015.02.004

APA

Singh, R., Singh, R., Kim, I. W., Sigdel, S., Kalia, V. C., Kang, Y. C., & Lee, J. K. (2015). An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes. Enzyme and Microbial Technology, 72, 56-64. https://doi.org/10.1016/j.enzmictec.2015.02.004

Vancouver

Singh R, Singh R, Kim IW, Sigdel S, Kalia VC, Kang YC o.a. An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes. Enzyme and Microbial Technology. 2015 maj 1;72:56-64. https://doi.org/10.1016/j.enzmictec.2015.02.004

Author

Singh, Ranjitha ; Singh, Raushan ; Kim, In Won ; Sigdel, Sujan ; Kalia, Vipin C. ; Kang, Yun Chan ; Lee, Jung Kul. / An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes. I: Enzyme and Microbial Technology. 2015 ; Bind 72. s. 56-64.

Bibtex

@article{c6718d5d3735436e8a10409371fd485b,
title = "An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes",
abstract = "An NAD+-dependent ribitol dehydrogenase from Enterobacter aerogenes KCTC 2190 (EaRDH) was cloned and successfully expressed in Escherichia coli. The complete 729-bp gene was amplified, cloned, expressed, and subsequently purified in an active soluble form using nickel affinity chromatography. The enzyme had an optimal pH and temperature of 11.0 and 45°C, respectively. Among various polyols, EaRDH exhibited activity only toward ribitol, with Km, Vmax, and kcat/Km values of 10.3mM, 185Umg-1, and 30.9s-1mM-1, respectively. The enzyme showed strong preference for NAD+ and displayed no detectable activity with NADP+. Homology modeling and sequence analysis of EaRDH, along with its biochemical properties, confirmed that EaRDH belongs to the family of NAD+-dependent ribitol dehydrogenases, a member of short-chain dehydrogenase/reductase (SCOR) family. EaRDH showed the highest activity and unique substrate specificity among all known RDHs. Homology modeling and docking analysis shed light on the molecular basis of its unusually high activity and substrate specificity.",
keywords = "Enterobacter aerogenes, Homology modeling, Ribitol dehydrogenase, Short-chain dehydrogenase/reductase",
author = "Ranjitha Singh and Raushan Singh and Kim, {In Won} and Sujan Sigdel and Kalia, {Vipin C.} and Kang, {Yun Chan} and Lee, {Jung Kul}",
year = "2015",
month = may,
day = "1",
doi = "10.1016/j.enzmictec.2015.02.004",
language = "English",
volume = "72",
pages = "56--64",
journal = "Enzyme and Microbial Technology",
issn = "0141-0229",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - An efficient ribitol-specific dehydrogenase from Enterobacter aerogenes

AU - Singh, Ranjitha

AU - Singh, Raushan

AU - Kim, In Won

AU - Sigdel, Sujan

AU - Kalia, Vipin C.

AU - Kang, Yun Chan

AU - Lee, Jung Kul

PY - 2015/5/1

Y1 - 2015/5/1

N2 - An NAD+-dependent ribitol dehydrogenase from Enterobacter aerogenes KCTC 2190 (EaRDH) was cloned and successfully expressed in Escherichia coli. The complete 729-bp gene was amplified, cloned, expressed, and subsequently purified in an active soluble form using nickel affinity chromatography. The enzyme had an optimal pH and temperature of 11.0 and 45°C, respectively. Among various polyols, EaRDH exhibited activity only toward ribitol, with Km, Vmax, and kcat/Km values of 10.3mM, 185Umg-1, and 30.9s-1mM-1, respectively. The enzyme showed strong preference for NAD+ and displayed no detectable activity with NADP+. Homology modeling and sequence analysis of EaRDH, along with its biochemical properties, confirmed that EaRDH belongs to the family of NAD+-dependent ribitol dehydrogenases, a member of short-chain dehydrogenase/reductase (SCOR) family. EaRDH showed the highest activity and unique substrate specificity among all known RDHs. Homology modeling and docking analysis shed light on the molecular basis of its unusually high activity and substrate specificity.

AB - An NAD+-dependent ribitol dehydrogenase from Enterobacter aerogenes KCTC 2190 (EaRDH) was cloned and successfully expressed in Escherichia coli. The complete 729-bp gene was amplified, cloned, expressed, and subsequently purified in an active soluble form using nickel affinity chromatography. The enzyme had an optimal pH and temperature of 11.0 and 45°C, respectively. Among various polyols, EaRDH exhibited activity only toward ribitol, with Km, Vmax, and kcat/Km values of 10.3mM, 185Umg-1, and 30.9s-1mM-1, respectively. The enzyme showed strong preference for NAD+ and displayed no detectable activity with NADP+. Homology modeling and sequence analysis of EaRDH, along with its biochemical properties, confirmed that EaRDH belongs to the family of NAD+-dependent ribitol dehydrogenases, a member of short-chain dehydrogenase/reductase (SCOR) family. EaRDH showed the highest activity and unique substrate specificity among all known RDHs. Homology modeling and docking analysis shed light on the molecular basis of its unusually high activity and substrate specificity.

KW - Enterobacter aerogenes

KW - Homology modeling

KW - Ribitol dehydrogenase

KW - Short-chain dehydrogenase/reductase

U2 - 10.1016/j.enzmictec.2015.02.004

DO - 10.1016/j.enzmictec.2015.02.004

M3 - Journal article

C2 - 25837508

AN - SCOPUS:84924869389

VL - 72

SP - 56

EP - 64

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

SN - 0141-0229

ER -

ID: 229901023