Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

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[FeFe]-hydrogenase maturation: insights into the role HydE plays in dithiomethylamine biosynthesis.

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Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

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http://www.wikidata.org/entity/Q43500181

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2013 nî lūn-bûn

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2013年の論文

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年學術文章

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2013年學術文章

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name

Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

@en

Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

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type

Item

label

Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

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Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

@nl

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Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

@en

Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

@nl

P1476

Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

@en

P2093

Huihui Zhang

http://www.w3.org/2001/XMLSchema#string

Junling Zhang

http://www.w3.org/2001/XMLSchema#string

Lianghua Tang

http://www.w3.org/2001/XMLSchema#string

Ling Zhu

http://www.w3.org/2001/XMLSchema#string

Liying Chi

http://www.w3.org/2001/XMLSchema#string

Min Su

http://www.w3.org/2001/XMLSchema#string

P2860

Rational design of enantioselective enzymes requires considerations of entropy

Addressing the numbers problem in directed evolution.

Improvement of Yarrowia lipolytica lipase enantioselectivity by using mutagenesis targeted to the substrate binding site.

Dynamic kinetic resolutions and asymmetric transformations by enzymes coupled with metal catalysis.

Enantiomeric separation and determination of absolute stereochemistry of asymmetric molecules in drug discovery: building chiral technology toolboxes.

Substrate entropy in enzyme enantioselectivity: an experimental and molecular modeling study of a lipase.

Rationally engineered double substituted variants of Yarrowia lipolytica lipase with enhanced activity coupled with highly inverted enantioselectivity towards 2-bromo phenyl acetic acid esters.

Purification and application of a lipase from Penicillium expansum PED-03.

Highly enantioselective dynamic kinetic resolution of 1,2-diarylethanols by a lipase-ruthenium couple.

Cloning, expression, characterization and role of the leader sequence of a lipase from Rhizopus oryzae

P2888

s10529-013-1405-1

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633-639

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scholarly article

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10.1007/S10529-013-1405-1

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2013-12-11T00:00:00Z

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P921

enantioselectivity

Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

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Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase.

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P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P698

P921