organism: Neurospora crassa

substrate_name: Leu

proof_lines:
aminoacylation
ATP-diphosphate exchange reaction

substrate: Leu


enzyme_display_name: leucine--tRNA ligase

substrate_name: 8-bromoadenosine 5'-triphosphate

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: cofactor ATP

enzyme: leucine--tRNA ligase

substrate: 8-bromoadenosine 5'-triphosphate

source: brenda


enzyme_display_name: tyrosine--tRNA ligase

organism: Escherichia coli

substrate_name: tyrosine

proof_lines:
acylation
ATP-diphosphate exchange reaction

enzyme: tyrosine--tRNA ligase

substrate: tyrosine


substrate_name: ATP

substrate: ATP


enzyme_display_name: threonine--tRNA ligase

organism: Mycoplasma capricolum

substrate_name: L-serine

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

enzyme: threonine--tRNA ligase

substrate: L-serine


substrate_name: L-threonine

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

substrate: L-threonine


organism: Natrialba magadii

substrate_name: Natrialba magadii tRNALeu(CAA)

proof_lines: isoform LeuRS2, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C

proof_lines: isoform LeuRS1, in 20 mM Tris-HCl, pH 9.0, 3.5 M KCl, 30 mM MgCl2, 1 mM dithiohtreitol, at 40°C

substrate: Natrialba magadii tRNALeu(CAA)


substrate_name: L-leucine

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

substrate: L-leucine


organism: Phaseolus vulgaris

substrate_name: L-Leu

substrate: L-Leu


organism: Rattus norvegicus

substrate_name: tRNAThr

verification_status: unverified

substrate: tRNAThr

status: unverified


substrate_name: Formycin 5'-triphosphate

substrate: Formycin 5'-triphosphate


organism: Saccharomyces cerevisiae

substrate_name: tRNALeu

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

mutation_type: substitution

substrate: tRNALeu


enzyme_display_name: isoleucine--tRNA ligase

organism: Thermus thermophilus

substrate_name: L-isoleucine

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

proof_lines: pH 8.0, 65°C, recombinant wild-type enzyme

enzyme: isoleucine--tRNA ligase

substrate: L-isoleucine


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: pH 8.0, 65°C, recombinant wild-type enzyme, with respect to L-isoleucine

substrate: Unknown


organism: Staphylococcus aureus


organism: Saccharomyces pastorianus

substrate_name: L-threonyl-tRNAThr

substrate: L-threonyl-tRNAThr


substrate_name: threonine

substrate: threonine


organism: Trypanosoma brucei

proof_lines: pH and temperature not specified in the publication


organism: Aquifex aeolicus

assay_conditions_summary: pH 6.8; 338.15 K; cofactor ATP

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


organism: Comamonas testosteroni


enzyme_display_name: tryptophan--tRNA ligase

organism: Archaeoglobus fulgidus

substrate_name: bovine tRNATrp(G73, wild-type)

enzyme: tryptophan--tRNA ligase

substrate: bovine tRNATrp(G73, wild-type)


organism: Cyberlindnera jadinii

substrate_name: Leu-tRNALeu

substrate: Leu-tRNALeu


assay_conditions_summary: pH 7.9; 295.15 K; cofactor ATP

proof_lines: tRNAIle aminoacylation reaction, pH 7.9, 22°C

proof_lines: ATP-diphosphate exchange reaction, pH 7.9, 22°C


proof_lines: wild-type enzyme complementing the null mutant


mutation_signature: recombinant LS-domain deletion mutant

mutation_type: deletion

proof_lines: pH 7.5, 37°C, recombinant LS-domain deletion mutant


proof_lines: pH 7.2, 37°C, ThrRS, aminoacylation with Thr


substrate_name: isoleucine

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

substrate: isoleucine


organism: Geobacillus stearothermophilus


substrate_name: tRNAIle

substrate: tRNAIle


organism: Homo sapiens

substrate_name: L-tyrosine

proof_lines: 30°C, purified recombinant His-tagged enzyme

substrate: L-tyrosine


substrate_name: L-serine

protein_accession_database: UniProt

kcat_over_km_origin: calculated

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

proof_lines: in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C

data_origin: experimental

substrate: L-serine


substrate_name: L-threonine

substrate: L-threonine


substrate_name: tRNATrp

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

substrate: tRNATrp


substrate_name: L-tryptophan

proof_lines: wild type enzyme, in 0.1 M Tris-HCl (pH 7.5), 0.01 M potassium fluoride, 5 mM MnCl2, at 37°C

proof_lines: wild type enzyme, in 0.1 M Tris-HCl (pH 7.5), 0.01 M potassium fluoride, 5 mM MgCl2, at 37°C

substrate: L-tryptophan


enzyme_display_name: protoporphyrin ferrochelatase

enzyme: protoporphyrin ferrochelatase


enzyme_display_name: DNA 3'-5' helicase

substrate_name: ATP

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

enzyme: DNA 3'-5' helicase

substrate: ATP


enzyme_display_name: guanylate cyclase

substrate_name: GTP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: pH 7.5, 37°C, not stimulated recombinant enzyme

proof_lines: pH 7.5, 37°C, NO-stimulated recombinant enzyme

enzyme: guanylate cyclase

substrate: GTP


enzyme_display_name: DNA 5'-3' helicase

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, 30°C, with saturating concentration of M13 mp18 ssDNA

enzyme: DNA 5'-3' helicase


enzyme_display_name: channel-conductance-controlling ATPase

enzyme: channel-conductance-controlling ATPase


enzyme_display_name: E1 NEDD8-activating enzyme

substrate_name: diphosphate

enzyme: E1 NEDD8-activating enzyme

substrate: diphosphate


enzyme_display_name: DNA topoisomerase (ATP-hydrolyzing)

substrate_name: Supercoiled DNA

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, temperature not specified in the publication, recombinant topo2alpha

enzyme: DNA topoisomerase (ATP-hydrolyzing)

substrate: Supercoiled DNA


enzyme_display_name: phenylpyruvate tautomerase

proof_lines: pH and temperature not specified in the publication

enzyme: phenylpyruvate tautomerase


enzyme_display_name: cysteine-S-conjugate beta-lyase

enzyme: cysteine-S-conjugate beta-lyase


substrate_name: A22G mutated tRNATyr transcript

proof_lines: pH 7.6, 37°C, native Escherichia coli tRNATyr

proof_lines: pH 7.6, 37°C, human mitochondrial tRNATyr

substrate: A22G mutated tRNATyr transcript


enzyme_display_name: UDP-glucose 4-epimerase

substrate_name: UDP-galactose

proof_lines: mutant enzyme M284K, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 24°C

proof_lines: mutant enzyme M284K, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 37°C

enzyme: UDP-glucose 4-epimerase

substrate: UDP-galactose


enzyme_display_name: malonate--CoA ligase

substrate_name: malonate

assay_conditions_summary: pH 7.1; 310.15 K; cofactor CoA

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: malonate--CoA ligase

substrate: malonate


enzyme_display_name: inositol-3-phosphate synthase

substrate_name: 2-deoxy-D-glucose 6-phosphate

enzyme: inositol-3-phosphate synthase

substrate: 2-deoxy-D-glucose 6-phosphate


substrate_name: Unknown

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


enzyme_display_name: adenylate cyclase

proof_lines: isoform AC5, in 75 mM Tris/HCl, pH 7.4, at 37°C

proof_lines: isoform AC1, in 75 mM Tris/HCl, pH 7.4, at 37°C

proof_lines: isoform ACV, in 10 mM MnCl2, 100 mM KCl, 25 mM HEPES/NaOH, pH 7.4, at 30°C

enzyme: adenylate cyclase


enzyme_display_name: serine racemase

substrate_name: L-aspartate

enzyme: serine racemase

substrate: L-aspartate


enzyme_display_name: lactoylglutathione lyase

substrate_name: methylglyoxal

smiles: CC(=O)C=O

enzyme: lactoylglutathione lyase

substrate: methylglyoxal


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


enzyme_display_name: leucine--tRNA ligase

substrate_name: tRNACAGLeu

enzyme: leucine--tRNA ligase

substrate: tRNACAGLeu


substrate_name: UTP

verification_status: verified

sequence_source: uniprot

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

column_label: Table 2 reports Forked dsDNA row Km = 1.4 mM for UTP hydrolysis.

