MetaCyc Enzyme: N-carbamoylsarcosine amidohydrolase

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]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Enzymatic reaction of: N-carbamoylsarcosine amidohydrolase

EC Number:

N-carbamoylsarcosine + 2 H+ + H2O <=> ammonium + CO2 + sarcosine

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-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:

Km (μM)

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

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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