sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F162L to reconstruct the assayed variant sequence.

column_label: Table I; row F162L; columns Km, kcat, and kcat/Km; exact printed cells 0.78 +/- 0.11 mM, 120 +/- 10 min^-1, and 150000 +/- 20000 M^-1 min^-1; central values normalize to 0.78 mM, 2.0 s^-1, and 2.5 s^-1*mM^-1.

normalized_value_unit_evidence: Paper Km=0.78 mM; paper kcat=2.0 s^-1; paper printed kcat/Km=2.5 s^-1*mM^-1. Current tuple is Km=0.78 mM, kcat=2.0 s^-1, kcat/Km=2.564102564102564 s^-1*mM^-1.


enzyme_display_name: DEAD-box RNA helicase

organism: Saccharomyces cerevisiae

substrate_name: ATP

source_db: brenda

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T166A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table I; row T166A; columns Km, kcat, and kcat/Km; exact printed cells 0.51 +/- 0.04 mM, 120 +/- 10 min^-1, and 230000 +/- 20000 M^-1 min^-1; central values normalize to 0.51 mM, 2.0 s^-1, and 3.8333333333333335 s^-1*mM^-1.

table_label: Table I. Kinetic parameters for RNA-dependent ATPase activity

data_origin: experimental

enzyme: DEAD-box RNA helicase

substrate: ATP

status: corrected

source: brenda


mutation_signature: Unknown

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

assay_conditions_summary: pH 7.5; buffer used 50 mM potassium acetate; cofactor ATP

column_label: Table I; row WT; columns Km, kcat, and kcat/Km; raw cells 0.34 +/- 0.05 mM, 210 +/- 20 min^-1, and 620000 +/- 90000 M^-1 min^-1; kcat/Km is explicitly printed, while the package ratio is also derivable from rounded package kcat/Km.

normalized_value_unit_evidence: paper Km=0.34 mM; paper kcat=3.5 s^-1; paper printed kcat/Km=10.3333 s^-1*mM^-1; package kcat/Km=10.294117647058822 s^-1*mM^-1 is derived from the package rounded kcat/Km pair

row_label: WT


verification_status: verified

kcat_display: Not reported

km_display: Not reported

kcat_over_km_display: Not reported

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T166S to reconstruct the assayed variant sequence.

column_label: Table I; row T166S; column Ki(d) (mM); raw value 0.34 +/- 0.07 mM; normalized Ki=0.34 mM; footnote d identifies competitive inhibition by ADP; ATP is the ATPase substrate.

normalized_value_unit_evidence: Current Ki=0.34 mM; paper Ki=0.34 mM; inhibitor/modifier is ADP competitive inhibition and ATP is the substrate.

raw_value_unit_evidence: Table I row T166S, Ki(d) column: 0.34 +/- 0.07 mM.

status: verified


column_label: Table I; row WT; column Ki(d) (mM); raw value 0.36 +/- 0.07 mM; normalized Ki=0.36 mM; footnote d identifies competitive inhibition by ADP; ATP is the ATPase substrate.

normalized_value_unit_evidence: Current Ki=0.36 mM; paper Ki=0.36 mM; inhibitor/modifier is ADP competitive inhibition and ATP is the substrate.

raw_value_unit_evidence: Table I row WT, Ki(d) column: 0.36 +/- 0.07 mM.


column_label: Table I; row T166A; column Ki(d) (mM); raw value 0.36 +/- 0.08 mM; normalized Ki=0.36 mM; footnote d identifies competitive inhibition by ADP; ATP is the ATPase substrate.

raw_value_unit_evidence: Table I row T166A, Ki(d) column: 0.36 +/- 0.08 mM.


column_label: Table I; row F162L; column Ki(d) (mM); raw value 3.0 +/- 0.1 mM; normalized Ki=3.0 mM; footnote d identifies competitive inhibition by ADP; ATP is the ATPase substrate.

normalized_value_unit_evidence: Current Ki=3.0 mM; paper Ki=3.0 mM; inhibitor/modifier is ADP competitive inhibition and ATP is the substrate.

raw_value_unit_evidence: Table I row F162L, Ki(d) column: 3.0 +/- 0.1 mM.


organism: Bacillus subtilis

substrate_name: RNA

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: pH 7.5, 37°C, recombinant YxiN mutant S108C/S229C

substrate: RNA


proof_lines: pH 7.5, 37°C, recombinant YxiN mutant S108C/E224C


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

proof_lines: pH 7.5, 37°C, recombinant wild-type YxiN


proof_lines: pH 7.5, 37°C, recombinant YxiN mutantA115C/S229C


proof_lines: pH 7.5, 37°C, recombinant YxiN mutantA115C/E224C


proof_lines: pH 7.5, 37°C, recombinant YxiN mutantA115C/D262C


enzyme_display_name: RNA 3'-5' helicase

organism: Hepacivirus hominis

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant NS3-4A

enzyme: RNA 3'-5' helicase


proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant S1369R/M1708A

proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A S1369R/M1708A mutant


proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of wild-type NS3


proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant Y1702A

proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A Y1702A mutant


proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant M1708A

proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A M1708A mutant


assay_conditions_summary: cofactor ATP

proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A S1369R mutant


proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A S1369R/Y1702A mutant


substrate_name: dTTP

proof_lines: inhibition of NTPase activity of NS3 protein by NTP derivatives

substrate: dTTP


substrate_name: dGTP

substrate: dGTP


substrate_name: dATP

substrate: dATP


substrate_name: GTP

substrate: GTP


substrate_name: UTP

substrate: UTP


enzyme_display_name: DNA topoisomerase (ATP-hydrolyzing)

organism: Mycobacterium tuberculosis

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

sequence_source: UniProt P9WG47 canonical sequence.

enzyme: DNA topoisomerase (ATP-hydrolyzing)

status: unverified

source: oed


sequence_source: UniProt P9WG45 canonical sequence with GyrBA_mC-loop substitutions E221K/D225K/E228K/R236E/H244A.

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


sequence_source: UniProt P9WG47 canonical sequence with GyrBAKKKK substitution D211K/E212K/E213K/E214K.


sequence_source: UniProt P9WG45 canonical sequence with A57D substitution.


organism: Escherichia coli

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines: pH 7.5, 22°C, recombinant engineered enzyme


proof_lines: pH 7.5, 22°C, recombinant wild-type enzyme


enzyme_display_name: DNA 3'-5' helicase

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

proof_lines: i.e. ppopT, dTTP analogue, inhibition of NTPase activity of NS3 protein by NTP derivatives

enzyme: DNA 3'-5' helicase

substrate: Unknown


assay_conditions_summary: pH 6.5; 295.15 K; cofactor ATP

proof_lines: addition of polyuridylate lowers Km for the ATP substrate

proof_lines: pH 6.5, 22°C, recombinant enzyme, calculated by BRENDA


organism: Dengue virus

proof_lines: full-length enzyme in presence of cofactor CF40-Gly4-Ser-Gly4-NS3FL


proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A construct

proof_lines: RNA-stimulated ATPase activity, NS3, recombinant protein


enzyme_display_name: RNA 5'-3' helicase

organism: Homo sapiens

enzyme: RNA 5'-3' helicase


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Thermochaetoides thermophila

proof_lines: recombinant enzyme mutant ctPrp43-IDSB, pH and temperature not specified in the publication


organism: Saccharolobus solfataricus

sequence_variant_note: Mutation signature K323A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH and temperature not specified in the publication, mutant enzyme K323A


sequence_variant_note: Mutation signature R329A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH and temperature not specified in the publication, mutant enzyme R329A


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +23, so it is treated as a source-provided variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme E326A/D327A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D327A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme D327A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V324A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme V324A


sequence_variant_note: Mutation signature E326A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH and temperature not specified in the publication, mutant enzyme E326A


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +25, so it is treated as a source-provided variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme V324A/L325A


proof_lines: pH and temperature not specified in the publication, mutant enzyme L325A


organism: West Nile virus

proof_lines: pH 7.5, 37°C, native WNV NS3 protein purified from infected cells

proof_lines: recombinant protein including C-terminal portion the ATPase/helicase domain encompassing residues 181-619, ATP concentration 1mM ATP, ATPase but not RNA helicase activity

proof_lines: pH 7.5, 37°C, recombinant C-terminal portion of the NS3


enzyme_display_name: chaperonin ATPase

organism: Pseudomonas phage EL

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines:
at 100 mM KCl, at pH and 25°C
at 10 mM KCl, at pH and 25°C

enzyme: chaperonin ATPase


sequence_variant_note: Mutation signature E326A/D327A/R329A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH and temperature not specified in the publication, mutant enzyme E326A/D327A/R329A


sequence_variant_note: Mutation signature E202G/E203G/V204G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: + Y-DNA, pH and temperature not specified in the publication, mutant enzyme E202G/E203G/V204G


sequence_variant_note: Mutation signature I555D/L556S/I557D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: + Y-DNA, pH and temperature not specified in the publication, mutant enzyme I555D/L556S/I557D


proof_lines: + Y-DNA, pH and temperature not specified in the publication, wild-type enzyme


sequence_variant_note: Mutation signature T550G/P551G/D552G/S553G/P554G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: + Y-DNA, pH and temperature not specified in the publication, mutant enzyme T550G/P551G/D552G/S553G/P554G


