Comparative analysis of two types of methanol dehydrogenase from Methylophaga aminisulfidivorans MP T grown on methanol
Abstract Two types of methanol dehydrogenase (MDH) were obtained from a novel marine methylotrophic bacterium, Methylophaga aminisulfidivorans MP T , grown on methanol. Type I MDH consisted of two identical dimers of α (65.98 kDa) and β (7.58 kDa) subunits organized to form the α 2 β 2 tetramer. Typ...
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Published in | Journal of basic microbiology Vol. 52; no. 2; pp. 141 - 149 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
01.04.2012
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Abstract | Abstract
Two types of methanol dehydrogenase (MDH) were obtained from a novel marine methylotrophic bacterium,
Methylophaga aminisulfidivorans
MP
T
, grown on methanol. Type I MDH consisted of two identical dimers of α (65.98 kDa) and β (7.58 kDa) subunits organized to form the α
2
β
2
tetramer. Type II MDH contained an additional MxaJ protein (27.86 kDa) and had more specific activity than type I MDH. The
K
m
values of type I and II MDH for methanol under cytochrome
c
L
reduction assay system were estimated to be 50.3 and 13.0 μM, respectively, and the isoelectric points of type I and II MDH were determined to be 5.4 and 5.8, respectively. The average molar ratios of α:β, α:MxaJ, and β:MxaJ in type II MDH were approximately 1:0.99, 1:0.41 and 1:0.42, respectively. Based on these results, the original conformation of the MDH of
M. aminisulfidivorans
MP
T
is most likely the α
2
β
2
‐MxaJ complex. During purification, the lysozyme and freeze‐thawing cell disruption method significantly increased the amount of type II MDH in the soluble fraction compared with strong physical disruption methods such as sonication and French Press. (© 2011 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim) |
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AbstractList | Abstract
Two types of methanol dehydrogenase (MDH) were obtained from a novel marine methylotrophic bacterium,
Methylophaga aminisulfidivorans
MP
T
, grown on methanol. Type I MDH consisted of two identical dimers of α (65.98 kDa) and β (7.58 kDa) subunits organized to form the α
2
β
2
tetramer. Type II MDH contained an additional MxaJ protein (27.86 kDa) and had more specific activity than type I MDH. The
K
m
values of type I and II MDH for methanol under cytochrome
c
L
reduction assay system were estimated to be 50.3 and 13.0 μM, respectively, and the isoelectric points of type I and II MDH were determined to be 5.4 and 5.8, respectively. The average molar ratios of α:β, α:MxaJ, and β:MxaJ in type II MDH were approximately 1:0.99, 1:0.41 and 1:0.42, respectively. Based on these results, the original conformation of the MDH of
M. aminisulfidivorans
MP
T
is most likely the α
2
β
2
‐MxaJ complex. During purification, the lysozyme and freeze‐thawing cell disruption method significantly increased the amount of type II MDH in the soluble fraction compared with strong physical disruption methods such as sonication and French Press. (© 2011 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim) |
Author | Han, Gui Hwan Kim, Dockyu Kim, Si Wouk Kim, Hee Gon Choi, Jong‐Soon |
Author_xml | – sequence: 1 givenname: Hee Gon surname: Kim fullname: Kim, Hee Gon – sequence: 2 givenname: Gui Hwan surname: Han fullname: Han, Gui Hwan – sequence: 3 givenname: Dockyu surname: Kim fullname: Kim, Dockyu – sequence: 4 givenname: Jong‐Soon surname: Choi fullname: Choi, Jong‐Soon – sequence: 5 givenname: Si Wouk surname: Kim fullname: Kim, Si Wouk |
