proof_lines: kcat is 0.10 sec(-1) for the aminoacylation reaction (at 25 degrees Celsius).


enzyme_display_name: proline--tRNA ligase

organism: Cytophaga hutchinsonii

substrate_name: L-cysteine

source_db: brenda

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

smiles: C(C(C(=O)O)N)S

data_origin: experimental

enzyme: proline--tRNA ligase

substrate: L-cysteine

source: brenda


substrate_name: L-proline

substrate: L-proline


organism: Methanocaldococcus jannaschii

sequence_source: multiple

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: ATP-diphosphate exchange reaction, pH 7.5, 35°C

source_databases_merged: brenda uniprot


kcat_over_km_origin: calculated

proof_lines: 60°C, pH not specified in the publication, ATP-diphosphate exchange assay


enzyme_display_name: glycine--tRNA ligase

organism: Homo sapiens

substrate_name: glycine

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

smiles: C(C(=O)O)N

proof_lines: kcat is 0.049 sec(-1) for aminoacylation of tRNA(Gly).

enzyme: glycine--tRNA ligase

substrate: glycine

source: uniprot


enzyme_display_name: histidine--tRNA ligase

organism: Neurospora crassa

substrate_name: His

enzyme: histidine--tRNA ligase

substrate: His


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


enzyme_display_name: phenylalanine--tRNA ligase

substrate_name: L-phenylalanine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R117G with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: phenylalanine--tRNA ligase

substrate: L-phenylalanine


organism: Saccharomyces cerevisiae

substrate_name: L-tyrosine

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G458S to reconstruct the assayed variant sequence.

substrate: L-tyrosine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A333G to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature G458A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G458A to reconstruct the assayed variant sequence.


enzyme_display_name: cysteine--tRNA ligase

organism: Escherichia coli (strain K12)

proof_lines: kcat is 79 sec(-1) with cysteine as substrate. kcat is 91 sec(-1) with ATP as substrate. kcat is 0.9 sec(-1) with tRNA(Cys) as substrate.

enzyme: cysteine--tRNA ligase


enzyme_display_name: arginine--tRNA ligase

organism: Canavalia ensiformis

substrate_name: L-canavanine

smiles: C(CON=C(N)N)C(C(=O)O)N

proof_lines: assay method, aminoacylation of [32P]-labelled transcript tRNA

enzyme: arginine--tRNA ligase

substrate: L-canavanine


organism: Escherichia coli

source_db: skid

source_license: CC BY 4.0; CC BY-NC-ND 4.0

source_databases_merged: skid uniprot

source: skid


assay_conditions_summary: pH 7

proof_lines: aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70°C


assay_conditions_summary: pH 7; cofactor ATP

proof_lines: aminoacylation reaction with L-proline, recombinant wild-type enzyme, pH 7.0, 70°C

proof_lines: aminoacylation reaction with L-cysteine, recombinant wild-type enzyme, pH 7.0, 70°C


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.3
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=37°C, pH=8.5


assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

proof_lines: kcat is 2.8 min(-1), 2.0 min(-1) and 3.1 min(-1) with L-phenylalanine, L-tyrosine and m-tyrosine as substrate, respectively. Thus, the catalytic efficiency of the m-Tyr attachment is only 5-fold lower than that of the correct amino acid, wh


substrate_name: DL-m-tyrosine

substrate: DL-m-tyrosine


organism: Aquifex aeolicus

substrate_name: L-Proline; ATP; tRNA(Pro)

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

substrate: L-Proline; ATP; tRNA(Pro)


organism: Borrelia burgdorferi

substrate_name: tRNA(Pro); L-Proline; ATP

substrate: tRNA(Pro); L-Proline; ATP


organism: Clostridium sticklandii


substrate_name: L-Proline; tRNA(Pro); ATP

substrate: L-Proline; tRNA(Pro); ATP


source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Beta vulgaris

substrate_name: L-Pro

substrate: L-Pro


organism: Staphylococcus aureus

proof_lines:
ATP-diphosphate exchange
glycyl-tRNA synthesis


substrate_name: Gly

substrate: Gly


organism: Acetoanaerobium sticklandii


source_db: oed

verification_status: unverified

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

status: unverified

source: oed


sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


substrate_name: L-Cysteine

substrate: L-Cysteine


organism: Deinococcus radiodurans


organism: Paramagnetospirillum magnetotacticum


organism: Methanothermobacter thermautotrophicus


organism: Novosphingobium aromaticivorans

substrate_name: ATP; L-Proline; tRNA(Pro)

substrate: ATP; L-Proline; tRNA(Pro)


organism: Rhodopseudomonas palustris


organism: Thermus thermophilus


organism: Astragalus bisulcatus

substrate_name: ATP; L-Cysteine; tRNA(Cys)

substrate: ATP; L-Cysteine; tRNA(Cys)


organism: Homo sapiens

substrate_name: tRNA(Cys)

substrate: tRNA(Cys)


substrate_name: L-arginine

smiles: C(CC(C(=O)O)N)CN=C(N)N

proof_lines: pH 7.5, 30°C, recombinant HIS-/thioredoxin-tagged enzyme

proof_lines: pH 7.5, 30°C, recombinant detagged enzyme

substrate: L-arginine


assay_conditions_summary: pH 7.5; cofactor ATP


substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-proline

substrate: L-proline


organism: Saccharomyces cerevisiae

substrate_name: L-tryptophan

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N412G/T415G/S418C/S437F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication

substrate: L-tryptophan


substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Oryctolagus cuniculus

substrate_name: tRNACys

substrate: tRNACys


enzyme_display_name: glutamate--tRNA ligase

organism: Bacillus subtilis

substrate_name: L-Glutamate; tRNA(Glu); ATP

enzyme: glutamate--tRNA ligase

substrate: L-Glutamate; tRNA(Glu); ATP


organism: Escherichia coli

substrate_name: tRNA(Glu); L-Glutamate; ATP

substrate: tRNA(Glu); L-Glutamate; ATP


substrate_name: tRNA(Glu)

substrate: tRNA(Glu)


organism: Mycobacterium tuberculosis

substrate_name: L-glutamate

source_license: CC BY-NC-ND 4.0

substrate: L-glutamate


organism: Thermosynechococcus elongatus

substrate_name: L-Glutamate; ATP; tRNA(Glu)

substrate: L-Glutamate; ATP; tRNA(Glu)


enzyme_display_name: glutamine--tRNA ligase

substrate_name: L-Glutamine; tRNA(Gln); ATP

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0

enzyme: glutamine--tRNA ligase

substrate: L-Glutamine; tRNA(Gln); ATP


substrate_name: tRNA(Arg); ATP; L-Arginine

substrate: tRNA(Arg); ATP; L-Arginine


organism: Mycolicibacterium smegmatis

substrate_name: tRNAArg

substrate: tRNAArg


substrate_name: ATP; L-Histidine; tRNA(His)

substrate: ATP; L-Histidine; tRNA(His)


substrate_name: Cys

substrate: Cys


substrate_name: 2-aminobutyric acid

smiles: CCC(C(=O)O)N

substrate: 2-aminobutyric acid


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y330C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: L-histidine

substrate: L-histidine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V155G to reconstruct the assayed variant sequence.


substrate_name: histidine

proof_lines: kcat is 5.4 sec(-1) for aminoacylation of tRNA(His) (PubMed:29235198). kcat is 4.1 sec(-1) for histidine. (PubMed:29235198). kcat is 5.8 sec(-1) for ATP (PubMed:29235198).

substrate: histidine


organism: Methanocaldococcus jannaschii

substrate_name: tRNAPro

substrate: tRNAPro


organism: Escherichia coli (strain K12)

substrate_name: tRNA(Cys)

substrate: tRNA(Cys)


organism: Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)

proof_lines: The catalytic activity of the enzyme increases with increasing salt concentrations and has its maximum at 3 M potassium chloride.


organism: Halobacterium sp.

substrate_name: tRNACys

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D435A/D436A with inferred residue-numbering offset -30 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 40°C, recombinant mutant D435A/D436A

substrate: tRNACys


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D417A/E420A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 40°C, recombinant mutant D417A/E420A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D239A/D240A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 40°C, recombinant mutant D239A/D240A


substrate_name: ATP; tRNA(Gly); Glycine

proof_lines: kcat is 0.049 sec(-1) for aminoacylation of tRNA(Gly).

substrate: ATP; tRNA(Gly); Glycine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: tRNA(Gly) (at 25 degrees Celsius)

proof_lines: kcat is 0.38 sec(-1) for the aminoacylation reaction (at 25 degrees Celsius).

substrate: tRNA(Gly) (at 25 degrees Celsius)


proof_lines: kcat is 0.10 sec(-1) for the aminoacylation reaction (at 25 degrees Celsius).


organism: Staphylococcus aureus

substrate_name: tRNAGly

substrate: tRNAGly


organism: Deinococcus radiodurans

substrate_name: ATP; L-Proline; tRNA(Pro)

proof_lines:
steady-state
single turnover overall aminoacylation
single turnover of the transfer step

substrate: ATP; L-Proline; tRNA(Pro)


mutation_signature: C-terminal deletion mutant

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: deletion

proof_lines: pH 7.0, 55°C, C-terminal deletion mutant


proof_lines: pH 7.5, 40°C, recombinant wild-type enzyme


organism: Vigna radiata var. radiata

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Canavalia ensiformis

substrate_name: tRNAArg(ACG)

proof_lines: tRNA from Escherichia coli, pH and temperature not specified in the publication

proof_lines: tRNA from Glycine max, pH and temperature not specified in the publication

substrate: tRNAArg(ACG)


organism: Cricetulus griseus

substrate_name: tRNA(Arg); L-Arginine; ATP

substrate: tRNA(Arg); L-Arginine; ATP


organism: Pyrococcus horikoshii

substrate_name: tRNAArg

substrate: tRNAArg


sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.


organism: Homo sapiens

substrate_name: tRNA(Phe)

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines: kcat is 2.8 min(-1), 2.0 min(-1) and 3.1 min(-1) with L-phenylalanine, L-tyrosine and m-tyrosine as substrate, respectively. Thus, the catalytic efficiency of the m-Tyr attachment is only 5-fold lower than that of the correct amino acid, wh

substrate: tRNA(Phe)


substrate_name: tRNAPhe

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T210M with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.

substrate: tRNAPhe


organism: Saccharomyces cerevisiae


organism: Caulobacter vibrioides

substrate_name: tRNAHis

proof_lines: wild-type Caulobacter crescentus tRNAHis, pH 7.5, 30°C

substrate: tRNAHis


substrate_name: ATP

substrate: ATP


substrate_name: tRNA(His)

substrate: tRNA(His)


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Y330C to reconstruct the assayed variant sequence.


organism: Neurospora crassa


organism: Salmonella typhimurium

substrate_name: tRNA(His); ATP; L-Histidine

substrate: tRNA(His); ATP; L-Histidine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C599Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C599Y/M222I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C599Y/Y506S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M222I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y506S to reconstruct the assayed variant sequence.


substrate_name: L-Arginine

substrate: L-Arginine


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R259K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R259Q to reconstruct the assayed variant sequence.


substrate_name: L-Histidine

substrate: L-Histidine


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00962 and applied mutation signature D66E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), ATP block, GlnRS row 'D66E'; column 'KM (uM)' = 134; column 'kcat (min^-1)' = 37.6; column 'kcat/KM (min^-1 uM^-1)' = 0.280.

raw_value_unit_evidence: Table 2, ATP block, GlnRS row 'D66E': KM = 134 uM; kcat = 37.6 min^-1; printed kcat/KM = 0.280 min^-1 uM^-1.

row_label: Table 2, ATP block, GlnRS row 'D66E'

table_label: Table 2: Aminoacylation Kinetics of GlnRS with Gln and ATP (Biochemistry 1998, 37(27):9836-9842)

status: corrected


sequence_variant_note: Mutation signature D66F matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00962 and applied mutation signature F233D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), ATP block, GlnRS row 'F233D'; column 'KM (uM)' = 538; column 'kcat (min^-1)' = 2.54; column 'kcat/KM (min^-1 uM^-1)' = 0.00472.

