Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Minami, R.
Right arrow Articles by Honma, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Minami, R.
Right arrow Articles by Honma, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1998, Vol. 123, No. 6 1112-1118
© 1998 Japanese Biochemical Society

research-article

Properties, Sequence, and Synthesis in Escherichia coli of 1-Aminocyclopropane-l-Carboxylate Deaminase from Hansenula saturnus

Rie Minami, Kyoko Uchiyama, Toyotaka Murakami, Jun Kawai, Keiichi Mikami, Takashi Yamada, Daisuke Yokoi, Hiroyuki Ito, Hirokazu Matsui and Mamoru Honma1

Faculty of Agriculture, Hokkaido University kita 9 nishi 9, Kita-ku, Sapporo 060-8589

1To whom correspondence should be addressed. Tel: +81-11-706-2497, Fax: +81-11-706-3635, E-mail: mmrhonma{at}chem.agr.hokudai.ac.jp

The plant hormone ethylene is generated from a unique precursor, 1-aminocyclopropane-1-carboxylate (ACC). In previous studies, ACC deaminase, which degrades ACC to {alpha}-ketobutyrate and ammonia, was found in four strains of Pseudomonas, characterized, and sequenced. To verify the wider distribution of ACC deaminase in microorganisms, we purified and sequenced ACC deaminase from the yeast Hansenula saturnus. The purified enzyme was active toward ACC, D-serine and dl-coronamic acid, indicating the same stereospecificity as the Pseudomonas enzyme, but unlike the bacterial enzyme it was not active toward ß-chloro-D-alanine and O-acetyl-D-serine. Analyses of peptides from proteolytic digests of the purified and modified ACC deaminase covered more than 90% of its amino acid sequence and showed a blocked N-terminal residue as N-acetylserine. A cDNA encoding the ACC deaminase was isolated from H. saturnus cells incubated in {alpha}-aminoisobutyrate medium, and sequenced. The yeast enzyme has 441 amino acid residues, of which 60 to 63% are identical to those of reported Pseudomonas enzymes. The open reading frame encoding ACC deaminase was subcloned into pET-11d and expressed in Escherichia coli BL21 (DE3) as an active enzyme.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Appl. Environ. Microbiol.Home page
N. Hontzeas, A. O. Richardson, A. Belimov, V. Safronova, M. M. Abu-Omar, and B. R. Glick
Evidence for Horizontal Transfer of 1-Aminocyclopropane-1-Carboxylate Deaminase Genes
Appl. Envir. Microbiol., November 1, 2005; 71(11): 7556 - 7558.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
W. L. Kelly and C. A. Townsend
Mutational Analysis and Characterization of Nocardicin C-9' Epimerase
J. Biol. Chem., September 10, 2004; 279(37): 38220 - 38227.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Ose, A. Fujino, M. Yao, N. Watanabe, M. Honma, and I. Tanaka
Reaction Intermediate Structures of 1-Aminocyclopropane-1-carboxylate Deaminase: INSIGHT INTO PLP-DEPENDENT CYCLOPROPANE RING-OPENING REACTION
J. Biol. Chem., October 17, 2003; 278(42): 41069 - 41076.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Yao, T. Ose, H. Sugimoto, A. Horiuchi, A. Nakagawa, S. Wakatsuki, D. Yokoi, T. Murakami, M. Honma, and I. Tanaka
Crystal Structure of 1-Aminocyclopropane-1-carboxylate Deaminase from Hansenula saturnus
J. Biol. Chem., October 27, 2000; 275(44): 34557 - 34565.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.