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L189D/D191R with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

proof_lines: + Y-DNA, pH and temperature not specified in the publication, mutant enzyme L189D/D191R


organism: Thermoanaerobacter brockii

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

assay_conditions_summary: 343.15 K; cofactor ATP


organism: Enterobacteria phage T4

source_db: uniprot

source: uniprot


enzyme_display_name: myosin ATPase

organism: Acanthamoeba castellanii

proof_lines: myosin IA, 100-kDa fragment resulting from digestion of myosin heavy chain with alpha-chymotrypsin shows similar activity

enzyme: myosin ATPase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: ATP with dsDNA

proof_lines: kcat is 3180 min(-1) with dsDNA (PubMed:22628485). kcat is 61 min(-1) with mobile HJ, kcat is 46 min(-1) with immobile HJ (PubMed:23438087).

substrate: ATP with dsDNA


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)


organism: Drosophila melanogaster

substrate_name: ATP; negatively supercoiled circular DNA

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

sequence_source: multiple


substrate_name: ATP in helicase activity

substrate: ATP in helicase activity


organism: Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216)

substrate_name: 21-mer ssDNA substrate

substrate: 21-mer ssDNA substrate


enzyme_display_name: dynein ATPase

organism: Dictyostelium discoideum

proof_lines:
HFG380, basal activity
HFG380, microtubule-activated activity
HFG380, microtubule-activated

enzyme: dynein ATPase


proof_lines: kcat is 0.0095 sec(-1) for ATP. kcat is 0.0075 sec(-1) for GTP.


enzyme_display_name: DNA 5'-3' helicase

organism: Plasmodium falciparum (isolate 3D7)

substrate_name: dNTPs

proof_lines: kcat is 22 sec(-1) for polymerase activity (PubMed:27487482). kcat is 10 min(-1) for polymerase activity (PubMed:39490679). kcat is 1.69 min(-1) for polymerase activity on dA template with dTTP (PubMed:35220686, PubMed:32636411). kcat is 1.

enzyme: DNA 5'-3' helicase

substrate: dNTPs


proof_lines: kcat is 10 sec(-1) on a ssDNA 21-mer and about 50 sec(-1) on ssDNA 5kb template.


substrate_name: ssDNA

substrate: ssDNA


organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)

substrate_name: ATP in presence of forked DNA with 40 bp lagging strand arm

proof_lines: kcat is 9 sec(-1) for ATPase, in the presence of 100 nM monomeric PriB kcat is 14 sec(-1) for ATPase.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ATP hydrolysis by TFIIH in the absence of RAD3/XPD ATPase activity

proof_lines: kcat for ssDNA-dependent ATPase activity is 140 min(-1) of purified protein.


enzyme_display_name: plus-end-directed kinesin ATPase

assay_conditions_summary: pH 6.8; 298.15 K; cofactor ATP

proof_lines: pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain mutant L2

proof_lines: pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DSK

proof_lines: pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DVK

enzyme: plus-end-directed kinesin ATPase


proof_lines: pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain wild-type

proof_lines: pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain wild-type

proof_lines: in presence of wild type microtubles, pH 6.8, 25°C


organism: Geobacillus stearothermophilus

substrate_name: ATP (for hydrolysis activity)

proof_lines: kcat is 19 sec(-1) with ATP as substrate, and varies from 3-40 sec(-1) depending on the (d)NTP. In the absence of single-stranded (ss)DNA, kcat decreases 400-fold with ATP as substrate.

substrate: ATP (for hydrolysis activity)


substrate_name: dATP (for hydrolysis activity)

substrate: dATP (for hydrolysis activity)


substrate_name: CTP (for hydrolysis activity)

substrate: CTP (for hydrolysis activity)


substrate_name: GTP (for hydrolysis activity)

substrate: GTP (for hydrolysis activity)


substrate_name: dGTP (for hydrolysis activity)

substrate: dGTP (for hydrolysis activity)


substrate_name: dTTP (for hydrolysis activity)

substrate: dTTP (for hydrolysis activity)


substrate_name: 1,N6-ethenoadenosine 5'-triphosphate (for hydrolysis activity)


organism: Homo sapiens

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R334Q to reconstruct the assayed variant sequence.

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R354P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R357P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R374Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S369P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S369Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T457I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W315L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W474C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A318T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A359T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A475P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F485L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I367T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K319E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K319T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L381P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P335L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R303W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y508C with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E44Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


organism: Bacillus subtilis (strain 168)

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

proof_lines: kcat for ATP hydrolysis by AddAB is 88 sec(-1), ATPase is strongly stimulated by ssDNA.


substrate_name: ATP (at 30 degrees Celsius)

substrate: ATP (at 30 degrees Celsius)


substrate_name: dATP (at 30 degrees Celsius)

substrate: dATP (at 30 degrees Celsius)


substrate_name: ATP with dsDNA

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


organism: Escherichia coli (strain K12)

assay_conditions_summary: 308.15 K; cofactor ATP

column_label: Abstract reports ATP is the preferred substrate (Km 0.27 mM) and dephosphorylated at the gamma-position at a maximal rate near 10(4) molecules per enzyme monomer per min at 35 degrees C.

raw_value_unit_evidence: Km raw_value=0.27 mM raw_unit=mM

row_label: Escherichia coli DNA-dependent ATPase / ATP

table_label: PubMed XML abstract PMID 133022


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y564A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: mutant (RECQ1(T1))Y564A, a construct encompassing amino acids 49?616 (of 649) of RECQ1, followed by a C-terminal tag of 22 aa


substrate_name: dATP

substrate: dATP


organism: Helicobacter pylori (strain ATCC 700392 / 26695)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A475P with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: mutant A475P, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K319T to reconstruct the assayed variant sequence.

proof_lines: mutant K319T, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F485L to reconstruct the assayed variant sequence.

proof_lines: mutant F485L, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K319E to reconstruct the assayed variant sequence.

proof_lines: mutant K319E, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L381P to reconstruct the assayed variant sequence.

proof_lines: mutant L381P, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Mutation signature K897del could not be applied safely because the resolved sequence does not match the expected reference residue(s).

mutation_type: deletion


proof_lines: kcat is 0.0095 sec(-1) for ATP. kcat is 0.0075 sec(-1) for GTP.


substrate_name: UTP (using ssM13mp18 as DNA substrate)

substrate: UTP (using ssM13mp18 as DNA substrate)


organism: Leishmania major

assay_conditions_summary: pH 8.3; 310.15 K; cofactor ATP


column_label: Results text states EcoLhr has a Km of 0.17 +/- 0.076 mM ATP from a nonlinear Michaelis-Menten fit of ATP hydrolysis velocity versus ATP concentration.

raw_value_unit_evidence: Km raw_value=0.17 +/- 0.076 raw_unit=mM ATP

row_label: full-length Escherichia coli Lhr (EcoLhr-FL) / ATP hydrolysis

table_label: Results text and Figure 5C, Characterization of the EcoLhr ATPase


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)


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

proof_lines: mutant W474C, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant T457I, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R334Q, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant A359T, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant P335L, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant W315L, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R354P, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant A318T, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R357P, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant S369Y pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant Y508C, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant S369P, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R374Q , pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R303W, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant I367T, pH 7.5, 37°C, in the presence of calf thymus DNA


source_db: skid

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

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

source_databases_merged: skid uniprot

source: skid


column_label: The paper reports apparent Km values derived from ATPase activity versus ATP concentration and gives 0.05 mM for wild-type UvrD.

raw_value_unit_evidence: Km raw_value=0.05 raw_unit=mM

row_label: wild-type UvrD DNA helicase II ATPase activity

table_label: Results prose and Fig. 6, ATPase activity as a function of ATP concentration


substrate_name: DNA

substrate: DNA


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

proof_lines: pH 7.7, 37°C, DNA passage, wild-type enzyme


organism: Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 / NBRC 14880 / R51)