raw_value_unit_evidence: Km raw_value=1.4 raw_unit=mM

row_label: Forked dsDNA

table_label: PMC3340288 Table 2. Determination of Km and Vmax values of TWINKLE with UTP using different DNA substrates

substrate: UTP

status: verified


enzyme_display_name: microtubule-severing ATPase

mutation_signature: Δ1

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Δ1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines: DELTA1-226, basal turnover, pH 6.8, temperature not specified in the publication

proof_lines: DELTA1-226, microtuble activated turnover, pH 6.8, temperature not specified in the publication

enzyme: microtubule-severing ATPase


enzyme_display_name: prostaglandin-D synthase

proof_lines:
at pH 6.5 and 30°C
at pH 7.6 and 25°C
pH 8.0

enzyme: prostaglandin-D synthase


enzyme_display_name: steroid Delta-isomerase

enzyme: steroid Delta-isomerase


enzyme_display_name: glucose-6-phosphate isomerase

enzyme: glucose-6-phosphate isomerase


enzyme_display_name: UniProt Q9RHV9

substrate_name: L-lysine

source_db: skid

source_license: CC BY-NC-ND 4.0

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=8

enzyme: UniProt Q9RHV9

substrate: L-lysine

source: skid


enzyme_display_name: UniProt P00957

substrate_name: glycine

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

enzyme: UniProt P00957

substrate: glycine


substrate_name: L-serine

substrate: L-serine


substrate_name: L-alanine

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

substrate: L-alanine


enzyme_display_name: UniProt P56192

substrate_name: L-methionine

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

enzyme: UniProt P56192

substrate: L-methionine


substrate_name: ATP

substrate: ATP


enzyme_display_name: UniProt P21889

substrate_name: L-Asp

enzyme: UniProt P21889

substrate: L-Asp


enzyme_display_name: peptidylprolyl isomerase

proof_lines: using Trp-Phe-Tyr-pSer-Pro-Arg-4-nitroanilide as substrate, in 50 mM HEPES, 0.1 M NaCl, 5 mM NaN3, pH 7.4, at 22°C

proof_lines: using succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide as substrate, in 50 mM HEPES, 0.1 M NaCl, 5 mM NaN3, pH 7.4, at 22°C

enzyme: peptidylprolyl isomerase


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


enzyme_display_name: guanylate cyclase

substrate_name: GTP

proof_lines: pH and temperature not specified in the publication, wild-type and mutant V902L enzymes in presence of activator GCAP1

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

proof_lines: pH and temperature not specified in the publication, wild-type enzyme in presence of activator GCAP1

enzyme: guanylate cyclase

substrate: GTP


enzyme_display_name: cysteine-S-conjugate beta-lyase

substrate_name: S-(p-bromophenyl)-L-cysteine

enzyme: cysteine-S-conjugate beta-lyase

substrate: S-(p-bromophenyl)-L-cysteine


enzyme_display_name: glutamate--cysteine ligase

substrate_name: L-Glutamate; L-alpha-Aminobutyrate; ATP

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

proof_lines:
catalytic subunit, pH 8.0, 37°C
holoenzyme, pH 8.0, 37°C
heavy subunit

enzyme: glutamate--cysteine ligase

substrate: L-Glutamate; L-alpha-Aminobutyrate; ATP


enzyme_display_name: methionine--tRNA ligase

substrate_name: tRNAMet

proof_lines: recombinant mitochondrial isozyme as GST-fusion protein, pH 7.8, 25°C

proof_lines: recombinant cytoplasmic isozyme as GST-fusion protein, pH 7.8, 25°C

proof_lines: recombinant cytoplasmic isozyme, pH 7.8, 25°C

enzyme: methionine--tRNA ligase

substrate: tRNAMet


substrate_name: L-homocysteine

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

proof_lines: editing reaction, mitochondrial isozyme, pH 7.8, 25°C

proof_lines: editing reaction, cytoplasmic isozyme, pH 7.8, 25°C

substrate: L-homocysteine


substrate_name: CoA

assay_conditions_summary: pH 7.8; 298.15 K; cofactor CoA

proof_lines: methionylation reaction, cytoplasmic isozyme, pH 7.8, 25°C

proof_lines: methionylation reaction, mitochondrial isozyme, pH 7.8, 25°C

substrate: CoA


enzyme_display_name: bisphosphoglycerate mutase

proof_lines: in the absence of 2-phosphoglycolate, at pH 7.5 and 25°C

proof_lines: in the presence of 0.01 mM 2-phosphoglycolate, at pH 7.5 and 25°C

proof_lines: in the presence of 0.05 mM 2-phosphoglycolate, at pH 7.5 and 25°C

enzyme: bisphosphoglycerate mutase


enzyme_display_name: D-alanine--poly(phosphoribitol) ligase

organism: Lacticaseibacillus casei

substrate_name: D-Ala

enzyme: D-alanine--poly(phosphoribitol) ligase

substrate: D-Ala


substrate_name: D-2-amino-n-butyric acid

substrate: D-2-amino-n-butyric acid


enzyme_display_name: lysine--tRNA ligase

organism: Cricetinae

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: recombinant wild-type enzyme, pH 7.5, 25°C

enzyme: lysine--tRNA ligase


mutation_type: truncation

proof_lines: recombinant N-terminally truncated enzyme, pH 7.5, 25°C


mutation_signature: recombinant N-terminally truncated enzyme


substrate_name: human tRNALys3

substrate: human tRNALys3


substrate_name: yeast tRNALys

substrate: yeast tRNALys


organism: Lactiplantibacillus plantarum

substrate_name: diphosphate

substrate: diphosphate


proof_lines:
formation of D-alanine hydroxamate
ATP-diphosphate exchange reaction


enzyme_display_name: valine--tRNA ligase

organism: Euglena gracilis

substrate_name: tRNAVal

proof_lines: of Euglena gracilis, , chloroplastic enzyme

enzyme: valine--tRNA ligase

substrate: tRNAVal


substrate_name: L-valine

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

proof_lines:
chloroplastic enzyme
ATP, cytoplasmic enzyme
cytoplasmic enzyme

substrate: L-valine


enzyme_display_name: aspartate--tRNA ligase

organism: Pseudomonas aeruginosa

substrate_name: tRNAAsp

enzyme: aspartate--tRNA ligase

substrate: tRNAAsp


substrate_name: L-aspartate

substrate: L-aspartate


substrate_name: ATP

substrate: ATP


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

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

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


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

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


substrate_name: L-Aspartate

source_db: oed

substrate: L-Aspartate

source: oed


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

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


organism: Tetrahymena pyriformis

substrate_name: valine

substrate: valine


enzyme_display_name: serine--tRNA ligase

organism: Zea mays

substrate_name: tRNASer

proof_lines: in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication

enzyme: serine--tRNA ligase

substrate: tRNASer


substrate_name: L-serine

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: mitochondrial isozyme, aminoacylation reaction, pH 7.5, 30°C

proof_lines: mitochondrial isozyme, ATP-diphosphate exchange reaction, pH 7.2, 30°C

substrate: L-serine


organism: Mycolicibacterium smegmatis

substrate_name: L-Met

proof_lines:
ATP-diphosphate exchange, enzyme form A
ATP-diphosphate exchange, enzyme form B

substrate: L-Met


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: E.coli tRNAfMet

source_db: uniprot

proof_lines: kcat is 2.83 sec(-1) with E.coli tRNAfMet as substrate.

substrate: E.coli tRNAfMet

source: uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: tRNA(Met) (in the absence of ARC1)

proof_lines: The presence of ARC1 reduces the KM for tRNA(Met) to less than 0.1 uM and increases the catalytic efficiency more than 500-fold.

substrate: tRNA(Met) (in the absence of ARC1)


organism: Escherichia coli

substrate_name: tRNASecUX

sequence_variant_note: Mutation signature K86C/A87Y/D88F/S160T/D228K/T229M could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: tRNASecUX


substrate_name: tRNAUTuX

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

substrate: tRNAUTuX


sequence_variant_note: Mutation signature K86A/A87L/D88T/S160P/D228R/T229N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature A87T/D88V/S160N/D228R/T229N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Methanosarcina barkeri

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E338A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G340V/G341A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N435A/S437A/W396A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R267A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R347A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N435A to reconstruct the assayed variant sequence.


organism: Acanthamoeba polyphaga mimivirus

substrate_name: ATP; tRNA(Met); L-Methionine

sequence_source: multiple

substrate: ATP; tRNA(Met); L-Methionine


organism: Enterococcus faecalis

substrate_name: ATP; L-Methionine; tRNA(Met)

substrate: ATP; L-Methionine; tRNA(Met)


substrate_name: tRNA-Met

substrate: tRNA-Met


organism: Saccharomyces cerevisiae


organism: Bacillus subtilis

substrate_name: ATP; tRNA(Lys); L-Lysine

substrate: ATP; tRNA(Lys); L-Lysine


substrate_name: ATP; Valine

substrate: ATP; Valine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E273A/D277A/K280A to reconstruct the assayed variant sequence.


organism: Methanosarcina barkeri (strain Fusaro / DSM 804)

substrate_name: tRNA(Ser CGA)

proof_lines: Catalytic efficiency is similar with the tRNA(Ser CGA) and tRNA(Ser GGA) isoacceptors, but is 5-fold lower with tRNA(Ser GCU).

substrate: tRNA(Ser CGA)


proof_lines: Catalytic efficiency is similar with the tRNA(Ser CGA) and tRNA(Ser GGA) isoacceptors, but is 2-fold higher with tRNA(Ser GCU).


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

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


organism: Thermococcus kodakaraensis

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

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

proof_lines: kcat is 0.061 sec(-1) for tRNA(Asp) aspartylation (at 60 degrees Celsius).

