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Metal active site elasticity linked to activation of homocysteine in methionine synthases

Metal active site elasticity linked to activation of homocysteine in methionine synthases

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_fao_agris_US201300868561

Metal active site elasticity linked to activation of homocysteine in methionine synthases

About this item

Full title

Metal active site elasticity linked to activation of homocysteine in methionine synthases

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2008-03, Vol.105 (9), p.3286-3291

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Enzymes possessing catalytic zinc centers perform a variety of fundamental processes in nature, including methyl transfer to thiols. Cobalamin-independent (MetE) and cobalamin-dependent (MetH) methionine synthases are two such enzyme families. Although they perform the same net reaction, transfer of a methyl group from methyltetrahydrofolate to hom...

Alternative Titles

Full title

Metal active site elasticity linked to activation of homocysteine in methionine synthases

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_fao_agris_US201300868561

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_fao_agris_US201300868561

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0709960105

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