raw_value_unit_evidence: Table 2, ATP block, GlnRS row 'F233D': KM = 538 uM; kcat = 2.54 min^-1; printed kcat/KM = 0.00472 min^-1 uM^-1.

row_label: Table 2, ATP block, GlnRS row 'F233D'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F233L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00962 and applied mutation signature F233Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), ATP block, GlnRS row 'F233Y'; column 'KM (uM)' = 420; column 'kcat (min^-1)' = 148; column 'kcat/KM (min^-1 uM^-1)' = 0.352.

raw_value_unit_evidence: Table 2, ATP block, GlnRS row 'F233Y': KM = 420 uM; kcat = 148 min^-1; printed kcat/KM = 0.352 min^-1 uM^-1.

row_label: Table 2, ATP block, GlnRS row 'F233Y'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y211F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00962 and applied mutation signature Y211F/F233Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), ATP block, GlnRS row 'Y211F/F233Y'; column 'KM (uM)' = 246; column 'kcat (min^-1)' = 27.8; column 'kcat/KM (min^-1 uM^-1)' = 0.113.

raw_value_unit_evidence: Table 2, ATP block, GlnRS row 'Y211F/F233Y': KM = 246 uM; kcat = 27.8 min^-1; printed kcat/KM = 0.113 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00962 and applied mutation signature Y211L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), ATP block, GlnRS row 'Y211L'; column 'KM (uM)' = 315; column 'kcat (min^-1)' = 19.1; column 'kcat/KM (min^-1 uM^-1)' = 0.0606.

raw_value_unit_evidence: Table 2, ATP block, GlnRS row 'Y211L': KM = 315 uM; kcat = 19.1 min^-1; printed kcat/KM = 0.0606 min^-1 uM^-1.

row_label: Table 2, ATP block, GlnRS row 'Y211L'


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.


substrate_name: L-Glutamine

column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), Gln block, GlnRS row 'D66E'; column 'KM (uM)' = 2020; column 'kcat (min^-1)' = 42; column 'kcat/KM (min^-1 uM^-1)' = 0.0209.

raw_value_unit_evidence: Table 2, Gln block, GlnRS row 'D66E': KM = 2020 uM; kcat = 42 min^-1; printed kcat/KM = 0.0209 min^-1 uM^-1.

row_label: Table 2, Gln block, GlnRS row 'D66E'

substrate: L-Glutamine


sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), Gln block, GlnRS row 'F233D'; column 'KM (uM)' = 7760; column 'kcat (min^-1)' = 2.87; column 'kcat/KM (min^-1 uM^-1)' = 0.000370.

raw_value_unit_evidence: Table 2, Gln block, GlnRS row 'F233D': KM = 7760 uM; kcat = 2.87 min^-1; printed kcat/KM = 0.000370 min^-1 uM^-1.

row_label: Table 2, Gln block, GlnRS row 'F233D'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00962 and applied mutation signature F233L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), Gln block, GlnRS row 'F233L'; column 'KM (uM)' = 2210; column 'kcat (min^-1)' = 97.2; column 'kcat/KM (min^-1 uM^-1)' = 0.0439.

raw_value_unit_evidence: Table 2, Gln block, GlnRS row 'F233L': KM = 2210 uM; kcat = 97.2 min^-1; printed kcat/KM = 0.0439 min^-1 uM^-1.

row_label: Table 2, Gln block, GlnRS row 'F233L'


column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), Gln block, GlnRS row 'F233Y'; column 'KM (uM)' = 525; column 'kcat (min^-1)' = 181; column 'kcat/KM (min^-1 uM^-1)' = 0.345.

raw_value_unit_evidence: Table 2, Gln block, GlnRS row 'F233Y': KM = 525 uM; kcat = 181 min^-1; printed kcat/KM = 0.345 min^-1 uM^-1.

row_label: Table 2, Gln block, GlnRS row 'F233Y'


column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), Gln block, GlnRS row 'wild-type'; column 'KM (uM)' = 114; column 'kcat (min^-1)' = 157; column 'kcat/KM (min^-1 uM^-1)' = 1.38.

raw_value_unit_evidence: Table 2, Gln block, GlnRS row 'wild-type': KM = 114 uM; kcat = 157 min^-1; printed kcat/KM = 1.38 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00962 and applied mutation signature Y211F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), Gln block, GlnRS row 'Y211F'; column 'KM (uM)' = 7050; column 'kcat (min^-1)' = 88.7; column 'kcat/KM (min^-1 uM^-1)' = 0.0126.

raw_value_unit_evidence: Table 2, Gln block, GlnRS row 'Y211F': KM = 7050 uM; kcat = 88.7 min^-1; printed kcat/KM = 0.0126 min^-1 uM^-1.

row_label: Table 2, Gln block, GlnRS row 'Y211F'


column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), Gln block, GlnRS row 'Y211F/F233Y'; column 'KM (uM)' = 584; column 'kcat (min^-1)' = 33.1; column 'kcat/KM (min^-1 uM^-1)' = 0.0589.

raw_value_unit_evidence: Table 2, Gln block, GlnRS row 'Y211F/F233Y': KM = 584 uM; kcat = 33.1 min^-1; printed kcat/KM = 0.0589 min^-1 uM^-1.


column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), Gln block, GlnRS row 'Y211L'; column 'KM (uM)' = 118; column 'kcat (min^-1)' = 24.1; column 'kcat/KM (min^-1 uM^-1)' = 0.205.

raw_value_unit_evidence: Table 2, Gln block, GlnRS row 'Y211L': KM = 118 uM; kcat = 24.1 min^-1; printed kcat/KM = 0.205 min^-1 uM^-1.

row_label: Table 2, Gln block, GlnRS row 'Y211L'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00962 and applied mutation signature Y211S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Aminoacylation Kinetics of GlnRS with Gln and ATP), Gln block, GlnRS row 'Y211S'; column 'KM (uM)' = 6050; column 'kcat (min^-1)' = 4.92; column 'kcat/KM (min^-1 uM^-1)' = 0.000812.

raw_value_unit_evidence: Table 2, Gln block, GlnRS row 'Y211S': KM = 6050 uM; kcat = 4.92 min^-1; printed kcat/KM = 0.000812 min^-1 uM^-1.

row_label: Table 2, Gln block, GlnRS row 'Y211S'


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: arginine (ATP-PPi exchange at 37 degrees Celsius)


substrate_name: ATP (ATP-PPi exchange at 37 Celsius)

substrate: ATP (ATP-PPi exchange at 37 Celsius)


substrate_name: proline

substrate: proline


substrate_name: alanine

smiles: CC(C(=O)O)N

substrate: alanine


substrate_name: cysteine

substrate: cysteine


substrate_name: L-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E218A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

substrate: L-alanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G217A to reconstruct the assayed variant sequence.


substrate_name: L-proline

substrate: L-proline


substrate_name: DL-m-tyrosine

substrate: DL-m-tyrosine


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Methanothermobacter thermautotrophicus

substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-Cysteine

verification_status: verified

column_label: Primary JBC Table I, row M. thermautotrophicus / C, substrate code C (cysteine), columns Km mM, kcat s^-1, and kcat/Km.

raw_value_unit_evidence: Table I row M. thermautotrophicus / C: Km 0.05 mM; kcat 0.020 s^-1; kcat/Km 0.40

row_label: M. thermautotrophicus / C

table_label: Table I

substrate: L-Cysteine

status: verified


substrate_name: L-Proline

substrate: L-Proline


organism: Aquifex aeolicus

column_label: Table I, organism block A. aeolicus, substrate sub-row C, columns Km (mM), kcat (s^-1) and kcat/Km: 0.05, 0.090 and 1.80. All three cells sit in the same organism block and the same substrate sub-row, so kcat and Km form one tuple; no value is taken from a neighbouring row, column or cofactor block.

normalized_value_unit_evidence: Km 0.05 mM; kcat 0.090 s^-1; kcat/Km 1.8 s^-1 mM^-1, all read from the single Table I sub-row C of organism block A. aeolicus. Table I prints the kcat/Km cell for this row as 1.80, which decimal-matches the exported ratio.

raw_value_unit_evidence: Table I row "A. aeolicus", substrate sub-row C: Km 0.05 mM; kcat 0.090 s^-1; kcat/Km 1.80.

row_label: A. aeolicus | L-Cysteine

table_label: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes


column_label: Table I, organism block A. aeolicus, substrate sub-row P, columns Km (mM), kcat (s^-1) and kcat/Km: 0.06, 15 and 250. All three cells sit in the same organism block and the same substrate sub-row, so kcat and Km form one tuple; no value is taken from a neighbouring row, column or cofactor block.

normalized_value_unit_evidence: Km 0.06 mM; kcat 15 s^-1; kcat/Km 250.0 s^-1 mM^-1, all read from the single Table I sub-row P of organism block A. aeolicus. Table I prints the kcat/Km cell for this row as 250, which decimal-matches the exported ratio.

raw_value_unit_evidence: Table I row "A. aeolicus", substrate sub-row P: Km 0.06 mM; kcat 15 s^-1; kcat/Km 250.

row_label: A. aeolicus | L-Proline


organism: Borrelia burgdorferi

column_label: Table I, organism block B. burgdorferi, substrate sub-row C, columns Km (mM), kcat (s^-1) and kcat/Km: 0.18, 0.022 and 0.12. All three cells sit in the same organism block and the same substrate sub-row, so kcat and Km form one tuple; no value is taken from a neighbouring row, column or cofactor block.

normalized_value_unit_evidence: Km 0.18 mM; kcat 0.022 s^-1; kcat/Km 0.12222222222222222 s^-1 mM^-1, all read from the single Table I sub-row C of organism block B. burgdorferi. Table I prints the kcat/Km column for this row rounded to 0.12; the strict comparison uses the exact quotient of the same row's printed kcat (0.022 s^-1) and Km (0.18 mM) cells, which is the unrounded form of that same printed cell.

raw_value_unit_evidence: Table I row "B. burgdorferi", substrate sub-row C: Km 0.18 mM; kcat 0.022 s^-1; kcat/Km 0.12.

row_label: B. burgdorferi | L-Cysteine


column_label: Table I, organism block B. burgdorferi, substrate sub-row P, columns Km (mM), kcat (s^-1) and kcat/Km: 0.17, 5.8 and 34. All three cells sit in the same organism block and the same substrate sub-row, so kcat and Km form one tuple; no value is taken from a neighbouring row, column or cofactor block.

normalized_value_unit_evidence: Km 0.17 mM; kcat 5.8 s^-1; kcat/Km 34.11764705882353 s^-1 mM^-1, all read from the single Table I sub-row P of organism block B. burgdorferi. Table I prints the kcat/Km column for this row rounded to 34; the strict comparison uses the exact quotient of the same row's printed kcat (5.8 s^-1) and Km (0.17 mM) cells, which is the unrounded form of that same printed cell.

raw_value_unit_evidence: Table I row "B. burgdorferi", substrate sub-row P: Km 0.17 mM; kcat 5.8 s^-1; kcat/Km 34.

row_label: B. burgdorferi | L-Proline


organism: Clostridium sticklandii

column_label: Primary JBC Table I, row C. sticklandii / C, substrate code C (cysteine), columns Km mM, kcat s^-1, and kcat/Km.

raw_value_unit_evidence: Table I row C. sticklandii / C: Km 0.01 mM; kcat 0.390 s^-1; kcat/Km 39

row_label: C. sticklandii / C


column_label: Primary JBC Table I, row C. sticklandii / P, substrate code P (proline), columns Km mM, kcat s^-1, and kcat/Km.

raw_value_unit_evidence: Table I row C. sticklandii / P: Km 0.05 mM; kcat 60 s^-1; kcat/Km 1200

row_label: C. sticklandii / P


organism: Aquifex aeolicus (strain VF5)

substrate_name: proline (at 60 degrees Celsius)

substrate: proline (at 60 degrees Celsius)


substrate_name: cysteine (at 60 degrees Celsius)

substrate: cysteine (at 60 degrees Celsius)


organism: Cytophaga hutchinsonii

column_label: Table I, organism block C. hutchinsonii, substrate sub-row C, columns Km (mM), kcat (s^-1) and kcat/Km: 0.19, 0.083 and 0.44. All three cells sit in the same organism block and the same substrate sub-row, so kcat and Km form one tuple; no value is taken from a neighbouring row, column or cofactor block.