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Cites_doi | 10.1099/mic.0.26105-0 10.1042/bj2600857 10.1021/bi00072a012 10.1093/oxfordjournals.jbchem.a123829 10.1099/mic.0.28243-0 10.1128/AEM.63.8.3218-3224.1997 10.1002/pmic.200300713 10.1021/bi051877j 10.1016/0003-2697(91)90094-A 10.1111/j.1464-410X.2007.07202.x 10.1016/0003-2697(76)90527-3 10.1042/bj1990245 10.1016/S0065-2911(08)60305-7 10.1111/j.1574-6968.1997.tb10167.x 10.1042/bj2870709 10.1128/jb.173.21.6962-6970.1991 10.1016/j.jmb.2004.05.028 10.1016/0005-2744(78)90164-X 10.1016/0385-6380(87)90132-4 10.1002/(SICI)1521-4028(199807)38:3<189::AID-JOBM189>3.0.CO;2-S 10.1111/j.1432-1033.1987.tb11014.x 10.1099/ijs.0.65139-0 10.1128/jb.169.9.3969-3975.1987 |
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References | Koh M.J. (e_1_2_1_19_2) 2002; 12 Matsushita K. (e_1_2_1_28_2) 1992; 111 Ghosh R. (e_1_2_1_8_2) 1981; 199 e_1_2_1_22_2 e_1_2_1_23_2 e_1_2_1_21_2 e_1_2_1_26_2 e_1_2_1_27_2 e_1_2_1_24_2 e_1_2_1_25_2 Kim H.G. (e_1_2_1_17_2) 2005; 43 e_1_2_1_6_2 e_1_2_1_7_2 e_1_2_1_4_2 e_1_2_1_5_2 e_1_2_1_2_2 e_1_2_1_11_2 e_1_2_1_3_2 e_1_2_1_12_2 Anthony C. (e_1_2_1_20_2) 1967; 104 e_1_2_1_10_2 e_1_2_1_15_2 e_1_2_1_16_2 e_1_2_1_13_2 e_1_2_1_14_2 e_1_2_1_9_2 e_1_2_1_18_2 |
References_xml | – ident: e_1_2_1_6_2 doi: 10.1099/mic.0.26105-0 – ident: e_1_2_1_5_2 doi: 10.1042/bj2600857 – ident: e_1_2_1_15_2 doi: 10.1021/bi00072a012 – volume: 111 start-page: 739 year: 1992 ident: e_1_2_1_28_2 article-title: Methanol and ethanol oxidase respiratory chains of the methylotrophic acetic acid bacterium, Acetobacter methanolicus publication-title: J. Biochem. doi: 10.1093/oxfordjournals.jbchem.a123829 contributor: fullname: Matsushita K. – ident: e_1_2_1_7_2 doi: 10.1099/mic.0.28243-0 – ident: e_1_2_1_24_2 doi: 10.1128/AEM.63.8.3218-3224.1997 – ident: e_1_2_1_16_2 doi: 10.1002/pmic.200300713 – volume: 104 start-page: 614 year: 1967 ident: e_1_2_1_20_2 article-title: The microbial oxidation of methanol. Purification and properties of methanol dehydrogenase of Pseudomonas sp. M27 publication-title: Biochem. J. contributor: fullname: Anthony C. – ident: e_1_2_1_21_2 doi: 10.1021/bi051877j – ident: e_1_2_1_26_2 doi: 10.1016/0003-2697(91)90094-A – ident: e_1_2_1_23_2 doi: 10.1111/j.1464-410X.2007.07202.x – ident: e_1_2_1_22_2 doi: 10.1016/0003-2697(76)90527-3 – volume: 199 start-page: 245 year: 1981 ident: e_1_2_1_8_2 article-title: Purification and properties of the methanol dehydrogenase from Methylophilus methylotrophus publication-title: Biochem. J. doi: 10.1042/bj1990245 contributor: fullname: Ghosh R. – ident: e_1_2_1_2_2 doi: 10.1016/S0065-2911(08)60305-7 – ident: e_1_2_1_27_2 doi: 10.1111/j.1574-6968.1997.tb10167.x – ident: e_1_2_1_13_2 doi: 10.1042/bj2870709 – volume: 43 start-page: 499 year: 2005 ident: e_1_2_1_17_2 article-title: Characterization of Methylophaga sp. strain SK1 cytochrome cL expressed in Escherichia coli publication-title: J. Microbiol. contributor: fullname: Kim H.G. – ident: e_1_2_1_14_2 doi: 10.1128/jb.173.21.6962-6970.1991 – volume: 12 start-page: 476 year: 2002 ident: e_1_2_1_19_2 article-title: Properties of electron carriers in the process of methanol oxidation in a new restricted facultative marine methylotrophic bacterium, Methylophaga sp. MP publication-title: J. Microbiol. Biotechnol. contributor: fullname: Koh M.J. – ident: e_1_2_1_25_2 doi: 10.1016/j.jmb.2004.05.028 – ident: e_1_2_1_10_2 doi: 10.1016/0005-2744(78)90164-X – ident: e_1_2_1_3_2 doi: 10.1016/0385-6380(87)90132-4 – ident: e_1_2_1_12_2 doi: 10.1002/(SICI)1521-4028(199807)38:3<189::AID-JOBM189>3.0.CO;2-S – ident: e_1_2_1_11_2 doi: 10.1111/j.1432-1033.1987.tb11014.x – ident: e_1_2_1_18_2 doi: 10.1099/ijs.0.65139-0 – ident: e_1_2_1_9_2 doi: 10.1128/jb.169.9.3969-3975.1987 – ident: e_1_2_1_4_2 |
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Snippet | Abstract
Two types of methanol dehydrogenase (MDH) were obtained from a novel marine methylotrophic bacterium,
Methylophaga aminisulfidivorans
MP
T
, grown on... |
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Title | Comparative analysis of two types of methanol dehydrogenase from Methylophaga aminisulfidivorans MP T grown on methanol |
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