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Literature summary for 3.5.1.14 extracted from

  • Hollingsworth, E.J.;Isupov, M.N.; Littlechild, J.A.
    Crystallization and preliminary X-ray diffraction analysis of L-aminoacylase from the hyperthermophilic archaeon Thermococcus litoralis (2002), Acta Crystallogr. Sect. D, 58, 507-510.
    View publication on PubMed
Search for more literature for 3.5.1.14

Crystallization (Commentary)

Crystallization (Comment) Organism
the enzyme is crystallized from ammonium sulfate using the sitting-drop vapour-diffusion method. The crystals diffract to 2.8 A resolution and belong to the rhombohedral space group R32, with unit-cell parameters a = b = 102.4, c = 178.5 A, gamma = 120° in a hexagonal lattice setting. The asymmetric unit contains one enzyme monomer, containing a single zinc ion Thermococcus litoralis

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains one Zn2+ per monomer, zinc-containing enzyme Thermococcus litoralis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
 4 * 43000, SDS-PAGE Thermococcus litoralis
170000
-
 gel filtration Thermococcus litoralis

Organism

Organism UniProt Comment Textmining
Thermococcus litoralis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermococcus litoralis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0092
-
 pH 8.0, temperature not specified in the publication, substrate: acetyl-DL-Trp Thermococcus litoralis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-DL-Trp + H2O
-
 Thermococcus litoralis acetate + DL-Trp
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 43000, SDS-PAGE Thermococcus litoralis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Thermococcus litoralis