Literature summary for 5.3.3.18 extracted from

Kichise, T.; Hisano, T.; Takeda, K.; Miki, K.
Crystal structure of phenylacetic acid degradation protein PaaG from Thermus thermophilus HB8 (2009), Proteins, 76, 779-786.

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.85 A resolution. Enzyme consists of three identical subunits related by local three-fold symmetry. The monomer is comprised of a spiral and a helical domain with a fold characteristic of the crotonase superfamily. A putative active site residue, Asp136, is situated in an active site cavity and surrounded by several hydrophobic and hydrophilic residues. The active site cavity is sufficiently large to accommodate a ring substrate. Two conformations are observed for helix H2 located adjacent to the active site. Helix H2 is kinked at Asn81 in two subunits, whereas it is kinked at Leu77 in the other subunit, and the side chain of Tyr80 is closer to Asp136. This indicates that catalytic reaction of PaaG may proceed with large conformational changes at the active site	Thermus thermophilus

Crystallization (Comment)

Organism

to 1.85 A resolution. Enzyme consists of three identical subunits related by local three-fold symmetry. The monomer is comprised of a spiral and a helical domain with a fold characteristic of the crotonase superfamily. A putative active site residue, Asp136, is situated in an active site cavity and surrounded by several hydrophobic and hydrophilic residues. The active site cavity is sufficiently large to accommodate a ring substrate. Two conformations are observed for helix H2 located adjacent to the active site. Helix H2 is kinked at Asn81 in two subunits, whereas it is kinked at Leu77 in the other subunit, and the side chain of Tyr80 is closer to Asp136. This indicates that catalytic reaction of PaaG may proceed with large conformational changes at the active site

Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q5SLK3	-	-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579	Q5SLK3	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme may undergo isomerization or a ring-opening reaction via a Delta3,Delta2-enoyl-CoA isomerase-like mechanism	Thermus thermophilus	?	-	?
additional information	enzyme may undergo isomerization or a ring-opening reaction via a Delta3,Delta2-enoyl-CoA isomerase-like mechanism	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	?	-	?

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Release 2023.1 (January 2023)