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Literature summary for 6.1.1.11 extracted from

  • Bilokapic, S.; Maier, T.; Ahel, D.; Gruic-Sovulj, I.; Soell, D.; Weygand-Durasevic, I.; Ban, N.
    Structure of the unusual seryl-tRNA synthetase reveals a distinct zinc-dependent mode of substrate recognition (2006), EMBO J., 25, 2498-2509.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.11

Cloned(Commentary)

Cloned (Comment) Organism
expression of SerRS in Escherichia coli Methanosarcina barkeri

Crystallization (Commentary)

Crystallization (Comment) Organism
SerRS free and in complex with ATP, serine and the nonhydrolysable seryl-adenylate analogue 5'-O-(N-serylsulfamoyl) adenosine, X-ray diffraction structure determination and anaylsis at 2.5 A resolution Methanosarcina barkeri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000104
-
 L-serine
-
 Methanosarcina barkeri

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Methanosarcina barkeri
Zn2+ absolute requirement of the metal ion for enzymatic activity, active site binding structure, tetra-coordinated by Cys306, Glu355 and Cys461, binds the amino group of the serine substrate Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-serine + tRNASer Methanosarcina barkeri
-
 AMP + diphosphate + L-seryl-tRNASer
-
 ?

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant SerRS from Escherichia coli by Ni2þ-chelating and cation-exchange chromatography, and gel filtration Methanosarcina barkeri

Reaction

Reaction Comment Organism Reaction ID
ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer reaction mechanism Methanosarcina barkeri
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Methanosarcina barkeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNASer
-
 Methanosarcina barkeri AMP + diphosphate + L-seryl-tRNASer
-
 ?
ATP + L-serine + tRNASer zinc-dependent serine recognition mechanism, N-terminal tRNA-binding domain structure, serine-binding site structure, overview Methanosarcina barkeri AMP + diphosphate + L-seryl-tRNASer
-
 ?
additional information L-threonine is a poor substrate, L-cysteine is no substrate for the SerRS, the methanogenic enzyme has evolved two distinct mechanisms for the recognition of the same amino-acid substrate, overview Methanosarcina barkeri ?
-
 ?

Subunits

Subunits Comment Organism
More homology modelling of the tRNA-enzyme complex Methanosarcina barkeri

Synonyms

Synonyms Comment Organism
SerRS
-
 Methanosarcina barkeri
Seryl-tRNA synthetase
-
 Methanosarcina barkeri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Methanosarcina barkeri

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7
-
 L-serine
-
 Methanosarcina barkeri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Methanosarcina barkeri

Cofactor

Cofactor Comment Organism Structure
ATP ATP-binding site structure, overview Methanosarcina barkeri