Crystallization (Comment) | Organism |
---|---|
to 2.5 A resolution. Renalase adopts the p-hydroxybenzoate hydroxylase fold topology, comprising a Rossmann-fold-based flavin adenine dinucleotide-binding domain and a putative substrate-binding domain, the latter of which contains a five-stranded anti-parallel beta-sheet. A large cavity, facing the flavin ring, presumably represents the active site. The renalase active site is fully solvent exposed and lacks an aromatic cage for binding the substrate amino group | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q5VYX0 | - |
- |
Source Tissue | Comment | Organism | Textmining |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | renalase has an extremely low diaphorase activity, displaying lower kcat but higher kcat/Km for NADH compared to NADPH | Homo sapiens | ? | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | the FAD prosthetic group becomes slowly reduced when the enzyme is incubated with NADPH under anaerobiosis | Homo sapiens | |
additional information | a recognizable NADP-binding site is absent in the protein structure, enzyme shows poor affinity for, and poor reactivity towards, NADH and NADPH with Kd values of ca 2 mM | Homo sapiens |