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

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

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

row_label: C. hutchinsonii | L-Proline


enzyme_display_name: proline--tRNA ligase

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

substrate_name: proline

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

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

normalized_value_unit_evidence: Km 0.17 mM

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

row_label: B. burgdorferi / P

table_label: Table I

data_origin: experimental

enzyme: proline--tRNA ligase

substrate: proline

status: verified

source: uniprot


substrate_name: cysteine

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

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

normalized_value_unit_evidence: Km 0.18 mM

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

row_label: B. burgdorferi / C

substrate: cysteine


organism: Deinococcus radiodurans

substrate_name: L-Cysteine

source_db: oed

kcat_over_km_origin: calculated

substrate: L-Cysteine

source: oed


substrate_name: L-Proline

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

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

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

row_label: D. radiodurans | L-Proline

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

substrate: L-Proline


enzyme_display_name: glycine--tRNA ligase

organism: Homo sapiens

substrate_name: glycine

verification_status: unverified

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

mutation_type: substitution

enzyme: glycine--tRNA ligase

substrate: glycine

status: unverified


organism: Novosphingobium aromaticivorans

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

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

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

row_label: N. aromaticivorans | L-Cysteine


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

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

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

row_label: N. aromaticivorans / P


organism: Methanocaldococcus jannaschii

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

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

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

row_label: M. jannaschii / C


organism: Rhodopseudomonas palustris

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

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

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

row_label: R. palustris / C


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

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

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

row_label: R. palustris / P


enzyme_display_name: cysteine--tRNA ligase

organism: Oryctolagus cuniculus

substrate_name: L-cysteine

source_db: brenda

enzyme: cysteine--tRNA ligase

substrate: L-cysteine

source: brenda


substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

substrate: ATP


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

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


enzyme_display_name: glutamate--tRNA ligase

organism: Escherichia coli

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

enzyme: glutamate--tRNA ligase


substrate_name: L-Glutamate

substrate: L-Glutamate


organism: Thermus thermophilus

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

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

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

row_label: T. thermophilus / C


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

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

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

row_label: T. thermophilus / P


organism: Methanococcus maripaludis

substrate_name: L-proline

substrate: L-proline


enzyme_display_name: phenylalanine--tRNA ligase

substrate_name: L-Phenylalanine

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

enzyme: phenylalanine--tRNA ligase

substrate: L-Phenylalanine


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


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


enzyme_display_name: arginine--tRNA ligase

organism: Mycolicibacterium smegmatis

substrate_name: Arg

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

assay_conditions_summary: 310.15 K; cofactor ATP

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

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

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

row_label: M. smegmatis SN2 arginyl-tRNA synthetase

table_label: PDF Table II and adjacent kinetic text

enzyme: arginine--tRNA ligase

substrate: Arg


substrate_name: tubercidin 5'-triphosphate

assay_conditions_summary: cofactor ATP

substrate: tubercidin 5'-triphosphate


organism: Escherichia coli (strain K12)

