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MetaCyc Enzyme: N-carbamoylsarcosine amidohydrolase

Species: Pseudomonas putida 77

Subunit composition of N-carbamoylsarcosine amidohydrolase = [N-carbamoylsarcosine amidohydrolase subunit]

Summary:
N-carbamoylsarcosine amidohydrolase from Pseudomonas putida 77 was purified and characterized. Different methods for determining the molecular mass of the enzyme gave different results - 102 kDa by ultracentrifugal equilibrium, 88 kDa by gel filtration, and 75 kDa by HPLC, making it impossible to calculate the number of subunits in the enzyme complex [Kim86].

The enzyme has a fairly broad substrate specificity, and N-carbamoyl amino acids with a methyl group or a hydrogen atom on the amino-N atom and possessing glycine, D-alanine, or one of their derivatives as an amino acid moyety served well as substrates.

The Km and Vm values for N-carbamoylsarcosine were 3.2 mM and 1.75 U/mg protein, respectively [Kim86].

Molecular Weight of Polypeptide: 27 kD (experimental) [Kim86]

Molecular Weight of Multimer: 102 kD (experimental) [Kim86]

pI: 5.6 [Kim86]

Gene-Reaction Schematic

Gene-Reaction Schematic


Enzymatic reaction of: N-carbamoylsarcosine amidohydrolase

Inferred from experiment

EC Number: 3.5.1.59

N-carbamoylsarcosine + 2 H+ + H2O → ammonium + CO2 + sarcosine

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Alternative Substrates for N-carbamoylsarcosine: N-carbamoyl-D-phenylglycine [Kim86], N-carbamoyl-4-hydroxy-D-phenylglycine [Kim86], 2-ureido-propanoate [Kim86], N-carbamoylglycine [Kim86], N-methyl-N-carbamoyl-D-alanine [Kim86]

In Pathways: creatinine degradation II

Inhibitors (Unknown Mechanism): Ag+ [Kim86], Cu2+ [Kim86], Hg2+ [Kim86]Kinetic Parameters:
Substrate Km (μM) Citations
N-carbamoylsarcosine 3200.0 [Kim86]

T(opt): 37 °C [Kim86]

pH(opt): 7-8 [Kim86]


References

Kim86: Kim JM, Shimizu S, Yamada H (1986). "Purification and characterization of a novel enzyme, N-carbamoylsarcosine amidohydrolase, from Pseudomonas putida 77." J Biol Chem 261(25);11832-9. PMID: 3745168


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Tue May 3, 2016, biocyc14.