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


proof_lines: enzyme dimeric mutant GyrBA5, pH 7.5, 30°C

proof_lines: enzyme dimeric mutant GyrBA57DELTAC-loop, pH 7.5, 30°C

proof_lines: enzyme mutant GyrBADELTAC-loop, pH 7.5, 30°C


proof_lines: enzyme mutant GyrBAmC-loop (E221K/D225K/E228K/R236E/H244A), pH 7.5, 30°C


proof_lines: enzyme mutant GyrBAKKK (D211K/E212K/E213K/E214K), pH 7.5, 30°C


assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: mutant DELTA Q25, pH 7.4, 30°C, in the absence of DNA

proof_lines: mutant DELTA Q25, pH 7.4, 30°C, in the presence of M13 ssDNA


proof_lines: mutant K52R, pH 7.4, 30°C, in the presence of M13 ssDNA


proof_lines: mutant Q25A, pH 7.4, 30°C, in the absence of DNA

proof_lines: mutant Q25A, pH 7.4, 30°C, in the presence of M13 ssDNA


proof_lines: wild-type, pH 7.4, 30°C, in the absence of DNA

proof_lines: wild-type wit His-tag, pH 7.5, 37°C, in the presence of calf thymus DNA

proof_lines: wild-type without His-tag, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines:
pH 8.0, 30°C, without ssDNA
pH 8.0, 30°C, in presence of ssDNA


assay_conditions_summary: pH 7.5; 293.15 K; cofactor ATP

proof_lines:
pH 7.5, 20°C, without DNA
pH 7.5, 20°C, in presence of DNA


organism: Bos taurus

proof_lines:
relaxation reaction
ATPase reaction
in presence of supercoiled plasmid DNA


organism: Leishmania donovani

proof_lines: pH 7.5, 30°C, recombinant N-terminal domain, ATPase activity


substrate_name: Unknown

proof_lines: pH 7.5, 30°C, recombinant N-terminal domain, inhibition of ATPase activity

substrate: Unknown


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.7; 303.15 K; cofactor ATP

proof_lines: pH 7.7, 30°C, recombinant Y50F mutant enzyme, in absence of DNA

proof_lines: pH 7.7, 30°C, recombinant Y50F mutant enzyme, in presence of DNA


proof_lines: pH 7.7, 30°C, recombinant Y28F mutant enzyme


assay_conditions_summary: pH 7.9; 303.15 K; cofactor ATP

proof_lines: recombinant mutant enzyme K168A from Saccharomyces cerevisiae cells, at pH 7.9 and 30°C


proof_lines: recombinant enzyme from Saccharomyces cerevisiae cells, at pH 7.9 and 30°C

proof_lines: recombinant enzyme from BHK-21 cells, at pH 7.9 and 30°C


organism: Saccharolobus solfataricus

assay_conditions_summary: 353.15 K; cofactor ATP

proof_lines: 80°C, pH not specified in the publication, wild-type enzyme


proof_lines: 80°C, pH not specified in the publication, mutant enzyme Y965F


proof_lines: pH 7.7, 30°C, recombinant wild-type or Y50F mutant enzyme, in absence of DNA

proof_lines: pH 7.7, 30°C, recombinant wild-type enzyme, in presence of DNA


proof_lines: pH 7.7, 30°C, recombinant Y50F mutant enzyme


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K230A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: below, recombinant mutant K230A, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K335A with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K333A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K328A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K334A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K330A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K329A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


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

column_label: Figure 2A; row WT; kmax and KDNA cells; kcat/Km derived from those same cells.

raw_value_unit_evidence: Figure 2A row WT: kmax 130 +/- 5 min^-1; KDNA 100 +/- 20 nM.

table_label: Figure 2A PriA DNA-dependent ATPase kmax and KDNA labels


organism: Bacillus anthracis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: pH 7.5, 37°C, addition of 60-mer oligonucleotide


proof_lines: pH 7.7, 30°C, recombinant wild-type enzyme, in absence of DNA


assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: mutant Y782F, presence of 68 bp DNA duplex, pH 7.5


organism: Drosophila melanogaster

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: 22-25°C, pH 7.2, kinesin-microtubules complex

proof_lines: pH and temperature not specified in the publication


organism: Cereibacter sphaeroides

assay_conditions_summary: cofactor ATP


proof_lines: in the absence of target protein, without cofactor A


enzyme_display_name: isobutyryl-CoA mutase

organism: Geobacillus kaustophilus

substrate_name: isobutyryl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM sodium phosphate; cofactor CoA

proof_lines: recombinant enzyme, in the presence of GTP, in 50 mM sodium phosphate buffer, pH 7.5, 250 mM NaCl at 37°C

proof_lines: recombinant enzyme, in the presence of GDP, in 50 mM sodium phosphate buffer, pH 7.5, 250 mM NaCl at 37°C

proof_lines: recombinant enzyme, in 50 mM sodium phosphate buffer, pH 7.5, 250 mM NaCl at 37°C

enzyme: isobutyryl-CoA mutase

substrate: isobutyryl-CoA


organism: Aeropyrum pernix

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

assay_conditions_summary: pH 5; 363.15 K; cofactor ATP

column_label: PMID 17092293 Figure 4/prose, ApcpnA ATP hydrolysis, Km = 10.04 mM and kcat = 2.21 min^-1.

raw_value_unit_evidence: Figure 4/prose reports Km = 10.04 mM and kcat = 2.21 min^-1 for ATP hydrolysis by ApcpnA.

row_label: ApcpnA ATP hydrolysis

table_label: Figure 4/prose


enzyme_display_name: DNA topoisomerase

substrate_name: negatively supercoiled plasmid pXXZ06 DNA

enzyme: DNA topoisomerase


organism: Geobacillus stearothermophilus


enzyme_display_name: L-arabinose isomerase

substrate_name: L-arabinose

enzyme: L-arabinose isomerase

substrate: L-arabinose


substrate_name: D-galactose

proof_lines: recombinant mutant H18T/Y234C, pH 6.0, 60°C

proof_lines: recombinant mutant H18T/Y234C, pH 7.5, 60°C

substrate: D-galactose


enzyme_display_name: alanine racemase

enzyme: alanine racemase


enzyme_display_name: triose-phosphate isomerase

organism: Giardia duodenalis

substrate_name: D-glyceraldehyde 3-phosphate

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

proof_lines: presence of 2-carboxyethyl methanethiosulfonate

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: glucose-6-phosphate isomerase