normalized_value_unit_evidence: Km 0.19 mM; kcat 0.083 s^-1; kcat/Km 0.4368421052631579 s^-1 mM^-1, all read from the single Table I sub-row C of organism block C. hutchinsonii. Table I prints the kcat/Km column for this row rounded to 0.44; the strict comparison uses the exact quotient of the same row's printed kcat (0.083 s^-1) and Km (0.19 mM) cells, which is the unrounded form of that same printed cell.

raw_value_unit_evidence: Table I row "C. hutchinsonii", substrate sub-row C: Km 0.19 mM; kcat 0.083 s^-1; kcat/Km 0.44.

row_label: C. hutchinsonii | L-Cysteine


column_label: Table I, organism block C. hutchinsonii, substrate sub-row P, columns Km (mM), kcat (s^-1) and kcat/Km: 0.08, 19 and 238. All three cells sit in the same organism block and the same substrate sub-row, so kcat and Km form one tuple; no value is taken from a neighbouring row, column or cofactor block.

normalized_value_unit_evidence: Km 0.08 mM; kcat 19 s^-1; kcat/Km 237.5 s^-1 mM^-1, all read from the single Table I sub-row P of organism block C. hutchinsonii. Table I prints the kcat/Km column for this row rounded to 238; the strict comparison uses the exact quotient of the same row's printed kcat (19 s^-1) and Km (0.08 mM) cells, which is the unrounded form of that same printed cell.

raw_value_unit_evidence: Table I row "C. hutchinsonii", substrate sub-row P: Km 0.08 mM; kcat 19 s^-1; kcat/Km 238.

row_label: C. hutchinsonii | L-Proline


organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)

column_label: Primary JBC Table I, row B. burgdorferi / P, substrate code P (proline), columns Km mM, kcat s^-1, and kcat/Km.

normalized_value_unit_evidence: Km 0.17 mM

raw_value_unit_evidence: Table I row B. burgdorferi / P: Km 0.17 mM; kcat 5.8 s^-1; kcat/Km 34

row_label: B. burgdorferi / P


column_label: Primary JBC Table I, row B. burgdorferi / C, substrate code C (cysteine), columns Km mM, kcat s^-1, and kcat/Km.

normalized_value_unit_evidence: Km 0.18 mM

raw_value_unit_evidence: Table I row B. burgdorferi / C: Km 0.18 mM; kcat 0.022 s^-1; kcat/Km 0.12

row_label: B. burgdorferi / C


organism: Deinococcus radiodurans


column_label: Table I, organism block D. radiodurans, substrate sub-row P, columns Km (mM), kcat (s^-1) and kcat/Km: 0.16, 32 and 200. All three cells sit in the same organism block and the same substrate sub-row, so kcat and Km form one tuple; no value is taken from a neighbouring row, column or cofactor block.

normalized_value_unit_evidence: Km 0.16 mM; kcat 32 s^-1; kcat/Km 200.0 s^-1 mM^-1, all read from the single Table I sub-row P of organism block D. radiodurans. Table I prints the kcat/Km cell for this row as 200, which decimal-matches the exported ratio.

raw_value_unit_evidence: Table I row "D. radiodurans", substrate sub-row P: Km 0.16 mM; kcat 32 s^-1; kcat/Km 200.

row_label: D. radiodurans | L-Proline


substrate_name: glycine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S581L with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

substrate: glycine


organism: Novosphingobium aromaticivorans

column_label: Table I, organism block N. aromaticivorans, substrate sub-row C, columns Km (mM), kcat (s^-1) and kcat/Km: 0.20, 0.065 and 0.33. All three cells sit in the same organism block and the same substrate sub-row, so kcat and Km form one tuple; no value is taken from a neighbouring row, column or cofactor block.

normalized_value_unit_evidence: Km 0.20 mM; kcat 0.065 s^-1; kcat/Km 0.325 s^-1 mM^-1, all read from the single Table I sub-row C of organism block N. aromaticivorans. Table I prints the kcat/Km column for this row rounded to 0.33; the strict comparison uses the exact quotient of the same row's printed kcat (0.065 s^-1) and Km (0.20 mM) cells, which is the unrounded form of that same printed cell.

raw_value_unit_evidence: Table I row "N. aromaticivorans", substrate sub-row C: Km 0.20 mM; kcat 0.065 s^-1; kcat/Km 0.33.

row_label: N. aromaticivorans | L-Cysteine


column_label: Table label: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes. Row: N. aromaticivorans / P (proline activation). Columns read: K M (mm) cell 0.14, k cat (s-1) cell 26, k cat /K M cell 186. metric: kcat; raw value: 26; raw unit: s^-1; normalized value: 26.0 s^(-1); metric: Km; raw value: 0.14; raw unit: mM; normalized value: 0.14 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 185.7142857142857 s^-1 mM^-1; assay condition: Proline activation kinetic parameters of Table I; individual kinetic parameters are based on three independent determinations with standard deviations from 3-10% (Table I footnote). The locally preserved Table I text does not print an assay temperature or pH. Export row conditions: pH 7.2; 310.15 K.

normalized_value_unit_evidence: Table I row N. aromaticivorans / P: kcat 26 s^-1 = 26.0 s^(-1) (no conversion; table prints s^-1); Km 0.14 mM = 0.14 mM (no conversion; table header prints the K M unit as mm, i.e. mM); kcat/Km derived from this row's own quoted cells: 26 s^-1 / 0.14 mM = 185.7142857142857 s^-1 mM^-1. The printed Table I kcat/Km cell for this row is 186; the quotient rounds to 186 at the printed cell's own precision, so the two agree and the difference is printed precision only. In the transcription the table is flattened to tab-separated text: superscripts are lost, the kcat header renders as `k cats-1` and the Km unit line as `mm`.

raw_value_unit_evidence: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes | header row: Source of proS / Domain b / ProRS c type / Length d (amino acid) / A e / K M mm / k cat s-1 / k cat /K M / P/C; the second header line repeats the units 'mm' under K M and 's-1' under k cat, so K M is printed in mM and k cat in s^-1, and k cat /K M is therefore in s^-1 mM^-1 | data rows for N. aromaticivorans (P row, then unlabeled-organism C row): `N. aromaticivorans B A 515 P 0.14 26 186 564` and continuation `C 0.20 0.065 0.33` | N. aromaticivorans / P cells read: K M = 0.14 mM; k cat = 26 s^-1; k cat /K M = 186 s^-1 mM^-1

row_label: N. aromaticivorans / P


organism: Methanocaldococcus jannaschii

column_label: Table label: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes. Row: M. jannaschii / C (cysteine activation). Columns read: K M (mm) cell 0.09, k cat (s-1) cell 0.190, k cat /K M cell 2.11. metric: kcat; raw value: 0.190; raw unit: s^-1; normalized value: 0.19 s^(-1); metric: Km; raw value: 0.09; raw unit: mM; normalized value: 0.09 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 2.111111111111111 s^-1 mM^-1; assay condition: Cysteine activation was measured in the presence of 1 mg/ml unfractionated tRNA; kinetic parameters are based on three independent determinations with standard deviations from 3-10% (Table I footnote). The locally preserved Table I text does not print an assay temperature or pH. Export row conditions: pH 7.2; 333.15 K.

normalized_value_unit_evidence: Table I row M. jannaschii / C: kcat 0.190 s^-1 = 0.19 s^(-1) (no conversion; table prints s^-1); Km 0.09 mM = 0.09 mM (no conversion; table header prints the K M unit as mm, i.e. mM); kcat/Km derived from this row's own quoted cells: 0.190 s^-1 / 0.09 mM = 2.111111111111111 s^-1 mM^-1. The printed Table I kcat/Km cell for this row is 2.11; the quotient rounds to 2.11 at the printed cell's own precision, so the two agree and the difference is printed precision only. In the transcription the table is flattened to tab-separated text: superscripts are lost, the kcat header renders as `k cats-1` and the Km unit line as `mm`, and the C rows carry empty leading cells so the row reads `C 0.09 0.190 2.11`.

raw_value_unit_evidence: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes | header row: Source of proS / Domain b / ProRS c type / Length d (amino acid) / A e / K M mm / k cat s-1 / k cat /K M / P/C; the second header line repeats the units 'mm' under K M and 's-1' under k cat, so K M is printed in mM and k cat in s^-1, and k cat /K M is therefore in s^-1 mM^-1 | data rows for M. jannaschii (P row, then unlabeled-organism C row): `M. jannaschii A A 455 P 0.28 63 225 107` and continuation `C 0.09 0.190 2.11` | M. jannaschii / C cells read: K M = 0.09 mM; k cat = 0.190 s^-1; k cat /K M = 2.11 s^-1 mM^-1; the trailing P/C column value belongs to the P row only

row_label: M. jannaschii / C


organism: Rhodopseudomonas palustris

column_label: Table label: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes. Row: R. palustris / C (cysteine activation). Columns read: K M (mm) cell 0.17, k cat (s-1) cell 0.025, k cat /K M cell 0.15. metric: kcat; raw value: 0.025; raw unit: s^-1; normalized value: 0.025 s^(-1); metric: Km; raw value: 0.17; raw unit: mM; normalized value: 0.17 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.14705882352941177 s^-1 mM^-1; assay condition: Cysteine activation was measured in the presence of 1 mg/ml unfractionated tRNA; kinetic parameters are based on three independent determinations with standard deviations from 3-10% (Table I footnote). The locally preserved Table I text does not print an assay temperature or pH. Export row conditions: pH 7.2; 310.15 K.

normalized_value_unit_evidence: Table I row R. palustris / C: kcat 0.025 s^-1 = 0.025 s^(-1) (no conversion; table prints s^-1); Km 0.17 mM = 0.17 mM (no conversion; table header prints the K M unit as mm, i.e. mM); kcat/Km derived from this row's own quoted cells: 0.025 s^-1 / 0.17 mM = 0.14705882352941177 s^-1 mM^-1. The printed Table I kcat/Km cell for this row is 0.15; the quotient rounds to 0.15 at the printed cell's own precision, so the two agree and the difference is printed precision only. In the transcription the table is flattened to tab-separated text: superscripts are lost, the kcat header renders as `k cats-1` and the Km unit line as `mm`, and the C rows carry empty leading cells so the row reads `C 0.17 0.025 0.15`.

raw_value_unit_evidence: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes | header row: Source of proS / Domain b / ProRS c type / Length d (amino acid) / A e / K M mm / k cat s-1 / k cat /K M / P/C; the second header line repeats the units 'mm' under K M and 's-1' under k cat, so K M is printed in mM and k cat in s^-1, and k cat /K M is therefore in s^-1 mM^-1 | data rows for R. palustris (P row, then unlabeled-organism C row): `R. palustris B B 438 P 0.28 14 50 333` and continuation `C 0.17 0.025 0.15` | R. palustris / C cells read: K M = 0.17 mM; k cat = 0.025 s^-1; k cat /K M = 0.15 s^-1 mM^-1; the trailing P/C column value belongs to the P row only

row_label: R. palustris / C


column_label: Table label: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes. Row: R. palustris / P (proline activation). Columns read: K M (mm) cell 0.28, k cat (s-1) cell 14, k cat /K M cell 50. metric: kcat; raw value: 14; raw unit: s^-1; normalized value: 14.0 s^(-1); metric: Km; raw value: 0.28; raw unit: mM; normalized value: 0.28 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 49.99999999999999 s^-1 mM^-1; assay condition: Proline activation kinetic parameters of Table I; individual kinetic parameters are based on three independent determinations with standard deviations from 3-10% (Table I footnote). The locally preserved Table I text does not print an assay temperature or pH. Export row conditions: pH 7.2; 310.15 K.

normalized_value_unit_evidence: Table I row R. palustris / P: kcat 14 s^-1 = 14.0 s^(-1) (no conversion; table prints s^-1); Km 0.28 mM = 0.28 mM (no conversion; table header prints the K M unit as mm, i.e. mM); kcat/Km derived from this row's own quoted cells: 14 s^-1 / 0.28 mM = 49.99999999999999 s^-1 mM^-1. The printed Table I kcat/Km cell for this row is 50; the quotient rounds to 50 at the printed cell's own precision, so the two agree and the difference is printed precision only. In the transcription the table is flattened to tab-separated text: superscripts are lost, the kcat header renders as `k cats-1` and the Km unit line as `mm`.

