Abstract

Copper containing amine oxidases represent a major experimental challenge with regard to the identity of a covalently bound cofactor, the role of active site copper and chemical mechanism. Recent evidence suggests that bovine plasma amine oxidase (BPAO) may contain pyrroloquinoline quinone, a new redox cofactor hitherto seen exclusively in prokaryotes. The goals of this proposal to obtain characterization a detailed of structure and mechanism in BPAO with the expectation that such studies will expand our knowledge of the general class of copper amine oxidases. Our work will focus on four areas: (I) Structure of the organic cofactor; (II) Substrate-cofactor interactions; (III) Active site copper; and (IV) Relationship among pro-and eukaryotic enzymes containing pyrroloquinoline quinone

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM039296-04
Application #
3296149
Study Section
Biochemistry Study Section (BIO)
Project Start
1988-02-01
Project End
1992-01-31
Budget Start
1991-02-01
Budget End
1992-01-31
Support Year
4
Fiscal Year
1991
Total Cost
Indirect Cost

  Institution

Name
University of California Berkeley
Department
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704

  Publications

Evans 3rd, Robert L; Latham, John A; Klinman, Judith P et al. (2016) (1)H, (13)C, and (15)N resonance assignments and secondary structure information for Methylobacterium extorquens PqqD and the complex of PqqD with PqqA. Biomol NMR Assign 10:385-9
Kulik, Heather J; Zhang, Jianyu; Klinman, Judith P et al. (2016) How Large Should the QM Region Be in QM/MM Calculations? The Case of Catechol O-Methyltransferase. J Phys Chem B 120:11381-11394
Barr, Ian; Latham, John A; Iavarone, Anthony T et al. (2016) Demonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD. J Biol Chem 291:8877-84
Zhang, Jianyu; Klinman, Judith P (2016) Convergent Mechanistic Features between the Structurally Diverse N- and O-Methyltransferases: Glycine N-Methyltransferase and Catechol O-Methyltransferase. J Am Chem Soc 138:9158-65
Latham, John A; Iavarone, Anthony T; Barr, Ian et al. (2015) PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway. J Biol Chem 290:12908-18
Zhang, Jianyu; Kulik, Heather J; Martinez, Todd J et al. (2015) Mediation of donor-acceptor distance in an enzymatic methyl transfer reaction. Proc Natl Acad Sci U S A 112:7954-9
Zhang, Jianyu; Klinman, Judith P (2015) High-performance liquid chromatography separation of the (S,S)- and (R,S)-forms of S-adenosyl-L-methionine. Anal Biochem 476:81-3
Klinman, Judith P; Bonnot, Florence (2014) Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ. Chem Rev 114:4343-65
Johnson, Bryan J; Yukl, Erik T; Klema, Valerie J et al. (2013) Structural snapshots from the oxidative half-reaction of a copper amine oxidase: implications for O2 activation. J Biol Chem 288:28409-17
Arnison, Paul G; Bibb, Mervyn J; Bierbaum, Gabriele et al. (2013) Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature. Nat Prod Rep 30:108-60

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