Crystallization of a truncated soluble human semicarbazide-sensitive amine oxidase

Jakobsson, Emma; Nilsson, Joakim; Källström, Ulla; Ogg, D.; Kleywegt, Gerard J.

doi:10.1107/s1744309105002678

Cited by 13 publications

(10 citation statements)

References 41 publications

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“…Recombinant forms of AOC3 (rAOC3) have been produced in Chinese hamster ovary (CHO) cells (46,60), Ax endothelial cells (67), HEK293 cells (68,69), and Drosophila S 2 cells (70). Recombinant AOC3s produced in HEK and S2 cells were expressed without the transmembrane domain (i.e.…”

Section: Amine Oxidase (Copper-containing) Familymentioning

confidence: 99%

Human copper-dependent amine oxidases

Finney

Moon

Ronnebaum

et al. 2014

Archives of Biochemistry and Biophysics

112

121

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Copper amine oxidases (CAOs) are a class of enzymes that contain Cu2+ and a tyrosine-derived quinone cofactor, catalyze the conversion of a primary amine functional group to an aldehyde, and generate hydrogen peroxide and ammonia as byproducts. These enzymes can be classified into two non-homologous families: 2,4,5-trihydroxyphenylalanine quinone (TPQ)-dependent CAOs and the lysine tyrosylquinone (LTQ)-dependent lysyl oxidase (LOX) family of proteins. In this review, we will focus on recent developments in the field of research concerning human CAOs and the LOX family of proteins. The aberrant expression of these enzymes is linked to inflammation, fibrosis, tumor metastasis/invasion and other diseases. Consequently, there is a critical need to understand the functions of these proteins at the molecular level, so that strategies targeting these enzymes can be developed to combat human diseases.

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Section: Amine Oxidase (Copper-containing) Familymentioning

confidence: 99%

Human copper-dependent amine oxidases

Finney

Moon

Ronnebaum

et al. 2014

Archives of Biochemistry and Biophysics

112

121

View full text Add to dashboard Cite

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“…Based on the model (Fig. 4a), AOC2 forms a heart-shaped dimeric structure similar to that of AOC3 [18,19]. The AOC2 model has a 68% sequence identity with AOC3, and the monomers superimpose with a root mean square deviation (RMDS) of 0.91 Å .…”

Section: Homology Modeling and Ligand Docking Reveal Structural Diffementioning

confidence: 99%

“…The active site is only accessible through a cavity formed by the D3 and D4 domains. The crystal structure of the human AOC3 [18,19] shows several amino acids with potential key roles in substrate selectivity and binding.…”

Section: Introductionmentioning

confidence: 99%

The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase

Kaitaniemi

Elovaara

Grön

et al. 2009

Cell. Mol. Life Sci.

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Semicarbazide-sensitive amine oxidases (SSAOs) catalyze oxidative deamination of primary amines, but the true physiological function of these enzymes is still poorly understood. Here, we have studied the functional and structural characteristics of a human cell-surface SSAO, AOC2, which is homologous to the better characterized family member, AOC3. The preferred in vitro substrates of AOC2 were found to be 2-phenylethylamine, tryptamine and p-tyramine instead of methylamine and benzylamine, the favored substrates of AOC3. Molecular modeling suggested structural differences between AOC2 and AOC3, which provide AOC2 with the capability to use the larger monoamines as substrates. Even though AOC2 mRNA was expressed in many tissues, the only tissues with detectable AOC2-like enzyme activity were found in the eye. Characterization of AOC2 will help in evaluating the contribution of this enzyme to the pathological processes attributed to the SSAO activity and in designing specific inhibitors for the individual members of the SSAO family.

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“…Crystallographically, disulfide bonds involving a cysteine residue near the C-terminus have been observed in VAP-1 (Airenne et al, 2005;Jakobsson et al, 2005) and PPLO (Duff et al, 2003). In VAP-1, the chains of the dimer are linked by a disulfide bond between CysA748 and CysB748.…”

Section: Resultsmentioning

confidence: 99%

“…1). The others are Escherichia coli amine oxidase (ECAO; Parsons et al, 1995), Arthrobacter globiformis amine oxidase (AGAO; Wilce et al, 1997), Hansenula polymorpha amine oxidase (HPAO; Li et al, 1998), Pichia pastoris lysyl oxidase (PPLO; Duff et al, 2003), bovine serum amine oxidase (BSAO; Lunelli et al, 2005) and the human vascular adhesion protein (VAP-1; Airenne et al, 2005;Jakobsson et al, 2005). All are homodimers of similar size and topology.…”

Section: Introductionmentioning

confidence: 99%

A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer

et al. 2006

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The structure of a newly crystallized form of the copper-dependent amine oxidase from pea seedlings has been refined at a resolution of 2.2 Å to a final R factor of 0.181. The structure (form II) was originally discovered during a study of xenon binding to copper-dependent amine oxidases as a probe for dioxygenbinding sites [Duff et al. (2004), J. Mol. Biol. 344, 599-607]. The form II crystals belong to space group P2 1 , with two dimers in the asymmetric unit. The overall structure is very similar to the crystals of form I in space group P2 1 2 1 2 1 with a dimer in the asymmetric unit [Kumar et al. (1996), Structure, 4,[943][944][945][946][947][948][949][950][951][952][953][954][955]. In form I the last three residues (644-647) observable in the two subunits were apparently splayed apart. It was noted that the absence of a disulfide bond between the Cys647 residues of the two subunits was inconsistent with chemical evidence for the absence of free sulfhydryl groups. In both of the crystallographically independent dimers of form II the two subunits are clearly joined by a disulfide bridge between the C-terminal cysteine residues. This is only possible if the two polypeptide chains in the dimer adopt different conformations near the C-terminus so that the twofold symmetry is lost. A proline residue (645) two residues before the cysteine has a cis conformation in one chain and a trans conformation in the other. As a result, the disulfide bond lies more than 5 Å from the twofold axis. The loss of local twofold symmetry in form II can be explained by intermolecular contacts, which provide an asymmetric environment.

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Crystallization of a truncated soluble human semicarbazide-sensitive amine oxidase

Cited by 13 publications

References 41 publications

Human copper-dependent amine oxidases

Human copper-dependent amine oxidases

The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase

A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer

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