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


organism: Thermococcus kodakarensis

substrate_name: tRNAAsn

substrate: tRNAAsn


organism: Cricetulus griseus

substrate_name: tRNA(Lys); ATP; L-Lysine

substrate: tRNA(Lys); ATP; L-Lysine


organism: Homo sapiens

substrate_name: tRNA(Lys); L-Lysine; ATP

proof_lines: kcat is 0.31 sec(-1) for aminoacylation for tRNA(Lys).

substrate: tRNA(Lys); L-Lysine; ATP


organism: Pyrococcus horikoshii

substrate_name: tRNALysGUU

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: wild type enzyme, at 37°C in 100 mM HEPES (pH 7.2), 25 mM KCl, 10 mM MgCl2, 4 mM dithiothreitol, and 5 mM ATP

substrate: tRNALysGUU


enzyme_display_name: alanine--tRNA ligase

substrate_name: tRNA(Ala) (at 37 Celsius)

enzyme: alanine--tRNA ligase

substrate: tRNA(Ala) (at 37 Celsius)


organism: Geobacillus stearothermophilus

substrate_name: Threonine

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11931 and applied mutation signature G85R to reconstruct the assayed variant sequence.

column_label: Table 1: Amino Acid Activation by ValRS Mutants at pH 7.5, 37 C (Biochemistry 1996, volume 35, number 17, pages 5596-5601); printed column heads ValRS | Km (uM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Val group and Km (mM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Thr group; enzyme row G85R, Thr column group; column Km (mM) = 26; column kcat (s-1) = 0.173; column kcat/Km (M-1 s-1) = 6.7.

normalized_value_unit_evidence: Km: printed Table 1 Thr-group cell 26 mM; the Thr column head prints mM, so the cell is already in the export's canonical unit and no unit conversion applies, giving 26.0 mM. kcat: printed Table 1 cell 0.173 s-1; already in s^-1, so no unit conversion applies and the paper value is 0.173 s^(-1). kcat/Km: printed Table 1 cell 6.7 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.7 / 1000 = 0.0067 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row G85R, Thr column group: Km = 26 mM; kcat = 0.173 s-1; printed kcat/Km = 6.7 M-1 s-1.

row_label: Table 1, ValRS row G85R, Thr column group

substrate: Threonine

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11931 and applied mutation signature P47A to reconstruct the assayed variant sequence.

column_label: Table 1: Amino Acid Activation by ValRS Mutants at pH 7.5, 37 C (Biochemistry 1996, volume 35, number 17, pages 5596-5601); printed column heads ValRS | Km (uM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Val group and Km (mM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Thr group; enzyme row P47A, Thr column group; column Km (mM) = 19; column kcat (s-1) = 8.43; column kcat/Km (M-1 s-1) = 4.4 x 10^2.

normalized_value_unit_evidence: Km: printed Table 1 Thr-group cell 19 mM; the Thr column head prints mM, so the cell is already in the export's canonical unit and no unit conversion applies, giving 19.0 mM. kcat: printed Table 1 cell 8.43 s-1; already in s^-1, so no unit conversion applies and the paper value is 8.43 s^(-1). kcat/Km: printed Table 1 cell 4.4 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.4 x 10^2 / 1000 = 0.44 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row P47A, Thr column group: Km = 19 mM; kcat = 8.43 s-1; printed kcat/Km = 4.4 x 10^2 M-1 s-1.

row_label: Table 1, ValRS row P47A, Thr column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11931 and applied mutation signature P47G to reconstruct the assayed variant sequence.

column_label: Table 1: Amino Acid Activation by ValRS Mutants at pH 7.5, 37 C (Biochemistry 1996, volume 35, number 17, pages 5596-5601); printed column heads ValRS | Km (uM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Val group and Km (mM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Thr group; enzyme row P47G, Thr column group; column Km (mM) = 38; column kcat (s-1) = 0.583; column kcat/Km (M-1 s-1) = 1.5 x 10^1.

normalized_value_unit_evidence: Km: printed Table 1 Thr-group cell 38 mM; the Thr column head prints mM, so the cell is already in the export's canonical unit and no unit conversion applies, giving 38.0 mM. kcat: printed Table 1 cell 0.583 s-1; already in s^-1, so no unit conversion applies and the paper value is 0.583 s^(-1). kcat/Km: printed Table 1 cell 1.5 x 10^1 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.5 x 10^1 / 1000 = 0.015 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row P47G, Thr column group: Km = 38 mM; kcat = 0.583 s-1; printed kcat/Km = 1.5 x 10^1 M-1 s-1.

row_label: Table 1, ValRS row P47G, Thr column group


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


substrate_name: valine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11931 and applied mutation signature D87A to reconstruct the assayed variant sequence.

column_label: Table 1: Amino Acid Activation by ValRS Mutants at pH 7.5, 37 C (Biochemistry 1996, volume 35, number 17, pages 5596-5601); printed column heads ValRS | Km (uM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Val group and Km (mM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Thr group; enzyme row D87A, Val column group; column Km (uM) = 6 400; column kcat (s-1) = 0.067; column kcat/Km (M-1 s-1) = 1.1 x 10^1.

normalized_value_unit_evidence: Km: printed Table 1 Val-group cell 6 400 uM; 1 uM is 1/1000 mM, so 6400 / 1000 = 6.4 mM. kcat: printed Table 1 cell 0.067 s-1; already in s^-1, so no unit conversion applies and the paper value is 0.067 s^(-1). kcat/Km: printed Table 1 cell 1.1 x 10^1 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^1 / 1000 = 0.011 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row D87A, Val column group: Km = 6 400 uM; kcat = 0.067 s-1; printed kcat/Km = 1.1 x 10^1 M-1 s-1.

row_label: Table 1, ValRS row D87A, Val column group

substrate: valine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G85R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P47A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P47G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P47I to reconstruct the assayed variant sequence.


column_label: Table 1: Amino Acid Activation by ValRS Mutants at pH 7.5, 37 C (Biochemistry 1996, volume 35, number 17, pages 5596-5601); printed column heads ValRS | Km (uM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Val group and Km (mM) | kcat (s-1) | kcat/Km (M-1 s-1) for the Thr group; enzyme row WT, Val column group; column Km (uM) = 59; column kcat (s-1) = 18.1; column kcat/Km (M-1 s-1) = 3.1 x 10^5.

normalized_value_unit_evidence: Km: printed Table 1 Val-group cell 59 uM; 1 uM is 1/1000 mM, so 59 / 1000 = 0.059 mM. kcat: printed Table 1 cell 18.1 s-1; already in s^-1, so no unit conversion applies and the paper value is 18.1 s^(-1). kcat/Km: printed Table 1 cell 3.1 x 10^5 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.1 x 10^5 / 1000 = 310.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row WT, Val column group: Km = 59 uM; kcat = 18.1 s-1; printed kcat/Km = 3.1 x 10^5 M-1 s-1.

row_label: Table 1, ValRS row WT, Val column group


organism: Escherichia coli (strain K12)

substrate_name: L-methionine

substrate: L-methionine


substrate_name: ATP

substrate: ATP


substrate_name: tRNAAsp

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

substrate: tRNAAsp


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W26H/K85P with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines:
pH 6.0, 60°C, mutant enzyme W26H/K85P
pH 6.0, 60°C, mutant enzyme W26HK85P


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W26H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K85P to reconstruct the assayed variant sequence.


organism: Thermus thermophilus

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

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

proof_lines: kcat is 0.77 sec(-1) for tRNA(Asp) aspartylation at 37 degrees Celsius and 2.7 sec(-1) at 70 degrees Celsius. kcat is 0.12 sec(-1) for tRNA(Asn) aspartylation at 70 degrees Celsius.

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


organism: Vigna radiata var. radiata

substrate_name: threo-3-hydroxyaspartic acid

substrate: threo-3-hydroxyaspartic acid


substrate_name: Ser

substrate: Ser


substrate_name: L-serine

substrate: L-serine


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

substrate_name: L-aspartate (at 37 degrees Celsius)

substrate: L-aspartate (at 37 degrees Celsius)


substrate_name: ATP (at 37 degrees Celsius)

substrate: ATP (at 37 degrees Celsius)


substrate_name: L-Ser

substrate: L-Ser


sequence_variant_note: Mutation signature N435A/S437A/W396A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Cryptosporidium parvum

proof_lines: K0.5 value, Hill coefficient 0.71, pH not specified in the publication, temperature not specified in the publication


substrate_name: L-lysine

proof_lines: K0.5 value, Hill coefficient 0.49, pH not specified in the publication, temperature not specified in the publication

substrate: L-lysine


substrate_name: Valine; ATP

substrate: Valine; ATP


substrate_name: L-Valine; tRNA(Val); ATP

substrate: L-Valine; tRNA(Val); ATP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: methionine

substrate: methionine


organism: Escherichia coli

assay_conditions_summary: pH 8.8; cofactor ATP

source_databases_merged: brenda uniprot


organism: Methanosarcina barkeri

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F397P/A399G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

proof_lines: mutant enzyme F397P/A399G, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C


enzyme_display_name: serine racemase

substrate_name: Unknown

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

proof_lines: pH and temperature not specified in the publication

enzyme: serine racemase

substrate: Unknown


substrate_name: L-Lysine

substrate: L-Lysine


substrate_name: lysine

substrate: lysine


substrate_name: Met

substrate: Met


substrate_name: ATP

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K277A to reconstruct the assayed variant sequence.


substrate_name: valine

substrate: valine


organism: Saccharomyces cerevisiae


substrate_name: L-Aspartate

substrate: L-Aspartate


organism: Acanthamoeba polyphaga mimivirus

substrate_name: L-Methionine

substrate: L-Methionine


organism: Paracoccus denitrificans

substrate_name: L-Met

substrate: L-Met


substrate_name: selenomethionine

smiles: C[Se]CCC(C(=O)O)N

substrate: selenomethionine


substrate_name: norleucine

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

substrate: norleucine


organism: Mycolicibacterium smegmatis

column_label: Abstract reports Km values of 1.25 microM, 0.1 mM and 1.0 microM for valine, ATP and tRNA, respectively.