raw_value_unit_evidence: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes | header row: Source of proS / Domain b / ProRS c type / Length d (amino acid) / A e / K M mm / k cat s-1 / k cat /K M / P/C; the second header line repeats the units 'mm' under K M and 's-1' under k cat, so K M is printed in mM and k cat in s^-1, and k cat /K M is therefore in s^-1 mM^-1 | data rows for R. palustris (P row, then unlabeled-organism C row): `R. palustris B B 438 P 0.28 14 50 333` and continuation `C 0.17 0.025 0.15` | R. palustris / P cells read: K M = 0.28 mM; k cat = 14 s^-1; k cat /K M = 50 s^-1 mM^-1

row_label: R. palustris / P


organism: Oryctolagus cuniculus


substrate_name: ATP

substrate: ATP


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)


organism: Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)


substrate_name: L-Glutamate

substrate: L-Glutamate


organism: Thermus thermophilus

column_label: Table label: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes. Row: T. thermophilus / C (cysteine activation). Columns read: K M (mm) cell 0.02, k cat (s-1) cell 0.042, k cat /K M cell 2.10. metric: kcat; raw value: 0.042; raw unit: s^-1; normalized value: 0.042 s^(-1); metric: Km; raw value: 0.02; raw unit: mM; normalized value: 0.02 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 2.1 s^-1 mM^-1; assay condition: Cysteine activation was measured in the presence of 1 mg/ml unfractionated tRNA; kinetic parameters are based on three independent determinations with standard deviations from 3-10% (Table I footnote). The locally preserved Table I text does not print an assay temperature or pH. Export row conditions: pH 7.2; 333.15 K.

normalized_value_unit_evidence: Table I row T. thermophilus / C: kcat 0.042 s^-1 = 0.042 s^(-1) (no conversion; table prints s^-1); Km 0.02 mM = 0.02 mM (no conversion; table header prints the K M unit as mm, i.e. mM); kcat/Km printed cell 2.10 = 2.1 s^-1 mM^-1, which equals this row's own quotient 0.042 s^-1 / 0.02 mM. In the transcription the table is flattened to tab-separated text: superscripts are lost, the kcat header renders as `k cats-1` and the Km unit line as `mm`, and the C rows carry empty leading cells so the row reads `C 0.02 0.042 2.10`.

raw_value_unit_evidence: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes | header row: Source of proS / Domain b / ProRS c type / Length d (amino acid) / A e / K M mm / k cat s-1 / k cat /K M / P/C; the second header line repeats the units 'mm' under K M and 's-1' under k cat, so K M is printed in mM and k cat in s^-1, and k cat /K M is therefore in s^-1 mM^-1 | data rows for T. thermophilus (P row, then unlabeled-organism C row): `T. thermophilus B A 477 P 0.15 35 233 111` and continuation `C 0.02 0.042 2.10` | T. thermophilus / C cells read: K M = 0.02 mM; k cat = 0.042 s^-1; k cat /K M = 2.10 s^-1 mM^-1; the trailing P/C column value belongs to the P row only

row_label: T. thermophilus / C


column_label: Table label: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes. Row: T. thermophilus / P (proline activation). Columns read: K M (mm) cell 0.15, k cat (s-1) cell 35, k cat /K M cell 233. metric: kcat; raw value: 35; raw unit: s^-1; normalized value: 35.0 s^(-1); metric: Km; raw value: 0.15; raw unit: mM; normalized value: 0.15 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 233.33333333333334 s^-1 mM^-1; assay condition: Proline activation kinetic parameters of Table I; individual kinetic parameters are based on three independent determinations with standard deviations from 3-10% (Table I footnote). The locally preserved Table I text does not print an assay temperature or pH. Export row conditions: pH 7.2; 333.15 K.

normalized_value_unit_evidence: Table I row T. thermophilus / P: kcat 35 s^-1 = 35.0 s^(-1) (no conversion; table prints s^-1); Km 0.15 mM = 0.15 mM (no conversion; table header prints the K M unit as mm, i.e. mM); kcat/Km derived from this row's own quoted cells: 35 s^-1 / 0.15 mM = 233.33333333333334 s^-1 mM^-1. The printed Table I kcat/Km cell for this row is 233; the quotient rounds to 233 at the printed cell's own precision, so the two agree and the difference is printed precision only. In the transcription the table is flattened to tab-separated text: superscripts are lost, the kcat header renders as `k cats-1` and the Km unit line as `mm`.

raw_value_unit_evidence: Table I. Properties and kinetic parameters for proline and cysteine activation of various ProRS enzymes | header row: Source of proS / Domain b / ProRS c type / Length d (amino acid) / A e / K M mm / k cat s-1 / k cat /K M / P/C; the second header line repeats the units 'mm' under K M and 's-1' under k cat, so K M is printed in mM and k cat in s^-1, and k cat /K M is therefore in s^-1 mM^-1 | data rows for T. thermophilus (P row, then unlabeled-organism C row): `T. thermophilus B A 477 P 0.15 35 233 111` and continuation `C 0.02 0.042 2.10` | T. thermophilus / P cells read: K M = 0.15 mM; k cat = 35 s^-1; k cat /K M = 233 s^-1 mM^-1

row_label: T. thermophilus / P


organism: Methanococcus maripaludis


organism: Homo sapiens

substrate_name: L-Phenylalanine

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.

substrate: L-Phenylalanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R117G with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)


organism: Mycolicibacterium smegmatis

substrate_name: Arg

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

assay_conditions_summary: 310.15 K; cofactor ATP

column_label: Downloaded OUP/JB PDF states the apparent Km at 37 C for arginine was 0.6 uM and Table II lists M. smegmatis SN2 Km(Arg)=0.6 uM.

normalized_value_unit_evidence: Km normalized_value=0.0006 normalized_unit=mM from 0.6 uM.

raw_value_unit_evidence: Text and Table II report Km(Arg) raw_value=0.6 raw_unit=uM for M. smegmatis SN2.

row_label: M. smegmatis SN2 arginyl-tRNA synthetase

table_label: PDF Table II and adjacent kinetic text

substrate: Arg


substrate_name: tubercidin 5'-triphosphate

substrate: tubercidin 5'-triphosphate


organism: Escherichia coli (strain K12)

substrate_name: Glu

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature C100Y to reconstruct the assayed variant sequence.

smiles: C(CC(=O)O)C(C(=O)O)N

substrate: Glu


organism: Escherichia coli

substrate_name: Alanine

substrate: Alanine


sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines: mutant enzyme H40A/R42A, pH and temperature not specified in the publication


proof_lines: mutant enzyme H40A, pH and temperature not specified in the publication


proof_lines: mutant enzyme M294A/R427A, pH and temperature not specified in the publication


proof_lines: mutant enzyme R427A, pH and temperature not specified in the publication


proof_lines: mutant enzyme E354Q, pH and temperature not specified in the publication


proof_lines: mutant enzyme M294A/H297A, pH and temperature not specified in the publication


proof_lines: mutant enzyme M294A, pH and temperature not specified in the publication


proof_lines: mutant enzyme H297A, pH and temperature not specified in the publication


proof_lines: mutant enzyme E354Q/R427A, pH and temperature not specified in the publication


proof_lines: mutant enzyme R42A, pH and temperature not specified in the publication


sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: wild type enzyme, pH and temperature not specified in the publication

proof_lines: ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme


substrate_name: L-glutamine

smiles: C(CC(=O)N)C(C(=O)O)N

substrate: L-glutamine


mutation_signature: truncated mutant

mutation_type: truncation


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: L-Phe

proof_lines: mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit

substrate: L-Phe


proof_lines:
wild-type enzyme
wild-type EcPheRS


proof_lines: mutant enzyme with A294G mutation in alpha-subunit


proof_lines: mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit


proof_lines: mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit


proof_lines: mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit


proof_lines: mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit


column_label: Primary JBC Table I, row E. coli / C, columns Km mM, kcat s^-1, and kcat/Km.

normalized_value_unit_evidence: Km 0.17 mM and kcat 0.022 s^-1 match; explicit table kcat/Km is 0.13 s^-1*mM^-1, not the exported recomputed 0.12941176470588234.

raw_value_unit_evidence: Table I row E. coli / C: Km 0.17 mM; kcat 0.022 s^-1; kcat/Km 0.13.

row_label: E. coli / C


substrate_name: His

proof_lines: mutant enzyme form V-HisRS-R259K, aminoacylation

proof_lines: mutant enzyme form V-HisRS, mutant enzyme form V-His-RS-R259K, aminoacylation

substrate: His


proof_lines: mutant enzyme form des(A2-G10)-HisRS, ATP-diphosphate exchange

proof_lines: enzyme form with N-terminal addition of valine V-HisRS, mutant enzyme form des(A2-Q6)-HisRS, ATP-diphosphate exchange

proof_lines: mutant enzyme form des(A2-Q6), ATP-diphosphate exchange


proof_lines: mutant enzyme form V-HisRS-R259Q, ATP-diphosphate exchange


proof_lines: mutant enzyme form des(A2-G10)-HisRS, aminoacylation

proof_lines: mutant enzyme form des(A2-Q6)-HisRS, aminoacylation, ATP, and mutant enzyme form with N-terminal addition of methionine M-HisRS, ATP-diphosphate exchange

proof_lines: mutant enzyme form M-HisRS, aminoacylation


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: enzyme form with N-terminal addition of methionine M-HisRS, enzyme form with N-terminal addition of valineV-HisRS, aminoacylation


proof_lines: wild-type HisRS, ATP-diphosphate exchange


proof_lines:
HisRS, ATP-diphosphate exchange
pH 8.0, 37°C, diphosphate exchange


proof_lines: mutant enzyme form V-HisRS-R259K, ATP-diphosphate exchange


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C100Y with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


substrate_name: tRNAPro

proof_lines: pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation

substrate: tRNAPro


proof_lines: pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation


proof_lines: pH 7.0, 37°C, recombinant wild-type enzyme, aminoacylation

proof_lines: ATP-diphosphate exchange reaction, pH 7.0, 37°C, recombinant wild-type enzyme


substrate_name: L-alanine

proof_lines: pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation

substrate: L-alanine


substrate_name: L-proline

substrate: L-proline


organism: Bombyx mori

substrate_name: Gly

substrate: Gly


mutation_signature: N55-truncation mutant


substrate_name: tRNAGly

mutation_signature: N55-truncation mutant enzyme

substrate: tRNAGly


substrate_name: tRNAArg

substrate: tRNAArg


substrate_name: ATP

substrate: ATP


proof_lines: wild-type enzyme, ATP-diphosphate exchange


substrate_name: Pro

substrate: Pro


proof_lines: mutant enzyme F415A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C


proof_lines: mutant enzyme N305A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C


proof_lines: mutant enzyme E234A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C


proof_lines: mutant enzyme D198A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C


proof_lines: mutant enzyme H302A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C


proof_lines: mutant enzyme H302A/G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C


proof_lines: mutant enzyme G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C


proof_lines: mutant enzyme K297E/E303K, at pH 7.5 and 22°C


proof_lines: wild type enzyme, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C


substrate_name: tRNAHis

substrate: tRNAHis


substrate_name: L-histidine

substrate: L-histidine


proof_lines: 37°C, pH 7.5, arginylation, full-length enzyme


substrate_name: L-arginine

substrate: L-arginine


mutation_signature: Δ1

proof_lines: 37°C, pH 7.5, arginylation, mutant enzyme DELTA1-72


organism: Phaseolus vulgaris

substrate_name: L-Pro

substrate: L-Pro


substrate_name: L-azetidine-2-carboxylic acid

substrate: L-azetidine-2-carboxylic acid


substrate_name: thiazolidine-4-carboxylic acid

substrate: thiazolidine-4-carboxylic acid


substrate_name: N-methylglycine

smiles: CNCC(=O)O

substrate: N-methylglycine


substrate_name: N-Methyl-L-alanine

smiles: CC(C(=O)O)NC

substrate: N-Methyl-L-alanine


organism: Plasmodium falciparum

substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: Unknown

substrate: Unknown


substrate_name: tRNAPhe

substrate: tRNAPhe


proof_lines:
wild type enzyme, at pH 8.5 and 37°C
wild type enzyme, at pH 7.5 and 37°C


