PDBsum entry 1zoi

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protein Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
275 a.a. *
Waters ×317
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of a stereoselective esterase from pseudomonas putida ifo12996
Structure: Esterase. Chain: a, b, c. Engineered: yes
Source: Pseudomonas putida. Organism_taxid: 303. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Trimer (from PQS)
1.60Å     R-factor:   0.220     R-free:   0.239
Authors: F.Elmi,H.T.Lee,J.Y.Huang,Y.C.Hsieh,Y.L.Wang,Y.J.Chen, S.Y.Shaw,C.J.Chen
Key ref: F.Elmi et al. (2005). Stereoselective esterase from Pseudomonas putida IFO12996 reveals alpha/beta hydrolase folds for D-beta-acetylthioisobutyric acid synthesis. J Bacteriol, 187, 8470-8476. PubMed id: 16321951
13-May-05     Release date:   02-May-06    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q3HWU8  (Q3HWU8_PSEPU) -  Esterase
276 a.a.
275 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


J Bacteriol 187:8470-8476 (2005)
PubMed id: 16321951  
Stereoselective esterase from Pseudomonas putida IFO12996 reveals alpha/beta hydrolase folds for D-beta-acetylthioisobutyric acid synthesis.
F.Elmi, H.T.Lee, J.Y.Huang, Y.C.Hsieh, Y.L.Wang, Y.J.Chen, S.Y.Shaw, C.J.Chen.
Esterase (EST) from Pseudomonas putida IFO12996 catalyzes the stereoselective hydrolysis of methyl dl-beta-acetylthioisobutyrate (dl-MATI) to produce d-beta-acetylthioisobutyric acid (DAT), serving as a key intermediate for the synthesis of angiotensin-converting enzyme inhibitors. The EST gene was cloned and expressed in Escherichia coli; the recombinant protein is a non-disulfide-linked homotrimer with a monomer molecular weight of 33,000 in both solution and crystalline states, indicating that these ESTs function as trimers. EST hydrolyzed dl-MATI to produce DAT with a degree of conversion of 49.5% and an enantiomeric excess value of 97.2% at an optimum pH of about 8 to 10 and an optimum temperature of about 57 to 67 degrees C. The crystal structure of EST has been determined by X-ray diffraction to a resolution of 1.6 A, confirming that EST is a member of the alpha/beta hydrolase fold superfamily of enzymes and includes a catalytic triad of Ser97, Asp227, and His256. The active site is located approximately in the middle of the molecule at the end of a pocket approximately 12 A deep. EST can hydrolyze the methyl ester group without affecting the acetylthiol ester moiety in dl-MATI. The examination of substrate specificity of EST toward other linear esters revealed that the enzyme showed specific activity toward methyl esters and that it recognized the configuration at C-2.

Literature references that cite this PDB file's key reference

  PubMed id Reference
23275166 A.Gao, G.Y.Mei, S.Liu, P.Wang, Q.Tang, Y.P.Liu, H.Wen, X.M.An, L.Q.Zhang, X.X.Yan, and D.C.Liang (2013).
High-resolution structures of AidH complexes provide insights into a novel catalytic mechanism for N-acyl homoserine lactonase.
  Acta Crystallogr D Biol Crystallogr, 69, 82-91.
PDB codes: 4g5x 4g8b 4g8c 4g8d 4g9e 4g9g
21247902 J.Hwang, Y.Kim, H.B.Kang, L.Jaroszewski, A.M.Deacon, H.Lee, W.C.Choi, K.J.Kim, C.H.Kim, B.S.Kang, J.O.Lee, T.K.Oh, J.W.Kim, I.A.Wilson, and M.H.Kim (2011).
Crystal structure of the human N-Myc downstream-regulated gene 2 protein provides insight into its role as a tumor suppressor.
  J Biol Chem, 286, 12450-12460.
PDB codes: 2qmq 2xmq 2xmr 2xms
19957260 G.Labar, C.Bauvois, F.Borel, J.L.Ferrer, J.Wouters, and D.M.Lambert (2010).
Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling.
  Chembiochem, 11, 218-227.
PDB code: 3hju
20099871 K.M.McCulloch, T.Mukherjee, T.P.Begley, and S.E.Ealick (2010).
Structure determination and characterization of the vitamin B6 degradative enzyme (E)-2-(acetamidomethylene)succinate hydrolase.
  Biochemistry, 49, 1226-1235.
PDB code: 3kxp
19184135 M.C.Hanna, and C.Blackstone (2009).
Interaction of the SPG21 protein ACP33/maspardin with the aldehyde dehydrogenase ALDH16A1.
  Neurogenetics, 10, 217-228.  
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