Species: Pseudomonas putida 77
Subunit composition of N-carbamoylsarcosine amidohydrolase = [N-carbamoylsarcosine amidohydrolase subunit]
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]
Enzymatic reaction of: N-carbamoylsarcosine amidohydrolase
EC Number: 188.8.131.52N-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 IIInhibitors (Unknown Mechanism): Ag+ [Kim86], Cu2+ [Kim86], Hg2+ [Kim86]Kinetic Parameters:
T(opt): 37 °C [Kim86]
pH(opt): 7-8 [Kim86]
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
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493