organism: Methanosarcina mazei

proof_lines: value above, substrate tRNA3Cys isoacceptor 3

proof_lines: value above, substrate tRNA2Cys isoacceptor 2

proof_lines: value above, substrate tRNA1Cys isoacceptor 1


proof_lines: value above, substrate tRNA3Cys isoacceptor 3, containing a U33A mutation

proof_lines: value above, substrate tRNA1Cys isoacceptor 1, containing a A33U mutation


proof_lines: value above, substrate tRNA3Cys isoacceptor 3, containing a G57A mutation


proof_lines: value above, substrate tRNA3Cys isoacceptor 3, containing a C20U/U21C/A44U/C46A/A47G mutation


proof_lines: value above, substrate tRNA3Cys isoacceptor 3, containing a C20U/U21C/A44U/C46A/A47G/G57A mutation


substrate_name: synthetic tRNAHis A-1

substrate: synthetic tRNAHis A-1


proof_lines:
7.5, 37°C, wild-type enzyme
wild-type, pH 7.5, 37°C


substrate_name: tRNACys

proof_lines: mutant enzyme N351D, mutant tRNACys(G15-C48)

substrate: tRNACys


proof_lines: mutant enzyme E354A, mutant tRNACys(G15-C48)


proof_lines: mutant enzyme E354Q, mutant tRNACys(G15-C48)


proof_lines: mutant enzyme N351D, wild-type tRNACys(G15-G48)

proof_lines: mutant enzyme E354A, wild-type tRNACys(G15-G48)

proof_lines: mutant enzyme E354Q, wild-type tRNACys(G15-G48)


proof_lines: mutant enzyme N351A, mutant tRNACys(G15-C48)


substrate_name: L-cysteine

substrate: L-cysteine


proof_lines: pH 8.0, wild-type enzyme, ATP-diphosphate exchange

proof_lines: ATP-diphosphate exchange reaction, recombinant His-tagged Co2+-wild-type enzyme


proof_lines: tuncated enzyme form NcatHisRS, aminoacylation


mutation_signature: truncated enzyme form NcatHisRS / aminoacylation truncated enzyme form NcatHisRS

proof_lines: truncated enzyme form NcatHisRS, aminoacylation


mutation_signature: truncated enzyme form NcatHisRS / ATP-diphosphate exchange truncated enzyme form NcatHisRS

proof_lines: truncated enzyme form NcatHisRS, ATP-diphosphate exchange


substrate_name: His

substrate: His


substrate_name: ATP

proof_lines: wild-type HisRS, ATP-diphosphate exchange

substrate: ATP


proof_lines: aminoacylation reaction, recombinant C28S/C209S mutant enzyme


proof_lines: aminoacylation reaction, recombinant W205Y mutant enzyme


proof_lines: ATP-diphosphate exchange reaction, recombinant W205Y mutant enzyme


substrate_name: L-glutamine

substrate: L-glutamine


proof_lines: pH 7.2, 37°C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae

proof_lines: pH 7.2, 37°C, full-length PheRSA294G, substrate from Escherichia coli


mutation_signature: truncated mutant PheRSDELTAB2A294G

proof_lines: pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae

proof_lines: pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli


proof_lines: pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G


substrate_name: tRNAHis

substrate: tRNAHis


substrate_name: tRNAGln

substrate: tRNAGln


proof_lines: recombinant wild-type enzyme, pH 7.2, 37°C


substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-proline

substrate: L-proline


proof_lines: mutant enzyme E218A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C


mutation_signature: recombinant His-tagged deletion mutant

proof_lines: recombinant His-tagged deletion mutant, amino acid activation step


proof_lines: recombinant His-tagged wild-type full-length enzyme, amino acid activation step


organism: Methanosarcina barkeri

substrate_name: 2-Chloroadenosine 5'-triphosphate

substrate: 2-Chloroadenosine 5'-triphosphate


substrate_name: N6-methyladenosine 5'-triphosphate

substrate: N6-methyladenosine 5'-triphosphate


substrate_name: 3'-Deoxyadenosine 5'-triphosphate

substrate: 3'-Deoxyadenosine 5'-triphosphate


organism: Saccharomyces cerevisiae

mutation_signature: full-length enzyme and truncated enzyme full-length enzyme and truncated enzyme


substrate_name: Gln

mutation_signature: truncated enzyme truncated enzyme

substrate: Gln


organism: Cricetulus griseus

substrate_name: L-arginine

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines: ATP-diphosphate exchange reaction, pH 8, 25°C

proof_lines: ATP-diphosphate exchange reaction, pH 8, 37°C

substrate: L-arginine


substrate_name: tRNAArg

proof_lines:
aminoacylation reaction, pH 8, 25°C
aminoacylation reaction, pH 8, 37°C

substrate: tRNAArg


proof_lines:
pH 7.4, 37°C
aminoacylation reaction
aminoacylation


substrate_name: L-glutamate

substrate: L-glutamate


proof_lines:
pH 7.5, 22°C, wild-type enzyme
wild-type enzyme, strain UT172
wild-type tRNAGln


substrate_name: Arg

proof_lines: 2'-deoxyadenosine 5'-triphosphate, , aminoacylation

substrate: Arg


proof_lines: aminoacylation and ATP-diphosphate exchange, mutant enzyme


substrate_name: tRNAGly

proof_lines:
glycyl-tRNA formation
native substrate from E. coli
native substrate from yeast

substrate: tRNAGly


proof_lines: ATP, , ATP-diphosphate exchange, without tRNA

proof_lines: ATP-diphosphate exchange in presence of tRNA


substrate_name: Gly

substrate: Gly


substrate_name: tubercidin 5'-triphosphate

proof_lines: tubercidine 5'-triphosphate, , aminoacylation

proof_lines: 3'-methoxyadenosine 5'-triphosphate, , NTP-diphosphate exchange

substrate: tubercidin 5'-triphosphate


substrate_name: 2'-deoxyadenosine 5'-triphosphate

substrate: 2'-deoxyadenosine 5'-triphosphate


substrate_name: selenocysteine

smiles: C(C(C(=O)O)N)[SeH]

substrate: selenocysteine


substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-tyrosine

proof_lines: mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C

proof_lines: cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C

substrate: L-tyrosine


substrate_name: DL-m-tyrosine

substrate: DL-m-tyrosine


substrate_name: L-proline

substrate: L-proline


proof_lines: recombinant wild-type enzyme, pH 7.0, 37°C


organism: Pseudomonas aeruginosa

substrate_name: tRNAPhe

proof_lines:
at pH 7.5 and 37°C
at pH 7.5 and 37?

substrate: tRNAPhe


substrate_name: ATP

substrate: ATP


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: tRNAPro

substrate: tRNAPro


substrate_name: tRNAHis

substrate: tRNAHis


substrate_name: L-histidine

substrate: L-histidine


organism: Gallus gallus

proof_lines: substrate from calf liver, , mitochondrial, aminoacylation


substrate_name: Phe

proof_lines:
mitochondrial, aminoacylation
cytoplasmic, aminoacylation
mitochondrial, ATP-diphosphate exchange

substrate: Phe


proof_lines:
aminoacylation
mitochondrial
ATP, , cytoplasmic, aminoacylation


organism: Rattus norvegicus

substrate_name: Arg

proof_lines:
complexed enzyme
free enzyme

substrate: Arg


substrate_name: tRNAArg

proof_lines:
free enzyme
complexed enzyme

substrate: tRNAArg


substrate_name: RNA microhelix

substrate: RNA microhelix


substrate_name: Pro

substrate: Pro


substrate_name: gamma-thiaproline

substrate: gamma-thiaproline


substrate_name: Cys

substrate: Cys


substrate_name: diphosphate

substrate: diphosphate


mutation_signature: truncated DELTANhcArgRS / truncated DELTANhcArgRS

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

proof_lines: pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, presence of hemin, Escherichia coli tRNAArg

proof_lines: pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, absence of hemin, Escherichia coli tRNAArg


proof_lines: pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, presence of hemin

proof_lines: pH 7.5, 37°C, recombinant, truncated DELTANhcArgRS, absence of hemin


substrate_name: L-arginine

substrate: L-arginine


substrate_name: His

proof_lines:
peptite mutant EB2 mitochondrial enzyme
petite mutant EB2 cytoplasmic enzyme

substrate: His


proof_lines:
wild-type mitochondrial enzyme
wild-type cytoplasmic enzyme


proof_lines:
cytoplasmic
ATP, , mitochondrial, aminoacylation
mitochondrial


substrate_name: 2'-deoxyadenosine 5'-triphosphate

substrate: 2'-deoxyadenosine 5'-triphosphate


substrate_name: 3'-Deoxyadenosine 5'-triphosphate

substrate: 3'-Deoxyadenosine 5'-triphosphate


substrate_name: L-tyrosine

proof_lines:
wild-type mtPheRS
wild-type ctPheRS

substrate: L-tyrosine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Salmonella enterica subsp. enterica serovar Typhimurium


substrate_name: ATP

substrate: ATP


substrate_name: tRNAGly

substrate: tRNAGly


substrate_name: Gly

substrate: Gly


organism: Streptococcus pneumoniae

substrate_name: tRNAPhe

proof_lines:
at pH 7.5 and 37°C
at pH 7.5 and 37?
larger than 0.064

substrate: tRNAPhe


organism: Borreliella burgdorferi

substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-proline

substrate: L-proline


organism: Saccharomyces pastorianus

substrate_name: tRNAArgIII

proof_lines:
aminoacylation
Arg, , ATP-diphosphate exchange

substrate: tRNAArgIII


substrate_name: Arg

substrate: Arg


organism: Vigna radiata var. radiata

substrate_name: selenocysteine

substrate: selenocysteine


substrate_name: Cys

substrate: Cys


substrate_name: 2-aminobutyric acid

substrate: 2-aminobutyric acid


organism: Cricetulus sp.

substrate_name: tRNAArg

proof_lines: 25°C, pH 7.5, native tRNAArg from beef liver, wild type enzyme

substrate: tRNAArg


proof_lines: 25°C, pH 7.5, native tRNAArg from beef liver, mutant enzyme DELTA1-73


organism: Escherichia coli

proof_lines: ATP, , 56000 MW subunit and 46000 MW subunit


substrate_name: Glu

proof_lines:
56000 MW subunit and 46000 MW subunit
56000 MW subunit alone

substrate: Glu


proof_lines: 3-thiaproline, , ATP-diphosphate exchange


organism: Thermus thermophilus

substrate_name: tRNAGlu

assay_conditions_summary: pH 7.5; 338.15 K; cofactor ATP

proof_lines:
substrate from E. coli
substrate from Thermus thermophilus
pH 7.5, 65°C

substrate: tRNAGlu


substrate_name: L-Glu

substrate: L-Glu


substrate_name: 2'-deoxyadenosine 5'-triphosphate

substrate: 2'-deoxyadenosine 5'-triphosphate


organism: Glycine max

substrate_name: L-arginine

proof_lines: assay method, aminoacylation of transcript tRNA with [14C]-labelled amino acid

proof_lines: assay method, aminoacylation of [32P]-labelled transcript tRNA

substrate: L-arginine


substrate_name: L-canavanine

substrate: L-canavanine


organism: Geobacillus stearothermophilus

proof_lines: substrate from E. coli, , ATP-diphosphate exchange, pH 6.0


substrate_name: Phe

substrate: Phe


substrate_name: ATP

substrate: ATP


organism: Methanothermobacter thermautotrophicus

assay_conditions_summary: pH 7.2; 333.15 K; cofactor ATP

proof_lines:
recombinant enzyme, pH 7.2, 60°C
ATP-diphosphate exchange, pH 7.5, 35°C


proof_lines: presence of bovine serum albumine and leucyl-tRNA synthetase, 50°C, pH 7.5

proof_lines: ATP-diphosphate exchange reaction, pH 7.5, 35°C


organism: Homo sapiens

substrate_name: L-alanine

substrate: L-alanine


organism: Mus musculus


substrate_name: Unknown

substrate: Unknown


organism: Oryctolagus cuniculus

substrate_name: tRNAHisII

proof_lines: unfractionated substrate from rabbit liver or rabbit reticulocyte tRNAHisI

substrate: tRNAHisII


substrate_name: L-His

assay_conditions_summary: cofactor ATP

substrate: L-His


organism: Phaseolus vulgaris


column_label: ACS full text Results prose reports the ordered enzyme forms hcArgRS and DeltaNhcArgRS with ordered kcat values 0.36 and 0.8 s^-1; hcArgRS maps to 0.36 s^-1.

