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Literature summary extracted from

  • Alterio, V.; Aurilia, V.; Romanelli, A.; Parracino, A.; Saviano, M.; D'Auria, S.; De Simone, G.
    Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125 (2010), Biopolymers, 93, 669-677.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.2.12 N-terminus His6-S-tagged protein from pET28a construct overexpressed in Escherichia coli strain BL21(DE3) under the control of the T7 RNA polymerase transcription system Pseudoalteromonas haloplanktis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.2.12 by the hanging drop vapor diffusion technique, to 2.2 A resolution. Crystals belong to space group P212121 with unit cell dimensions of a = 49.49 A, b = 129.75 A, c = 152.67 A, with 4 molecules per asymmetric unit Pseudoalteromonas haloplanktis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.2.12 30000
-
 2 * 30000, SDS-PAGE Pseudoalteromonas haloplanktis
3.1.2.12 60000
-
 gel filtration Pseudoalteromonas haloplanktis

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.12 Pseudoalteromonas haloplanktis
-
 TAC125
-
3.1.2.12 Pseudoalteromonas haloplanktis TAC 125
-
 TAC125
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.2.12 to homogeneity by a single-step Ni2+ affinity chromatography Pseudoalteromonas haloplanktis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.12 4-nitrophenyl thioacetate + H2O substrate with small acyl moiety Pseudoalteromonas haloplanktis 4-nitrophenol + thioacetate
-
 ?
3.1.2.12 4-nitrophenyl thioacetate + H2O substrate with small acyl moiety Pseudoalteromonas haloplanktis TAC 125 4-nitrophenol + thioacetate
-
 ?
3.1.2.12 additional information PhEst contains a catalytic triad formed by residues Ser147, Asp225 and His258. It shows no activity toward substrates with bulky acyl groups such as S-lactoylglutathione. Has a very narrow acyl-binding pocket in a typical alpha/beta-hydrolase fold Pseudoalteromonas haloplanktis ?
-
 ?
3.1.2.12 additional information PhEst contains a catalytic triad formed by residues Ser147, Asp225 and His258. It shows no activity toward substrates with bulky acyl groups such as S-lactoylglutathione. Has a very narrow acyl-binding pocket in a typical alpha/beta-hydrolase fold Pseudoalteromonas haloplanktis TAC 125 ?
-
 ?
3.1.2.12 S-acetylglutathione + H2O substrate with small acyl moiety, high activity Pseudoalteromonas haloplanktis glutathione + acetate
-
 ?
3.1.2.12 S-acetylglutathione + H2O substrate with small acyl moiety, high activity Pseudoalteromonas haloplanktis TAC 125 glutathione + acetate
-
 ?
3.1.2.12 S-formylglutathione + H2O substrate with small acyl moiety, lower activity than compared to S-acetylglutathione Pseudoalteromonas haloplanktis glutathione + formate
-
 ?
3.1.2.12 S-formylglutathione + H2O substrate with small acyl moiety, lower activity than compared to S-acetylglutathione Pseudoalteromonas haloplanktis TAC 125 glutathione + formate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.2.12 dimer 2 * 30000, SDS-PAGE Pseudoalteromonas haloplanktis

Synonyms

EC Number Synonyms Comment Organism
3.1.2.12 FGH
-
 Pseudoalteromonas haloplanktis
3.1.2.12 PhEst
-
 Pseudoalteromonas haloplanktis
3.1.2.12 S-formylglutathione hydrolase
-
 Pseudoalteromonas haloplanktis