raw_value_unit_evidence: Km raw_value=0.1 mM raw_unit=mM

row_label: Mycobacterium smegmatis valyl-tRNA synthetase / ATP

table_label: PubMed XML abstract PMID 109126


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


organism: Clostridioides difficile

substrate_name: tRNAMet

proof_lines: mutant V216F/L203S, second step of reaction, tRNA aminoacylation

substrate: tRNAMet


proof_lines: mutant G54S, second step of reaction, tRNA aminoacylation


proof_lines: mutant G54S/L203S, second step of reaction, tRNA aminoacylation


proof_lines: mutant I57N/H101N, second step of reaction, tRNA aminoacylation


proof_lines: mutant I57N, second step of reaction, tRNA aminoacylation


proof_lines: mutant D229E, second step of reaction, tRNA aminoacylation


proof_lines: mutant V216A, second step of reaction, tRNA aminoacylation


proof_lines: wild-type, second step of reaction, tRNA aminoacylation


substrate_name: L-methionine

proof_lines: mutant G54S, first step of reaction, methionyl-adenylate formation

substrate: L-methionine


proof_lines: mutant I57N/H101N, first step of reaction, methionyl-adenylate formation


proof_lines: mutant H101N/G213C, first step of reaction, methionyl-adenylate formation


proof_lines: mutant I57N, first step of reaction, methionyl-adenylate formation


proof_lines: mutant H101D, first step of reaction, methionyl-adenylate formation


proof_lines: mutant G54S/L203S, first step of reaction, methionyl-adenylate formation


proof_lines: wild-type, first step of reaction, methionyl-adenylate formation


proof_lines: mutant V216A, first step of reaction, methionyl-adenylate formation


proof_lines: mutant V216F/L203S, first step of reaction, methionyl-adenylate formation


proof_lines: mutant D229E, first step of reaction, methionyl-adenylate formation


organism: Staphylococcus aureus

proof_lines: mutant G54A/A64P, aminoacylation reaction


proof_lines: mutant I57N/G54S, aminoacylation reaction


proof_lines: mutant I57N/A247E, aminoacylation reaction


proof_lines:
mutant G54S, aminoacylation reaction
mutant G54S


proof_lines:
mutant I57N, aminoacylation reaction
mutant I57N


proof_lines:
mutant G223C, aminoacylation reaction
mutant G223C


proof_lines:
mutant A247E, aminoacylation reaction
mutant A247E


proof_lines: mutant I57N/I238F, aminoacylation reaction


proof_lines: mutant I57N/V242F, aminoacylation reaction


proof_lines:
wild-type, aminoacylation reaction
wild-type


proof_lines:
mutant L213W, aminoacylation reaction
mutant L213W


proof_lines:
mutant V108M, aminoacylation reaction
mutant V108M


proof_lines: mutant G54A/A64P, ATP:diphosphate exchange reaction


proof_lines: mutant G54S, ATP:diphosphate exchange reaction


proof_lines: mutant I57N/G54S, ATP:diphosphate exchange reaction


proof_lines: mutant L213W, ATP:diphosphate exchange reaction


proof_lines: mutant G223C, ATP:diphosphate exchange reaction


proof_lines: mutant A247E, ATP:diphosphate exchange reaction


proof_lines: mutant I57N/A247E, ATP:diphosphate exchange reaction


proof_lines: mutant I57N/I238F, ATP:diphosphate exchange reaction


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


substrate_name: threonine

substrate: threonine


proof_lines: mutant I57N, ATP:diphosphate exchange reaction


proof_lines: mutant I57N/V242F, ATP:diphosphate exchange reaction


proof_lines: mutant V108M, ATP:diphosphate exchange reaction


proof_lines: wild-type, ATP:diphosphate exchange reaction


organism: Borreliella burgdorferi

substrate_name: L-lysine

substrate: L-lysine


substrate_name: tRNALysUUU

substrate: tRNALysUUU


proof_lines:
wild type enzyme
wild-type tRNALys


proof_lines: mutant H101N/G213C, first step of reaction, methionyl-adenylate formation


proof_lines: mutant H101D, first step of reaction, methionyl-adenylate formation


proof_lines: mutant V216A, first step of reaction, methionyl-adenylate formation


proof_lines: mutant V216F/L203S, first step of reaction, methionyl-adenylate formation


proof_lines: mutant D229E, first step of reaction, methionyl-adenylate formation


proof_lines: mutant I57N, first step of reaction, methionyl-adenylate formation


proof_lines: mutant G54S/L203S, first step of reaction, methionyl-adenylate formation


proof_lines: mutant I57N/H101N, first step of reaction, methionyl-adenylate formation


organism: Homo sapiens


proof_lines:
wild-type, pH 7.5, 25°C
wild-type, pH 7.4, 37°C


substrate_name: tRNAAsp

proof_lines: pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme E93K

substrate: tRNAAsp


proof_lines: pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme A471T


proof_lines: pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), wild-type enzyme


proof_lines: pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme L30F


proof_lines: pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme E118K


substrate_name: aspartate

substrate: aspartate


substrate_name: Asp

substrate: Asp


substrate_name: 2-aminomalonic acid

substrate: 2-aminomalonic acid


substrate_name: L-serine

substrate: L-serine


substrate_name: glycine

substrate: glycine


substrate_name: L-alanine

substrate: L-alanine


assay_conditions_summary: pH 8; 295.15 K; cofactor ATP

proof_lines: wild-type, treated with H2O2, pH 7.2, 37°C


organism: Geobacillus stearothermophilus

substrate_name: ATP

proof_lines: ATP-diphosphate exchange reaction, recombinant mutant Y271F, pH 8.0, 37°C

substrate: ATP


proof_lines: aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C

proof_lines: ATP-diphosphate exchange reaction, recombinant mutant W332F, pH 8.0, 37°C


proof_lines: aminoacylation reaction, recombinant mutant W314F, pH 8.0, 37°C

proof_lines: ATP-diphosphate exchange reaction, recombinant mutant W314F, pH 8.0, 37°C


proof_lines: aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C

proof_lines: ATP-diphosphate exchange reaction, recombinant wild-type enzyme and mutant W314F/W332F, pH 8.0, 37°C


proof_lines: aminoacylation reaction, recombinant mutant W314F/W332F, pH 8.0, 37°C

proof_lines: aminoacylation reaction, recombinant mutants W314F and W314F/W332F, pH 8.0, 37°C


proof_lines: ATP-diphosphate exchange reaction, recombinant mutant W314F/W332F, pH 8.0, 37°C


proof_lines: ATP-diphosphate exchange reaction, recombinant wild-type enzyme, pH 8.0, 37°C


organism: Xanthomonas citri


assay_conditions_summary: cofactor ATP


proof_lines: wild-type AlaRS and mutant AlaRS(K73E), AlaRS(K73Q), ATP-diphosphate exchange


proof_lines:
Cys665Ser mutant
Cys665Ser mtant


substrate_name: alanine

substrate: alanine


substrate_name: L-valine

proof_lines: aminoacylation reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C

proof_lines: ATP-diphosphate exchange reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C

substrate: L-valine


proof_lines: aminoacylation reaction, His-tagged wild-type enzyme, pH 7.5, 25°C

proof_lines: ATP-diphosphate exchange reaction, native wild-type enzyme, pH 7.5, 25°C


substrate_name: tRNAVal

proof_lines: aminoacylation reaction with L-valine, K277A mutant enzyme, pH 7.5, 25°C

proof_lines: ATP-diphosphate exchange reaction, K277A mutant enzyme, pH 7.5, 25°C

proof_lines: aminoacylation reaction with L-valine, His-tagged K277A mutant enzyme, pH 7.5, 25°C

substrate: tRNAVal


proof_lines: aminoacylation reaction with L-valine, wild-type enzyme, pH 7.5, 25°C

proof_lines: ATP-diphosphate exchange reaction, wild-type enzyme, pH 7.5, 25°C

proof_lines: aminoacylation reaction with L-valine, His-tagged wild-type enzyme, pH 7.5, 25°C


substrate_name: L-threonine

substrate: L-threonine


substrate_name: tRNAAla

substrate: tRNAAla


proof_lines:
mutant AlaRS(K73A), aminoacylation
mutant AlaR(K73A), aminoacylation


proof_lines: mutant AlaRS(K73Q), ATP-diphosphate exchange


proof_lines: mutant AlaRS(K73A), ATP-diphosphate exchange


proof_lines: mutant AlaRS(K73E), ATP-diphosphate exchange


substrate_name: tRNAMet

substrate: tRNAMet


proof_lines: ATP-diphosphate exchange reaction, mutant M665


substrate_name: DL-threonine

substrate: DL-threonine


substrate_name: (S)-2-aminohex-5-enoic acid

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

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: ATP-diphosphate exchange reaction, pH 7.6

