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

Valerie J. Klema, Bryan J. Johnson, Judith P. Klinman, Carrie M. Wilmot

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their corresponding aldehydes, with the concomitant reduction of O2 to H2O2. 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 I and Co II have also been solved, providing structural insight into metal binding prior to biogenesis.

Original languageEnglish (US)
Pages (from-to)501-510
Number of pages10
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number5
DOIs
StatePublished - May 2012
Externally publishedYes

Fingerprint

Amine Oxidase (Copper-Containing)
Pichia
oxidase
quinones
biological evolution
amines
copper
Metals
tyrosine
metals
Tyrosine
Copper
Deamination
yeast
Post Translational Protein Processing
Static Electricity
Catalysis
aldehydes
Aldehydes
Acidity

Keywords

  • Amine oxidases
  • Biogenesis
  • Cofactor
  • Copper
  • TPQ

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with Cu I and Co II . / Klema, Valerie J.; Johnson, Bryan J.; Klinman, Judith P.; Wilmot, Carrie M.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 68, No. 5, 05.2012, p. 501-510.

Research output: Contribution to journalArticle

@article{4037aa3cada54aa5b3594451f2553b0d,
title = "The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with Cu I and Co II",
abstract = "Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their corresponding aldehydes, with the concomitant reduction of O2 to H2O2. 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 I and Co II have also been solved, providing structural insight into metal binding prior to biogenesis.",
keywords = "Amine oxidases, Biogenesis, Cofactor, Copper, TPQ",
author = "Klema, {Valerie J.} and Johnson, {Bryan J.} and Klinman, {Judith P.} and Wilmot, {Carrie M.}",
year = "2012",
month = "5",
doi = "10.1107/S1744309112012857",
language = "English (US)",
volume = "68",
pages = "501--510",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "5",

}

TY - JOUR

T1 - The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with Cu I and Co II

AU - Klema, Valerie J.

AU - Johnson, Bryan J.

AU - Klinman, Judith P.

AU - Wilmot, Carrie M.

PY - 2012/5

Y1 - 2012/5

N2 - Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their corresponding aldehydes, with the concomitant reduction of O2 to H2O2. 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 I and Co II have also been solved, providing structural insight into metal binding prior to biogenesis.

AB - Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their corresponding aldehydes, with the concomitant reduction of O2 to H2O2. 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 I and Co II have also been solved, providing structural insight into metal binding prior to biogenesis.

KW - Amine oxidases

KW - Biogenesis

KW - Cofactor

KW - Copper

KW - TPQ

UR - http://www.scopus.com/inward/record.url?scp=84861556188&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84861556188&partnerID=8YFLogxK

U2 - 10.1107/S1744309112012857

DO - 10.1107/S1744309112012857

M3 - Article

C2 - 22691777

AN - SCOPUS:84861556188

VL - 68

SP - 501

EP - 510

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 5

ER -