substrate_name: fructose 6-phosphate

smiles: C(C(C(C(C(=O)CO)O)O)O)OP(=O)(O)O

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


substrate_name: L-Ala

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

substrate: L-Ala


enzyme_display_name: chalcone isomerase

organism: Glycine max

substrate_name: liquiritigenin

enzyme: chalcone isomerase

substrate: liquiritigenin


enzyme_display_name: peptidylprolyl isomerase

organism: Halobacterium salinarum

enzyme: peptidylprolyl isomerase


organism: Helicobacter pylori

substrate_name: D-alanine

proof_lines:
Vmax 37.9 micromol/min/mg
Vmax 909 micromol/min/mg

substrate: D-alanine


enzyme_display_name: D-sedoheptulose-7-phosphate isomerase

substrate_name: D-sedoheptulose 7-phosphate

smiles: C(C(C(C(C(C(=O)CO)O)O)O)O)OP(=O)(O)O

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

enzyme: D-sedoheptulose-7-phosphate isomerase

substrate: D-sedoheptulose 7-phosphate


organism: Heyndrickxia coagulans

proof_lines:
at pH 7.0 and 70°C
pH 7.0, 70°C, recombinant enzyme
pH 7.5, 60°C


enzyme_display_name: D-alanine--D-alanine ligase

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP

proof_lines:
pH 7.4, 25°C, versus ATP
pH 7.4, 25°C, versus D-Ala

enzyme: D-alanine--D-alanine ligase


enzyme_display_name: microtubule-severing ATPase

organism: Caenorhabditis elegans

substrate_name: ATP

sequence_source: UniProtKB/Swiss-Prot Q8MNV0

assay_conditions_summary: pH 8.8; 310.15 K; cofactor ATP

enzyme: microtubule-severing ATPase


enzyme_display_name: protein disulfide-isomerase

organism: Homo sapiens

substrate_name: RNase

enzyme: protein disulfide-isomerase

substrate: RNase


enzyme_display_name: glutamate--cysteine ligase

substrate_name: L-alpha-aminobutyrate

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

enzyme: glutamate--cysteine ligase

substrate: L-alpha-aminobutyrate


enzyme_display_name: channel-conductance-controlling ATPase

assay_conditions_summary: pH 7.5; 306.15 K; cofactor ATP

proof_lines: pH 7.5, 33°C, mutant enzyme R347D, in presence of protein kinase A

proof_lines: pH 7.5, 33°C, mutant enzyme R347D, in absence of protein kinase A

enzyme: channel-conductance-controlling ATPase

substrate: ATP


enzyme_display_name: phosphoacetylglucosamine mutase

substrate_name: N-acetyl-alpha-D-glucosamine

enzyme: phosphoacetylglucosamine mutase

substrate: N-acetyl-alpha-D-glucosamine


enzyme_display_name: glutamine synthetase

substrate_name: L-Glutamine; ADP; Phosphate

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ADP

enzyme: glutamine synthetase

substrate: L-Glutamine; ADP; Phosphate


enzyme_display_name: thromboxane-A synthase

proof_lines:
recombinant TXAS
23°C, pH 7.5
native TXAS

enzyme: thromboxane-A synthase


enzyme_display_name: steroid Delta-isomerase

mutation_type: truncation

proof_lines: 22°C, pH 7.4, truncated cytosolic enzyme DEALTA283-310

enzyme: steroid Delta-isomerase


enzyme_display_name: UDP-N-acetylglucosamine 4-epimerase

enzyme: UDP-N-acetylglucosamine 4-epimerase


enzyme_display_name: adenylate cyclase

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

enzyme: adenylate cyclase


enzyme_display_name: leukotriene-C4 synthase

substrate_name: leukotriene A4

proof_lines:
human recombinant enzyme
pH 7.4, 25°C
pH 6.5, 30°C

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

proof_lines:
pH 8.0, 20°C
kidney
alpha-D-glucose, liver

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


substrate_name: leukotriene A4 methyl ester

substrate: leukotriene A4 methyl ester


enzyme_display_name: prostaglandin-E synthase

proof_lines: in the presence of 0.3 mM dodecylmaltoside

enzyme: prostaglandin-E synthase


enzyme_display_name: lactoylglutathione lyase

substrate_name: (R)-S-lactoylglutathione

enzyme: lactoylglutathione lyase

substrate: (R)-S-lactoylglutathione


proof_lines: recombinant catalytic subunit, pH 8.0, 37°C


substrate_name: prostaglandin G2

substrate: prostaglandin G2


enzyme_display_name: pancreatic ribonuclease

substrate_name: poly(C)

enzyme: pancreatic ribonuclease

substrate: poly(C)


enzyme_display_name: prostaglandin-I synthase

substrate_name: prostaglandin H2

enzyme: prostaglandin-I synthase

substrate: prostaglandin H2


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: phosphomannomutase

proof_lines:
isoform alpha-PMM2, pH 6.5, 25°C
isoform PMM2, at pH 7.5 and 32°C

enzyme: phosphomannomutase


enzyme_display_name: UniProt P0AGJ9

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P0AGJ9


enzyme_display_name: UniProt P0A8M3

substrate_name: hydroxynorvaline

smiles: CCCC(C(=O)O)NO

enzyme: UniProt P0A8M3

substrate: hydroxynorvaline


substrate_name: L-serine

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

substrate: L-serine


substrate_name: L-threonine

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

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.2

substrate: L-threonine


enzyme_display_name: UniProt Q58597

organism: Methanocaldococcus jannaschii

enzyme: UniProt Q58597


proof_lines:
Raw SKiD Env: Temp=60°C, pH=7.2
Raw SKiD Env: Temp=65°C, pH=7.5


enzyme_display_name: UniProt P07813

substrate_name: L-leucine

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

enzyme: UniProt P07813

substrate: L-leucine


enzyme_display_name: UniProt Q9P2J5

enzyme: UniProt Q9P2J5


substrate_name: L-isoleucine

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

substrate: L-isoleucine


enzyme_display_name: UniProt P09436

organism: Saccharomyces cerevisiae

substrate_name: AMP

enzyme: UniProt P09436

substrate: AMP


enzyme_display_name: Isoleucine--tRNA ligase 2

organism: Pseudomonas fluorescens

substrate_name: isoleucine

enzyme: Isoleucine--tRNA ligase 2

substrate: isoleucine


substrate_name: ATP

substrate: ATP


substrate_name: cyclic 2',3'-cytidine monophosphate

proof_lines: mutant R4A/K6A/Q9E/D16G/S17N, 25°C, pH 5.0

substrate: cyclic 2',3'-cytidine monophosphate


enzyme_display_name: peptidylprolyl isomerase

enzyme: peptidylprolyl isomerase


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

substrate_name: isopentenyl diphosphate

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

assay_conditions_summary: pH 8

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: bisphosphoglycerate mutase

proof_lines:
pH 7.5, low salt concentration
pH 7.8
pH 7.2, 0.1 M KCl

enzyme: bisphosphoglycerate mutase


enzyme_display_name: DNA topoisomerase

proof_lines: with 0.63 microM camptothecin or more numerous shifted htopoI bands detected

enzyme: DNA topoisomerase


enzyme_display_name: threonine--tRNA ligase

organism: Escherichia coli

substrate_name: tRNA(Thr); L-Threonine; ATP

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

enzyme: threonine--tRNA ligase

substrate: tRNA(Thr); L-Threonine; ATP


substrate_name: ATP; tRNA(Thr); L-Threonine

substrate: ATP; tRNA(Thr); L-Threonine


substrate_name: tRNA(Thr); ATP; L-Threonine

substrate: tRNA(Thr); ATP; L-Threonine


enzyme_display_name: leucine--tRNA ligase

organism: Methanothermobacter thermautotrophicus

substrate_name: L-Leucine; tRNA(Leu); ATP

enzyme: leucine--tRNA ligase

substrate: L-Leucine; tRNA(Leu); ATP


organism: Euglena gracilis

substrate_name: tRNALeu

substrate: tRNALeu


substrate_name: L-Leu

substrate: L-Leu


enzyme_display_name: isoleucine--tRNA ligase

proof_lines:
pH 7.5, recombinant isozyme IleRS-R1
pH 7.5, recombinant isozyme IleRS-R2
pH 7.5, native isozyme IleRS-R2

enzyme: isoleucine--tRNA ligase


proof_lines:
pH 7.5, recombinant isozyme IleRS-R1
pH 7.5, native isozyme IleRS-R2
pH 7.5, recombinant isozyme IleRS-R2


substrate_name: Unknown

proof_lines: pH 7.5, recombinant isozyme IleRS-R1, versus L-isoleucine

proof_lines: pH 7.5, recombinant isozyme IleRS-R1, versus ATP

substrate: Unknown


proof_lines: 37°C, pH 7.6, tRNALeu from calf liver, leucylation, full-length enzyme

proof_lines: recombinant mitochondrial isozyme, pH 7.6, 37°C


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: 37°C, pH 7.6, leucylation, full-length enzyme

proof_lines: 37°C, pH 7.6, ATP-diphosphate exchange, full-length enzyme


proof_lines: recombinant mitochondrial isozyme mutant, 37°C


assay_conditions_summary: 310.15 K; cofactor ATP


organism: Brevundimonas vesicularis


organism: Pyrococcus horikoshii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E113A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R106A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 338.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R97A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I104A to reconstruct the assayed variant sequence.


column_label: Table 3 (Steady-state leucine activation kinetics of Ph LeuRS and its single-point mutants), Leucine column group, enzyme row 'Ph LeuRS'; column 'K m (uM)' = 5.92; column 'k cat (s-1)' = 6.0; column 'k cat /K m (s-1 . mM-1)' = 1013. The ATP column group of the same enzyme row prints 'K m (uM)' = 578, 'k cat (s-1)' = 6.8 and 'k cat /K m (s-1 . mM-1)' = 11.8 for the separate ATP-substrate export row.

normalized_value_unit_evidence: Km: printed Table 3 Leucine-group cell 5.92 under the column head K m (uM); 1 uM is 1/1000 mM, so 5.92 / 1000 = 0.00592 mM. kcat: printed Table 3 Leucine-group cell 6.0 under the column head k cat (s-1); the printed turnover column is already per second, so no unit conversion applies and the paper value is 6.0 s^(-1). kcat/Km: printed Table 3 Leucine-group cell 1013 under the column head k cat /K m (s-1 . mM-1); that column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 1013.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Leucine column group, enzyme row Ph LeuRS: K m = 5.92 uM; k cat = 6.0 s^-1; printed k cat /K m = 1013 s^-1 . mM^-1.

table_label: Table 3: Steady-state leucine activation kinetics of Ph LeuRS and its single-point mutants (Biochem. J. 2010, 429(3):505-513)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D121A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y105A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W103A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T118A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I115A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K100A/Y105A with inferred residue-numbering offset -33 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E114A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D98A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F119A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T101A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K100A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V108A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N96A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K100A/Y109A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R106A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y109A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R97A to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

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

proof_lines: kcat is 47 sec(-1) for HCCA, 19 sec(-1) for THBPA and 39 sec(-1) for glutathion.


substrate_name: glutathione (at pH 7 and 25 degrees Celsius)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D173A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E167A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8.2; 318.15 K; cofactor ATP


enzyme_display_name: lactoylglutathione lyase

substrate_name: glutathione-methylglyoxal

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

enzyme: lactoylglutathione lyase

substrate: glutathione-methylglyoxal


enzyme_display_name: tyrosine--tRNA ligase

substrate_name: L-tyrosine

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

proof_lines:
mutant TyrRS, RMSSS
mutant TyrRS, AMSSS
mutant TyrRS, KMGCA

enzyme: tyrosine--tRNA ligase

substrate: L-tyrosine


substrate_name: L-leucine

proof_lines: mutant lacking residues Q281 to D294, 45°C

proof_lines: mutant lacking residues S295 to L304, 45°C


assay_conditions_summary: 318.15 K; cofactor ATP


organism: Saccharolobus solfataricus

substrate_name: L-serine

proof_lines: pH 7.2, 60°C, recombinant wild-type enzyme

substrate: L-serine


substrate_name: L-threonine

substrate: L-threonine


proof_lines: kcat is 5.8 sec(-1) for the activation reaction of L-threonine. kcat is 1.1 sec(-1) for the activation reaction of L-serine. kcat is 0.061 sec(-1) for the aminoacylation of tRNA(Thr) with L-threonine.


