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- Table of Contents
Facts about Acyl-coenzyme A thioesterase 8.
Shows a preference for medium-length fatty acyl-CoAs (C2 to C20) (PubMed:9299485, PubMed:9153233). Inactive towards substrates with more than C20 aliphatic chains (PubMed:9153233).
Human | |
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Gene Name: | ACOT8 |
Uniprot: | O14734 |
Entrez: | 10005 |
Belongs to: |
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C/M/P thioester hydrolase family |
ACTEIII; acyl-CoA thioesterase 8HNAACTE; Choloyl-coenzyme A thioesterase; EC 3.1.2.27; hACTEIII; HIV-Nef-associated acyl-CoA thioesterase; hTEcholoyl-CoA hydrolase; long-chain fatty-acyl-CoA hydrolase; palmitoyl-CoA hydrolase; peroxisomal acyl-CoA thioesterase 1; peroxisomal acyl-CoA thioesterase; Peroxisomal acyl-coenzyme A thioester hydrolase 1; Peroxisomal long-chain acyl-CoA thioesterase 1; PTE-1; PTE1HIV-Nef associated acyl-CoA thioesterase; PTE2; PTE-2hACTE-IIIacyl-coenzyme A thioesterase 8; Thioesterase II; thioesterase III
Mass (kDA):
35.914 kDA
Human | |
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Location: | 20q13.12 |
Sequence: | 20; NC_000020.11 (45841721..45857405, complement) |
Detected in a T-cell line (at protein level). Ubiquitous (PubMed:9153233, PubMed:9299485).
Peroxisome matrix. Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded.
PMID: 9299485 by Watanabe H., et al. A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef.
PMID: 9153233 by Liu L.X., et al. Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation.