Alginate lyases from alginate-degrading Vibrio splendidus 12B01 are endolytic.

Szczegóły
Abstrakt

Tytuł:: Alginate lyases from alginate-degrading Vibrio splendidus 12B01 are endolytic.
Autorzy:: Badur AH; Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Jagtap SS; Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA Department of Chemical Engineering, Konkuk University, Seoul, Republic of Korea.
Yalamanchili G; Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Lee JK; Department of Chemical Engineering, Konkuk University, Seoul, Republic of Korea.
Zhao H; Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Rao CV; Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA .
Źródło:: Applied and environmental microbiology [Appl Environ Microbiol] 2015 Mar; Vol. 81 (5), pp. 1865-73. Date of Electronic Publication: 2015 Jan 02.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
Język:: English
Imprint Name(s):: Original Publication: Washington, American Society for Microbiology.
MeSH Terms:: Alginates/*metabolism
Lyases/*metabolism
Vibrio/*enzymology
Glucuronic Acid/metabolism ; Hexuronic Acids/metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Lyases/isolation & purification ; Models, Molecular ; Protein Conformation ; Temperature
References:: Can J Microbiol. 2011 Dec;57(12):1032-41. (PMID: 22145710)
Mar Biotechnol (NY). 2009 Jan-Feb;11(1):10-6. (PMID: 18553118)
Appl Environ Microbiol. 2005 Jan;71(1):98-104. (PMID: 15640176)
J Protein Chem. 1998 Jan;17(1):29-36. (PMID: 9491925)
J Biol Chem. 2014 Mar 21;289(12):8645-55. (PMID: 24478312)
Appl Environ Microbiol. 2014 Jul;80(14):4207-14. (PMID: 24795372)
J Biol Chem. 2013 Aug 9;288(32):23021-37. (PMID: 23782694)
Curr Biol. 2009 Jan 27;19(2):169-75. (PMID: 19167225)
J Biosci Bioeng. 2000;89(2):199-202. (PMID: 16232727)
Nat Methods. 2011;8(10):785-6. (PMID: 21959131)
Biotechnol Lett. 2013 May;35(5):703-8. (PMID: 23299986)
J Biol Chem. 2009 Dec 4;284(49):34019-27. (PMID: 19801541)
FEMS Microbiol Lett. 1993 Jun 1;110(1):101-6. (PMID: 8319887)
Biochim Biophys Acta. 1979 Aug 15;569(2):259-66. (PMID: 476128)
J Biol Chem. 1962 Feb;237:309-16. (PMID: 14488584)
Nucleic Acids Res. 2014 Jul;42(Web Server issue):W252-8. (PMID: 24782522)
Can J Microbiol. 2009 Sep;55(9):1113-8. (PMID: 19898554)
J Biol Chem. 2004 Jul 23;279(30):31863-72. (PMID: 15136569)
Biomacromolecules. 2006 Jul;7(7):2108-21. (PMID: 16827577)
Biochem J. 2010 Dec 15;432(3):437-44. (PMID: 20925655)
Carbohydr Res. 1997 Oct 28;304(1):69-76. (PMID: 9403996)
J Biol Chem. 2006 Dec 8;281(49):37748-57. (PMID: 16990278)
Glycobiology. 2010 Dec;20(12):1547-73. (PMID: 20805221)
Annu Rev Microbiol. 2000;54:289-340. (PMID: 11018131)
J Bacteriol. 1998 Aug;180(15):3779-84. (PMID: 9683471)
J Mol Biol. 2005 Sep 9;352(1):11-21. (PMID: 16081095)
Nature. 2014 Jan 9;505(7482):239-43. (PMID: 24291791)
Curr Opin Chem Biol. 2006 Apr;10(2):147-55. (PMID: 16495121)
Carbohydr Res. 2012 May 1;352:44-50. (PMID: 22429771)
Appl Environ Microbiol. 2005 Sep;71(9):5107-15. (PMID: 16151093)
Carbohydr Res. 1996 Aug 19;289:11-23. (PMID: 8805773)
J Mol Graph. 1996 Feb;14(1):33-8, 27-8. (PMID: 8744570)
Methods Mol Biol. 2000;132:365-86. (PMID: 10547847)
Biochim Biophys Acta. 1957 May;24(2):439. (PMID: 13436456)
Appl Environ Microbiol. 1992 Aug;58(8):2474-8. (PMID: 1514793)
J Biol Chem. 1959 Apr;234(4):705-9. (PMID: 13654246)
Bioresour Technol. 2011 Jan;102(1):10-6. (PMID: 20615690)
Science. 2012 Jan 20;335(6066):308-13. (PMID: 22267807)
Curr Microbiol. 2006 Aug;53(2):135-40. (PMID: 16802207)
J Am Chem Soc. 2004 Jul 14;126(27):8354-5. (PMID: 15237973)
Carbohydr Res. 2004 Jun 1;339(8):1475-81. (PMID: 15178390)
Mar Biotechnol (NY). 2006 Sep-Oct;8(5):481-90. (PMID: 16810458)
Biochim Biophys Acta. 2011 Dec;1814(12):1739-47. (PMID: 21945375)
Environ Microbiol. 2009 Aug;11(8):1959-70. (PMID: 19364337)
PLoS One. 2012;7(12):e50689. (PMID: 23226535)
Substance Nomenclature:: 0 (Alginates)
0 (Hexuronic Acids)
8A5D83Q4RW (Glucuronic Acid)
EC 4.- (Lyases)
Entry Date(s):: Date Created: 20150104 Date Completed: 20151027 Latest Revision: 20181202
Update Code:: 20240104
PubMed Central ID:: PMC4325137
DOI:: 10.1128/AEM.03460-14
PMID:: 25556193
: Czasopismo naukowe

Alginate lyases are enzymes that degrade alginate through β-elimination of the glycosidic bond into smaller oligomers. We investigated the alginate lyases from Vibrio splendidus 12B01, a marine bacterioplankton species that can grow on alginate as its sole carbon source. We identified, purified, and characterized four polysaccharide lyase family 7 alginates lyases, AlyA, AlyB, AlyD, and AlyE, from V. splendidus 12B01. The four lyases were found to have optimal activity between pH 7.5 and 8.5 and at 20 to 25°C, consistent with their use in a marine environment. AlyA, AlyB, AlyD, and AlyE were found to exhibit a turnover number (kcat) for alginate of 0.60 ± 0.02 s(-1), 3.7 ± 0.3 s(-1), 4.5 ± 0.5 s(-1), and 7.1 ± 0.2 s(-1), respectively. The Km values of AlyA, AlyB, AlyD, and AlyE toward alginate were 36 ± 7 μM, 22 ± 5 μM, 60 ± 2 μM, and 123 ± 6 μM, respectively. AlyA and AlyB were found principally to cleave the β-1,4 bonds between β-d-mannuronate and α-l-guluronate and subunits; AlyD and AlyE were found to principally cleave the α-1,4 bonds involving α-l-guluronate subunits. The four alginate lyases degrade alginate into longer chains of oligomers.
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