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Literature summary extracted from

  • Rodriguez-Guilbe, M.; Oyola-Robles, D.; Schreiter, E.R.; Baerga-Ortiz, A.
    Structure, activity, and substrate selectivity of the Orf6 thioesterase from Photobacterium profundum (2013), J. Biol. Chem., 288, 10841-10848.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.2.2 expressed as a GST-fusion protein in Escherichia coli Photobacterium profundum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.2.2 determined at 1.05 A, revealing a hotdog hydrolase fold arranged as a dimer of dimers. A second crystal structure at 1.40 A iss obtained from a crystal that is grown in the presence of Mg2+, which reveals the presence of a binding site for divalent cations at a crystal contact. The Mg2+-bound structure shows localized conformational changes, and its active site is unoccupied, suggesting a mechanism to open the active site for substrate entry or product release Photobacterium profundum

Protein Variants

EC Number Protein Variants Comment Organism
3.1.2.2 D17A mutant shows no activity Photobacterium profundum

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.2 Photobacterium profundum Q93CG9
-
-
3.1.2.2 Photobacterium profundum SS9 Q93CG9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.2.2 using affinity chromatography Photobacterium profundum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.2 3-hydroxybutyryl-CoA + H2O
-
 Photobacterium profundum CoA + 3-hydroxybutyrate
-
 ?
3.1.2.2 arachidonoyl-CoA + H2O
-
 Photobacterium profundum CoA + arachidonate
-
 ?
3.1.2.2 arachidonoyl-CoA + H2O
-
 Photobacterium profundum SS9 CoA + arachidonate
-
 ?
3.1.2.2 benzoyl-CoA + H2O
-
 Photobacterium profundum CoA + benzoate
-
 ?
3.1.2.2 benzoyl-CoA + H2O
-
 Photobacterium profundum SS9 CoA + benzoate
-
 ?
3.1.2.2 eicosapentaenoyl-CoA + H2O
-
 Photobacterium profundum CoA + eicosapentaenoate
-
 ?
3.1.2.2 eicosapentaenoyl-CoA + H2O
-
 Photobacterium profundum SS9 CoA + eicosapentaenoate
-
 ?
3.1.2.2 additional information enzyme assays reveal that Orf6 has a higher specific activity toward long-chain fatty acyl-CoA substrates (palmitoyl-CoA and eicosapentaenoyl-CoA) than toward short-chain or aromatic acyl-CoA substrates Photobacterium profundum ?
-
 ?
3.1.2.2 additional information enzyme assays reveal that Orf6 has a higher specific activity toward long-chain fatty acyl-CoA substrates (palmitoyl-CoA and eicosapentaenoyl-CoA) than toward short-chain or aromatic acyl-CoA substrates Photobacterium profundum SS9 ?
-
 ?
3.1.2.2 palmitoyl-CoA + H2O
-
 Photobacterium profundum CoA + palmitate
-
 ?
3.1.2.2 palmitoyl-CoA + H2O
-
 Photobacterium profundum SS9 CoA + palmitate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.2.2 dimer crystal structure, dimer of dimer Photobacterium profundum

Synonyms

EC Number Synonyms Comment Organism
3.1.2.2 Orf6 thioesterase
-
 Photobacterium profundum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.2.2 25
-
 assay at Photobacterium profundum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.2.2 7.5
-
 assay at Photobacterium profundum