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ID 119010
Author
Takami, Naoki Kagawa University
Yoneda, Kazunari Tokai University
Ohmori, Taketo Osaka Institute of Technology
Sakuraba, Haruhiko Kagawa University
Keywords
L-Arginine dehydrogenase
μ-Crystallin/ornithine cyclodeaminase family
Crystal structure
Amino acid dehydrogenase
Site-directed mutagenesis
Content Type
Journal Article
Description
Crystal structures of Pseudomonas veronii L-arginine dehydrogenase (L-ArgDH), belonging to the μ-crystallin/ornithine cyclodeaminase family, were determined for the enzyme in complex with L-lysine and NADP+ and with L-arginine and NADPH. The main chain coordinates of the P. veronii L-ArgDH monomer showed notable similarity to those of Archaeoglobus fulgidus L-AlaDH, belonging to the same family, and pro-R specificity similar to L-AlaDH for hydride transfer to NADP+ was postulated. However, the residues recognizing the α-amino group of the substrates differed between the two enzymes. Based on a substrate modeling study, it was proposed that in A. fulgidus L-AlaDH, the amino group of L-alanine interacts via a water molecule (W510) with the side chains of Lys41 and Arg52. By contrast, the α-amino group of L-arginine formed hydrogen bonds with the side chains of Thr224 and Asn225 in P. veronii L-ArgDH. Moreover, the guanidino group of L-arginine was fixed into the active site via hydrogen bonds with the side chain of Asp54. Site-directed mutagenesis suggested that Asp54 plays an important role in maintaining high reactivity against the substrate and that Tyr58 and Lys71 play critical roles in enzyme catalysis.
Journal Title
International Journal of Biological Macromolecules
ISSN
01418130
18790003
NCID
AA00233999
AA1153092X
Publisher
Elsevier
Volume
249
Start Page
126070
Published Date
2023-07-29
Rights
© 2023. This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/
EDB ID
DOI (Published Version)
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
Author
departments
Bioscience and Bioindustry