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Literature DB >> 3593209

The organic cofactor in plasma amine oxidase: evidence for pyrroloquinoline quinone and against pyridoxal phosphate.

P F Knowles, K B Pandeya, F X Rius, C M Spencer, R S Moog, M A McGuirl, D M Dooley.

Abstract

Plasma amine oxidases (EC 1.4.3.6) are classified as containing the organic cofactor pyridoxal phosphate. Biochemical and bioassays on the pig plasma amine oxidase fail to reveal the presence of pyridoxal phosphate and 31P n.m.r. evidence is also inconsistent with pyridoxal phosphate in the enzyme. Resonance Raman spectral studies on phenylhydrazone derivatives of the pig and bovine plasma enzymes have been carried out and comparisons made with the corresponding derivatives of pyridoxal phosphate and pyrroloquinoline quinone (PQQ). The resonance Raman evidence indicates that the cofactor in both plasma amine oxidases is PQQ or a closely related species and not pyridoxal phosphate. The results substantiate earlier reports concerning the identity of the organic cofactor.

Entities: Chemical Species

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Year: 1987 PMID： 3593209 PMCID： PMC1147602 DOI： 10.1042/bj2410603

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

14 in total

1. MONOAMINE OXIDASE. IV. NATURE OF THE SECOND PROSTHETIC GROUP OF PLASMA MONOAMINE OXIDASE.

Authors: H YAMADA; K T YASUNOBU
Journal: J Biol Chem Date: 1963-08 Impact factor: 5.157

2. PYRIDOXAL PHOSPHATE AS A CONSTITUENT OF THE HISTAMINASE (BENZYLAMINE OXIDASE) OF PIG PLASMA.

Authors: H BLASCHKO; F BUFFONI
Journal: Proc R Soc Lond B Biol Sci Date: 1965-08-24

3. The isolation and crystallization of rabbit skeletal muscle phosphorylase b.

Authors: E H FISCHER; E G KREBS
Journal: J Biol Chem Date: 1958-03 Impact factor: 5.157

4. Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods.

Authors: R Barker; N Boden; G Cayley; S C Charlton; R Henson; M C Holmes; I D Kelly; P F Knowles
Journal: Biochem J Date: 1979-01-01 Impact factor: 3.857

5. Recent investigations on the prosthetic group of beef plasma amine oxidase.

Authors: K Watanabe; R A Smith; M Inamasu; K T Yasunobu
Journal: Adv Biochem Psychopharmacol Date: 1972

6. Phosphorylase from dogfish skeletal muscle. Purification and a comparison of its physical properties to those of rabbit muscle phosphorylase.

Authors: P Cohen; T Duewer; E H Fischer
Journal: Biochemistry Date: 1971-07-06 Impact factor: 3.162

Review 3. Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.

Authors: Judith P Klinman; Florence Bonnot
Journal: Chem Rev Date: 2013-12-18 Impact factor: 60.622

4. The role of protein crystallography in defining the mechanisms of biogenesis and catalysis in copper amine oxidase.

Authors: Valerie J Klema; Carrie M Wilmot
Journal: Int J Mol Sci Date: 2012-05-03 Impact factor: 6.208

4 in total

The organic cofactor in plasma amine oxidase: evidence for pyrroloquinoline quinone and against pyridoxal phosphate.

1. MONOAMINE OXIDASE. IV. NATURE OF THE SECOND PROSTHETIC GROUP OF PLASMA MONOAMINE OXIDASE.

2. PYRIDOXAL PHOSPHATE AS A CONSTITUENT OF THE HISTAMINASE (BENZYLAMINE OXIDASE) OF PIG PLASMA.

3. The isolation and crystallization of rabbit skeletal muscle phosphorylase b.

4. Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods.

5. Recent investigations on the prosthetic group of beef plasma amine oxidase.

6. Phosphorylase from dogfish skeletal muscle. Purification and a comparison of its physical properties to those of rabbit muscle phosphorylase.

7. Studies on the mechanism of action of plasma amine oxidase.

8. Mechanism of action of plasma amine oxidase products released under anaerobic conditions.

9. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure.

10. Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group.

1. Studies on the active site of pig plasma amine oxidase.

2. Reactions of bovine serum amine oxidase with NN-diethyldithiocarbamate. Selective removal of one copper ion.

Review 3. Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.

4. The role of protein crystallography in defining the mechanisms of biogenesis and catalysis in copper amine oxidase.