Human reference: https://www.uniprot.org/uniprotkb/Q9NXA8/entry
Primary source: PMID:22076378 Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase..
We found that Sirt5
is an efficient protein lysine desuccinylase and demalonylase in vitro. The
preference for succinyl and malonyl groups was explained by the presence of an
arginine residue (Arg(105)) and tyrosine residue (Tyr(102)) in the acyl pocket
of Sirt5.
The horse sequence comparison is in SIRT5-bioinformatics/RESULTS.md. Transfer is assessed for this exact accession; human biochemical evidence is not equine experimental validation.
A horse-specific Falcon/Edison investigation was requested because PMID:36361948 studies equine chondrocytes and reports SIRT5-expression changes. Edison rejected task creation with HTTP429; the configured Perplexity fallback returned HTTP401 insufficient quota. No horse provider report was generated. Expression-level evidence does not resolve the divergent F6S899 protein model or validate catalytic activity.