- Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase
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Jisub Hwang , Chang-Sook Jeong , Chang Woo Lee , Seung Chul Shin , Han-Woo Kim , Sung Gu Lee , Ui Joung Youn , Chang Sup Lee , Tae-Jin Oh , Hak Jun Kim , Hyun Park , Hyun Ho Park , Jun Hyuck Lee
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J. Microbiol. 2020;58(7):606-613. Published online April 22, 2020
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DOI: https://doi.org/10.1007/s12275-020-0089-1
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 Abstract
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Crystal structures of enoyl-coenzyme A (CoA) isomerase from
Bosea sp. PAMC 26642 (BoECI) and enoyl-CoA hydratase
from Hymenobacter sp. PAMC 26628 (HyECH) were determined
at 2.35 and 2.70 Å resolution, respectively. BoECI
and HyECH are members of the crotonase superfamily and
are enzymes known to be involved in fatty acid degradation.
Structurally, these enzymes are highly similar except for the
orientation of their C-terminal helix domain. Analytical ultracentrifugation
was performed to determine the oligomerization
states of BoECI and HyECH revealing they exist as
trimers in solution. However, their putative ligand-binding
sites and active site residue compositions are dissimilar. Comparative
sequence and structural analysis revealed that the
active site of BoECI had one glutamate residue (Glu135), this
site is occupied by an aspartate in some ECIs, and the active
sites of HyECH had two highly conserved glutamate residues
(Glu118 and Glu138). Moreover, HyECH possesses a salt
bridge interaction between Glu98 and Arg152 near the active
site. This interaction may allow the catalytic Glu118 residue
to have a specific conformation for the ECH enzyme reaction.
This salt bridge interaction is highly conserved in known
bacterial ECH structures and ECI enzymes do not have this
type of interaction. Collectively, our comparative sequential
and structural studies have provided useful information to
distinguish and classify two similar bacterial crotonase superfamily
enzymes.
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