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: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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-propionate [Kim86 ] , N-carbamoylglycine [Kim86 ] , N-methyl-N-carbamoyl-D-alanine [Kim86 ]
In Pathways: creatinine degradation II
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
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493