METAP1D Human
Description
Biological Functions
METAP1D catalyzes the removal of initiator methionine from nascent mitochondrial proteins, requiring prior deformylation by peptide deformylase (PDF) . Key functional insights include:
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Substrate specificity: Lower efficiency for Met-Ala-Ser peptides compared to cytosolic isoforms
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Mitochondrial localization: Mediated by an N-terminal targeting signal (residues 1–43)
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Evolutionary origin: Likely ancestral to cytosolic MetAP1 via gene duplication
Clinical and Genetic Relevance
Recent Mendelian randomization studies implicate METAP1D in cerebrovascular and neurodegenerative diseases:
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Stroke and dementia: Genetically elevated METAP1D levels associate with:
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Cancer associations:
Interaction Network
STRING-DB analysis identifies functional partners involved in mitochondrial metabolism :
| Interacting Protein | Function | Association Score |
|---|---|---|
| FDX1 | Electron transport for steroidogenesis | 0.719 |
| ETFB | Fatty acid oxidation | 0.888 |
| PDF (Peptide deformylase) | N-terminal methionine processing | 0.664 |
| TUFM | Mitochondrial translation | 0.651 |
Regulatory Dynamics
Gene expression studies reveal METAP1D modulation by:
Product Specs
Product Science Overview
MAP1D is localized in the mitochondria and plays a crucial role in the N-terminal methionine excision pathway . This pathway involves the removal of the N-terminal methionine from many proteins, facilitating subsequent protein modifications . The enzyme requires the deformylation of the N(alpha)-formylated initiator methionine before it can hydrolyze the methionine .
The activity of MAP1D is essential for cell growth and viability . It has been observed that MAP1D is over-expressed in colon cancer cell lines and colon tumors, suggesting a potential role in tumorigenesis . The enzyme’s ability to remove methionine from nascent proteins is critical for maintaining cellular homeostasis and function .
Recombinant Human Methionine Aminopeptidase 1D is produced using baculovirus expression systems in Spodoptera frugiperda (Sf 21) cells . The recombinant protein typically includes an N-terminal methionine and a C-terminal 10-His tag for purification purposes . The protein is supplied as a 0.2 μm filtered solution in Tris, NaCl, and Glycerol, and is shipped with polar packs to maintain stability .
