Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Kittisak Thotsaporn"'
Autor:
Chatchaya Petchphayaprai, Chutimon Chotipan, Pitchayapa Sa-ngiampak, Kittisak Thotsaporn, Ruchanee Salingcarnboriboon Ampornaramveth
Publikováno v:
BDJ Open, Vol 9, Iss 1, Pp 1-5 (2023)
Abstract Objective Dental Unit Waterlines (DUWLs) are contaminated by various species of microorganisms. DUWLs should be disinfected appropriately to control microbial contamination. This study investigated the effectiveness of devices continuously r
Externí odkaz:
https://doaj.org/article/4af81c9fc51a403aa4f425b7d16f1393
Autor:
Soraya Pornsuwan, Somchart Maenpuen, Philaiwarong Kamutira, Pratchaya Watthaisong, Kittisak Thotsaporn, Chanakan Tongsook, Maneerat Juttulapa, Sarayut Nijvipakul, Pimchai Chaiyen
Publikováno v:
PLoS ONE, Vol 12, Iss 2, p e0171135 (2017)
3,4-dihydroxyphenylacetate (DHPA) dioxygenase (DHPAO) from Pseudomonas aeruginosa (PaDHPAO) was overexpressed in Escherichia coli and purified to homogeneity. As the enzyme lost activity over time, a protocol to reactivate and conserve PaDHPAO activi
Externí odkaz:
https://doaj.org/article/6dc49729a017410780d7ae3edf35cc65
Autor:
Kittisak Thotsaporn, Ruchanok Tinikul, Pimchai Chaiyen, Pirom Chenprakhon, Somchart Maenpuen, Jittima Phonbuppha, Pratchaya Watthaisong
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 134:353-366
p-Hydroxyphenylacetate (HPA) can be derived from the biodegradation of lignin or from man-made compounds. The pathway involved for HPA degradation has been characterized for several species, but little is known on the degradation of HPA in Acinetobac
The accumulation of chlorophenols (CPs) in the environment, due to their wide use as agrochemicals, has become a serious environmental problem. These organic halides can be degraded by aerobic microorganisms, where the initial steps of various biodeg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef1351cdac49d0a519443edb1de5c8ab
https://europepmc.org/articles/PMC5377798/
https://europepmc.org/articles/PMC5377798/
Autor:
Worrapoj Oonanant, Jirundon Yuvaniyama, David P. Ballou, Jisnuson Svasti, Thanawat Phongsak, Pimchai Chaiyen, Kittisak Thotsaporn, Jeerus Sucharitakul
Publikováno v:
Journal of Biological Chemistry. 287:26213-26222
p-Hydroxyphenylacetate (HPA) 3-hydroxylase from Acinetobacter baumannii consists of a reductase component (C(1)) and an oxygenase component (C(2)). C(1) catalyzes the reduction of FMN by NADH to provide FMNH(-) as a substrate for C(2). The rate of re
Publikováno v:
Journal of Biological Chemistry. 286:28170-28180
p-Hydroxyphenylacetate (HPA) 3-hydroxylase is a two-component flavin-dependent monooxygenase. Based on the crystal structure of the oxygenase component (C(2)), His-396 is 4.5 Å from the flavin C4a locus, whereas Ser-171 is 2.9 Å from the flavin N5
Autor:
Pimchai Chaiyen, Marco W. Fraaije, Willem J. H. van Berkel, Pirom Chenprakhon, J. Andrew McCammon, Riccardo Baron, Andrea Mattevi, Conor T. Riley, Federico Forneris, Andrea Alfieri, Remko T. Winter, Kittisak Thotsaporn
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 106(26), 10603-10608
Proceedings of the National Academy of Sciences of the United States of America 106 (2009) 26
Proceedings of the National Academy of Sciences of the United States of America, 106(26), 10603-10608. NATL ACAD SCIENCES
Proceedings of the National Academy of Sciences of the United States of America 106 (2009) 26
Proceedings of the National Academy of Sciences of the United States of America, 106(26), 10603-10608. NATL ACAD SCIENCES
Dioxygen (O 2 ) and other gas molecules have a fundamental role in a variety of enzymatic reactions. However, it is only poorly understood which O 2 uptake mechanism enzymes employ to promote efficient catalysis and how general this is. We investigat
Autor:
Pimchai Chaiyen, Soraya Pornsuwan, Pratchaya Watthaisong, Sarayut Nijvipakul, Maneerat Juttulapa, Chanakan Tongsook, Kittisak Thotsaporn, Philaiwarong Kamutira, Somchart Maenpuen
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 2, p e0171135 (2017)
PLoS ONE, Vol 12, Iss 2, p e0171135 (2017)
3,4-dihydroxyphenylacetate (DHPA) dioxygenase (DHPAO) from Pseudomonas aeruginosa (PaDHPAO) was overexpressed in Escherichia coli and purified to homogeneity. As the enzyme lost activity over time, a protocol to reactivate and conserve PaDHPAO activi
Autor:
Pirom Chenprakhon, Jeerus Sucharitakul, Duangthip Trisrivirat, Kittisak Thotsaporn, Pimchai Chaiyen
Publikováno v:
Biochemistry. 53(25)
The protonation status of the peroxide moiety in C4a-(hydro)peroxyflavin of p-hydroxyphenylacetate-3-hydroxylase can be directly monitored using transient kinetics. The pKa for the wild-type (WT) enzyme is 9.8 ± 0.2, while the values for the H396N,
Autor:
Wichit Thaveekarn, Ruchanok Tinikul, Sarawut Jitrapakdee, Kittisak Thotsaporn, Pimchai Chaiyen
Publikováno v:
Journal of biotechnology. 162(2-3)
Bacterial luciferase from Vibrio campbellii is a thermostable enzyme with an in vitro thermal inactivation half-life of ∼1020 min at 37 °C. The enzyme also binds tightly to reduced FMN. In this study, a V. campbellii fusion luciferase construct in