Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person Mitochondrial 3-hydroxyisobutyrate dehydrogenase (HIBADH) ca...
| Class:Id | Summation:508467 |
|---|---|
| _displayName | Mitochondrial 3-hydroxyisobutyrate dehydrogenase (HIBADH) ca... |
| _timestamp | 2010-02-12 15:25:59 |
| created | [InstanceEdit:508464] D'Eustachio, P, 2010-02-12 |
| modified | [InstanceEdit:508479] D'Eustachio, P, 2010-02-12 |
| text | Mitochondrial 3-hydroxyisobutyrate dehydrogenase (HIBADH) catalyzes the reversible reaction of methylmalonyl semialdehyde and NADH + H+ to form beta-hydroxyisobutyrate and NAD+. The biochemical properties of human HIBADH are inferred from those of its better-studied porcine homologue (Robinson and Coon 1957). Unpublished crystallographic studies (PDB 2GF2) have shown the active enzyme to be a tetramer of HIBADH polypeptides whose aminoterminal 40 residues, a mitochondrial targeting sequence, have been removed. |
| (summation) | [Reaction:508473] methylmalonyl semialdehyde + NADH + H+ <=> beta-hydroxyisobutyrate + NAD+ [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by Mitochondrial 3-hydroxyisobutyrate dehydrogenase (HIBADH) ca... (508467)
