TYSND1 cleaves HSD17B4

Stable Identifier
Reaction [transition]
Homo sapiens
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The trypsin-like serine-type endopeptidase TYSND1 cleaves HSD17B4 (Peroxisomal multifunctional enzyme type 2, MFP-2) between amino acid residues 311 and 312, yielding HSD17B4(1-311) and HSD17B4(312-736) (Okumoto et al. 2011, also inferred from mouse homologs). HSD17B4(1-311) dehydrogenates 3-hydroxyacyl-CoA; HSD17B4(312-736) acts as an enoyl-CoA hydratase (Jiang et al. 1997, reviewed in Huyghe et al. 2006). (In vitro, HSD17B4(312-736) facilitates the transfer of 7-dehydrocholesterol and phosphatidylcholine between membranes.) The uncleaved protein (HSD17B4) also catalyzes these reactions.

Literature References
PubMed ID Title Journal Year
22002062 Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid β-oxidation in peroxisomal matrix

Kametani, Y, Okumoto, K, Fujiki, Y

J. Biol. Chem. 2011
9089413 Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein

Souri, M, Hashimoto, T, Jiang, LL, Miyazawa, S

J Biochem 1997
16766224 Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model

Baes, M, Van Veldhoven, PP, Huyghe, S, Mannaerts, GP

Biochim Biophys Acta 2006
Catalyst Activity

serine-type endopeptidase activity of TYSND1 [peroxisomal matrix]

Inferred From
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