substrate: (S)-2-aminohex-5-enoic acid


substrate_name: L-norleucine

substrate: L-norleucine


substrate_name: (S)-2-aminohex-5-ynoic acid

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

substrate: (S)-2-aminohex-5-ynoic acid


substrate_name: L-methionine

substrate: L-methionine


proof_lines: wild-type, treated with H2O2, pH 7.2, 37°C

proof_lines: wild-type substrate from Escherichia coli, pH 7.5, 37°C


proof_lines: mutant C666A, treated with H2O2, pH 7.2, 37°C


proof_lines: mutant M658A, treated with H2O2, pH 7.2, 37°C


proof_lines: mutant M785A, treated with H2O2, pH 7.2, 37°C


proof_lines: mutant M217A, treated with H2O2, pH 7.2, 37°C


substrate_name: tRNASer

substrate: tRNASer


substrate_name: L-Ser

substrate: L-Ser


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines:
wild-type, pH 7.4, 37°C
wild-type, pH 7.5, 25°C


organism: Zea mays

proof_lines: mutant ZmcSerRSDELTAC12 (deletion of 12 C-terminal residues), using maize tRNA


proof_lines: mutant ZmcSerRSDELTAC18 (deletion of 18 C-terminal residues), using maize tRNA


proof_lines:
wild-type, pH 7.5, 37°C
wild-type, pH 9, 37°C
wild-type enzyme


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: cosubstrate L-methionine, wild-type, pH 9, 37°C

proof_lines: cosubstrate beta3-methionine, wild-type, pH 9, 37°C


assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

proof_lines: cosubstrate L-methionine, mutant V298I, pH 9, 37°C

proof_lines: cosubstrate beta3-methionine, mutant V298I, pH 9, 37°C


proof_lines: human tRNALys mutant + human tRNALys,3'-7mer mutant, 20°C, wild-type enzyme

proof_lines: human wild-type tRNALys, 30°C, N-terminally truncated mutant enzyme

proof_lines: human tRNALys mutant + human tRNALys,3'-14mer mutant, 20°C, wild-type enzyme


mutation_signature: human mutant tRNALys / N-terminally truncated mutant enzyme

proof_lines: human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme


substrate_name: Unknown

mutation_signature: N-terminally truncated mutant enzyme

proof_lines: 3'-oxidized by periodate, 30°C, N-terminally truncated mutant enzyme

substrate: Unknown


organism: Plasmodium falciparum

substrate_name: tRNAAsp

proof_lines: Plasmodium falciparum aspartyl-tRNA synthetase, mutated RNA binding motif

substrate: tRNAAsp


proof_lines: Plasmodium falciparum wild type aspartyl-tRNA synthetase, amino acids 49-626


proof_lines: Plasmodium falciparum wild type aspartyl-tRNA synthetase, amino acids 49-626, ATP-diphosphate exchange


proof_lines: Plasmodium falciparum aspartyl-tRNA synthetase, mutated RNA binding motif, ATP-diphosphate exchange


substrate_name: L-aspartate

substrate: L-aspartate


substrate_name: L-serine

proof_lines: mutant enzyme H250A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C

substrate: L-serine


proof_lines: mutant enzyme P395A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C


proof_lines: mutant enzyme Q400A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C


proof_lines: mutant enzyme G402A/G405A, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C


proof_lines: wild type enzyme, in 50 mM HEPES pH 7.0, 15 mM MgCl2, 40 mM KCl, at 37°C


organism: Lupinus luteus


substrate_name: Ser

substrate: Ser


substrate_name: ATP

substrate: ATP


substrate_name: dATP

substrate: dATP


proof_lines: pH 8.2, 37°C, mitochondrial tRNAMet from Bos taurus, recombinant enzyme


proof_lines: pH 8.2, 37°C, human mitochondrial wild-type tRNAMet, recombinant enzyme

proof_lines: wild-type enzyme in the multi-enzyme complex, pH 7.5, 25°C


assay_conditions_summary: pH 8.2; 310.15 K; cofactor ATP


assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

proof_lines: serine-dependent ATP-diphosphate exchange, mutant enzymes


proof_lines:
aminoacylation, mutant enzymes
mutant SerRS11, pH 7.2, 30°C
mutant SerRS12, pH 7.2, 30°C


mutation_signature: truncated enzyme Ser / truncated enzyme


mutation_signature: truncated enzyme aminoacylation / truncated enzyme


organism: Anabaena sp.

substrate_name: L-valine

proof_lines: in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C

substrate: L-valine


substrate_name: tRNAVal(GAC)

substrate: tRNAVal(GAC)


proof_lines: mutant enzyme DELTAG75-N97/DELTAG254-N261, at pH 7.5 and 37°C


proof_lines: mutant enzyme DELTAG75-N97, at pH 7.5 and 37°C


proof_lines: mutant enzyme DELTAG254-N261, at pH 7.5 and 37°C


substrate_name: L-isoleucine

substrate: L-isoleucine


organism: Bacillus cereus

substrate_name: L-lysine

proof_lines: mutant enzyme G469A, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C

substrate: L-lysine


proof_lines: wild type enzyme, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C


proof_lines: mutant enzyme A233S, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C


organism: Escherichia coli

substrate_name: L-methionyl-tRNAMet

proof_lines: mutant enzyme S209A/S825A, at pH 7.4 and 37°C

substrate: L-methionyl-tRNAMet


proof_lines: mutant enzyme S209D/S825D, at pH 7.4 and 37°C


proof_lines:
wild type enzyme, at pH 7.4 and 37°C
pH 7.5, 25°C, wild-type enzyme
aminoacylation reaction, wild-type


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

proof_lines: Homo sapiens wild type aspartyl-tRNA synthetase, amino acids 1-500


organism: Leishmania donovani

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


proof_lines: substrate ATP, 23°C, pH not specified in the publication

proof_lines: substrate L-methionine, 23°C, pH not specified in the publication


organism: Haemophilus influenzae


organism: Mycobacterium tuberculosis


assay_conditions_summary: pH 7.7; 310.15 K; cofactor ATP


organism: Lupinus sp.

substrate_name: tRNAMet

substrate: tRNAMet


substrate_name: Met

substrate: Met


organism: Pseudomonas aeruginosa

substrate_name: tRNALys

substrate: tRNALys


substrate_name: Asp

substrate: Asp


proof_lines: pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), wild-type enzyme


organism: Rattus norvegicus

substrate_name: tRNAVal

proof_lines:
tetrameric enzyme form
monomeric enzyme form

substrate: tRNAVal


substrate_name: valine

proof_lines:
monomeric enzyme form
tetrameric enzyme form

substrate: valine


organism: Saccharomyces cerevisiae

proof_lines: serine-dependent ATP-diphosphate exchange, wild-type enzyme


proof_lines:
wild-type enzyme, pH 7.2, 30°C
wild-type, using yeast tRNA
ATP, , aminoacylation, wild-type enzyme


substrate_name: tRNASer

proof_lines:
wild-type enzyme, pH 7.2, 30°C
aminoacylation, wild-type enzyme
wild-type, using yeast tRNA

substrate: tRNASer


enzyme_display_name: threonine--tRNA ligase

substrate_name: Formycin 5'-triphosphate

enzyme: threonine--tRNA ligase

substrate: Formycin 5'-triphosphate


substrate_name: 2-Chloroadenosine 5'-triphosphate

substrate: 2-Chloroadenosine 5'-triphosphate


organism: Streptococcus pneumoniae

substrate_name: L-methionine

substrate: L-methionine


substrate_name: ATP

substrate: ATP


substrate_name: Unknown

substrate: Unknown


organism: Streptomyces sp.

proof_lines:
30°C, aminoacylation
37°C, aminoacylation
aminoacylation


substrate_name: L-serine

substrate: L-serine


substrate_name: aspartyl-tRNA

substrate: aspartyl-tRNA


substrate_name: tRNAAla

substrate: tRNAAla


substrate_name: alanine

substrate: alanine


organism: Sus scrofa

substrate_name: tRNAAsp

substrate: tRNAAsp


substrate_name: L-cysteine

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

proof_lines: in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication

substrate: L-cysteine


substrate_name: L-threonine

substrate: L-threonine


substrate_name: DL-Serine hydroxamate

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

substrate: DL-Serine hydroxamate


organism: Thermus thermophilus

mutation_signature: C-terminally truncated mutant enzyme

proof_lines: C-terminally truncated mutant enzyme, pH 7.7, 65°C


organism: Vigna radiata var. radiata

substrate_name: Met

substrate: Met


substrate_name: selenomethionine

substrate: selenomethionine


organism: Bombyx mori

proof_lines:
substrate from Bombyx mori
substrate from rabbit liver


organism: Bos taurus

substrate_name: L-aspartate

substrate: L-aspartate


substrate_name: liver tRNA

substrate: liver tRNA


substrate_name: L-Ser

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

substrate: L-Ser


substrate_name: L-lysyl-tRNALys

proof_lines: deacylation reaction, pH 7.4, 37°C, in absence of DTT

proof_lines: deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT

substrate: L-lysyl-tRNALys


substrate_name: L-lysine

proof_lines:
L-lysine lactam formation, pH 7.4, 37°C
aminoacylation
aminoacylation, enzyme form EII

substrate: L-lysine


substrate_name: tRNAMet

proof_lines: ATP-diphosphate exchange reaction, mutant D666A

substrate: tRNAMet


mutation_signature: C-terminally truncated mutant

proof_lines: aminoacylation reaction, C-terminally truncated mutant

proof_lines: ATP-diphosphate exchange reaction, C-terminally truncated mutant


substrate_name: Asp

substrate: Asp


substrate_name: ATP

substrate: ATP


organism: Geobacillus stearothermophilus

substrate_name: valine

proof_lines:
enzyme expressed in E. coli
enzyme expressed on E. coli

substrate: valine


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: recombinant T7-tagged enzyme, pH 8.0, 30°C


