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Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase

Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_901000782

Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase

About this item

Full title

Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2011-10, Vol.478 (7370), p.538-541

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

One active site, two activities
The archaeal enzyme fructose 1,6-bisphosphate (FBP) aldolase/phosphatase catalyses two successive reactions in gluconeogenesis: an aldol condensation of dihydroxyacetone phosphate and glyceraldehyde-3-phosphate to form FBP, and its subsequent hydrolysis to fructose-6-phosphate. Two groups present a series of struc...

Alternative Titles

Full title

Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_901000782

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_901000782

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/nature10457

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