organism: Escherichia coli (strain K12)

substrate_name: azatyrosine

proof_lines: kcat is 0.74 sec(-1) with L-tyrosine as substrate. kcat is 0.11 sec(-1) with azatyrosine as substrate.

substrate: azatyrosine


enzyme_display_name: diaminopimelate epimerase

organism: Haemophilus influenzae

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

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

enzyme: diaminopimelate epimerase


organism: Acidithiobacillus ferrooxidans

substrate_name: ATP


substrate_name: tyrosine

substrate: tyrosine


organism: Bacillus subtilis

substrate_name: L-Isoleucine; tRNA(Ile); ATP

substrate: L-Isoleucine; tRNA(Ile); ATP


substrate_name: ATP; Isoleucine

substrate: ATP; Isoleucine


substrate_name: ATP; L-Isoleucine; tRNA(Ile)

substrate: ATP; L-Isoleucine; tRNA(Ile)


substrate_name: tRNA(Ile); L-Isoleucine; ATP

substrate: tRNA(Ile); L-Isoleucine; ATP


organism: Staphylococcus aureus

substrate_name: L-Isoleucine; ATP; tRNA(Ile)

substrate: L-Isoleucine; ATP; tRNA(Ile)


organism: Aeropyrum pernix

substrate_name: tRNATyr

proof_lines: wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl

substrate: tRNATyr


substrate_name: ATP; tRNA(Tyr); L-Tyrosine

substrate: ATP; tRNA(Tyr); L-Tyrosine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D268R with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: tRNA(Tyr)

proof_lines: The catalytic activity is reduced by substitutions of residues forming the specificity determinant on the target tRNA(Tyr).

substrate: tRNA(Tyr)


substrate_name: Unknown

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


enzyme_display_name: tryptophan--tRNA ligase

substrate_name: tRNA(Trp); ATP; L-Tryptophan

enzyme: tryptophan--tRNA ligase

substrate: tRNA(Trp); ATP; L-Tryptophan


organism: Mus musculus

substrate_name: tRNA(Thr)

substrate: tRNA(Thr)


substrate_name: tRNA(Leu); L-Leucine; ATP

substrate: tRNA(Leu); L-Leucine; ATP


organism: Homo sapiens

substrate_name: L-Leucine; ATP; tRNA(Leu)

substrate: L-Leucine; ATP; tRNA(Leu)


substrate_name: tRNA

substrate: tRNA


organism: Thiobacillus ferrooxidans

substrate_name: tRNA(Tyr); L-Tyrosine; ATP

substrate: tRNA(Tyr); L-Tyrosine; ATP


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

substrate_name: L-threonine activation

substrate: L-threonine activation


organism: Burkholderia thailandensis

proof_lines: Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication

substrate: Unknown


proof_lines: kcat is 36, 22 and 26 sec(-1) for L-threonine, beta-hydroxynorvaline and L-serine respectively.


organism: Methanocaldococcus jannaschii


organism: Giardia duodenalis

substrate_name: L-leucine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q154A to reconstruct the assayed variant sequence.

substrate: L-leucine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K152A to reconstruct the assayed variant sequence.


substrate_name: ATP

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K170A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K166A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E165A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W155A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K139A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S153A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K141A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K142A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D173A to reconstruct the assayed variant sequence.


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: L-serine activation

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

proof_lines: kcat is 12.3 sec(-1) for L-serine, 13.5 for L-threonine at 60 degrees Celsius (PubMed:15240874). kcat is 1.2 sec(-1) (PubMed:15507440).

substrate: L-serine activation


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

proof_lines: kcat is 1.3 sec(-1) for L-serine, 1.9 for L-threonine at 60 degrees Celsius (PubMed:15240874).


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D423A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D423A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R439A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R439A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R434A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R434A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N400A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N400A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S409E with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S409E, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K408A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K408A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E405A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E405A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


organism: Yersinia pestis

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

proof_lines: Ki above 0.05 mM with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication


organism: Aquifex aeolicus

substrate_name: tRNALeu

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q269ter with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

substrate: tRNALeu


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -3, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -11, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -13, so it is treated as a source-provided variant sequence.


proof_lines:
wild-type, pH 8.2, 45°C
wild-type, 45°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V286ter to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K238A to reconstruct the assayed variant sequence.


substrate_name: L-isoleucyl-tRNALeu

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y520A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

substrate: L-isoleucyl-tRNALeu


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

proof_lines:
wild-type, pH 7.5, 37°C
wild-type, 45°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y520H with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: Pseudomonas putida


organism: Acanthamoeba polyphaga mimivirus


organism: Geobacillus stearothermophilus

substrate_name: L-Tyrosine; ATP

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

unit: molwedgeoneswedgeone

substrate: L-Tyrosine; ATP


substrate_name: L-Tyrosine; ATP; tRNA(Tyr)

substrate: L-Tyrosine; ATP; tRNA(Tyr)


organism: Bacillus subtilis

substrate_name: L-Tryptophan; ATP; tRNA(Trp)

substrate: L-Tryptophan; ATP; tRNA(Trp)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E167A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D173A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K139A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S153A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K166A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K170A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K152A to reconstruct the assayed variant sequence.


proof_lines: pH 8.2, 45°C, recombinant mutant DELTAESI/DELTAHsESI

proof_lines: mutant lacking residues Q281 to D294, 45°C

proof_lines: mutant lacking residues S295 to L304, 45°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T341A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R338A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: Streptomyces griseus

substrate_name: AMP

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

proof_lines: pH 7.5, 30°C, deacylation, recombinant mutant D334A

substrate: AMP


proof_lines: pH 7.5, 30°C, deacylation, recombinant wild-type enzyme


organism: Pyrococcus horikoshii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Δ911 to reconstruct the assayed variant sequence.

proof_lines: truncation mutant DELTA911-913, pH 7.5, 37°C


substrate_name: tRNAGAGLeu

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K696A to reconstruct the assayed variant sequence.

substrate: tRNAGAGLeu


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

assay_conditions_summary: pH 7.8; 310.15 K; buffer pH this article states; cofactor ATP

column_label: Table 1 (Kinetic constants of LeuRSs and their mutants at basic residues from various species for their cognate tRNAs in aminoacylation reaction), Enzyme block 'PhLeuRS', Mutant row 'WTb'; column 'Km' (micromolar) = 0.20; column 'kcat' (s^-1) = 0.020; column 'kcat/Km' (s^-1 uM^-1) = 0.11; column 'Relative value' is the unitless efficiency of the row against the wild type of the same enzyme block.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.20 under the micromolar Km column head; 1 uM is 1/1000 mM, so 0.20 / 1000 = 0.0002 mM. kcat: printed Table 1 cell 0.020 under the column head kcat (s^-1); the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.02 s^(-1). kcat/Km: printed Table 1 cell 0.11 under the column head kcat/Km (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.11 x 1000 = 110.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme block PhLeuRS, mutant row WTb: Km = 0.20 uM; kcat = 0.020 s^-1; printed kcat/Km = 0.11 s^-1 uM^-1.

table_label: Table 1: Kinetic constants of LeuRSs and their mutants at basic residues from various species for their cognate tRNAs in aminoacylation reaction (J. Biol. Chem. 2015, 290(19):12256-12267)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R703A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K692A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K699A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K142A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W155A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q154A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K141A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E165A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


organism: Escherichia coli (strain K12)

proof_lines: kcat is 36, 22 and 26 sec(-1) for L-threonine, beta-hydroxynorvaline and L-serine respectively.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D444A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: Homo sapiens

substrate_name: tRNALeuUUR

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K600R to reconstruct the assayed variant sequence.

proof_lines: human derived substrate, pH 7.0, 37°C, recombinant mutant K600R

proof_lines: Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant K600R

substrate: tRNALeuUUR


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K600L to reconstruct the assayed variant sequence.

proof_lines: human derived substrate, pH 7.0, 37°C, recombinant mutant K600L

proof_lines: Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant K600L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K600F to reconstruct the assayed variant sequence.

proof_lines: human derived substrate, pH 7.0, 37°C, recombinant mutant K600F

proof_lines: Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant K600F


organism: Methanothermobacter thermautotrophicus

substrate_name: tRNA(Leu); ATP; L-Leucine

substrate: tRNA(Leu); ATP; L-Leucine


organism: [Mycoplasma] mobile

substrate_name: tRNALeu(GAG)

proof_lines: in 100 mM Tris-HCl (pH 7.8), 30 mM KCl, 12 mM MgCl2, 5 mM dithiothreitol, at 30°C

substrate: tRNALeu(GAG)


substrate_name: tRNAUAALeu

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K452E to reconstruct the assayed variant sequence.

