Information on EC 6.1.1.15 - Proline-tRNA ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
6.1.1.15
-
RECOMMENDED NAME
GeneOntology No.
Proline-tRNA ligase
PATHWAY
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
tRNA charging
-
SYSTEMATIC NAME
IUBMB Comments
L-Proline:tRNAPro ligase (AMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
class II prolyl-tRNA synthetase
-
-
class II prolyl-tRNA synthetase
-
-
class II prolyl-tRNA synthetase
-
-
class II ProRS
-
-
Global RNA synthesis factor
-
-
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
Global RNA synthesis factor
-
-
glutamyl-/prolyl-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Pro-tRNA synthetase
-
-
Proline translase
-
-
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline translase
-
-
Proline--tRNA ligase
-
-
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Proline--tRNA ligase
-
-
Prolyl RNA synthetase
-
-
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
Prolyl RNA synthetase
-
-
prolyl-cysteinyl-tRNA synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleate synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
-
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Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer ribonucleic acid synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-transfer RNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
Q831W7
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
-
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Prolyl-tRNA synthetase
-
-
Prolyl-tRNA synthetase
Q6N5P6
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Prolyl-tRNA synthetase
-
-
ProRS
-
-
-
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ProRS
Q831W7
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glutamyl-prolyl tRNA synthetase
-
-
additional information
-
cf. EC 6.1.1.17
CAS REGISTRY NUMBER
COMMENTARY
9055-68-9
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain K1
-
-
Manually annotated by BRENDA team
bacterial enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
bacterial enzyme type
-
-
Manually annotated by BRENDA team
class II enzyme, purified recombinant wild-type and mutant enzymes
-
-
Manually annotated by BRENDA team
strain 9723
-
-
Manually annotated by BRENDA team
wild-type enzyme and mutant enzymes C443A, C443G, and C443S
-
-
Manually annotated by BRENDA team
Escherichia coli 9723
strain 9723
-
-
Manually annotated by BRENDA team
enzyme with dual substrate specificity
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-
Manually annotated by BRENDA team
isoform glutamyl-prolyl-tRNA synthetase
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-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
enzyme with dual substrate specificity
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-
Manually annotated by BRENDA team
eukaryotic-like enzyme type
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-
Manually annotated by BRENDA team
prolyl-cysteinyl-tRNA synthetase, enzyme with dual specificity
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-
Manually annotated by BRENDA team
enzyme with dual substrate specificity
-
-
Manually annotated by BRENDA team
MuLV, produced in murine cells
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-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
purified multisynthetase complex, the enzyme is a bifunctional glutamyl-/prolyl-tRNA synthetase
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
bacterial enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
archaeal enzyme type
-
-
Manually annotated by BRENDA team
class IIa synthetase of the eukaryote/archaeon-like structure type
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-
Manually annotated by BRENDA team
enzyme with dual substrate specificity
-
-
Manually annotated by BRENDA team
strain HB8, purified class IIa enzyme
-
-
Manually annotated by BRENDA team
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
tRNA
-
stimulates l-cysteine activation 2-3fold
tRNACys
-
promotes the L-cysteine activation
additional information
-
activity is not affected by addition of diphosphate
-
additional information
-
a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0000043
0.000088
5'-O-[N-(L-alanyl)-sulfamoyl]adenosine
-
ATP-diphosphate exchange reaction, pH 7.0, 37C, recombinant wild-type enzyme
0.00005
-
prolyl-sulfamoyl-adenylate
-
versus L-proline, pH 7.5, 35C
0.000025
-
cysteinyl-sulfamoyl-adenylate
-
versus L-proline, pH 7.5, 35C
additional information
-
additional information
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
pH 6.0: about 30% of maximal activity, pH 9.0: about 40% of maximal activity
6.8
7.6
-
variation of the pH in this range has little effect on activity
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
even at 85C the enzyme retains its specificity towards its cognate substrate
PDB
SCOP
CATH
ORGANISM
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.8
-
90C, 30 min, enzyme contains considerable activity, no activity retained after exposure to 95C
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
-
-
complete loss of activity after 30 min, in absence of glycerol and mercaptoethanol
25
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, without stabilizing reagent
51
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, without stabilizing reagent
