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Literature summary for 6.1.1.11 extracted from

  • Mocibob, M.; Weygand-Durasevic, I.
    The proximal region of a noncatalytic eukaryotic seryl-tRNA synthetase extension is required for protein stability in vitro and in vivo (2008), Arch. Biochem. Biophys., 470, 129-138.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed as a His-tagged fusion protein in Escherichia coli Saccharomyces cerevisiae
expressed as a His-tagged fusion protein in Escherichia coli Zea mays

Protein Variants

Protein Variants Comment Organism
additional information ZmcSerRS does not bind yeast Pex21 protein. Although the yeast C-terminal SerRS extension is required for Pex21p binding, the maize counterpart with an appended yeast SerRS extension remains incapable of Pex21p binding, implying that additional regions of yeast SerRS also contribute to the interaction with the peroxin Zea mays
ScSerRSDELTAC13 mutant containing a deletion of 13 C-terminal residues, mutant is readily complement a ScSerRS null allele, Km and Kcat values comparable to wild-type, T50: 44.5°C, interaction with Pex21p is lost Saccharomyces cerevisiae
ScSerRSDELTAC203 mutant containing a deletion of 20 C-terminal residues, mutant does not complement a ScSerRS null allele, T50: 44.5°C Saccharomyces cerevisiae
ZmcSerRSDELTAC12 mutant containing a deletion of 12 C-terminal residues, mutant readily complements a yeast SerRS null allele, Km and Kcat values comparable to wild-type Zea mays
ZmcSerRSDELTAC18 mutant containing a deletion of 18 C-terminal residues, mutant readily complements a yeast SerRS null allele, Km and Kcat values comparable to wild-type, T50: 31.5°C, interaction with Pex21p is lost Zea mays
ZmcSerRSDELTAC26 mutant containing a deletion of 26 C-terminal residues, mutant does not complement a yeast SerRS null allele, enzymatic activity of mutant protein is comparable to negative control. Expression of mutant protein is probably severly hindered due to intrinsic instability of the truncated protein Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00058
-
tRNASer wild-type, using maize tRNA Zea mays
0.00065
-
tRNASer mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA Saccharomyces cerevisiae
0.00065
-
tRNASer mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA Zea mays
0.00066
-
tRNASer mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA Zea mays
0.00071
-
tRNASer wild-type, using yeast tRNA Saccharomyces cerevisiae
0.047
-
L-Ser wild-type, using yeast tRNA Saccharomyces cerevisiae
0.051
-
L-Ser mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA Saccharomyces cerevisiae
0.108
-
L-Ser mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA Zea mays
0.145
-
L-Ser mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA Zea mays
0.149
-
L-Ser wild-type, using maize tRNA Zea mays

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Zea mays
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNASer
-
Saccharomyces cerevisiae AMP + diphosphate + L-seryl-tRNASer
-
?
ATP + L-serine + tRNASer
-
Zea mays AMP + diphosphate + L-seryl-tRNASer
-
?

Synonyms

Synonyms Comment Organism
SCSerS
-
Saccharomyces cerevisiae
Seryl-tRNA synthetase
-
Saccharomyces cerevisiae
Seryl-tRNA synthetase
-
Zea mays
ZmSerS
-
Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Saccharomyces cerevisiae
30
-
assay at Zea mays

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
ScSerRS (wild-type) T50: 31°C, ScSerRSDELTAC13 (deletion of 13 C-terminal residues) T50: 44.5°C, ScSerRSDELTAC20 (deletion of 20 C-terminal residues) T50: 44.5°. Enzyme destabilization occurs upon removal of the proximal region of the extension, rich in proline and hydrophobic amino acids, since ScSerRSDC20 displays markedly decreased thermal stability Saccharomyces cerevisiae
additional information
-
ZmcSerRS (wild-type) T50: 31°C, ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues) T50: 31.5. This indicates that deletion of the major part of the extension comprising polar and charged amino acids does not affect enzyme structure and stability Zea mays

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.46
-
L-Ser wild-type, using yeast tRNA Saccharomyces cerevisiae
0.47
-
L-Ser mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA Saccharomyces cerevisiae
0.54
-
tRNASer mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA Saccharomyces cerevisiae
0.58
-
tRNASer wild-type, using yeast tRNA Saccharomyces cerevisiae
1.28
-
tRNASer mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA Zea mays
1.43
-
tRNASer mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA Zea mays
1.48
-
tRNASer wild-type, using maize tRNA Zea mays
2.8
-
L-Ser wild-type, using maize tRNA Zea mays
3.2
-
L-Ser mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA Zea mays
3.7
-
L-Ser mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Saccharomyces cerevisiae
7.5
-
assay at Zea mays