proof_lines:
ATP-diphosphate exchange
native enzyme, pH 8.0, 30°C
aminoacylation


substrate_name: L-methionine

proof_lines: ATP-diphosphate exchange reaction, pH 7.6

substrate: L-methionine


proof_lines:
strain 547, ATP-diphosphate exchange
ATP-diphosphate exchange


organism: Homo sapiens

substrate_name: L-alanine

substrate: L-alanine


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


substrate_name: tRNAAsp

mutation_signature: truncated enzyme truncated enzyme

substrate: tRNAAsp


organism: Methanothermobacter thermautotrophicus

proof_lines: at 25°C, in 250 mM KCl, 100 mM HEPES, pH 7.5, 10 mM dithiothreitol, 10 mM MgCl2, 0.05 mg/ml bovine serum albumin


substrate_name: tRNALys

substrate: tRNALys


organism: Plasmodium falciparum

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


proof_lines: K0.5 value, Hill coefficient 0.89, pH not specified in the publication, temperature not specified in the publication


organism: Oryza sativa

substrate_name: tRNA fraction from Saccharomyces cerevisiae

mutation_signature: truncated mutant

proof_lines: in vitro synthesized tRNAMet from Saccharomyces cerevisiae, pH 7.5, 25°C, truncated mutant


proof_lines: in vitro synthesized tRNAMet from Saccharomyces cerevisiae, pH 7.5, 25°C, wild-type enzyme


organism: Pyrococcus abyssi

proof_lines: mutant D666A, pH and temperature not specified in the publication


proof_lines:
lysylation, 28S synthetase complex
5',5'''-P1,P4-tetraphosphate formation


substrate_name: Lys

proof_lines:
lysylation, 18S synthetase complex
lysylation, free enzyme
ATP, , lysylation, free enzyme

substrate: Lys


organism: Escherichia coli

proof_lines: pH 7.5, 37°C, mutant D286A, in presence of tRNA


proof_lines: pH 7.5, 37°C, mutant K277P, in presence of tRNA


proof_lines: pH 7.5, 37°C, mutant K277P/D286A, in presence of tRNA


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

proof_lines: ATP-diphosphate exchange reaction, His-tagged wild-type enzyme, pH 7.5, 25°C

proof_lines: ATP-diphosphate exchange reaction, His-tagged wild-type and mutant enzymes, pH 7.5, 25°C


proof_lines: mutant ScSerRSDELTAC13 (deletion of 13 C-terminal residues), using yeast tRNA


substrate_name: tRNASer

substrate: tRNASer


substrate_name: L-valyl-tRNAVal

substrate: L-valyl-tRNAVal


proof_lines: substrate from cytoplasm, , mitochondrial enzyme

proof_lines: substrate from mitochondria, , mitochondrial and cytoplasmic enzyme


proof_lines: aspartyl-tRNA synthetase as a component of the multisynthetase complex or recombinant native enzyme


proof_lines: tRNAAsp, , truncated enzymes AspRS-DELTAN36 and AspRS-DELTAN20


proof_lines: Homo sapiens wild type aspartyl-tRNA synthetase, amino acids 1-500, ATP-diphosphate exchange


substrate_name: L-aspartate

column_label: Table 2 row H. sapiens wild type (1-500), header group Kinetic constants of small ligands, column Km / Asp, units uM, value 16 +/- 3.

normalized_value_unit_evidence: Km central normalized_value=0.016 normalized_unit=mM.

raw_value_unit_evidence: Table 2 reports Asp Km raw_value=16 +/- 3 raw_unit=uM for H. sapiens wild type (1-500).

row_label: H. sapiens wild type (1-500)

table_label: PMC2707213 Table 2


substrate_name: D-Ser

substrate: D-Ser


substrate_name: Formycin 5'-triphosphate

substrate: Formycin 5'-triphosphate


organism: Triticum aestivum

substrate_name: Met

substrate: Met


proof_lines:
ligase B
ligase A


substrate_name: tRNAAsn

substrate: tRNAAsn


assay_conditions_summary: pH 7.2; 343.15 K; cofactor ATP

proof_lines: 37°C, tRNA aminoacylation, enzyme form AspRS1

proof_lines: 70°C, ATP-diphosphate exchange, enzyme form AspRS1


organism: Arabidopsis thaliana

substrate_name: tRNALysCUU

substrate: tRNALysCUU


proof_lines: presence of protein BEN1, ratio 1:1, pH 7.5, temperature not specified in the publication


substrate_name: tRNASerGCU

proof_lines: recombinant wild-type enzyme, pH 8.5, 37°C

substrate: tRNASerGCU


organism: Borreliella burgdorferi

substrate_name: tRNALysUUC

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

substrate: tRNALysUUC


substrate_name: ATP


substrate_name: tmRNA

proof_lines: pH 7.6, 37°C, 0.001 mg recombinant His-tagged enzyme

proof_lines: pH 7.6, 37°C, 0.00025 mg recombinant His-tagged enzyme

proof_lines: native dual specific tRNAPhe substrate from Saccharomyces cerevisiae, pH 7.5, 37°C

substrate: tmRNA


substrate_name: tRNAPhe(57); tRNAAla; tRNAPhe(17); tRNAPhe(38)

proof_lines: tRNAPhe mutant tRNAPhe(57), pH 7.5, 37°C

proof_lines: mutant substrate from Escherichia coli, pH 7.5, 37°C

proof_lines: tRNAPhe mutant tRNAPhe(17), pH 7.5, 37°C


proof_lines:
pH 7.8, 28°C
recombinant enzyme, at pH 7.5 and 25°C
pH 7.5, 37°C


proof_lines:
aminoacylation, enzyme form EII
aminoacylation, enzyme form EI

substrate: ATP


proof_lines:
pH 8.5, 37°C
substrate from yeast
bovine substrate


substrate_name: L-trans-alpha-crotylglycine

proof_lines: ATP-diphosphate exchange reaction, pH 7.6

substrate: L-trans-alpha-crotylglycine


substrate_name: L-Lysine amide

substrate: L-Lysine amide


substrate_name: L-norvaline

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

substrate: L-norvaline


substrate_name: L-valine

proof_lines: with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C

proof_lines: with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C

proof_lines: with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C

substrate: L-valine


substrate: L-aspartate


enzyme_display_name: thromboxane-A synthase

substrate_name: Unknown

enzyme: thromboxane-A synthase

substrate: Unknown


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

proof_lines:
isomerase a
isomerase c
isomerase b

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


enzyme_display_name: lactoylglutathione lyase

substrate_name: Phenylglyoxal

enzyme: lactoylglutathione lyase

substrate: Phenylglyoxal


substrate_name: tRNAMet

proof_lines: recombinant C-terminally truncated enzyme, 37°C

substrate: tRNAMet


substrate_name: tRNAAsp

proof_lines:
native enzyme, at pH 7.5 and 25°C
recombinant enzyme, at pH 7.5 and 25°C
human mitochondrial tRNAAsp

substrate: tRNAAsp


enzyme_display_name: prostaglandin-D synthase

substrate_name: prostaglandin H2

assay_conditions_summary: pH 8

enzyme: prostaglandin-D synthase

substrate: prostaglandin H2


enzyme_display_name: pancreatic ribonuclease

substrate_name: cyclic 2',3'-CMP

enzyme: pancreatic ribonuclease

substrate: cyclic 2',3'-CMP


substrate_name: L-Met

substrate: L-Met


enzyme_display_name: channel-conductance-controlling ATPase

proof_lines: partially phosphorylated enzyme, at pH 7.4 and 37°C

proof_lines: isolated NBD1/NBD2 mixture, pH 8.0, 25°C

proof_lines: isolated NBD1/NBD2 mixture, presence of 12 nM 2-pyrimidin-7,8-benzoflavone, pH 8.0, 25°C

enzyme: channel-conductance-controlling ATPase


enzyme_display_name: methylmalonyl-CoA mutase

assay_conditions_summary: 303.15 K; cofactor CoA

enzyme: methylmalonyl-CoA mutase


enzyme_display_name: leukotriene-C4 synthase

substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

proof_lines:
pH 7.4, 25°C
human recombinant enzyme

enzyme: leukotriene-C4 synthase

substrate: glutathione


substrate_name: tRNASec mutant without anticodon arm

proof_lines: at pH 7.6, temperature not specified in the publication

substrate: tRNASec mutant without anticodon arm


organism: Hordeum vulgare


enzyme_display_name: glutamate--cysteine ligase

substrate_name: L-Glu

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

proof_lines:
holoenzyme, pH 8.0, 37°C
recombinant holoenzyme, pH 8.0, 37°C
pH 8.2, 37°C

enzyme: glutamate--cysteine ligase

substrate: L-Glu


enzyme_display_name: dichloromethane dehalogenase

organism: Hyphomicrobium sp.