substrate: tRNAUAALeu


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -7, so it is treated as a source-provided variant sequence.


assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP

column_label: Table 1 (Kinetic constants of LeuRSs and their mutants at basic residues from various species for their cognate tRNAs in aminoacylation reaction), Enzyme block 'MmLeuRS', Mutant row 'WT'; column 'Km' (micromolar) = 1.5; column 'kcat' (s^-1) = 3.3; column 'kcat/Km' (s^-1 uM^-1) = 2.2; column 'Relative value' is the unitless efficiency of the row against the wild type of the same enzyme block.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.5 under the micromolar Km column head; 1 uM is 1/1000 mM, so 1.5 / 1000 = 0.0015 mM. kcat: printed Table 1 cell 3.3 under the column head kcat (s^-1); the printed turnover column is already per second, so no unit conversion applies and the paper value is 3.3 s^(-1). kcat/Km: printed Table 1 cell 2.2 under the column head kcat/Km (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.2 x 1000 = 2200.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme block MmLeuRS, mutant row WT: Km = 1.5 uM; kcat = 3.3 s^-1; printed kcat/Km = 2.2 s^-1 uM^-1.


sequence_variant_note: Mutation signature K456E 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_unique and applied mutation signature K452A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +14, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R451K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R449K to reconstruct the assayed variant sequence.


organism: Lacticaseibacillus casei

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N23K to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature S13K 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_accession and applied mutation signature P15K to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K22V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature G19N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature A18G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature A18G/G19N to reconstruct the assayed variant sequence.


substrate_name: tRNAIle

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

substrate: tRNAIle


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T252D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T252E to reconstruct the assayed variant sequence.


substrate_name: L-Leucine

substrate: L-Leucine


substrate_name: L-Isoleucine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00956 and applied mutation signature D342A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

column_label: Table 2: Steady-State Parameters for Activation of Cognate and Noncognate Amino Acids by Y59 IleRS Variants (Biochemistry 2014, 53, 6189-6198); enzyme row 'D342A'; column 'Km(Ile) (uM)' = 5.2; column 'kcat(Ile) (s^-1)' = 47; column 'kcat/Km(Ile)' = 9.04. The remaining printed columns of the same row report the valine reaction and the Ile-over-Val discrimination ratio.

normalized_value_unit_evidence: Km: printed cell 5.2 uM; 5.2 / 1000 = 0.0052 mM. kcat: printed cell 47 s^-1; the printed unit is already s^-1 and no unit conversion applies. kcat/Km: printed cell 9.04 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 9.04 x 1000 = 9040.0 s^(-1)*mM^(-1), which is the printed cell at the precision Table 2 prints it; the catalog value 9038.461538461539 s^(-1)*mM^(-1) is the full-precision quotient 47.0 / 0.0052 of the same two printed cells.

raw_value_unit_evidence: Table 2, enzyme row 'D342A': Km(Ile) = 5.2 uM; kcat(Ile) = 47 s^-1; printed kcat/Km(Ile) = 9.04 s^-1 uM^-1.

row_label: Table 2, enzyme row 'D342A', the three isoleucine cells (Km(Ile), kcat(Ile), kcat/Km(Ile))

substrate: L-Isoleucine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00956 and applied mutation signature Y59F to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Parameters for Activation of Cognate and Noncognate Amino Acids by Y59 IleRS Variants (Biochemistry 2014, 53, 6189-6198); enzyme row 'Y59F'; column 'Km(Ile) (uM)' = 2.6; column 'kcat(Ile) (s^-1)' = 21; column 'kcat/Km(Ile)' = 8.1. The remaining printed columns of the same row report the valine reaction and the Ile-over-Val discrimination ratio.

normalized_value_unit_evidence: Km: printed cell 2.6 uM; 2.6 / 1000 = 0.0026 mM. kcat: printed cell 21 s^-1; the printed unit is already s^-1 and no unit conversion applies. kcat/Km: printed cell 8.1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 8.1 x 1000 = 8100.0 s^(-1)*mM^(-1), which is the printed cell at the precision Table 2 prints it; the catalog value 8076.923076923077 s^(-1)*mM^(-1) is the full-precision quotient 21.0 / 0.0026 of the same two printed cells.

raw_value_unit_evidence: Table 2, enzyme row 'Y59F': Km(Ile) = 2.6 uM; kcat(Ile) = 21 s^-1; printed kcat/Km(Ile) = 8.1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Y59F', the three isoleucine cells (Km(Ile), kcat(Ile), kcat/Km(Ile))


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00956 and applied mutation signature Y59F/D342A to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Parameters for Activation of Cognate and Noncognate Amino Acids by Y59 IleRS Variants (Biochemistry 2014, 53, 6189-6198); enzyme row 'Y59F/D342A'; column 'Km(Ile) (uM)' = 1.9; column 'kcat(Ile) (s^-1)' = 23; column 'kcat/Km(Ile)' = 12.1. The remaining printed columns of the same row report the valine reaction and the Ile-over-Val discrimination ratio.

normalized_value_unit_evidence: Km: printed cell 1.9 uM; 1.9 / 1000 = 0.0019 mM. kcat: printed cell 23 s^-1; the printed unit is already s^-1 and no unit conversion applies. kcat/Km: printed cell 12.1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 12.1 x 1000 = 12100.0 s^(-1)*mM^(-1), which is the printed cell at the precision Table 2 prints it; the catalog value 12105.263157894737 s^(-1)*mM^(-1) is the full-precision quotient 23.0 / 0.0019 of the same two printed cells.

raw_value_unit_evidence: Table 2, enzyme row 'Y59F/D342A': Km(Ile) = 1.9 uM; kcat(Ile) = 23 s^-1; printed kcat/Km(Ile) = 12.1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Y59F/D342A', the three isoleucine cells (Km(Ile), kcat(Ile), kcat/Km(Ile))


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00956 and applied mutation signature Y59T to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Parameters for Activation of Cognate and Noncognate Amino Acids by Y59 IleRS Variants (Biochemistry 2014, 53, 6189-6198); enzyme row 'Y59T'; column 'Km(Ile) (uM)' = 41.5; column 'kcat(Ile) (s^-1)' = 11.4; column 'kcat/Km(Ile)' = 0.27. The remaining printed columns of the same row report the valine reaction and the Ile-over-Val discrimination ratio.

normalized_value_unit_evidence: Km: printed cell 41.5 uM; 41.5 / 1000 = 0.0415 mM. kcat: printed cell 11.4 s^-1; the printed unit is already s^-1 and no unit conversion applies. kcat/Km: printed cell 0.27 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.27 x 1000 = 270.0 s^(-1)*mM^(-1), which is the printed cell at the precision Table 2 prints it; the catalog value 274.69879518072287 s^(-1)*mM^(-1) is the full-precision quotient 11.4 / 0.0415 of the same two printed cells.

raw_value_unit_evidence: Table 2, enzyme row 'Y59T': Km(Ile) = 41.5 uM; kcat(Ile) = 11.4 s^-1; printed kcat/Km(Ile) = 0.27 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Y59T', the three isoleucine cells (Km(Ile), kcat(Ile), kcat/Km(Ile))


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00956 and applied mutation signature Y59T/D342A to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Parameters for Activation of Cognate and Noncognate Amino Acids by Y59 IleRS Variants (Biochemistry 2014, 53, 6189-6198); enzyme row 'Y59T/D342A'; column 'Km(Ile) (uM)' = 38.3; column 'kcat(Ile) (s^-1)' = 10.7; column 'kcat/Km(Ile)' = 0.28. The remaining printed columns of the same row report the valine reaction and the Ile-over-Val discrimination ratio.

normalized_value_unit_evidence: Km: printed cell 38.3 uM; 38.3 / 1000 = 0.0383 mM. kcat: printed cell 10.7 s^-1; the printed unit is already s^-1 and no unit conversion applies. kcat/Km: printed cell 0.28 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.28 x 1000 = 280.0 s^(-1)*mM^(-1), which is the printed cell at the precision Table 2 prints it; the catalog value 279.3733681462141 s^(-1)*mM^(-1) is the full-precision quotient 10.7 / 0.0383 of the same two printed cells.

raw_value_unit_evidence: Table 2, enzyme row 'Y59T/D342A': Km(Ile) = 38.3 uM; kcat(Ile) = 10.7 s^-1; printed kcat/Km(Ile) = 0.28 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Y59T/D342A', the three isoleucine cells (Km(Ile), kcat(Ile), kcat/Km(Ile))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A133E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D112E with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D112E/P129S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G329S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L91F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M196I with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P129S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T60R to reconstruct the assayed variant sequence.


