Literature summary for 6.1.1.15 extracted from

Hati, S.; Ziervogel, B.; Sternjohn, J.; Wong, F.C.; Nagan, M.C.; Rosen, A.E.; Siliciano, P.G.; Chihade, J.W.; Musier-Forsyth, K.
Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in 'selective release' of noncognate amino acids (2006), J. Biol. Chem., 281, 27862-27872.

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Cloned(Commentary)

Cloned (Comment)	Organism
gene proS, expression in Escherichia coli strain BL21(DE3)	Methanothermobacter thermautotrophicus
gene proS, expression in Escherichia coli strain BL21(DE3)	Methanocaldococcus jannaschii
gene proS, expression in Escherichia coli strain SG13009	Methanococcus maripaludis
gene proS, overexpression of His-tagged wild-type ProRS and truncation mutant ScDELTA183	Saccharomyces cerevisiae
gene proS, overexpression of wild-type and mutant His-tagged ProRS	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a truncated Sc ProRS mutant lacking the N-terminal 183 residues, ScDELTA183, which shows reduced enzyme activity compared to the wild-type enzyme, overview	Saccharomyces cerevisiae
additional information	replacement of 163 residues of the INS domain, amino acids 232-394, with either an 8-residue Gly6Ser2 linker or a 16-residue Gly12Ser4 linker by PCR amplification of the full-length plasmid pCS-M1S	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
5'-O-[N-(L-alanyl)-sulfamoyl]adenosine	a non-hydrolyzable adenylate analogue, a potent inhibitor of the ATP-diphosphate exchange reaction	Escherichia coli
5'-O-[N-(L-Prolyl)-sulfamoyl]adenosine	a non-hydrolyzable adenylate analogue	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.000131	-	tRNAPro	pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation	Escherichia coli
0.01414	-	tRNAPro	pH 7.0, 37°C, recombinant wild-type enzyme, aminoacylation	Escherichia coli
0.25	-	L-proline	pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation	Escherichia coli
2	37	trans-4-hydroxyproline	pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation	Escherichia coli
50	-	L-proline	pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation	Escherichia coli
53	-	cis-4-hydroxyproline	pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation	Escherichia coli
55	-	cis-4-hydroxyproline	pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation	Escherichia coli
140	-	L-alanine	pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Escherichia coli
Mg2+	-	Saccharomyces cerevisiae
Mg2+	-	Methanothermobacter thermautotrophicus
Mg2+	-	Methanocaldococcus jannaschii
Mg2+	-	Methanococcus maripaludis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-proline + tRNAPro	Escherichia coli	-	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	Saccharomyces cerevisiae	-	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	Methanothermobacter thermautotrophicus	-	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	Methanocaldococcus jannaschii	-	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	Methanococcus maripaludis	-	AMP + diphosphate + L-prolyl-tRNAPro	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Methanocaldococcus jannaschii	-	gene proS	-
Methanococcus maripaludis	-	gene proS	-
Methanothermobacter thermautotrophicus	-	gene proS	-
Saccharomyces cerevisiae	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Saccharomyces cerevisiae
additional information	-	-	Methanothermobacter thermautotrophicus
additional information	-	-	Methanocaldococcus jannaschii
additional information	-	-	Methanococcus maripaludis
additional information	-	activities of wild-type and mutant enzymes, pre-transfer editing activity, overview	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + cis-4-hydroxyproline + tRNAPro	-	Escherichia coli	AMP + diphosphate + cis-4-hydroxyprolyl-tRNAPro	-	?
ATP + L-alanine + tRNAPro	L-alanine is a poor substrate	Escherichia coli	AMP + diphosphate + L-alanyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	-	Escherichia coli	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	-	Saccharomyces cerevisiae	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	-	Methanothermobacter thermautotrophicus	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	-	Methanocaldococcus jannaschii	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	-	Methanococcus maripaludis	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + L-proline + tRNAPro	editing mechanism, the aminoacylation active site plays a significant role in preserving the fidelity of translation by acting as a filter that selectively releases non-cognate adenylates into solution, while protecting the cognate adenylate from hydrolysis, overview, scheme showing proposed pre-transfer and posttransfer editing pathways, overview	Escherichia coli	AMP + diphosphate + L-prolyl-tRNAPro	-	?
ATP + trans-4-hydroxyproline + tRNAPro	-	Escherichia coli	AMP + diphosphate + trans-4-hydroxyprolyl-tRNAPro	-	?

Synonyms

Synonyms	Comment	Organism
class II prolyl-tRNA synthetase	-	Escherichia coli
class II prolyl-tRNA synthetase	-	Saccharomyces cerevisiae
class II prolyl-tRNA synthetase	-	Methanothermobacter thermautotrophicus
class II prolyl-tRNA synthetase	-	Methanocaldococcus jannaschii
class II prolyl-tRNA synthetase	-	Methanococcus maripaludis
Prolyl-tRNA synthetase	-	Escherichia coli
Prolyl-tRNA synthetase	-	Saccharomyces cerevisiae
Prolyl-tRNA synthetase	-	Methanothermobacter thermautotrophicus
Prolyl-tRNA synthetase	-	Methanocaldococcus jannaschii
Prolyl-tRNA synthetase	-	Methanococcus maripaludis
ProRS	-	Escherichia coli
ProRS	-	Saccharomyces cerevisiae
ProRS	-	Methanothermobacter thermautotrophicus
ProRS	-	Methanocaldococcus jannaschii
ProRS	-	Methanococcus maripaludis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Saccharomyces cerevisiae
37	-	assay at	Methanothermobacter thermautotrophicus
37	-	assay at	Methanocaldococcus jannaschii
37	-	assay at	Methanococcus maripaludis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.0091	-	tRNAPro	pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation	Escherichia coli
0.056	-	cis-4-hydroxyproline	pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation	Escherichia coli
0.239	-	tRNAPro	pH 7.0, 37°C, recombinant wild-type enzyme, aminoacylation	Escherichia coli
1.7	-	L-alanine	pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation	Escherichia coli
12	-	L-proline	pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation	Escherichia coli
15	-	trans-4-hydroxyproline	pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation	Escherichia coli
21	-	cis-4-hydroxyproline	pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation	Escherichia coli
70	-	L-proline	pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Saccharomyces cerevisiae
7	-	assay at	Methanothermobacter thermautotrophicus
7	-	assay at	Methanocaldococcus jannaschii
7	-	assay at	Methanococcus maripaludis

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli
ATP	-	Saccharomyces cerevisiae
ATP	-	Methanothermobacter thermautotrophicus
ATP	-	Methanocaldococcus jannaschii
ATP	-	Methanococcus maripaludis

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0000043	0.000088	5'-O-[N-(L-alanyl)-sulfamoyl]adenosine	ATP-diphosphate exchange reaction, pH 7.0, 37°C, recombinant wild-type enzyme	Escherichia coli

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Release 2023.1 (January 2023)