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PMID:29456767
| Citation |
Bulku, A, Weaver, TM and Berkmen, MB (2018) Biochemical Characterization of Two Clinically-Relevant Human Fumarase Variants Defective for Oligomerization. Open Biochem J 12:1-15 |
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| Abstract |
Fumarase, a significant enzyme of energy metabolism, catalyzes the reversible hydration of fumarate to L-malate. Mutations in the gene, encoding human fumarase, are associated with fumarate hydratase deficiency (FHD) and hereditary leiomyomatosis and renal cell cancer (HLRCC). Fumarase assembles into a homotetramer, with four active sites. Interestingly, residues from three of the four subunits within the homotetramer comprise each active site. Hence, any mutation affecting oligomerization is predicted to disrupt enzyme activity. |
| Links |
PubMed PMC5806193 Online version:10.2174/1874091X01812010001 |
| Keywords |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004333: fumarate hydratase activity |
ECO:0000315: |
F |
Figure 5 shows the HsFH mutants, A308T and H318Y, decrease in enzyme function. |
complete | ||||
Notes
See also
References
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