raw_value_unit_evidence: kcat raw_value=0.36 raw_unit=s^-1

row_label: hcArgRS aminoacylation activity prose

table_label: ACS full text Results prose


sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.

proof_lines: mutant enzyme DELTANhcArgRS, in 50 mM Tris-HCl (pH 7.5)


organism: Plasmodium falciparum

substrate_name: tRNAGln

proof_lines: in the presence of diphosphatase, in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C

substrate: tRNAGln


proof_lines: in 100 mM HEPES-KOH, pH 7.2, 30 mM KOH, 12 mM MgCl2, 2 mM dithiothreitol, at 37°C


organism: Rhodopseudomonas palustris

substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-proline

substrate: L-proline


organism: Saccharomyces cerevisiae


enzyme_display_name: threonine--tRNA ligase

substrate_name: tRNAThr

proof_lines:
pH 7.2, 37°C, tRNAThr1(G-1), MST1
pH 8.5, 30°C, recombinant enzyme
pH 7.2, 37°C, tRNAThr2, MST1

enzyme: threonine--tRNA ligase

substrate: tRNAThr


substrate_name: tRNAHis

substrate: tRNAHis


substrate_name: tRNAGly

proof_lines: wild type isoform GlyRS1 without insertion peptide, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

proof_lines: wild type isoform GlyRS1, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

proof_lines: wild type isoform GlyRS2, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

substrate: tRNAGly


substrate_name: glycine

proof_lines: wild type isoform GlyRS1(KMM1), in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

proof_lines: wild type isoform GlyRS1 without K motif, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

substrate: glycine


proof_lines: pH and temperature not specified in the publication


substrate_name: L-glutamine

substrate: L-glutamine


proof_lines:
at pH 7.5 and 37°C
substrate from yeast, , aminoacylation
substrate from yeast


substrate_name: L-phenylalanine

proof_lines:
at pH 7.5 and 37°C
pH 7.2, 37°C, mitochondrial enzyme
pH 7.2, 37°C, cytosolic enzyme

substrate: L-phenylalanine


substrate_name: tubercidin 5'-triphosphate

proof_lines: formycin 5'-triphosphate, 2'-deoxyadenosine 5'-triphosphate, 3'-O-methyladenosine 5'-triphosphate

substrate: tubercidin 5'-triphosphate


proof_lines:
2'-O-methyladenosine 5'-triphosphate
aminoacylation
ATP-diphosphate exchange


enzyme_display_name: UniProt Q8PWY1

organism: Methanosarcina mazei

substrate_name: N-acetyl-L-lysine

smiles: CC(=O)NC(CCCCN)C(=O)O

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=and

enzyme: UniProt Q8PWY1

substrate: N-acetyl-L-lysine


organism: Staphylococcus aureus

proof_lines:
recombinant enzyme, pH 7.9, 22°C
native enzyme, pH 7.9, 22°C


assay_conditions_summary: pH 7.9; 295.15 K; cofactor ATP


substrate_name: tRNAGlu mutant C36G

proof_lines:
recombinant wild-type enzyme, 65°C
wild-type enzyme

substrate: tRNAGlu mutant C36G


proof_lines:
recombinant mutant enzyme R358Q, 65°C
recombinant mutant R358Q, 65°C


enzyme_display_name: D-alanine--(R)-lactate ligase

substrate_name: D-lactate

smiles: CC(C(=O)O)O

proof_lines:
mutant S150A, pH 6.0, 37°C
mutant S150A, pH 7.5, 37°C

enzyme: D-alanine--(R)-lactate ligase

substrate: D-lactate


proof_lines:
mutant Y216F, pH 6.0, 37°C
mutant Y216F, pH 7.5, 37°C


proof_lines:
isoform VanA, pH 6.0, 37°C
isoform VanA, pH 7.5, 37°C
isoform VanA, pH 8.3, 37°C


substrate_name: D-Ala

substrate: D-Ala


proof_lines: isoform VanA, above 100 mM, pH 7.5, 37°C


enzyme_display_name: glutamate--tRNA(Gln) ligase

proof_lines: recombinant hybrid GlnRS S1/L1/L2, pH not specified in the publication, temperature not specified in the publication

enzyme: glutamate--tRNA(Gln) ligase


substrate_name: L-Glu

substrate: L-Glu


substrate_name: ATP

substrate: ATP


enzyme_display_name: pyrrolysine--tRNA(Pyl) ligase

proof_lines: mutant enzyme N346A/C348L, pH and temperature not specified in the publication

enzyme: pyrrolysine--tRNA(Pyl) ligase


proof_lines: mutant enzyme A302L/Y306M/N346S/C348L/Y384L, pH and temperature not specified in the publication


proof_lines: mutant enzyme A302F/Y306L/N346T/C348F/Y384L, pH and temperature not specified in the publication


substrate_name: L-glutamate

substrate: L-glutamate


enzyme_display_name: aspartate--tRNA(Asn) ligase

organism: Halalkalibacterium halodurans

substrate_name: tRNAAsn

enzyme: aspartate--tRNA(Asn) ligase

substrate: tRNAAsn


organism: Thermosynechococcus vestitus

substrate_name: tRNAGln

substrate: tRNAGln


organism: Bacillus subtilis

proof_lines:
homologous tRNAGln
homologous tRNAGlu
tRNAGln from E. coli


organism: Enterococcus faecalis

smiles: CCC(C(=O)O)O

proof_lines: pH not specified in the publication, temperature not specified in the publication


smiles: CCCC(C(=O)[O-])O


proof_lines: cosubstrate D-Ala, binding of N-terminal Ala residue. pH not specified in the publication, temperature not specified in the publication

proof_lines: cosubstrate D-Ala, binding of C-terminal Ala residue. pH not specified in the publication, temperature not specified in the publication


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: L-aspartate (at 37 degrees Celsius)

proof_lines: kcat is 0.09 sec(-1) for tRNA aspartylation at 37 degrees Celsius and 0.24 sec(-1) at 70 degrees Celsius. kcat is 0.092 sec(-1) for tRNA(Asn) aspartylation at 70 degrees Celsius.

substrate: L-aspartate (at 37 degrees Celsius)


substrate_name: ATP (at 37 degrees Celsius)

substrate: ATP (at 37 degrees Celsius)


organism: Escherichia coli

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, mutant enzyme DELTA328-461, ATP-diphosphate exchange


proof_lines: pH 8.0, mutant enzyme DELTA288-461, ATP-diphosphate exchange


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Chlamydia trachomatis

substrate_name: L-Aspartate; tRNA(Asn); ATP

substrate: L-Aspartate; tRNA(Asn); ATP


substrate_name: L-Glutamate; ATP; tRNA(Gln)

substrate: L-Glutamate; ATP; tRNA(Gln)


substrate_name: tRNA(Glu)

substrate: tRNA(Glu)


enzyme_display_name: serine--tRNA ligase

organism: Methanothermobacter thermautotrophicus

substrate_name: tRNASer

proof_lines: pH 7.5, 50°C, recombinant MtSerRS in presence of recombinant MtArgRS

enzyme: serine--tRNA ligase

substrate: tRNASer


substrate_name: tRNAArg

proof_lines: pH 7.5, 50°C, recombinant MtArgRS in presence of recombinant MtSerRS

substrate: tRNAArg


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP


substrate_name: tRNAGlu

proof_lines:
pH 7.3, 37°C
substrate ATP, pH 7.3, 37°C
substrate L-glutamate, pH 7.3, 37°C

substrate: tRNAGlu


substrate_name: tRNA(Asp) (at 37 degrees Celsius)

substrate: tRNA(Asp) (at 37 degrees Celsius)


organism: Desulfitobacterium hafniense

substrate_name: tRNAPyl

substrate: tRNAPyl


substrate_name: more

proof_lines: equilibrium binding analysis, dissociation constants of the enzyme with tRNAPyl from different species, overview

substrate: more


organism: Methanosarcina barkeri

substrate_name: L-Pyrrolysine; ATP

source_databases_merged: sabio_rk brenda uniprot

substrate: L-Pyrrolysine; ATP


enzyme_display_name: O-phosphoserine--tRNA ligase

organism: Methanocaldococcus jannaschii

substrate_name: tRNA(Cys); ATP; O-Phospho-L-serine

assay_conditions_summary: pH 6; 333.15 K; cofactor ATP

proof_lines: pH 7.5, 37°C, recombinant enzyme, m1G37 tRNACys

proof_lines: pH 7.5, 37°C, recombinant enzyme, native tRNACys

enzyme: O-phosphoserine--tRNA ligase

substrate: tRNA(Cys); ATP; O-Phospho-L-serine


substrate_name: tRNACys

substrate: tRNACys


enzyme_display_name: asparagine--tRNA ligase

organism: Escherichia coli (strain K12)

substrate_name: ATP

column_label: Table 1 row WT, substrate ATP, column Km gives 0.5 mM; mutation rows are separate and do not describe this CatLog wild-type row.

raw_value_unit_evidence: Table 1 reports WT ATP Km 0.5 mM and kcat 2.2 s^-1; Y426S ATP is 7 mM.

row_label: WT enzyme / ATP substrate

table_label: FEBS Letters PDF p.164 Table 1

enzyme: asparagine--tRNA ligase

substrate: ATP


organism: Deinococcus radiodurans

substrate_name: tRNAAsp

proof_lines:
37°C, pH 7.0, wild-type enzyme
37°C, pH 7.0, wild-type enzym

substrate: tRNAAsp


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P77K/H28Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H28Q with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P77K with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

substrate_name: tRNA(Asp)

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines: kcat is 0.15 sec(-1) for tRNA(Asp) aspartylation and 0.51 sec(-1) for tRNA(Asn) aspartylation.

substrate: tRNA(Asp)


organism: Helicobacter pylori (strain ATCC 700392 / 26695)

proof_lines: kcat is 0.022 sec(-1) for tRNA(Asp) aspartylation and 0.014 sec(-1) for tRNA(Asn) aspartylation.


organism: Methanosarcina mazei

substrate_name: O-phospho-L-threonine

smiles: CC(C(C(=O)O)N)OP(=O)(O)O

substrate: O-phospho-L-threonine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T307S with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


substrate_name: O-phospho-L-serine

substrate: O-phospho-L-serine


substrate_name: asparagine

column_label: Table I reports WT asparagine Km 15.3 uM for E. coli asparaginyl-tRNA synthetase.

