3.5.1.59: N-carbamoylsarcosine amidase

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For detailed information about N-carbamoylsarcosine amidase, go to the full flat file.

Word Map on EC 3.5.1.59

3.5.1.59

creatinine

arthrobacter

intersubunit

n-methylhydantoin

pyrazinamidase

putida

isomorphous

r-factor

cytosine

isochorismatase

sheet

six-stranded

cis-peptide

Reaction

Synonyms

amidase, carbamoylsarcosine, CSHase, N-carbamoylsarcosine amidase Ta0454, N-carbamoylsarcosine amidohydrolase

ECTree

3 Hydrolases

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.5.1 In linear amides

3.5.1.59 N-carbamoylsarcosine amidase

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Results	in table
283	AA Sequence
1	CAS Registry Number
4	Cloned(Commentary)
4	Crystallization (Commentary)
1	General Information
11	Inhibitors
4	KM Value [mM]
1	Metals/Ions
6	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
10	Organism
5	Pathway
6	PDB ID
3	pH Optimum
1	pH Range
2	pH Stability
1	Posttranslational Modification
4	Purification (Commentary)
2	Reaction
1	Reaction Type
10	Reference
3	Specific Activity [micromol/min/mg]
21	Substrates and Products (Substrate)
3	Subunits
5	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]

Crystallization

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Crystallization on EC 3.5.1.59 - N-carbamoylsarcosine amidase

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2 entries

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

Thermoplasma acidophilum

Q9HKY9

712888