Mitochondrial trifunctional protein (MTP) is a
protein attached to the
inner mitochondrial membrane which
catalyzes three out of the four steps in
beta oxidation. MTP is a hetero-octamer composed of four alpha and four beta subunits:
Fatty acid beta-oxidation (FAO) and
oxidative phosphorylation (OXPHOS) are two major metabolic pathways in the
mitochondria. Reducing equivalents from FAO enter OXPHOS at the level of
complexes I and
III. In 2010, Wang et al. discovered a functional and physical association between MTP and ETC
respirasomes. Not only does MTP appear to be bound to Complex I, but it also appears to
channel substrates between the two enzymes.[2] This is especially interesting, because up until then it was unknown exactly how MTP was associated with the inner mitochondrial membrane, and this discovery may provide the explanation.
In 2009, Taylor et al. identified a human mitochondrial protein,
monolysocardiolipin acyltransferase (MLCL AT-1), that is identical in
amino acid sequence to the 59-kDa
C-terminal end of MTP, linking MTP to the remodeling of
cardiolipin from
monolysocardiolipin.[5] Although MLCL AT-1 and MTP are different proteins, in 2012 the same lab discovered that MTP did indeed have cardiolipin remodeling capabilities.[6] This suggests a possible link between mitochondrial membrane cardiolipin content and
beta oxidation.