ILVBL
ILVBL, also known as HACL2 or 2-hydroxyacyl-CoA lyase 2, is an endoplasmic reticulum enzyme that removes a single carbon from 2-hydroxy acyl-CoA substrates during fatty acid alpha-oxidation. It depends on thiamine pyrophosphate and is also called ilvB-like, AHAS, ILV2H or HACL1L. Browse Assay Genie's current range of ILVBL research reagents below, or read on for the biology behind the target.
ILVBL is an endoplasmic reticulum 2-hydroxy acyl-CoA lyase. It carries out the cleavage reaction, the removal of one carbon (C1) from the substrate, that forms part of fatty acid alpha-oxidation. The reaction is thiamine pyrophosphate (TPP)-dependent, which places the enzyme in the TPP enzyme family. ILVBL is also involved in the phytosphingosine degradation pathway.
The ILVBL gene encodes a protein that is classed by HGNC as a flavoprotein within the 2-hydroxyacyl-CoA lyase family, with the approved symbol HACL2 and the full name 2-hydroxyacyl-CoA lyase 2. Researchers studying this target may look for an ILVBL antibody, an ILVBL ELISA kit or recombinant ILVBL protein to examine its expression and activity in the endoplasmic reticulum membrane. The mouse ortholog is Hacl2.
The name ILVBL comes from the original description of the gene as ilvB (bacterial acetolactate synthase)-like. According to the NCBI Gene summary, the encoded protein resembles several thiamine pyrophosphate-binding proteins from bacteria, yeast and plants. The closest similarity is to bacterial acetolactate synthases (AHAS), which catalyse the first step of branched-chain amino acid biosynthesis. This explains aliases such as AHAS and ILV2H. The functional annotation for the human protein, however, concerns 2-hydroxy acyl-CoA cleavage in fatty acid metabolism. Other aliases include 209L8, MGC1269, FLJ39061 and MGC19535.
ILVBL catalyses the C1-removal cleavage of 2-hydroxy acyl-CoA in fatty acid alpha-oxidation, so it is a useful enzyme for studying this pathway.
ILVBL is involved in phytosphingosine degradation, which makes it relevant to research on how sphingoid bases are broken down.
As a member of the TPP enzyme family, ILVBL offers a model for studying thiamine pyrophosphate-dependent lyase reactions.
ILVBL is an endoplasmic reticulum membrane enzyme, which links it to studies of lipid-processing activities at this organelle.
ILVBL is an endoplasmic reticulum 2-hydroxy acyl-CoA lyase. It performs the cleavage reaction that removes one carbon (C1) in fatty acid alpha-oxidation, and it requires thiamine pyrophosphate. It is also involved in the phytosphingosine degradation pathway.
The gene was first named ilvB (bacterial acetolactate synthase)-like because of its similarity to bacterial acetolactate synthases. HGNC now uses HACL2 (2-hydroxyacyl-CoA lyase 2). Other aliases include AHAS, ILV2H, HACL1L, 209L8, MGC1269, FLJ39061 and MGC19535.
The NCBI summary reports similarity to thiamine pyrophosphate-binding proteins from bacteria, yeast and plants, and the closest match is bacterial acetolactate synthase. Mouse has an ortholog, Hacl2. Check the datasheet of any product for its validated reactivity.
Other 2-hydroxyacyl-CoA lyases, fatty acid alpha-oxidation enzymes and TPP-dependent proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt A1L0T0; product specifications from Assay Genie datasheets.