(Q48047984)

English

Molecular cloning, purification, and characterization of a novel polyMG-specific alginate lyase responsible for alginate MG block degradation in Stenotrophomas maltophilia KJ-2.

scientific article published on 18 July 2012

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scholarly article

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Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

Molecular cloning, purification, and characterization of a novel polyMG-specific alginate lyase responsible for alginate MG block degradation in Stenotrophomas maltophilia KJ-2. (English)

1 reference

Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

author name string

Su In Lee

1

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Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

Sung Hee Choi

2

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Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

Eun Yeol Lee

3

1 reference

Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

Hee Sook Kim

4

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PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

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publication date

18 July 2012

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Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

Applied Microbiology and Biotechnology

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Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

95

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Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

6

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Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

1643-1653

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Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

https://scigraph.springernature.com/pub.10.1007/s00253-012-4266-y

0 references

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1 reference

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The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics

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Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate

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Molecular identification of a polyM-specific alginate lyase from Pseudomonas sp. strain KS-408 for degradation of glycosidic linkages between two mannuronates or mannuronate and guluronate in alginate

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Cloning and characterization of alginate lyase from a marine bacterium Streptomyces sp. ALG-5.

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The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides unravels a calcium-dependent catalytic machinery

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A biosystem for alginate metabolism in Agrobacterium tumefaciens strain C58: molecular identification of Atu3025 as an exotype family PL-15 alginate lyase.

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Cloning and characterization of a novel oligoalginate lyase from a newly isolated bacterium Sphingomonas sp. MJ-3.

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21 January 2018

Structural and Mutational Characterization of the Catalytic A-module of the Mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii

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Heterologous expression of an alginate lyase from Streptomyces sp. ALG-5 in Escherichia coli and its use for preparation of the magnetic nanoparticle-immobilized enzymes.

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Biodiesel production--current state of the art and challenges

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An engineered microbial platform for direct biofuel production from brown macroalgae.

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The SUPERFAMILY database in 2007: families and functions

1 reference

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21 January 2018

ALGINATE LYASE: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications.

1 reference

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21 January 2018

Structure and function of a hypothetical Pseudomonas aeruginosa protein PA1167 classified into family PL-7: a novel alginate lyase with a beta-sandwich fold

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21 January 2018

Identifiers

10.1007/S00253-012-4266-Y

1 reference

Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

release_ykk544epa5d2xdbagbxhgb2nny

0 references

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

8 February 2018

http://europepmc.org/abstract/MED/22805784

ResearchGate publication ID

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