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


substrate_name: L-Tryptophan

substrate: L-Tryptophan


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


substrate_name: L-leucine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D399A to reconstruct the assayed variant sequence.

substrate: L-leucine


organism: Pseudomonas fluorescens

substrate_name: ATP

substrate: ATP


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


substrate_name: L-tyrosine

substrate: L-tyrosine


assay_conditions_summary: pH 9; 295.15 K; cofactor ATP


substrate_name: L-tryptophan

substrate: L-tryptophan


organism: Methanocaldococcus jannaschii

substrate_name: L-threonine

column_label: Table 1 reports M. jannaschii threonine kcat 1.9, KM 0.10 mM, and kcat/KM 19.

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.1 normalized_unit=mM; kcat/Km normalized_value=19 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; Km raw_value=0.10 raw_unit=mM; kcat/Km raw_value=19 raw_unit=s^-1/mM

row_label: M. jannaschii / Threonine

table_label: Table 1

substrate: L-threonine


substrate_name: L-serine

substrate: L-serine


substrate_name: L-Tyrosine

substrate: L-Tyrosine


organism: Mesomycoplasma mobile


substrate_name: L-Threonine

substrate: L-Threonine


substrate_name: isoleucine

substrate: isoleucine


assay_conditions_summary: cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F130S with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature F130S matches the mutant residue at offset +0 and the reference residue at offset +8; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: tyrosine

substrate: tyrosine


organism: Cricetulus griseus


organism: Mus musculus


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: leucine

substrate: leucine


substrate_name: tRNATrp

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

proof_lines: 22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153G, aminoacylation

substrate: tRNATrp


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


substrate_name: tRNALeu

substrate: tRNALeu


proof_lines: mutant E292D, E292A, and E292F pH 7.8, 37°C


proof_lines: mutants E292Q, E292D, and E292A, pH 7.8, 37°C


proof_lines: 22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149D/E153R, aminoacylation


proof_lines: 22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153K, aminoacylation


proof_lines: 22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme E153D, aminoacylation


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

proof_lines: 22°C, pH 7.5, tRNATrp from Bacillus subtilis, wild-type enzyme, aminoacylation


proof_lines: 22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149R, 0.32 aminoacylation

proof_lines: 22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149R, aminoacylation


proof_lines: 22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149E, aminoacylation


proof_lines: 22°C, pH 7.5, tRNATrp from Bacillus subtilis, mutant enzyme K149G, aminoacylation


substrate_name: Trp

proof_lines: 25°C, pH 9.0, mutant enzyme K149D/E153R, activation of Trp

substrate: Trp


assay_conditions_summary: pH 9; 298.15 K; cofactor ATP

proof_lines: 25°C, pH 9.0, mutant enzyme K149G, activation of Trp


proof_lines: 25°C, pH 9.0, mutant enzyme K149E, activation of Trp


proof_lines: 25°C, pH 9.0, mutant enzyme E153D, activation of Trp


proof_lines: 25°C, pH 9.0, wild-type enzyme, activation of Trp


proof_lines: 25°C, pH 9.0, mutant enzyme K149R, activation of Trp


proof_lines: 25°C, pH 9.0, mutant enzyme E153K, activation of Trp


organism: Mycobacterium tuberculosis


proof_lines: aminoacylation reaction, mutant enzyme, pH 7.8, 37°C


proof_lines: ATP-diphosphate exchange reaction, mutant enzyme, pH 7.8, 37°C


proof_lines: wild type enzyme, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C


proof_lines: aminoacylation reaction, wild-type enzyme, pH 7.8, 37°C


substrate_name: L-isoleucine

substrate: L-isoleucine


substrate_name: L-methionine

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

substrate: L-methionine


proof_lines: ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.8, 37°C


organism: Aquifex aeolicus


proof_lines:
37°C, pH 7.8, mutant enzyme R94A
pH 7.8, 65°C, recombinant mutant R94A


proof_lines: pH 6.8, 65°C, recombinant wild-type enzyme


organism: Saccharomyces cerevisiae

proof_lines: mutant enzyme T357A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


proof_lines: wild type enzyme, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


proof_lines: mutant enzyme N432A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


proof_lines: mutant enzyme Q362A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


proof_lines: mutant enzyme D437A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


proof_lines: mutant enzyme N356A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


proof_lines: mutant enzyme N359A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


proof_lines: mutant enzyme Y405A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


proof_lines: mutant enzyme E401A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


proof_lines: mutant enzyme K440A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


substrate_name: tRNACUA

proof_lines: wild-type, 37°C, pH not specified in the publication

substrate: tRNACUA


substrate_name: D-tyrosine

substrate: D-tyrosine


proof_lines: pH 7.6, 30°C, wild-type enzyme, radioisotopic assay

proof_lines: pH 7.6, 30°C, wild-type enzyme, spectrophotometric assay


organism: Geobacillus stearothermophilus


substrate_name: ATP

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: L-tyrosine

substrate: L-tyrosine


proof_lines: wild-type enzyme and mutant L105V, pH 7.8, 25°C


organism: Acidithiobacillus ferrooxidans

mutation_signature: recombinant truncated mutant


substrate_name: L-tryptophan

substrate: L-tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S226A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S224A to reconstruct the assayed variant sequence.

column_label: Table I page 28397; row S224A; columns KTyr and k3; units uM and s^-1

normalized_value_unit_evidence: Km=0.05 mM from 50 uM KTyr; kcat=6 s^-1; kcat/Km=120 s^-1 mM^-1 from 6/0.05

table_label: Table I


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K231A to reconstruct the assayed variant sequence.

column_label: Table I page 28397; row K231A; columns KTyr and k3; units uM and s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S225A to reconstruct the assayed variant sequence.

column_label: Table I page 28397; row S225A; columns KTyr and k3; units uM and s^-1


column_label: Table I page 28397; row Wild-type; columns KTyr and k3; units uM and s^-1

raw_value_unit_evidence: Table I Wild-type row: KTyr=34 (+/-8) uM; k3=45 (+/-4) s^-1

row_label: Wild-type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S225A/K231A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant S225A and mutant K231A


assay_conditions_summary: pH 7.5; buffer standard; cofactor ATP

column_label: Table I. Dissociation and rate constants for each of the tyrosyl-tRNA synthetase variants; row Wild-type / K_ATP; Km=4.0 mM.

normalized_value_unit_evidence: Km=4.0 mM

raw_value_unit_evidence: K_ATP=4.0 mM

row_label: Wild-type / K_ATP


column_label: Table I page 28397; row S226A; column K'ATP; unit row mM

normalized_value_unit_evidence: Km=4.1 mM for ATP from the K'ATP column

raw_value_unit_evidence: Table I S226A row: K'ATP=4.1 (+/-0.1) mM


substrate_name: K+

column_label: Table I page 28397; row S226A; column KK+; unit row mM

normalized_value_unit_evidence: Km=22 mM for K+ from the KK+ column

raw_value_unit_evidence: Table I S226A row: KK+=22 (+/-1) mM

substrate: K+


column_label: Table I page 28397; row S224A; column KK+; unit row mM

normalized_value_unit_evidence: Km=24 mM for K+ from the KK+ column

raw_value_unit_evidence: Table I S224A row: KK+=24 (+/-1) mM


column_label: Table I page 28397; row S225A; column KK+; unit row mM

normalized_value_unit_evidence: Km=30 mM for K+ from the KK+ column

raw_value_unit_evidence: Table I S225A row: KK+=30 (+/-5) mM


column_label: Table I. Dissociation and rate constants for each of the tyrosyl-tRNA synthetase variants; row Wild-type / KK+; Km=32.0 mM.