raw_value_unit_evidence: Km raw_value=15.3 uM raw_unit=uM

row_label: WT E. coli asparaginyl-tRNA synthetase / asparagine

substrate: asparagine


substrate_name: N-acetyl-L-lysine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L301M/Y306L/C348S/A315V to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/C348S/A315V

substrate: N-acetyl-L-lysine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L301M/Y306L/L309A/C348F to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme L301M/Y306L/L309A/C348F


proof_lines: Asn, , mutant Y426S, ATP-diphosphate exchange


substrate_name: Asn

proof_lines:
mutant Y426S, aminoacylation
mutant Y426S, ATP-diphosphate exchange

substrate: Asn


proof_lines: mutant Y426F, , ATP-diphosphate exchange


proof_lines:
mutant Y426F, ATP-diphosphate exchange
mutant Y426F, aminoacylation


substrate_name: L-Pyrrolysine

substrate: L-Pyrrolysine


organism: Vigna radiata var. radiata

substrate_name: S-adenosyl-L-methionine

proof_lines: without chilling in the presence of xanthine?xanthine oxidase and catalase

substrate: S-adenosyl-L-methionine


proof_lines:
tRNA esterification
ATP-diphosphate exchange


substrate_name: isoasparagine

substrate: isoasparagine


smiles: C(C#N)C(C(=O)O)N


organism: Cricetulus griseus

substrate_name: tRNAAsn

substrate: tRNAAsn


substrate_name: L-pyrrolysine

assay_conditions_summary: pH 7.2; 310.15 K; buffer 10 mM HEPES; cofactor ATP

proof_lines: wild type enzyme, at 37°C in 50 mM KCl, 10 mM MgCl2, 5 mM ATP, and 5 mM dithiothreitol in 10 mM HEPES buffer, pH 7.2

substrate: L-pyrrolysine


organism: Enterococcus faecium

substrate_name: D-lactate

substrate: D-lactate


substrate_name: D-Ala

substrate: D-Ala


smiles: CCCCC(C(=O)[O-])O


organism: Helicobacter pylori


proof_lines:
pH 7.2, 37°C
pH 7.2, 37°C, recombinant enzyme


organism: Thermus thermophilus


substrate_name: aspartate

substrate: aspartate


organism: Archaeoglobus fulgidus

substrate_name: tRNACys

proof_lines: 50°C, pH 7.6, tRNACys containing the (pyrrole-2-carbaldehyde)UA anticodon, mutant enzyme D418N D420N T423V

proof_lines: 50°C, pH 7.6, tRNACys containing the C(pyrrole-2-carbaldehyde)A anticodon, mutant enzyme D418N D420N T423V

substrate: tRNACys


proof_lines: 50°C, pH 7.6, tRNACys with the GCA anticodon, wild-type enzyme


organism: Plasmodium falciparum

proof_lines: in 50 mM HEPES-NaOH, pH 7.2, 10 mM MgCl2, at 37°C


substrate_name: L-asparagine

substrate: L-asparagine


substrate_name: ATP

substrate: ATP


proof_lines: in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-Glu

substrate: L-Glu


organism: Escherichia coli

proof_lines: mutant P231L, 25°C, ATP-diphosphate exchange

proof_lines: mutant P231L, 37°C, ATP-diphosphate exchange


proof_lines: wild-type, 37°C, ATP-diphosphate exchange


substrate_name: Unknown

proof_lines:
versus ATP
versus L-Phe

substrate: Unknown


organism: Bacillus subtilis


organism: Bombyx mori

proof_lines:
aminoacylation
tRNA2Gly, , aminoacylation
substrate from liver


organism: Bdellovibrio bacteriovorus


enzyme_display_name: proline--tRNA ligase

organism: Bos taurus

enzyme: proline--tRNA ligase


substrate_name: Phe

substrate: Phe


organism: Cricetulus sp.

substrate_name: tRNAArg

proof_lines: 25°C, pH 7.5, mammalian tRNAArg, aminoacylation

proof_lines: 25°C, pH 7.5, tRNAArg from Saccharomyces cerevisiae, aminoacylation

substrate: tRNAArg


enzyme_display_name: glycine--tRNA ligase

substrate_name: Gly

smiles: C(C(=O)O)N

enzyme: glycine--tRNA ligase

substrate: Gly


organism: Triticum aestivum

substrate_name: tRNAGlu

proof_lines: enzyme forms GluRSC and GluRSP, aminoacylation

substrate: tRNAGlu


substrate_name: Glu

proof_lines: enzyme forms GluRSP and GluRSE, aminoacylation

substrate: Glu


organism: Chlamydomonas reinhardtii


substrate_name: L-alanine

substrate: L-alanine


enzyme_display_name: UniProt Q9VCC6

organism: Drosophila melanogaster

substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

enzyme: UniProt Q9VCC6

substrate: lauric acid


substrate_name: linoleic acid

smiles: CCCCCC=CCC=CCCCCCCCC(=O)O

substrate: linoleic acid


enzyme_display_name: UniProt Q9P2R7

organism: Homo sapiens

substrate_name: succinate

enzyme: UniProt Q9P2R7

substrate: succinate


enzyme_display_name: succinate--CoA ligase (GDP-forming)

organism: Blastocystis hominis

substrate_name: GTP

proof_lines: mutant enzyme K46E/K114D/V113L/L227F, at pH 7.4 and 21°C

enzyme: succinate--CoA ligase (GDP-forming)

substrate: GTP


assay_conditions_summary: pH 7.4; 294.15 K; cofactor ATP


proof_lines: mutant enzyme K46E/K114D, at pH 7.4 and 21°C


proof_lines: mutant enzyme V113L/L227F, at pH 7.4 and 21°C


enzyme_display_name: acetate--CoA ligase

organism: Pyrococcus furiosus

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 353.15 K; cofactor ADP

proof_lines:
pH 7.5, 80°C, wild-type alpha-subunit
pH 7.5, 55°C, wild-type enzyme
pH 7.5, 80°C, wild-type enzyme

enzyme: acetate--CoA ligase

substrate: acetyl-CoA


substrate_name: CoA

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ADP

substrate: CoA


substrate_name: ADP

substrate: ADP


substrate_name: ATP

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP

substrate: ATP


substrate_name: phosphate

proof_lines:
pH 7.5, 80°C, wild-type enzyme
pH 7.5, 55°C, wild-type enzyme

substrate: phosphate


substrate_name: acetate

substrate: acetate


substrate_name: ATP; Coenzyme A; Acetate

assay_conditions_summary: cofactor CoA

substrate: ATP; Coenzyme A; Acetate


organism: Saccharomyces cerevisiae

substrate_name: Coenzyme A; ATP; Acetate

substrate: Coenzyme A; ATP; Acetate


substrate_name: Coenzyme A; ATP; Acrylate

substrate: Coenzyme A; ATP; Acrylate


organism: Columba livia

substrate_name: GTP; Succinate; Coenzyme A

substrate: GTP; Succinate; Coenzyme A


substrate_name: Succinyl-CoA; GDP; Phosphate

substrate: Succinyl-CoA; GDP; Phosphate


organism: Sus scrofa


substrate_name: GTP; Coenzyme A; Succinate

substrate: GTP; Coenzyme A; Succinate


enzyme_display_name: succinate--CoA ligase (ADP-forming)

organism: Thermococcus kodakarensis

assay_conditions_summary: 328.15 K; cofactor CoA

enzyme: succinate--CoA ligase (ADP-forming)


assay_conditions_summary: 328.15 K; cofactor ADP


assay_conditions_summary: 328.15 K; cofactor ATP


organism: Alcanivorax borkumensis

substrate_name: Itaconate

smiles: C=C(CC(=O)O)C(=O)O

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

substrate: Itaconate


substrate_name: L-malate

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ADP

substrate: L-malate


substrate_name: D-Malate

substrate: D-Malate


substrate_name: Succinyl-CoA; ADP; Phosphate

substrate: Succinyl-CoA; ADP; Phosphate


substrate_name: Coenzyme A; Succinate; ATP

substrate: Coenzyme A; Succinate; ATP


organism: Escherichia coli K-12

substrate_name: succinate

smiles: O=C(O)CCC(=O)O

substrate: succinate


organism: Calliphoridae

substrate_name: coenzyme A

substrate: coenzyme A


substrate_name: succinyl-CoA

substrate: succinyl-CoA


substrate_name: ADP

assay_conditions_summary: cofactor ADP

substrate: ADP


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


smiles: O=C(O)CCS(=O)O


substrate_name: CoA

substrate: CoA


enzyme_display_name: long-chain-fatty-acid--CoA ligase

organism: Rattus norvegicus

substrate_name: oleate

smiles: CCCCCCCCC=CCCCCCCCC(=O)[O-]

proof_lines:
pH 7.4, isoenzyme ACSL6_v2
pH 7.4, isoenzyme ACSL6_v1

enzyme: long-chain-fatty-acid--CoA ligase

substrate: oleate


substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

proof_lines:
pH 7.4, isoenzyme ACSL6_v2
pH 7.5, 37°C, ACS1
pH 7.5, 37°C, ACS4

substrate: palmitate


enzyme_display_name: medium-chain acyl-CoA ligase

organism: Pseudomonas aeruginosa

enzyme: medium-chain acyl-CoA ligase


organism: Aedes togoi

substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Nipponoluciola cruciata

substrate_name: lauric acid

substrate: lauric acid


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C, ACS4
CoA
pH 7.5, 37°C, ACS1


substrate_name: arachidonate

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)[O-]

substrate: arachidonate


organism: Advenella mimigardefordensis

normalized_value_unit_evidence: Km normalized_value=0.037 normalized_unit=mM; kcat normalized_value=40.3 normalized_unit=s^(-1); kcat_over_km normalized_value=1099.6 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=0.037 +/- 0.001 raw_unit=mM; kcat raw_value=40.3 raw_unit=s^-1; kcat_over_km raw_value=1099.6 raw_unit=s^-1 mM^-1

row_label: SucCD Am / CoA

table_label: Table 3. Kinetic parameters determined for SucCD BL21, SucCD Am, and SucCD AboHis


column_label: Table 3 row SucCD Am / Itaconate has Km=0.351 +/- 0.003 mM; kcat=5.3 s^-1; kcat/Km=15.1 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.351 normalized_unit=mM; kcat normalized_value=5.3 normalized_unit=s^(-1); kcat_over_km normalized_value=15.1 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=0.351 +/- 0.003 raw_unit=mM; kcat raw_value=5.3 raw_unit=s^-1; kcat_over_km raw_value=15.1 raw_unit=s^-1 mM^-1

row_label: SucCD Am / Itaconate


column_label: Table 3 row SucCD Am / L-malate has Km=3.095 +/- 0.354 mM; kcat=2.6 s^-1; kcat/Km=0.8 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=3.095 normalized_unit=mM; kcat normalized_value=2.6 normalized_unit=s^(-1); kcat_over_km normalized_value=0.8 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=3.095 +/- 0.354 raw_unit=mM; kcat raw_value=2.6 raw_unit=s^-1; kcat_over_km raw_value=0.8 raw_unit=s^-1 mM^-1

row_label: SucCD Am / L-malate


column_label: Table 3 row SucCD Am / D-malate has Km=3.588 +/- 0.111 mM; kcat=2.1 s^-1; kcat/Km=0.6 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=3.588 normalized_unit=mM; kcat normalized_value=2.1 normalized_unit=s^(-1); kcat_over_km normalized_value=0.6 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=3.588 +/- 0.111 raw_unit=mM; kcat raw_value=2.1 raw_unit=s^-1; kcat_over_km raw_value=0.6 raw_unit=s^-1 mM^-1

row_label: SucCD Am / D-malate


column_label: Table 3 row SucCD Am / Succinate has Km=0.182 +/- 0.003 mM; kcat=31.1 s^-1; kcat/Km=171.1 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.182 normalized_unit=mM; kcat normalized_value=31.1 normalized_unit=s^(-1); kcat_over_km normalized_value=171.1 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=0.182 +/- 0.003 raw_unit=mM; kcat raw_value=31.1 raw_unit=s^-1; kcat_over_km raw_value=171.1 raw_unit=s^-1 mM^-1

row_label: SucCD Am / Succinate


column_label: Table 3 row SucCD Am / 3SP has Km=2.964 +/- 0.275 mM; kcat=0.2 s^-1; kcat/Km=0.1 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=2.964 normalized_unit=mM; kcat normalized_value=0.2 normalized_unit=s^(-1); kcat_over_km normalized_value=0.1 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=2.964 +/- 0.275 raw_unit=mM; kcat raw_value=0.2 raw_unit=s^-1; kcat_over_km raw_value=0.1 raw_unit=s^-1 mM^-1

row_label: SucCD Am / 3SP


normalized_value_unit_evidence: Km normalized_value=0.201 normalized_unit=mM; kcat normalized_value=58.8 normalized_unit=s^(-1); kcat_over_km normalized_value=292.5 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=0.201 +/- 0.002 raw_unit=mM; kcat raw_value=58.8 raw_unit=s^-1; kcat_over_km raw_value=292.5 raw_unit=s^-1 mM^-1

