| Structural highlights
2vz2 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | 2c67, 1oja, 2v5z, 1s3e, 2c73, 1ojb, 2v60, 2byb, 2vrm, 2c65, 2c64, 1oj9, 1ojd, 1s3b, 2c66, 2bk4, 2bk5, 2c70, 1h8r, 2c75, 2bk3, 2v61, 2c72, 1s2y, 1gos, 1s2q, 2c76, 2vrl, 1ojc |
| Activity: | Monoamine oxidase, with EC number 1.4.3.4 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[AOFB_HUMAN] Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mechanistic and structural studies have been carried out to investigate the molecular basis for the irreversible inhibition of human MAO-B by mofegiline. Competitive inhibition with substrate shows an apparent K(i) of 28 nM. Irreversible inhibition of MAO-B occurs with a 1:1 molar stoichiometry with no observable catalytic turnover. The absorption spectral properties of mofegiline inhibited MAO-B show features (lambda(max) approximately 450 nm) unlike those of traditional flavin N(5) or C(4a) adducts. Visible and near-UV circular dichroism spectra of the mofegiline-MAO-B adduct shows a negative peak at 340 nm with an intensity similar to that of N(5) flavocyanine adducts. The X-ray crystal structure of the mofegiline-MAO-B adduct shows a covalent bond between the flavin cofactor N(5) with the distal allylamine carbon atom as well as the absence of the fluorine atom. A mechanism to explain these structural and spectral data is proposed.
Structural and Mechanistic Studies of Mofegiline Inhibition of Recombinant Human Monoamine Oxidase B ( parallel).,Milczek EM, Bonivento D, Binda C, Mattevi A, McDonald IA, Edmondson DE J Med Chem. 2008 Dec 2. PMID:19053775[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Milczek EM, Bonivento D, Binda C, Mattevi A, McDonald IA, Edmondson DE. Structural and Mechanistic Studies of Mofegiline Inhibition of Recombinant Human Monoamine Oxidase B ( parallel). J Med Chem. 2008 Dec 2. PMID:19053775 doi:10.1021/jm8011867
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