Maob Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
Monoamine Oxidase B (MAOB) protein is a mitochondrial flavin adenine dinucleotide (FAD)-dependent enzyme that plays a critical role in dopamine catabolism, trace amine metabolism, and xenobiotic detoxification[1]. It is primarily expressed in the brain (substantia nigra, striatum, hippocampus) and peripheral tissues including platelets, liver, and intestines[2]. MAOB is a key therapeutic target for Parkinson's disease (PD) and has been implicated in Alzheimer's disease (AD), Huntington's disease (HD), and amyotrophic lateral sclerosis (ALS)[3].
| Monoamine Oxidase B (MAOB) | |
|---|---|
| Protein Name | Monoamine Oxidase B |
| Gene | MAOB |
| UniProt ID | P50395 |
| PDB ID(s) | 1S2E, 1S3B, 2V7Z, 6BW2 |
| Molecular Weight | 58.7 kDa |
| Subcellular Localization | Mitochondrial outer membrane |
| Protein Family | Monoamine oxidase family |
| Cofactor | FAD (covalently bound) |
| Expression | Brain, platelets, liver, intestines |
The MAOB protein consists of two main domains:
The substrate-binding pocket exhibits distinct specificity compared to MAOA:
| Feature | MAOB | MAOA |
|---|---|---|
| Substrate preference | Phenylethylamine | Serotonin |
| Inhibitor sensitivity | Selegiline, rasagiline | Clorgyline |
| Brain expression | Higher in substantia nigra | Higher in cortex |
| Km for dopamine | ~100 µM | ~50 µM |
MAOB catalyzes the oxidative deamination of amines with the following reactions[5]:
Primary substrates:
Reaction chemistry:
MAOB is a primary therapeutic target in PD[6]:
MAOB inhibitors (selegiline, rasagiline, safinamide) provide:
MAOB involvement in AD includes[7]:
| Drug | Approval | Indication | Daily Dose |
|---|---|---|---|
| Selegiline | 1989 | Early PD | 5-10 mg |
| Rasagiline | 2006 | Early/mid PD | 1 mg |
| Safinamide | 2015 | Mid/late PD | 50-100 mg |
The study of Maob Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
Binda C, et al. (2003). "Structure and mechanism of action of human monoamine oxidase B." Chem Biol Interact. 143-144:39-47. PMID:12604186. ↩︎
Saura J, et al. (1992). "Monoamine oxidases in human brain." J Neurochem. 58(2):699-706. PMID:1732422. ↩︎
Youdim MB, Bakhsh M. (2006). "Monoamine oxidase B inhibitors in Parkinson's disease." Neurobiology. 14(1):37-46. PMID:16457099. ↩︎
De Colibus L, et al. (2005). "Three-dimensional structure of human monoamine oxidase B (MAO-B) with selective reversible inhibitors." J Neural Transm. 112(6):791-800. PMID:15959536. ↩︎
Edmondson DE. (2014). "Monoamine oxidase: structure, function, and regulation." Neurobiology. 22(1):1-14. PMID:24793845. ↩︎
Youdim MB, Bakhsh M. (2006). "Monoamine oxidase B inhibitors in Parkinson's disease." Neurobiology. 14(1):37-46. PMID:16457099. ↩︎
Tong J, et al. (2011). "Elevated monoamine oxidase B activity in the superior frontal cortex in Alzheimer's disease." J Neural Transm. 118(4):549-557. PMID:20571842. ↩︎