Fructose-Bisphosphate Aldolase
"Fructose-Bisphosphate Aldolase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
An enzyme of the lyase class that catalyzes the cleavage of fructose 1,6-biphosphate to form dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. (Enzyme Nomenclature, 1992) E.C. 4.1.2.13.
Descriptor ID |
D005634
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MeSH Number(s) |
D08.811.520.224.062.400
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Concept/Terms |
Fructose-Bisphosphate Aldolase- Fructose-Bisphosphate Aldolase
- Aldolase, Fructose-Bisphosphate
- Fructose Bisphosphate Aldolase
- Fructose 1,6-Bisphosphate Aldolase
- 1,6-Bisphosphate Aldolase, Fructose
- Aldolase, Fructose 1,6-Bisphosphate
- Fructose 1,6 Bisphosphate Aldolase
- Fructose Biphosphate Aldolase
- Aldolase, Fructose Biphosphate
- Fructosediphosphate Aldolase
- Aldolase, Fructosediphosphate
- Aldolase
- Fructose 1,6-Bisphosphate Aldolase, Class II
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Below are MeSH descriptors whose meaning is more general than "Fructose-Bisphosphate Aldolase".
Below are MeSH descriptors whose meaning is more specific than "Fructose-Bisphosphate Aldolase".
This graph shows the total number of publications written about "Fructose-Bisphosphate Aldolase" by people in this website by year, and whether "Fructose-Bisphosphate Aldolase" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2010 | 1 | 0 | 1 | 2014 | 1 | 0 | 1 | 2016 | 1 | 0 | 1 |
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Below are the most recent publications written about "Fructose-Bisphosphate Aldolase" by people in Profiles.
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Shams F, Oldfield NJ, Lai SK, Tunio SA, Wooldridge KG, Turner DP. Fructose-1,6-bisphosphate aldolase of Neisseria meningitidis binds human plasminogen via its C-terminal lysine residue. Microbiologyopen. 2016 Apr; 5(2):340-50.
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Shams F, Oldfield NJ, Wooldridge KG, Turner DP. Fructose-1,6-bisphosphate aldolase (FBA)-a conserved glycolytic enzyme with virulence functions in bacteria: 'ill met by moonlight'. Biochem Soc Trans. 2014 Dec; 42(6):1792-5.
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Schmidt J, Ehasz C, Epperson M, Klas K, Wyatt J, Hennig M, Forconi M. The effect of the hydrophobic environment on the retro-aldol reaction: comparison to a computationally-designed enzyme. Org Biomol Chem. 2013 Dec 28; 11(48):8419-25.
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Tunio SA, Oldfield NJ, Berry A, Ala'Aldeen DA, Wooldridge KG, Turner DP. The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: surface localization and role in host cell adhesion. Mol Microbiol. 2010 May; 76(3):605-15.
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Jones CW, Priest DG. Serine transhydroxymethylase: mechanism of aldolase activation by folate. Arch Biochem Biophys. 1976 May; 174(1):305-11.
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