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Literature summary for 3.5.1.81 extracted from

  • Wakayama, M.; Yada, H.; Kanda, S.; Hayashi, S.; Yatsuda, Y.; Sakai, K.; Moriguchi, M.
    Role of conserved histidine residues in D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (2000), Biosci. Biotechnol. Biochem., 64, 1-8.
    View publication on PubMed
Search for more literature for 3.5.1.81

Protein Variants

Protein Variants Comment Organism
H250N KM-value for N-acetyl-D-leucine is 6fold higher than the wild-type value, turnover number is 0.0246% of the wild-type value. Below 1% of the relative activity compared with wild-type enzyme.The zinc content of the mutant enzyme is 0.7 gatom per mol, compared to 2.3 gatom per mol for the wild-type enzyme Achromobacter xylosoxidans
H251N approximately 30% of the activity of wild-type enzyme. KM-value for N-acetyl-D-leucine is 32% of the wild-type value, turnover number is 48% of the wild-type value. Achromobacter xylosoxidans
H67I no detectable activity Achromobacter xylosoxidans
H67N KM-value for N-acetyl-D-leucine is 75% of the wild-type value, turnover number is 0.0012% of the wild-type value. The zinc content of the mutant enzyme is 2.2 gatom per mol, compared to 2.3 gatom per mol for the wild-type enzyme Achromobacter xylosoxidans

Inhibitors

Inhibitors Comment Organism Structure
1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide 16% inhibition at 1 mM, 45% inhibition at 10 mM Achromobacter xylosoxidans
2,4,6-Trinitrobenzene-1-sulfonate 40% inhihition at 1 mM, 86% inhibition at 10 mM Achromobacter xylosoxidans
3-Bromopyruvate 10 mM, 28% inhibition Achromobacter xylosoxidans
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride 17% inhibition at 1 mM, 42% inhibition at 10 mM Achromobacter xylosoxidans
5,5'-dithiobis(2-nitrobenzoic acid) 10 mM, 41% inhibition Achromobacter xylosoxidans
diethyl dicarbonate 93% inhibition by 93 mM, complete inhibition by 10 mM Achromobacter xylosoxidans
iodoacetate 10 mM, 37% inhibition Achromobacter xylosoxidans
N-Acetylimidazole 88% inhibition at 1 mM, 96% inhibition at 10 mM Achromobacter xylosoxidans
NEM 10 mM, 27% inhibition Achromobacter xylosoxidans
Phenylglyoxal 55% inhibition at 1 mM, 98% inhibition at 10 mM Achromobacter xylosoxidans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.61
-
 N-acetyl-D-leucine mutant enzyme H251N Achromobacter xylosoxidans
1.44
-
 N-acetyl-D-leucine mutant enzyme H67N Achromobacter xylosoxidans
1.93
-
 N-acetyl-D-leucine wild-type enzyme Achromobacter xylosoxidans
11.6
-
 N-acetyl-D-leucine mutant enzyme H250N Achromobacter xylosoxidans

Metals/Ions

Metals/Ions Comment Organism Structure
Zinc wild-type enzyme contains 2.3 gatom of zinc per mol of enzyme, mutant enzyme H67N contains 2.2 gatom of zinc per mol of enzyme, mutant enzyme H250N contains 0.7 gatom of zinc per mol of enzyme Achromobacter xylosoxidans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
 x * 52000, wild-type enzyme and mutant enzymes H167N, H67I, H250N and H251N, SDS-PAGE Achromobacter xylosoxidans

Organism

Organism UniProt Comment Textmining
Achromobacter xylosoxidans
-
 subsp. xylosoxydans A-6
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-D-leucine + H2O
-
 Achromobacter xylosoxidans acetate + D-leucine
-
 ?

Subunits

Subunits Comment Organism
? x * 52000, wild-type enzyme and mutant enzymes H167N, H67I, H250N and H251N, SDS-PAGE Achromobacter xylosoxidans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0147
-
 N-acetyl-D-leucine mutant enzyme H67N Achromobacter xylosoxidans
0.297
-
 N-acetyl-D-leucine mutant enzyme H250N Achromobacter xylosoxidans
593.3
-
 N-acetyl-D-leucine mutant enzyme H251N Achromobacter xylosoxidans
1225
-
 N-acetyl-D-leucine wild-type enzyme Achromobacter xylosoxidans