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Journal of Biochemistry 2005 138(1):27-33; doi:10.1093/jb/mvi093
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© 2005 The Japanese Biochemical Society

Regular Paper

Role of the N-Terminal Domain of Endoinulinase from Arthrobacter sp. S37 in Regulation of Enzyme Catalysis

Kyoung-Yun Kim, Sangkee Rhee* and Su-Il Kim*

School of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University, Seoul 151-742, Korea

* To whom correspondence should be addressed. Su-Il Kim: Tel: +82-2-880-4643, Fax: +82-2-873-3112, E-mail: sikim{at}plaza.snu.ac.kr; Sangkee Rhee: Tel: +82-2-880-4647. Fax: +82-2-873-3112, E-mail: srheesnu{at}snu.ac.kr

Endoinulinase from Arthrobacter sp. S37 (EnIA), a member of the glycoside hydrolase family 32, is unique in that, unlike other members of the family, it contains a 250-residue N-terminal domain including a "laminin-G like jelly-roll" fold. This unique N-terminal domain is here suggested to be involved in dimerization and catalysis. The essentially inactive nature of enzymes produced by N-terminal truncation ({Delta}15, {Delta}45, {Delta}70, and {Delta}250) supported the pivotal role of this unique domain in catalysis and the need for its structural integrity. Significant reductions in the enzyme efficiency (k cat/K m) were observed when mutations were introduced at highly conserved tryptophan residues (Trp75 and Trp141) in the laminin-G like jelly-roll fold, implying their involvement in catalysis. Results from size-exclusion chromatography of the native and chimeric enzymes in the presence and absence of the domain suggested that the N-terminal domain could mediate dimerization.


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