substrate_name: Dichloromethane

smiles: C(Cl)Cl

enzyme: dichloromethane dehalogenase

substrate: Dichloromethane


enzyme_display_name: L-ribulose-5-phosphate 4-epimerase

organism: Klebsiella aerogenes

substrate_name: L-ribulose 5-phosphate

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

enzyme: L-ribulose-5-phosphate 4-epimerase

substrate: L-ribulose 5-phosphate


enzyme_display_name: aspartate--ammonia ligase

substrate_name: Asp

enzyme: aspartate--ammonia ligase

substrate: Asp


enzyme_display_name: N-acylglucosamine 2-epimerase

substrate_name: N-acetyl-D-mannosamine

enzyme: N-acylglucosamine 2-epimerase

substrate: N-acetyl-D-mannosamine


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: protoporphyrin

enzyme: protoporphyrin ferrochelatase

substrate: protoporphyrin


organism: Komagataeibacter xylinus

substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


enzyme_display_name: xylose isomerase

organism: Lachnoclostridium phytofermentans

substrate_name: D-xylose

proof_lines:
pH 7.5, native enzyme
pH 7.5, recombinant enzyme

enzyme: xylose isomerase

substrate: D-xylose


enzyme_display_name: isomaltulose synthase

organism: Klebsiella sp. LX3

substrate_name: sucrose

proof_lines: recombinant enzyme, pH not specified in the publication, 35°C

enzyme: isomaltulose synthase

substrate: sucrose


enzyme_display_name: S-ribosylhomocysteine lyase

organism: Lactiplantibacillus plantarum

substrate_name: S-ribosylhomocysteine

proof_lines:
isoform LuxS2, pH 8.0, 37°C
isoform LuxS1, pH 8.0, 45°C

enzyme: S-ribosylhomocysteine lyase

substrate: S-ribosylhomocysteine


organism: Klebsiella sp.


enzyme_display_name: glutamate racemase

substrate_name: L-glutamate

enzyme: glutamate racemase

substrate: L-glutamate


enzyme_display_name: galactose-6-phosphate isomerase

organism: Lactococcus lactis

substrate_name: D-altrose

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

enzyme: galactose-6-phosphate isomerase

substrate: D-altrose


enzyme_display_name: UniProt P9WFV9

organism: Mycobacterium tuberculosis

substrate_name: ATP

enzyme: UniProt P9WFV9

substrate: ATP


enzyme_display_name: UniProt P00962

substrate_name: L-glutamine

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

enzyme: UniProt P00962

substrate: L-glutamine


enzyme_display_name: UniProt O95363

organism: Homo sapiens

enzyme: UniProt O95363


enzyme_display_name: aspartate--tRNA ligase

enzyme: aspartate--tRNA ligase


organism: Lactococcus lactis subsp. lactis


enzyme_display_name: beta-phosphoglucomutase

substrate_name: beta-D-glucose 1-phosphate

proof_lines: in the presence of beta-D-glucose 1,6-diphosphate and Mg2+

proof_lines: in 50 mM buffer (HEPES, pH 7.2), with 2 mM MgCl2

enzyme: beta-phosphoglucomutase

substrate: beta-D-glucose 1-phosphate


substrate_name: D-allose

substrate: D-allose


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: cysteine--tRNA ligase

enzyme: cysteine--tRNA ligase


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

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


substrate_name: L-Cysteine

substrate: L-Cysteine


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

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


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


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

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


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

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


enzyme_display_name: proline--tRNA ligase

organism: Delonix regia

substrate_name: L-Pro

enzyme: proline--tRNA ligase

substrate: L-Pro


substrate_name: L-thiazolidine-4-carboxylic acid

substrate: L-thiazolidine-4-carboxylic acid


substrate_name: N-methylglycine

smiles: CNCC(=O)O

proof_lines: approximate value, , ATP-diphosphate exchange

substrate: N-methylglycine


organism: Hemerocallis fulva


substrate_name: L-azetidine-2-carboxylic acid

substrate: L-azetidine-2-carboxylic acid


enzyme_display_name: phenylalanine--tRNA ligase

organism: Escherichia coli

substrate_name: tRNA(Phe); ATP; L-Phenylalanine

enzyme: phenylalanine--tRNA ligase

substrate: tRNA(Phe); ATP; L-Phenylalanine


enzyme_display_name: histidine--tRNA ligase

substrate_name: L-Histidine

enzyme: histidine--tRNA ligase

substrate: L-Histidine


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

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


organism: Ranunculus bulbosus


organism: Parkinsonia aculeata


proof_lines: ATP-diphosphate exchange, L-azetidine-2-carboxylic acid


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

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


enzyme_display_name: glutamate--tRNA ligase

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

enzyme: glutamate--tRNA ligase

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


organism: Saccharomyces cerevisiae


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

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


organism: Bacillus subtilis

substrate_name: ATP; L-Phenylalanine; tRNA(Phe)

substrate: ATP; L-Phenylalanine; tRNA(Phe)


organism: Astragalus crotalariae


substrate_name: Cys

substrate: Cys


substrate_name: selenocysteine

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

substrate: selenocysteine


substrate_name: 2-aminobutyric acid

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

substrate: 2-aminobutyric acid


organism: Astragalus lentiginosus

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

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


organism: Convallaria majalis


proof_lines: 3,4-dehydro-DL-proline, , ATP-diphosphate exchange


organism: Astragalus racemosus


substrate_name: tRNAPhe

proof_lines: aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37°C

proof_lines: recombinant His-tagged heterodimer, pH 8.0, 25°C

substrate: tRNAPhe


substrate_name: ATP

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

proof_lines: ATP-diphosphate exchange reaction, mitochondrial isozyme, pH 7.3, 37°C

proof_lines: ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C

substrate: ATP


organism: Arabidopsis thaliana

substrate_name: L-proline

proof_lines:
isozyme ProRS-Org, at pH 7.2 and 30°C
isozyme ProRS-Cyt, at pH 7.2 and 30°C

substrate: L-proline


organism: Magnetospirillum magnetotacticum

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

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


organism: Methanothermobacter thermautotrophicus

substrate_name: L-Proline

sequence_source: UniProt O26708

substrate: L-Proline


substrate_name: L-Cysteine

substrate: L-Cysteine


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

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


sequence_source: UniProt P21888

sequence_variant_note: Resolved canonical sequence from UniProt P21888 and applied mutation signature H234S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P21888 and applied mutation signature H235S to reconstruct the assayed variant sequence.


substrate_name: L-phenylalanine

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

proof_lines: mitochondrial chimeric enzyme with implanted editing module from Escherichia coli phenylalanine-tRNA synthetase, at pH 8.5 and 37°C

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

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

substrate: L-phenylalanine


organism: Paracoccus denitrificans

assay_conditions_summary: cofactor ATP


substrate_name: L-Cys

substrate: L-Cys


substrate_name: diphosphate

substrate: diphosphate


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


enzyme_display_name: glycine--tRNA ligase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: glycine (at 25 degrees Celsius)

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

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

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

enzyme: glycine--tRNA ligase

substrate: glycine (at 25 degrees Celsius)


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


organism: Cytophaga hutchinsonii

substrate_name: L-cysteine

substrate: L-cysteine


organism: Methanocaldococcus jannaschii

assay_conditions_summary: pH 7.2; cofactor ATP

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


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


organism: Homo sapiens

substrate_name: glycine

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

substrate: glycine


organism: Neurospora crassa

substrate_name: His

substrate: His


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


substrate_name: L-tyrosine

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

substrate: L-tyrosine


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


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


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


organism: Escherichia coli (strain K12)

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


enzyme_display_name: arginine--tRNA ligase

organism: Canavalia ensiformis

substrate_name: L-canavanine

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

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

enzyme: arginine--tRNA ligase

substrate: L-canavanine


organism: Escherichia coli

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

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

source_databases_merged: skid uniprot


assay_conditions_summary: pH 7

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


assay_conditions_summary: pH 7; cofactor ATP

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

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


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


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


substrate_name: DL-m-tyrosine

substrate: DL-m-tyrosine


organism: Aquifex aeolicus

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

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


organism: Borrelia burgdorferi

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

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


organism: Clostridium sticklandii


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

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


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Beta vulgaris

substrate_name: L-Pro

substrate: L-Pro


organism: Staphylococcus aureus

substrate_name: ATP

proof_lines:
ATP-diphosphate exchange
glycyl-tRNA synthesis

substrate: ATP


substrate_name: Gly

substrate: Gly


substrate_name: L-proline

substrate: L-proline


organism: Acetoanaerobium sticklandii


substrate_name: L-Cysteine

substrate: L-Cysteine


organism: Deinococcus radiodurans


organism: Paramagnetospirillum magnetotacticum


organism: Methanothermobacter thermautotrophicus


organism: Novosphingobium aromaticivorans

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

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


organism: Rhodopseudomonas palustris


organism: Thermus thermophilus


organism: Astragalus bisulcatus

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

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


organism: Homo sapiens

substrate_name: tRNA(Cys)

substrate: tRNA(Cys)


substrate_name: L-arginine

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

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

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

substrate: L-arginine


assay_conditions_summary: pH 7.5; cofactor ATP


substrate_name: L-cysteine

substrate: L-cysteine


organism: Saccharomyces cerevisiae

substrate_name: L-tryptophan

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

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

substrate: L-tryptophan


substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Oryctolagus cuniculus

substrate_name: tRNACys

substrate: tRNACys


organism: Bacillus subtilis

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

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


organism: Escherichia coli

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

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


substrate_name: tRNA(Glu)

substrate: tRNA(Glu)


organism: Mycobacterium tuberculosis

substrate_name: L-glutamate

substrate: L-glutamate


organism: Thermosynechococcus elongatus

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

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


enzyme_display_name: glutamine--tRNA ligase

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

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

enzyme: glutamine--tRNA ligase

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


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

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


organism: Mycolicibacterium smegmatis

substrate_name: tRNAArg

substrate: tRNAArg


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

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


substrate_name: Cys

substrate: Cys


substrate_name: 2-aminobutyric acid

substrate: 2-aminobutyric acid


substrate_name: ATP

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: L-histidine

substrate: L-histidine


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


substrate_name: histidine

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

substrate: histidine


organism: Methanocaldococcus jannaschii

substrate_name: tRNAPro

substrate: tRNAPro


organism: Escherichia coli (strain K12)

substrate_name: tRNA(Cys)

substrate: tRNA(Cys)


