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Literature summary extracted from

  • Zajc, A.; Romano, M.J.; Turk, B.; Huber, R.
    Crystallographic and fluorescence studies of ligand binding to N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. (1996), J. Mol. Biol., 263, 269-283.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.59 expressed in Escherichia coli Arthrobacter sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.59
-
Arthrobacter sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.59 glyoxylate
-
Arthrobacter sp.
3.5.1.59 ureidohydoxyacetic acid
-
Arthrobacter sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.59 3.5
-
N-carbamoylsarcosine
-
Arthrobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.59 Arthrobacter sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.59
-
Arthrobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.59 additional information high substrate specificity: no hydrolysis of substrate analoges (N-carbamoyl amino acids) Arthrobacter sp. ?
-
?
3.5.1.59 N-carbamoylsarcosine + H2O
-
Arthrobacter sp. sarcosine + CO2 + NH3
-
ir

Subunits

EC Number Subunits Comment Organism
3.5.1.59 tetramer alpha,beta Arthrobacter sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.59 8.3
-
assay at Arthrobacter sp.