The peroxisomal import signal of amine oxidase from the yeast <i>Hansenula polymorpha</i> is not universal

Hoop, M. J. De; Valkema, Romi; Kienhuis, C. B. M.; Hoyer, M. A.; Ab, Geert

doi:10.1002/yea.320080402

Cited by 16 publications

(11 citation statements)

References 33 publications

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“…For instance, H. polymorpha AMO or T. brucei aldolase are not sorted to S. cerevisiae peroxisomes [2,28]. Both proteins contain a sequence which is slightly aberrant from the PTS2 consensus, RL-Xs-QA or RV-Xs-HL, which might cause the mislocation in S. cerevisiae.…”

Section: Discussionmentioning

confidence: 99%

The N‐terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal

et al. 1995

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Section: Discussionmentioning

confidence: 99%

The N‐terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal

et al. 1995

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“…Similarly, pea seedling diamine oxidase, containing a signal peptide of 25 amino acids at the N-terminus, has also been cytochemically localized to the cell wall (Slocum and Furey III 1991). By contrast, yeast Hansenula polymorpha methylamine oxidase is located in peroxisomes (De Hoop et al 1992); it has a signal sequence of 16 amino acids at the N-terminus (Faber et al 1995). The amine oxidase of the gram-negative bacterium Escherichia coli K-12 is located in the periplasm and contains a signal peptide of 30 amino acids at the N-terminus (Roh et al 1994).…”

Section: Introductionmentioning

confidence: 99%

Cellular localization and metabolic function of n-butylamine-induced amine oxidases in the fungus Aspergillus niger AKU 3302

et al. 2000

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Using transmission electron microscopy, the amine oxidase activity in Aspergillus niger AKU 3302 was localized to the outer side of the cell wall but not inside the cell using the cerium perhydroxide deposition method. The presence of cerium in the deposit was confirmed by energy-dispersive microanalysis of X-rays. Interestingly, immunocytochemical localization using gold labeling with a specific antibody indicated the presence of amine oxidase protein inside the cell wall and not only on the outer surface. Besides labeling of the cell wall, a high level of labeling was also observed inside the cell in what seemed to be secretory vesicle structures. It is proposed that the highly active amine oxidase AO-I is located in the cell wall and serves primarily as a detoxifying agent, preventing amines from entering and damaging the cell. The amine oxidation exhibits an interesting spatial orientation involving a release of toxic hydrogen peroxide into the extracellular space. The inactive amine oxidase protein located inside the cell is most probably the amine oxidase AO-II, found in cell homogenates. It is also likely that the less active AO-II is an improperly folded precursor of AO-I, which acquired low-level activity after cell homogenization in the presence of Cu(II) and oxygen due to autooxidative formation of topaquinone.

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“…Although a peroxisomal protein in its native host organism, it was found in the cytosol of S. cerevisiae during recombinant expression (10). Characterized as a “methylamine oxidase,” HPAO-1 demonstrated much greater activity against methylamine than benzylamine.…”

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confidence: 99%

Kinetic and Structural Analysis of Substrate Specificity in Two Copper Amine Oxidases from Hansenula polymorpha

et al. 2010

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The structural underpinnings of enzyme substrate specificity are investigated in a pair of copper amine oxidases (CAOs) from Hansenula polymorpha (HPAO-1 and HPAO-2). The X-ray crystal structure (to 2.0 Å resolution) and steady state kinetic data of the second copper amine oxidase (HPAO-2) are presented for comparison to HPAO-1. Despite 34 % sequence identity and superimposable active site residues implicated in catalysis, the enzymes vary considerably in their substrate entry channel. The previously studied CAO, HPAO-1, has a narrow substrate channel. In contrast HPAO-2 has a wide funnel-shaped substrate channel, which also contains a side-chamber. In addition, there are a number of amino acid changes within the channels of HPAO-2 and HPAO-1 that may sterically impact the ability of substrates to form covalent Schiff base catalytic intermediates and to initiate chemistry. These differences can partially explain the greatly different substrate specificities as characterized by k cat /K m value differences: in HPAO-1, the k cat /K m for methylamine is 330-fold greater than for benzylamine, whereas in HPAO-2 it is benzylamine that is the better substrate by 750-fold. In HPAO-2 an inflated D k cat /K m (methylamine) in relation to D k cat / K m (benzylamine) indicates that proton abstraction has been impeded more than substrate release. In HPAO-1, D k cat /K m (S) changes little with the slow substrate, and indicates a similar increase in the energy barriers that control both substrate binding and subsequent catalysis. In neither case is k cat / K m for the second substrate, O 2, significantly altered. These results reinforce the modular nature of the active sites of CAOs and show that multiple factors contribute to substrate specificity and catalytic efficiency. In HPAO-1, the enzyme with the smaller substrate binding pocket, both initial substrate binding and proton loss are affected by an increase in substrate size, while in HPAO-2, the enzyme with the larger substrate binding pocket, the rate of proton loss is differentially affected when a phenyl substituent in substrate is reduced to the size of a methyl group. † This work was supported by NIH grants, GM39296 to J.P.K., GM66569 to C.M.W. and Chemistry-Biology Interface Training Grant GM-008700 to B.J.J, and Minnesota Medical Foundation grant 3714-9221-06, Office of the Dean of the Graduate School of the University of Minnesota grant 21087, and a Minnesota Partnership for Biotechnology and Medical Genomics grant SPAP-05-0013-P-FY06 to C.M.W. ‡ Co-ordinates and structure factors have been deposited in the Protein Data Bank as entry 3loy.*Address correspondence to: Carrie M. Wilmot, Tel: (612) 624-2406, Fax: (612) 624-5121, wilmo004@umn.edu and Judith P. Klinman, Tel: (510) 642-2668, Fax (510) NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author ManuscriptCopper amine oxidases (CAOs) 1 are virtually ubiquitous in aerobic organisms, and catalyze the oxidative deamination of primary amines in the following overall reaction:While usually...

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The peroxisomal import signal of amine oxidase from the yeast Hansenula polymorpha is not universal

Cited by 16 publications

References 33 publications

The N‐terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal

The N‐terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal

Cellular localization and metabolic function of n-butylamine-induced amine oxidases in the fungus Aspergillus niger AKU 3302

Kinetic and Structural Analysis of Substrate Specificity in Two Copper Amine Oxidases from Hansenula polymorpha

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