55
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP
56
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP
58
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.02 mM Pro
59
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.02 mM Pro
62
-
-
50% loss of activity after 5 min in Tris-HCl buffer
65
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, without stabilizing reagent
67
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP + 0.02 mM Pro
73
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP
78
-
-
50% loss of ATP-diphosphate exchange activity after 5 min, in presence of 0.002 mM ATP + 0.02 mM Pro
90
-
-
pH 6-7.8, 30 min, enzyme retains considerable activity
95
-
-
pH 6-7.8, 30 min, unstable
additional information
-
-
ATP, Pro and several Pro analogues prevent inactivation at 0C; inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2C; the enzyme from a number of higher plants that producing azetidine -2-carboxylic acid (A2C) is more rapidly inactivated in the cold than the enzyme from plants which do not contain A2C
additional information
-
-
at pH 6.5, 0.01 mM Mg2+ stabilizes against thermal inactivation; at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivation; bovine serum albumin and glycerol partially protect against thermal denaturation at 45C and 50C respectively; furan and tetrahydrothiophen, protect only in presence of ATP against thermal inactivation; mercaptoethanol or DTT stabilizes against heat inactivation; Pro or ATP markedly stabilizes against heat inactivation; several analogues of Pro protect against thermal inactivation
additional information
-
-
above 60C, little protection by bovine serum albumin and glycerol; at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivation; bovine serum albumin and glycerol partially protect against thermal denaturation at 45C and 50C respectively; furan and tetrahydrothiophen, protect only in presence of ATP against thermal inactivation; several analogues of Pro protect against thermal inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
at pH 6.5, 0.01 mM Mg2+ stabilizes against thermal inactivation
-
at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivation
-
ATP, Pro and several Pro analogues prevent inactivation at 0C
-
bovine serum albumin and glycerol partially protect against thermal denaturation at 45C and 50C respectively
-
furan and tetrahydrothiophen, only in presence of ATP protect against thermal inactivation
-
inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2C
-
L-azetidine-2-carboxylic acid, cis(exo)-3,4-methano-L-proline, 3,4-dehydro-DL-proline, L-thiazolidine-4-carboxylic acid, N-methylglycine, N-methyl-L-alanine or trans-3-hydroxy-L-proline protect against inactivation at 70C and 40C
-
mercaptoethanol or DTT stabilizes against heat inactivation
-
Pro or ATP markedly stabilizes against heat inactivation
-
rapid and reversible photoinactivation in absence of methylene blue. ATP or Pro protects
-
several analogues of Pro protect against thermal inactivation
-
the time taken for 4 M urea to reduced the activity by 50% is increased in presence of 15% glycerol from 0.7 min to 7 min and from 0.3 min to 1.5 min for the Phaseolus and Delonix enzymes respectively
-
Pro or ATP markedly stabilizes against heat inactivation
-
above 60C, little protection by bovine serum albumin and glycerol
-
at pH 8, in absence of Mg2+, ATP does not protect against thermal inactivation
-
ATP, Pro and several Pro analogues prevent inactivation at 0C
-
bovine serum albumin and glycerol partially protect against thermal denaturation at 45C and 50C respectively
-
furan and tetrahydrothiophen, only in presence of ATP protect against thermal inactivation
-
inclusion of a polyol together with the sulfhydryl-reducing reagent appears to synergistically enhance the stability on storage at 2C
-
L-azetidine-2-carboxylic acid, cis(exo)-3,4-methano-L-proline, 3,4-dehydro-DL-proline, L-thiazolidine-4-carboxylic acid, N-methylglycine, N-methyl-L-alanine or trans-3-hydroxy-L-proline protect against inactivation at 70C and 40C
-
photoinactivation in presence of methylene blue or rose bengal. Pro or several imino analogues protect, ATP is ineffective. In absence of methylene blue the enzyme is stable to light
-
Pro or ATP markedly stabilizes against heat inactivation
-
several analogues of Pro protect against thermal inactivation
-
the time taken for 4 M urea to reduced the activity by 50% is increased in presence of 15% glycerol from 0.7 min to 7 min and from 0.3 min to 1.5 min for the Phaseolus and Delonix enzymes respectively
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0.1 M Tris-maleate KOH buffer, pH 7.0, about 80% loss of activity in ATP-diphosphate exchange
-
0.1 M Tris-maleate KOH buffer, pH 8.0, about 85% loss of activity in ATP-diphosphate exchange
-
-20C, pH 6.8, 40% v/v glycerol, enzyme concentrated by ultrafiltration
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pharmacology
-
enzyme is a target for design of antibiotics targeting the editing active site since eukaryotic enzyme types are not able to edit misactivated alanine on tRNAPro
pharmacology
-
enzyme is a target for design of antibiotics targeting the active site since eukaryotic enzyme types are not able to edit misactivated alanine on tRNAPro