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- Structural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis
- Thinh-Phat Cao , Joong-Su Kim , Mi-Hee Woo , Jin Myung Choi , Youngsoo Jun , Kun Ho Lee , Sung Haeng Lee
- J. Microbiol. 2016;54(4):311-321. Published online April 1, 2016
- DOI: https://doi.org/10.1007/s12275-016-6029-4
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- 6 Crossref
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Abstract
-
2-deoxyribose-5-phosphate aldolase (DERA) is a class I aldolase
that catalyzes aldol condensation of two aldehydes in the
active site, which is particularly germane in drug manufacture.
Structural and biochemical studies have shown that the active
site of DERA is typically loosely packed and displays broader
substrate specificity despite sharing conserved folding architecture
with other aldolases. The most distinctive structural
feature of DERA compared to other aldolases is short
and flexible C-terminal region. This region is also responsible
for substrate recognition. Therefore, substrate tolerance may
be related to the C-terminal structural features of DERA. Here,
we determined the crystal structures of full length and C-terminal
truncated DERA from Streptococcus suis (SsDERA).
In common, both contained the typical (α/β)8 TIM-barrel
fold of class I aldolases. Surprisingly, C-terminal truncation
result
ing in missing the last α9 and β8 secondary elements, allowed DERA to maintain activity comparable to the fulllength enzyme. Specifically, Arg186 and Ser205 residues at the C-terminus appeared mutually supplemental or less indispensible for substrate phosphate moiety recognition. Our results suggest that DERA might adopt a shorter C-terminal region than conventional aldolases during evolution pathway, resulting in a broader range of substrate tolerance through active site flexibility. -
Citations
Citations to this article as recorded by
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An aldolase-dependent phloroglucinol degradation pathway in
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Yating Li, Tong Xu, Yanqin Tu, Tong Li, Yifeng Wei, Yan Zhou, Ning-Yi Zhou
Applied and Environmental Microbiology.2024;[Epub] CrossRef - Synthetic Activity of Recombinant Whole Cell Biocatalysts Containing 2‐Deoxy‐D‐ribose‐5‐phosphate Aldolase from Pectobacterium atrosepticum
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ACS Catalysis.2018; 8(5): 3971. CrossRef - 1H, 13C, and 15N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase
Marianne Schulte, Matthias Stoldt, Philipp Neudecker, Jӧrg Pietruszka, Dieter Willbold, Vineet Panwalkar
Biomolecular NMR Assignments.2017; 11(2): 197. CrossRef
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An aldolase-dependent phloroglucinol degradation pathway in
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