row_label: SucCD Am / ATP


column_label: Table 3 row SucCD AboHis / Succinate has Km=0.157 +/- 0.003 mM; kcat=2.7 s^-1; kcat/Km=17.2 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.157 normalized_unit=mM; kcat normalized_value=2.7 normalized_unit=s^(-1); kcat_over_km normalized_value=17.2 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=0.157 +/- 0.003 raw_unit=mM; kcat raw_value=2.7 raw_unit=s^-1; kcat_over_km raw_value=17.2 raw_unit=s^-1 mM^-1

row_label: SucCD AboHis / Succinate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines:
pH 7.5, 37°C, ACS5
pH 7.4, isoenzyme ACSL6_v2
pH 7.5, 37°C, ACS4


organism: Methanosarcina acetivorans


organism: Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)

substrate_name: butyrate

smiles: CCCC(=O)[O-]

proof_lines: kcat is 16.2 sec(-1) for ligase activity with propionate as substrate. kcat is 8.4 sec(-1) for ligase activity with butyrate as substrate. kcat is 6.4 sec(-1) for ligase activity with acetate as substrate. kcat is 5.6 sec(-1) for ligase act

substrate: butyrate


substrate_name: propionate

substrate: propionate


substrate_name: valerate

smiles: CCCCC(=O)[O-]

substrate: valerate


substrate_name: acetate

substrate: acetate


proof_lines: kcat is 0.24 sec(-1) for ligase activity with 4HB as substrate. kcat is 0.23 sec(-1) for ligase activity with butyrate as substrate. kcat is 0.22 sec(-1) for ligase activity with valerate as substrate. kcat is 0.21 sec(-1) for ligase activi


organism: Penicillium chrysogenum

substrate_name: phenylacetate

assay_conditions_summary: pH 8.5; cofactor ATP

substrate: phenylacetate


proof_lines: pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid

proof_lines: pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid


substrate_name: Phenoxyacetate

substrate: Phenoxyacetate


substrate_name: trans-cinnamic acid

substrate: trans-cinnamic acid


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: myristic acid


substrate_name: propionic acid

smiles: CCC(=O)O

substrate: propionic acid


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: CoA (at pH 8 and at 37 degrees Celsius)

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: kcat is 0.03 sec(-1) for palmitic acid (at pH 8 and at 37 degrees Celsius).

substrate: CoA (at pH 8 and at 37 degrees Celsius)


substrate_name: palmitic acid (at pH 8 and at 37 degrees Celsius)

assay_conditions_summary: pH 8


substrate_name: ATP (at pH 8 and at 37 degrees Celsius)

assay_conditions_summary: pH 8; cofactor ATP

substrate: ATP (at pH 8 and at 37 degrees Celsius)


substrate_name: 3-oxo-4-cholesten-26-oate (at pH 7.3 and 22 degrees Celsius)

assay_conditions_summary: pH 7.3; cofactor CoA

proof_lines: kcat is 0.75 sec(-1) for 3-oxo-4-cholesten-26-oate--CoA ligase activity (at pH 7.3 and 22 degrees Celsius).


organism: Populus trichocarpa

substrate_name: Sodium acetate

proof_lines:
isoform ACS1, at pH 7.8 and 25°C
isoform ACS2, at pH 7.8 and 25°C

substrate: Sodium acetate


substrate_name: CoA

assay_conditions_summary: pH 7.4; cofactor CoA

substrate: CoA


substrate_name: palmitate

substrate: palmitate


substrate_name: oleate

substrate: oleate


substrate_name: arachidonate


substrate_name: ATP

assay_conditions_summary: pH 7.4; cofactor ATP

substrate: ATP


substrate_name: butyrate

assay_conditions_summary: cofactor CoA


substrate_name: propionate


substrate_name: valerate


substrate_name: acetate


organism: Arabidopsis thaliana

substrate_name: 16-hydroxypalmitic acid

smiles: C(CCCCCCCC(=O)O)CCCCCCCO

substrate: 16-hydroxypalmitic acid


organism: Bacillus brevis

substrate_name: ATP; Coenzyme A; Phenylalanine

substrate: ATP; Coenzyme A; Phenylalanine


substrate_name: Coenzyme A; ATP; Tyrosine

substrate: Coenzyme A; ATP; Tyrosine


substrate_name: Coenzyme A; Phenylalanine; ATP

substrate: Coenzyme A; Phenylalanine; ATP


organism: Bacillus subtilis

substrate_name: Coenzyme A; ATP; D-Alanine

substrate: Coenzyme A; ATP; D-Alanine


substrate_name: ATP; 2,3-Dihydroxybenzoate; Coenzyme A

substrate: ATP; 2,3-Dihydroxybenzoate; Coenzyme A


substrate_name: Acetate; Coenzyme A; ATP

substrate: Acetate; Coenzyme A; ATP


organism: Escherichia coli

substrate_name: Acetate; ATP; Coenzyme A

substrate: Acetate; ATP; Coenzyme A


organism: Methanothrix thermoacetophila


organism: Saccharomyces cerevisiae

substrate_name: Coenzyme A; Acetate; ATP

substrate: Coenzyme A; Acetate; ATP


organism: Salmonella enterica

substrate_name: Propanoate; Coenzyme A; ATP

substrate: Propanoate; Coenzyme A; ATP


organism: Bos taurus

substrate_name: ATP (with (R)-lipoate as substrate)

substrate: ATP (with (R)-lipoate as substrate)


organism: Chromochloris zofingiensis

substrate_name: Sodium acetate


substrate_name: potassium acetate

substrate: potassium acetate


organism: Lathyrus oleraceus

substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens


organism: Mycobacterium avium


organism: Rattus norvegicus


substrate_name: ATP; Coenzyme A; Palmitate

substrate: ATP; Coenzyme A; Palmitate


substrate_name: ATP; Palmitate; Coenzyme A

substrate: ATP; Palmitate; Coenzyme A


substrate_name: Palmitate; Coenzyme A; ATP

substrate: Palmitate; Coenzyme A; ATP


substrate_name: ATP; Benzoate; Coenzyme A

substrate: ATP; Benzoate; Coenzyme A


substrate_name: Coenzyme A; Palmitate; ATP

substrate: Coenzyme A; Palmitate; ATP


substrate_name: Coenzyme A; Hexanoate; ATP

substrate: Coenzyme A; Hexanoate; ATP


substrate_name: ATP; Coenzyme A; Hexanoate

substrate: ATP; Coenzyme A; Hexanoate


substrate_name: Coenzyme A; Octanoate; ATP

substrate: Coenzyme A; Octanoate; ATP


organism: Sus scrofa


organism: Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII)

proof_lines: kcat is 133 min(-1) with ATP as substrate.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: Coenzyme A; ATP; Palmitate

substrate: Coenzyme A; ATP; Palmitate


substrate_name: Palmitate; ATP; Coenzyme A

substrate: Palmitate; ATP; Coenzyme A


substrate_name: palmitate

substrate: palmitate


substrate_name: ATP (Isoform 1)

substrate: ATP (Isoform 1)


substrate_name: CoA (Isoform 1)

substrate: CoA (Isoform 1)


substrate_name: palmitate (Isoform 1)

substrate: palmitate (Isoform 1)


substrate_name: oleate (Isoform 1)

substrate: oleate (Isoform 1)


substrate_name: arachidonate (Isoform 1)

substrate: arachidonate (Isoform 1)


substrate_name: benzoate

column_label: Table 2 reports HXM-B substrate benzoate, Km (μM) = 21±3; normalized Km = 0.021 mM.

normalized_value_unit_evidence: Km=0.021 mM after μM to mM conversion from Table 2 21±3 μM.

raw_value_unit_evidence: 21±3 μM in Table 2 HXM-B Km (μM) column

row_label: Benzoate / HXM-B / Km (μM) column

table_label: Table 2 / Kinetic analysis of the substrate specificity of HXM-A and HXM-B

substrate: benzoate


substrate_name: butyrate

column_label: Table 2 reports HXM-B substrate butyrate, Km (μM) = 570±190; normalized Km = 0.57 mM.

normalized_value_unit_evidence: Km=0.57 mM after μM to mM conversion from Table 2 570±190 μM.

raw_value_unit_evidence: 570±190 μM in Table 2 HXM-B Km (μM) column

row_label: Butyrate / HXM-B / Km (μM) column

substrate: butyrate


substrate_name: decanoate

smiles: CCCCCCCCCC(=O)[O-]

column_label: Table 2 reports HXM-B substrate decanoate, Km (μM) = 20±2; normalized Km = 0.02 mM.

normalized_value_unit_evidence: Km=0.02 mM after μM to mM conversion from Table 2 20±2 μM.

raw_value_unit_evidence: 20±2 μM in Table 2 HXM-B Km (μM) column

row_label: Decanoate / HXM-B / Km (μM) column

substrate: decanoate


substrate_name: hexanoate

smiles: CCCCCC(=O)[O-]

column_label: Table 2 reports HXM-B substrate hexanoate, Km (μM) = 34±4; normalized Km = 0.034 mM.

normalized_value_unit_evidence: Km=0.034 mM after μM to mM conversion from Table 2 34±4 μM.

raw_value_unit_evidence: 34±4 μM in Table 2 HXM-B Km (μM) column

row_label: Hexanoate / HXM-B / Km (μM) column

substrate: hexanoate


substrate_name: laurate

smiles: CCCCCCCCCCCC(=O)[O-]

column_label: Table 2 reports HXM-B substrate laurate, Km (μM) = 24±8; normalized Km = 0.024 mM.

normalized_value_unit_evidence: Km=0.024 mM after μM to mM conversion from Table 2 24±8 μM.

raw_value_unit_evidence: 24±8 μM in Table 2 HXM-B Km (μM) column

row_label: Laurate / HXM-B / Km (μM) column

substrate: laurate


substrate_name: phenylacetate

column_label: Table 2 reports HXM-B substrate phenylacetate, Km (μM) = 143±35; normalized Km = 0.143 mM.

normalized_value_unit_evidence: Km=0.143 mM after μM to mM conversion from Table 2 143±35 μM.

raw_value_unit_evidence: 143±35 μM in Table 2 HXM-B Km (μM) column

row_label: Phenylacetate / HXM-B / Km (μM) column

substrate: phenylacetate


substrate_name: salicylate

column_label: Table 2 reports HXM-B substrate salicylate, Km (μM) = 25±11; normalized Km = 0.025 mM.

normalized_value_unit_evidence: Km=0.025 mM after μM to mM conversion from Table 2 25±11 μM.

raw_value_unit_evidence: 25±11 μM in Table 2 HXM-B Km (μM) column

row_label: Salicylate / HXM-B / Km (μM) column

substrate: salicylate


column_label: Table 2 reports HXM-A substrate benzoate, Km (μM) = 13±4; normalized Km = 0.013 mM.

normalized_value_unit_evidence: Km=0.013 mM after μM to mM conversion from Table 2 13±4 μM.

raw_value_unit_evidence: 13±4 μM in Table 2 HXM-A Km (μM) column

row_label: Benzoate / HXM-A / Km (μM) column


column_label: Table 2 reports HXM-A substrate butyrate, Km (μM) = 800±190; normalized Km = 0.8 mM.

normalized_value_unit_evidence: Km=0.8 mM after μM to mM conversion from Table 2 800±190 μM.

raw_value_unit_evidence: 800±190 μM in Table 2 HXM-A Km (μM) column

row_label: Butyrate / HXM-A / Km (μM) column


column_label: Table 2 reports HXM-A substrate decanoate, Km (μM) = 110±20; normalized Km = 0.11 mM.

normalized_value_unit_evidence: Km=0.11 mM after μM to mM conversion from Table 2 110±20 μM.

raw_value_unit_evidence: 110±20 μM in Table 2 HXM-A Km (μM) column

row_label: Decanoate / HXM-A / Km (μM) column


substrate_name: ATP

substrate: ATP


substrate_name: CoA

substrate: CoA


substrate_name: oleate

substrate: oleate


substrate_name: arachidonate

substrate: arachidonate


substrate_name: 3-oxo-4-cholesten-26-oate (at pH 7.3 and 22 degrees Celsius)


substrate_name: succinate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V330M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: succinate


substrate_name: dodecanoate

substrate: dodecanoate


substrate_name: Octanoate

smiles: CCCCCCCC(=O)[O-]

substrate: Octanoate


substrate_name: Decanoate

substrate: Decanoate