HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tipping, A. J. Articles by McPherson, M. J. Search for Related Content PubMed PubMed Citation Articles by Tipping, A. J. Articles by McPherson, M. J. Social Bookmarking                      What's this?

Volume 270, Number 28, Issue of July 14, pp. 16939-16946, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Alex J. Tipping , Michael J. McPherson

A pea seedling amine oxidase cDNA has been isolated and sequenced. A single long open reading frame has amino acid sequences corresponding to those determined from active site peptide (Janes, S. M., Palcic, M. M., Scaman, C. H., Smith, A. J., Brown, D. E., Dooley, D. M., Mure, M., and Klinman, J. P.(1992) Biochemistry 31, 12147-12154) and N-terminal sequencing experiments. The latter reveals the protein to have a 25-amino acid leader sequence with characteristics of a secretion signal peptide, as expected for this extracellular enzyme. Comparisons of the amino acid sequence of the mature pea enzyme (649 amino acids) with that of the mature lentil enzyme (569 amino acids; Rossi, A., Petruzzelli, R., and Finazzi-Agr, A.(1992) FEBS Lett. 301, 253-257) reveal important and unexpected differences particularly with regard to protein length. Sequencing of part of the lentil gene identified several frameshift differences within the coding region resulting in a mature lentil protein of exactly the same length, 649 amino acids, as the pea enzyme. Multiple alignments of 10 copper amine oxidase sequences reveal 33 completely conserved residues of which 10 are found within 41 aligned residues at the C-terminal tails, the region missing from the original lentil sequence. One of only four conserved histidines is found in this region and may represent the third ligand to the copper. The pea enzyme contains around 3-4% carbohydrate as judged by deglycosylation experiments. We have also demonstrated by hybridization analysis that copper amine oxidase genes are present in a range of mono- and dicotyledonous plants.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				A. Katoh, T. Shoji, and T. Hashimoto Molecular Cloning of N-methylputrescine Oxidase from Tobacco Plant Cell Physiol., March 1, 2007; 48(3): 550 - 554. [Abstract] [Full Text] [PDF]

				C. Delis, M. Dimou, E. Flemetakis, G. Aivalakis, and P. Katinakis A root- and hypocotyl-specific gene coding for copper-containing amine oxidase is related to cell expansion in soybean seedlings J. Exp. Bot., January 1, 2006; 57(1): 101 - 111. [Abstract] [Full Text] [PDF]

				G. Rea, M. C. de Pinto, R. Tavazza, S. Biondi, V. Gobbi, P. Ferrante, L. De Gara, R. Federico, R. Angelini, and P. Tavladoraki Ectopic Expression of Maize Polyamine Oxidase and Pea Copper Amine Oxidase in the Cell Wall of Tobacco Plants Plant Physiology, April 1, 2004; 134(4): 1414 - 1426. [Abstract] [Full Text] [PDF]

				H. Kauss, M. Fauth, A. Merten, and W. Jeblick Cucumber Hypocotyls Respond to Cutin Monomers via Both an Inducible and a Constitutive H2O2-Generating System Plant Physiology, August 1, 1999; 120(4): 1175 - 1182. [Abstract] [Full Text]

				O. C. Hansen and P. Stougaard Hexose Oxidase from the Red Alga Chondrus crispus. PURIFICATION, MOLECULAR CLONING, AND EXPRESSION IN PICHIA PASTORIS J. Biol. Chem., April 25, 1997; 272(17): 11581 - 11587. [Abstract] [Full Text] [PDF]

				J. P. Klinman and J. P. Klinman New Quinocofactors in Eukaryotes J. Biol. Chem., November 1, 1996; 271(44): 27189 - 27192. [Full Text] [PDF]

				Y.-H. Choi, R. Matsuzaki, S. Suzuki, and K. Tanizawa Role of Conserved Asn-Tyr-Asp-Tyr Sequence in Bacterial Copper/2,4,5-Trihydroxyphenylalanyl Quinone-containing Histamine Oxidase J. Biol. Chem., September 13, 1996; 271(37): 22598 - 22603. [Abstract] [Full Text] [PDF]