Information on EC 3.5.1.59 - N-carbamoylsarcosine amidase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.5.1.59
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RECOMMENDED NAME
GeneOntology No.
N-carbamoylsarcosine amidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-carbamoylsarcosine + H2O = sarcosine + CO2 + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carbon-nitrogen bonds in linear amides
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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creatinine degradation II
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Metabolic pathways
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creatinine degradation
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SYSTEMATIC NAME
IUBMB Comments
N-carbamoylsarcosine amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
92767-52-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains FS23 and FS41
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain 77
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Manually annotated by BRENDA team
strains H21 and 0114
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
involved in the degradation of creatinine
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-carbamoyl-D-alanine + H2O
?
show the reaction diagram
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hydrolysis at 7% the rate of N-carbamoylsarcosine
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?
N-carbamoylglycine + H2O
?
show the reaction diagram
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hydrolysis at 10% the rate of N-carbamoylsarcosine
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?
N-carbamoylsarcosine + H2O
sarcosine + CO2 + NH3
show the reaction diagram
N-methyl-N-carbamoyl-D-alanine + H2O
?
show the reaction diagram
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hydrolysis at 13% the rate of N-carbamoylsarcosine
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-carbamoylsarcosine + H2O
sarcosine + CO2 + NH3
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
zinc ions play an important role in the favorable substrate bound staes
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
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glyoxylate
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Hg-compounds
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ureidohydoxyacetic acid
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additional information
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no inhibition by 2 mM MgCl2, FeSO4, CdCl2, MnCl2, BaCl2, FeCl3, CaCl2, PbCl2, DTT or 2-mercaptoethanol, 1 mM 1,10-phenanthroline, 2,2'-dipyridyl, hydrazine, phenylhydrazine, 8-hydroxyquinoline, 4 mM sarcosine, glycine, N-methyl-DL-valine, N-methyl-DL-alanine, N,N-dimethylglycine, N-methylleucine, methylurea, dimethylamine, trimethylamine or diethylamine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 3.5
N-carbamoylsarcosine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.096 - 0.165
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crude extract of cells grown on various inducing substrates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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Tris, HEPES or K4P2O7 buffer
8.3
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.7
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about half-maximal activity at pH 5 and 8.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
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about half-maximal activity at 30°C and 50°C
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
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x * 27000, SDS-PAGE
35000
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4 * 35000, SDS-PAGE
75000
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HPLC gel filtration
88000
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gel filtration
102000
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sedimentation equilibrium method
120000
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HPLC gel filtration at pH 6
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 27000, SDS-PAGE
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure solved and refined at a resolution of 2.35 A. The enzyme shares a similar fold and a highly conserved C-D-K-catalytic triad, Cys123, Asp9, and Lys90 with the structures of three cysteine hydrolases (PDB codes: 1NBA, 1IM5, and 2HOR). Molecular dynamics simulations of Ta0454/N-carbamoylsarcosine and Ta0454/pyrazinamide complexes are performed to determine the structural basis of the substrate binding pattern for each ligand. The predicted binding free energies suggest that Ta0454 is selective for N-carbamoylsarcosine over pyrazinamide, and zinc ions play an important role in the favorable substrate bound states
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
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stability maximum, phosphate buffer
209211
6 - 7
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10 min, stable at 40°C
209207
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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10 min, stable at pH 6-7
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from recombinant Escherichia coli
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the small regulatory subunit is cloned, expressed and purified
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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the small regulatory subunit is cloned, expressed and purified
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