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

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


organism: Halobacterium sp.

substrate_name: tRNACys

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

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

substrate: tRNACys


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

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


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

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


substrate_name: ATP; tRNA(Gly); Glycine

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

substrate: ATP; tRNA(Gly); Glycine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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

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

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


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


organism: Staphylococcus aureus

substrate_name: tRNAGly

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

substrate: tRNAGly


organism: Deinococcus radiodurans

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

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

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


mutation_signature: C-terminal deletion mutant

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

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


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


organism: Vigna radiata var. radiata

substrate_name: Unknown

substrate: Unknown


organism: Canavalia ensiformis

substrate_name: tRNAArg(ACG)

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

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

substrate: tRNAArg(ACG)


organism: Cricetulus griseus

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

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


organism: Pyrococcus horikoshii

substrate_name: tRNAArg

substrate: tRNAArg


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


organism: Homo sapiens

substrate_name: tRNA(Phe)

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

substrate: tRNA(Phe)


substrate_name: tRNAPhe

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

substrate: tRNAPhe


organism: Saccharomyces cerevisiae


organism: Caulobacter vibrioides

substrate_name: tRNAHis

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

substrate: tRNAHis


substrate_name: ATP

substrate: ATP


substrate_name: tRNA(His)

substrate: tRNA(His)


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


organism: Neurospora crassa

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


organism: Salmonella typhimurium

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

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


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


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


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


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


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


substrate_name: L-Arginine

substrate: L-Arginine


organism: Escherichia coli

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


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


substrate_name: L-Histidine

substrate: L-Histidine


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

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

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

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

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

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


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


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

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

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

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


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


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

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

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

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


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


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

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

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


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

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

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

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


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


substrate_name: L-Glutamine

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

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

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

substrate: L-Glutamine


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


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

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

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


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

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

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

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


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

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

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


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

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


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

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

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

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


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

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


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

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

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


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

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

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

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


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


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


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

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


substrate_name: proline

substrate: proline


substrate_name: alanine

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

substrate: alanine


substrate_name: cysteine

substrate: cysteine


substrate_name: L-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P16659 and applied mutation signature E218A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 295.15 K; cofactor ATP

column_label: Table 1, enzyme block 'E218A', printed amino acid row 'Alanine'; column 'kcat (sec-1)' = 3.26; column 'KM (mM)' = 1360; column 'kcat/KM (sec-1 mM-1)' = 0.0024; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it; the two right-hand columns of the line are the printed kcat/KM relative and Fold Change comparisons.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.26 under the column head sec-1; sec-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.26 s^(-1). Km: printed Table 1 cell 1360 under the column head mM; mM is already canonical, so no unit conversion applies and the value is 1360.0 mM. kcat/Km: printed Table 1 cell 0.0024 under the column head sec-1mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 0.0024 s^(-1)*mM^(-1). The quotient of the two printed component cells is 3.26 / 1360 = 0.0023970588235294114 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme block E218A, printed amino acid row Alanine: kcat = 3.26 in a column headed kcat (sec-1); KM = 1360 in a column headed KM (mM); printed kcat/KM = 0.0024 in a column headed kcat/KM (sec-1 mM-1).

table_label: Table 1, the only kinetics table of Biochemistry 2012, 51(10):2146-2156; printed column heads: Amino Acid; kcat (sec-1); KM (mM); kcat/KM (sec-1 mM-1); kcat/KM relative; Fold Change.

substrate: L-alanine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P16659 and applied mutation signature G217A to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme block 'G217A', printed amino acid row 'Alanine'; column 'kcat (sec-1)' = 2.18; column 'KM (mM)' = 454; column 'kcat/KM (sec-1 mM-1)' = 0.0048; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it; the two right-hand columns of the line are the printed kcat/KM relative and Fold Change comparisons.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.18 under the column head sec-1; sec-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.18 s^(-1). Km: printed Table 1 cell 454 under the column head mM; mM is already canonical, so no unit conversion applies and the value is 454.0 mM. kcat/Km: printed Table 1 cell 0.0048 under the column head sec-1mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 0.0048 s^(-1)*mM^(-1). The quotient of the two printed component cells is 2.18 / 454 = 0.004801762114537446 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme block G217A, printed amino acid row Alanine: kcat = 2.18 in a column headed kcat (sec-1); KM = 454 in a column headed KM (mM); printed kcat/KM = 0.0048 in a column headed kcat/KM (sec-1 mM-1).


column_label: Table 1, enzyme block 'WT', printed amino acid row 'Alanine'; column 'kcat (sec-1)' = 3.52; column 'KM (mM)' = 685; column 'kcat/KM (sec-1 mM-1)' = 0.00513; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it; the two right-hand columns of the line are the printed kcat/KM relative and Fold Change comparisons.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.52 under the column head sec-1; sec-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.52 s^(-1). Km: printed Table 1 cell 685 under the column head mM; mM is already canonical, so no unit conversion applies and the value is 685.0 mM. kcat/Km: printed Table 1 cell 0.00513 under the column head sec-1mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 0.00513 s^(-1)*mM^(-1). The quotient of the two printed component cells is 3.52 / 685 = 0.005138686131386861 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme block WT, printed amino acid row Alanine: kcat = 3.52 in a column headed kcat (sec-1); KM = 685 in a column headed KM (mM); printed kcat/KM = 0.00513 in a column headed kcat/KM (sec-1 mM-1).


substrate_name: L-proline

column_label: Table 1, enzyme block 'E218A', printed amino acid row 'Proline'; column 'kcat (sec-1)' = 4.4; column 'KM (mM)' = 3.40; column 'kcat/KM (sec-1 mM-1)' = 1.29; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it; the two right-hand columns of the line are the printed kcat/KM relative and Fold Change comparisons.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.4 under the column head sec-1; sec-1 is already the canonical s^(-1), so no unit conversion applies and the value is 4.4 s^(-1). Km: printed Table 1 cell 3.40 under the column head mM; mM is already canonical, so no unit conversion applies and the value is 3.4 mM. kcat/Km: printed Table 1 cell 1.29 under the column head sec-1mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 1.29 s^(-1)*mM^(-1). The quotient of the two printed component cells is 4.4 / 3.40 = 1.2941176470588236 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme block E218A, printed amino acid row Proline: kcat = 4.4 in a column headed kcat (sec-1); KM = 3.40 in a column headed KM (mM); printed kcat/KM = 1.29 in a column headed kcat/KM (sec-1 mM-1).

substrate: L-proline


column_label: Table 1, enzyme block 'G217A', printed amino acid row 'Proline'; column 'kcat (sec-1)' = 3.37; column 'KM (mM)' = 0.427; column 'kcat/KM (sec-1 mM-1)' = 7.89; the number after each plus/minus sign on the same printed line is the standard deviation of the cell beside it; the two right-hand columns of the line are the printed kcat/KM relative and Fold Change comparisons.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.37 under the column head sec-1; sec-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.37 s^(-1). Km: printed Table 1 cell 0.427 under the column head mM; mM is already canonical, so no unit conversion applies and the value is 0.427 mM. kcat/Km: printed Table 1 cell 7.89 under the column head sec-1mM-1; that unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 7.89 s^(-1)*mM^(-1). The quotient of the two printed component cells is 3.37 / 0.427 = 7.892271662763466 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme block G217A, printed amino acid row Proline: kcat = 3.37 in a column headed kcat (sec-1); KM = 0.427 in a column headed KM (mM); printed kcat/KM = 7.89 in a column headed kcat/KM (sec-1 mM-1).


substrate_name: DL-m-tyrosine

substrate: DL-m-tyrosine


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Methanothermobacter thermautotrophicus

substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-Cysteine

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

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

row_label: M. thermautotrophicus / C

table_label: Table I

substrate: L-Cysteine


substrate_name: L-Proline

substrate: L-Proline


organism: Aquifex aeolicus

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

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

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

row_label: A. aeolicus | L-Cysteine

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


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

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

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

row_label: A. aeolicus | L-Proline


organism: Borrelia burgdorferi

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

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

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

row_label: B. burgdorferi | L-Cysteine


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

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

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

row_label: B. burgdorferi | L-Proline


organism: Clostridium sticklandii

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

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

row_label: C. sticklandii / C


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

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

row_label: C. sticklandii / P


organism: Aquifex aeolicus (strain VF5)

substrate_name: proline (at 60 degrees Celsius)

substrate: proline (at 60 degrees Celsius)


substrate_name: cysteine (at 60 degrees Celsius)

substrate: cysteine (at 60 degrees Celsius)


organism: Cytophaga hutchinsonii

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

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

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

row_label: C. hutchinsonii | L-Cysteine