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Literature summary for 1.6.3.5 extracted from

  • Milani, M.; Ciriello, F.; Baroni, S.; Pandini, V.; Canevari, G.; Bolognesi, M.; Aliverti, A.
    FAD-binding site and NADP reactivity in human renalase: a new enzyme involved in blood pressure regulation (2011), J. Mol. Biol., 411, 463-473.
    View publication on PubMed

Crystallization (Commentary)

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

Organism UniProt Comment Textmining
Homo sapiens Q5VYX0
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Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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 ?
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Cofactor

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