raw_value_unit_evidence: KK+=32 mM

row_label: Wild-type / KK+


substrate_name: L-leucine

substrate: L-leucine


substrate_name: tRNALeu(UAA)

substrate: tRNALeu(UAA)


organism: Neisseria gonorrhoeae


substrate_name: L-threonine

substrate: L-threonine


substrate_name: Unknown

substrate: Unknown


substrate_name: tRNAGAGLeu

proof_lines: pH 7.8, 65°C, recombinant mutant R94E/R98E

substrate: tRNAGAGLeu


proof_lines: pH 7.8, 65°C, recombinant mutant R94A/R98A


substrate_name: hydroxynorvaline

mutation_signature: truncated enzyme DELTAN

substrate: hydroxynorvaline


substrate_name: L-serine

substrate: L-serine


substrate_name: tRNALeu

substrate: tRNALeu


organism: Bacillus subtilis

substrate_name: tRNATrp

mutation_signature: deletion 234-238 mutant

substrate: tRNATrp


mutation_signature: deletion 108-122 mutant


proof_lines: 25°C, pH 9.0, wild-type enzyme, activation of Trp


substrate_name: tRNALeuUUR

proof_lines: human derived substrate, pH 7.0, 37°C, recombinant mutant L570K

proof_lines: Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant L570K

substrate: tRNALeuUUR


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


proof_lines: human derived substrate, pH 7.0, 37°C, recombinant mutant L570F

proof_lines: Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant L570F


substrate_name: tRNALeuCUN

proof_lines: Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutant L570R

substrate: tRNALeuCUN


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


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


proof_lines: pH 7.5, 37°C, mutant T243R/D342A, in presence of tRNA


proof_lines: pH 7.5, 37°C, mutant D342A, in presence of tRNA


proof_lines: pH 7.5, 37°C, mutant T234R, in presence of tRNA


proof_lines: pH 7.5, 37°C, wild-type IleRS, in presence of tRNA


organism: Homo sapiens

substrate_name: L-isoleucine

substrate: L-isoleucine


proof_lines:
wild-type, pH 7.6, 30°C
pH 7.6, 37°C, wild-type enzyme


proof_lines:
mutant D399A, pH 7.6, 30°C
pH 7.6, 37°C, mutant D399A


proof_lines: pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK

proof_lines: pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK

proof_lines: pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK


substrate_name: tRNATyr

proof_lines: pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK

proof_lines: pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK

proof_lines: pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK

substrate: tRNATyr


substrate_name: ATP

substrate: ATP


substrate_name: adenosine 5'-O-(3-thiotriphosphate)

substrate: adenosine 5'-O-(3-thiotriphosphate)


substrate_name: tubercidin 5'-triphosphate

substrate: tubercidin 5'-triphosphate


substrate_name: 8-bromoadenosine 5'-triphosphate

substrate: 8-bromoadenosine 5'-triphosphate


substrate_name: tRNAIle

proof_lines: pH 7.5, 30°C, deacylation, recombinant mutant D334A

substrate: tRNAIle


substrate_name: AMP

substrate: AMP


proof_lines: pH 7.5, 30°C, deacylation, recombinant wild-type enzyme


substrate_name: L-threonine

proof_lines: wild-type, aminoacylation, pH 7.5, temperature not specified in the publication

substrate: L-threonine


proof_lines: chimeric protein, aminoacylation, pH 7.5, temperature not specified in the publication


proof_lines: chimeric protein, cosubstrate L-serine, activation reaction, pH 7.5, temperature not specified in the publication

proof_lines: chimeric protein, cosubstrate L-threonine, activation reaction, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, cosubstrate L-serine, activation reaction, pH 7.5, temperature not specified in the publication

proof_lines: wild-type, cosubstrate L-threonine, activation reaction, pH 7.5, temperature not specified in the publication


substrate_name: tRNALeu from Escherichia coli

proof_lines:
recombinant enzyme complex, 55°C
aminoacylation reaction, pH 7.8, 37°C
37°C, pH 7.8

substrate: tRNALeu from Escherichia coli


assay_conditions_summary: pH 7.8; 338.15 K; cofactor ATP

proof_lines:
recombinant enzyme complex, 65°C
aminoacylation reaction, pH 7.8, 60°C
65°C, recombinant His6-tagged enzyme


substrate_name: L-leucine

proof_lines:
recombinant enzyme complex, 65°C
aminoacylation reaction, pH 7.8, 37°C
aminoacylation reaction, pH 7.8, 60°C

substrate: L-leucine


substrate_name: L-methionine

substrate: L-methionine


substrate_name: L-norvaline

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

substrate: L-norvaline


organism: Drosophila melanogaster


substrate_name: tyrosine

substrate: tyrosine


organism: Bos taurus

substrate_name: tRNATrp

proof_lines:
aminoacylation
enzyme form TRS108, tRNA esterification
enzyme form TRS82, tRNA esterification

substrate: tRNATrp


substrate_name: Trp

proof_lines: enzyme form TRS82, tryptophan-dependent ATP-diphosphate exchange

proof_lines: enzyme form TRS108, tryptophan-dependent ATP-diphosphate exchange

substrate: Trp


proof_lines: diphosphate, tryptophan-dependent ATP-diphosphate exchange


organism: Escherichia coli

proof_lines:
recombinant enzyme
native enzyme
37°C, pH 7.8, native enzyme


substrate_name: tRNALeu

substrate: tRNALeu


proof_lines:
in absence of KCl, pH 7.4, 30°C
in presence of 50 mM KCl, pH 7.4, 30°C
in presence of 100 mM KCl, pH 7.4, 30°C


substrate_name: diphosphate

proof_lines:
in presence of 0.9 mM KCl, pH 7.4, 30°C
in presence of 0.5 mM KCl, pH 7.4, 30°C
in absence of KCl, pH 7.4, 30°C

substrate: diphosphate


proof_lines:
in absence of KCl, pH 7.4, 30°C
in presence of 0.5 mM KCl, pH 7.4, 30°C
in presence of 0.9 mM KCl, pH 7.4, 30°C


substrate_name: Ile-tRNALeu

proof_lines: mutant enzyme R286E, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C

substrate: Ile-tRNALeu


proof_lines: mutant enzyme R185E, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C


proof_lines: mutant enzyme E184R, in 100 mM HEPES (pH 7.8), 10 mM MgCl2, at 37°C


substrate_name: L-valine

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

proof_lines: presence of L-norvalyl-tRNAIle-ox, pH 7.5, 37°C

substrate: L-valine


substrate_name: L-isoleucine

substrate: L-isoleucine


substrate_name: ATP

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: phosphate exchange reaction, pH 8.0, wild-type enzyme

proof_lines: aminoacylation reaction, pH 8.0, wild-type enzyme

substrate: ATP


substrate_name: L-tyrosine

assay_conditions_summary: pH 8

substrate: L-tyrosine


substrate_name: tRNATyr

substrate: tRNATyr


organism: Glycine max

proof_lines: chloroplasts cytoplasm


proof_lines: cytoplasm chloroplasts


substrate_name: L-tryptophan

proof_lines: pH 9.0, 22°C, recombinant enzyme, exchange assay

substrate: L-tryptophan


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Lupinus luteus


proof_lines: 37°C, pH 7.6, tRNALeu from calf liver, leucylation, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: 37°C, pH 7.6, leucylation, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)

proof_lines: 37°C, pH 7.6, ATP-diphosphate exchange, DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)


mutation_signature: DELTAChcLeuRS (a C-terminal 89-amino acid truncated enzyme form)


organism: Pseudomonas aeruginosa


proof_lines:
isoform TyrS, pH 7.5, 37°C
isoform TyrZ, pH 7.5, 37°C


proof_lines:
isoform TyrZ, pH 7.5, 37°C
isoform TyrS, pH 7.5, 37°C


organism: Pseudomonas putida


substrate_name: L-threonine

substrate: L-threonine


organism: Rattus norvegicus


proof_lines: ATP-diphosphate exchange reaction and aminoacylation


substrate_name: norvaline

substrate: norvaline


substrate_name: L-leucine

substrate: L-leucine


organism: Triticum aestivum


organism: Aeropyrum pernix K1


substrate_name: tRNAArg

substrate: tRNAArg


organism: Archaeoglobus fulgidus


substrate_name: Unknown

substrate: Unknown


substrate_name: tRNAThr

proof_lines: pH 7.4, 30°C, recombinant wild-type enzyme

substrate: tRNAThr


mutation_signature: truncated enzyme core DELTAN truncated enzyme core DELTAN


substrate_name: L-oxonorvaline

substrate: L-oxonorvaline


substrate_name: tRNATrp

substrate: tRNATrp


organism: Cricetulus griseus

proof_lines: recombinant wild-type enzyme, pH 7.8, 25°C


mutation_signature: recombinant truncated mutant enzyme

proof_lines: recombinant truncated mutant enzyme, pH 7.8, 25°C


substrate_name: ammonia

smiles: N

substrate: ammonia


organism: Geobacillus stearothermophilus

substrate_name: diphosphate

proof_lines: in presence of 150 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30°C

proof_lines: in presence of 50 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30°C

proof_lines: in absence of KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30°C

substrate: diphosphate


substrate_name: AMP

substrate: AMP


organism: Haloferax volcanii


substrate_name: tRNASer mutant

proof_lines:
pH 7.5, 37°C
tRNALeu isoacceptor, pH 7.5, 37°C

substrate: tRNASer mutant


substrate_name: tRNALeuUUR

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

proof_lines: Escherichia coli derived substrate, pH 7.0, 37°C, recombinant wild-type enzyme

proof_lines: pH 7.8, 37°C, recombinant wild-type enzyme

substrate: tRNALeuUUR


substrate_name: tRNALeuCUN

proof_lines: Escherichia coli derived substrate, pH 7.0, 37°C, recombinant mutants K600L and K600R

substrate: tRNALeuCUN


substrate_name: tRNAGAGLeu

proof_lines: pH 7.5, 37°C, recombinant mutant R668E/R672E

substrate: tRNAGAGLeu


proof_lines: pH 7.5, 37°C, recombinant mutant R668A/R672A