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Journal of Bacteriology, January 2004, p. 411-418, Vol. 186, No. 2
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.2.411-418.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Molecular and Functional Characterization of a Unique Sucrose Hydrolase from Xanthomonas axonopodis pv. glycines

Hong-Suk Kim,1 Hyoung-Joon Park,1 Sunggi Heu,2 and Jin Jung1*

School of Agricultural Biotechnology, Seoul National University, Seoul 151-742,1 Plant Pathology Division, National Institute of Agricultural Science and Technology, RDA, Suwon 441-707, South Korea2

Received 11 August 2003/ Accepted 20 October 2003

A novel sucrose hydrolase (SUH) from Xanthomonas axonopodis pv. glycines, a causative agent of bacterial pustule disease on soybeans, was studied at the functional and molecular levels. SUH was shown to act rather specifically on sucrose (Km = 2.5 mM) but not on sucrose-6-phosphate. Protein analysis of purified SUH revealed that, in this monomeric enzyme with an estimated molecular mass of 70,223 ± 12 Da, amino acid sequences determined for several segments have corresponding nucleotide sequences in XAC3490, a protein-coding gene found in the genome of X. axonopodis pv. citri. Based on this information, the SUH gene, consisting of an open reading frame of 1,935 bp, was cloned by screening a genomic library of X. axonopodis pv. glycines 8ra. Database searches and sequence comparison revealed that SUH has significant homology to some family 13 enzymes, with all of the crucial invariant residues involved in the catalytic mechanism conserved, but it shows no similarity to known invertases belonging to family 32. suh expression in X. axonopodis pv. glycines requires sucrose induction, and insertional mutagenesis resulted in an absence of sucrose-inducible sucrose hydrolase activity in crude protein extracts and a sucrose-negative phenotype. Recombinant SUH, overproduced in Escherichia coli and purified, was shown to have the same enzymatic characteristics in terms of kinetic parameters.

* Corresponding author. Mailing address: School of Agricultural Biotechnology, Seoul National University, Kwanak-ku, Seoul 151-742, South Korea. Phone: (82) 2 880 4648. Fax: (82) 2 873 3112. E-mail: jinjung{at}snu.ac.kr.

Journal of Bacteriology, January 2004, p. 411-418, Vol. 186, No. 2
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.2.411-418.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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