Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities. - Wikidata - wikimedia - TriplyDB

Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities.

Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities.

http://www.wikidata.org/entity/Q37332296

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An Open and Shut Case: The Interaction of Magnesium with MST Enzymes Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism.Nonribosomal peptide synthetase biosynthetic clusters of ESKAPE pathogens.

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Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities.

http://www.wikidata.org/entity/Q37332296

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article científic

@ca

article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 19 September 2013

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Redesign of MST enzymes to tar ...... se and dehydratase activities.

@en

Redesign of MST enzymes to tar ...... se and dehydratase activities.

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type

label

Redesign of MST enzymes to tar ...... se and dehydratase activities.

@en

Redesign of MST enzymes to tar ...... se and dehydratase activities.

@nl

prefLabel

Redesign of MST enzymes to tar ...... se and dehydratase activities.

@en

Redesign of MST enzymes to tar ...... se and dehydratase activities.

@nl

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J.ABB.2013.09.007

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Archives of Biochemistry and Biophysics

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Redesign of MST enzymes to tar ...... ase and dehydratase activities

@en

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Kathleen M Meneely

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Qianyi Luo

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P2860

Altering the reaction specificity of eukaryotic ornithine decarboxylase

Mimicking natural evolution in vitro: An N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity

Lysine 190 is the catalytic base in MenF, the menaquinone-specific isochorismate synthase from Escherichia coli: implications for an enzyme family

Structure and mechanism of MbtI, the salicylate synthase from Mycobacterium tuberculosis

Structure of isochorismate synthase in complex with magnesium

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scholarly article

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10.1016/J.ABB.2013.09.007

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