The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with Cu[superscript I] and Co[superscript II]

Journal Article · Mon Nov 30 00:00:00 EST 2015 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309112012857· OSTI ID:1047888

Klema, Valerie J.; Johnson, Bryan J.; Klinman, Judith P.; Wilmot, Carrie M. ^[1]

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1. UMM

Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their corresponding aldehydes, with the concomitant reduction of O{sub 2} to H{sub 2}O{sub 2}. Catalysis requires two cofactors: a mononuclear copper center and the cofactor 2,4,5-trihydroxyphenylalanine quinone (TPQ). TPQ is synthesized through the post-translational modification of an endogenous tyrosine residue and requires only oxygen and copper to proceed. TPQ biogenesis in CAO can be supported by alternate metals, albeit at decreased rates. A variety of factors are thought to contribute to the degree to which a metal can support TPQ biogenesis, including Lewis acidity, redox potential and electrostatic stabilization capability. The crystal structure has been solved of one of two characterized CAOs from the yeast Hansenula polymorpha (HPAO-1) in its metal-free (apo) form, which contains an unmodified precursor tyrosine residue instead of fully processed TPQ (HPAO-1 was denoted HPAO in the literature prior to 2010). Structures of apoHPAO-1 in complex with Cu{sup I} and Co{sup II} have also been solved, providing structural insight into metal binding prior to biogenesis.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: OTHER U.S. STATESNIH
• OSTI ID: 1047888
• Journal Information: Acta Crystallographica. Section F, Vol. 68, Issue (5) ; 05, 2012; ISSN 1744-3091
• Country of Publication: United States
• Language: ENGLISH