substrate_name: Glu

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

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

substrate: Glu


substrate_name: Alanine

substrate: Alanine


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

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


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


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


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


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


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


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


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


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


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


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

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

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

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


enzyme_display_name: glutamine--tRNA ligase

substrate_name: L-glutamine

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

enzyme: glutamine--tRNA ligase

substrate: L-glutamine


mutation_signature: truncated mutant

mutation_type: truncation


substrate_name: L-glutamate

km_display: Not reported

ki_unit: mM

substrate: L-glutamate


substrate_name: L-Phe

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

substrate: L-Phe


proof_lines:
wild-type enzyme
wild-type EcPheRS


proof_lines: mutant enzyme with A294G mutation in alpha-subunit


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


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


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


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


substrate_name: L-Cysteine

verification_status: corrected

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

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

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

row_label: E. coli / C

substrate: L-Cysteine

status: corrected


enzyme_display_name: histidine--tRNA ligase

substrate_name: His

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

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

enzyme: histidine--tRNA ligase

substrate: His


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

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

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


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


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

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

proof_lines: mutant enzyme form M-HisRS, aminoacylation


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

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


proof_lines: wild-type HisRS, ATP-diphosphate exchange


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


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


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


substrate_name: tRNAPro

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

substrate: tRNAPro


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


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

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

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


substrate_name: L-alanine

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

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

substrate: L-alanine


organism: Bombyx mori

substrate_name: Gly

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

substrate: Gly


mutation_signature: N55-truncation mutant


substrate_name: tRNAGly

mutation_signature: N55-truncation mutant enzyme

substrate: tRNAGly


substrate_name: ATP

substrate: ATP


substrate_name: tRNAArg

substrate: tRNAArg


proof_lines: wild-type enzyme, ATP-diphosphate exchange


substrate_name: Pro

substrate: Pro


substrate_name: L-proline

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

substrate: L-proline


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


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


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


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


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


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


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


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


substrate_name: tRNAHis

substrate: tRNAHis


substrate_name: L-histidine

substrate: L-histidine


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

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


substrate_name: L-arginine

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

substrate: L-arginine


mutation_signature: Δ1

mutation_type: deletion

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


organism: Phaseolus vulgaris

substrate_name: L-Pro

substrate: L-Pro


substrate_name: L-azetidine-2-carboxylic acid

substrate: L-azetidine-2-carboxylic acid


substrate_name: thiazolidine-4-carboxylic acid

substrate: thiazolidine-4-carboxylic acid


substrate_name: N-methylglycine

smiles: CNCC(=O)O

substrate: N-methylglycine


substrate_name: N-Methyl-L-alanine

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

substrate: N-Methyl-L-alanine


organism: Plasmodium falciparum

substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: Unknown

substrate: Unknown


substrate_name: tRNAPhe

substrate: tRNAPhe


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


organism: Methanosarcina mazei

proof_lines: value above, substrate tRNA3Cys isoacceptor 3

proof_lines: value above, substrate tRNA2Cys isoacceptor 2

proof_lines: value above, substrate tRNA1Cys isoacceptor 1


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

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


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


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


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


substrate_name: synthetic tRNAHis A-1

substrate: synthetic tRNAHis A-1


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


substrate_name: tRNACys

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

substrate: tRNACys


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


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


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

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

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


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


substrate_name: ATP

substrate: ATP


substrate_name: L-cysteine

substrate: L-cysteine


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

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


proof_lines: tuncated enzyme form NcatHisRS, aminoacylation


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

proof_lines: truncated enzyme form NcatHisRS, aminoacylation


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

proof_lines: truncated enzyme form NcatHisRS, ATP-diphosphate exchange


substrate_name: His

substrate: His


proof_lines: wild-type HisRS, ATP-diphosphate exchange


proof_lines: aminoacylation reaction, recombinant C28S/C209S mutant enzyme


proof_lines: aminoacylation reaction, recombinant W205Y mutant enzyme


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


substrate_name: L-glutamine

substrate: L-glutamine


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

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


mutation_signature: truncated mutant PheRSDELTAB2A294G

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

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


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


substrate_name: tRNAHis

substrate: tRNAHis


organism: Homo sapiens

substrate_name: tRNAGln

substrate: tRNAGln


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


substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-proline

substrate: L-proline


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


mutation_signature: recombinant His-tagged deletion mutant

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


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


organism: Methanosarcina barkeri

substrate_name: 2-Chloroadenosine 5'-triphosphate

substrate: 2-Chloroadenosine 5'-triphosphate


substrate_name: N6-methyladenosine 5'-triphosphate

substrate: N6-methyladenosine 5'-triphosphate


substrate_name: 3'-Deoxyadenosine 5'-triphosphate

substrate: 3'-Deoxyadenosine 5'-triphosphate


organism: Saccharomyces cerevisiae

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


substrate_name: Gln

mutation_signature: truncated enzyme truncated enzyme

substrate: Gln


organism: Cricetulus griseus

substrate_name: L-arginine

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

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

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

substrate: L-arginine


substrate_name: tRNAArg

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

substrate: tRNAArg


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


proof_lines:
pH 7.4, 37°C
aminoacylation reaction
aminoacylation


substrate_name: L-glutamate

substrate: L-glutamate


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


substrate_name: Arg

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

substrate: Arg


proof_lines: aminoacylation and ATP-diphosphate exchange, mutant enzyme


substrate_name: tRNAGly

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

substrate: tRNAGly


substrate_name: ATP

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

proof_lines: ATP-diphosphate exchange in presence of tRNA

substrate: ATP


substrate_name: Gly

substrate: Gly


substrate_name: tubercidin 5'-triphosphate

proof_lines: tubercidine 5'-triphosphate, , aminoacylation

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

substrate: tubercidin 5'-triphosphate


substrate_name: 2'-deoxyadenosine 5'-triphosphate

substrate: 2'-deoxyadenosine 5'-triphosphate


substrate_name: selenocysteine

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

substrate: selenocysteine


substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-tyrosine

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

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

substrate: L-tyrosine


substrate_name: DL-m-tyrosine

substrate: DL-m-tyrosine


substrate_name: L-proline

substrate: L-proline


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


organism: Pseudomonas aeruginosa

substrate_name: tRNAPhe

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

substrate: tRNAPhe


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: tRNAPro

substrate: tRNAPro


substrate_name: tRNAHis

substrate: tRNAHis


substrate_name: L-histidine

substrate: L-histidine


organism: Gallus gallus

proof_lines: substrate from calf liver, , mitochondrial, aminoacylation


substrate_name: Phe

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

substrate: Phe


proof_lines:
aminoacylation
mitochondrial
ATP, , cytoplasmic, aminoacylation


organism: Rattus norvegicus

substrate_name: Arg

proof_lines:
complexed enzyme
free enzyme

substrate: Arg


substrate_name: tRNAArg

proof_lines:
free enzyme
complexed enzyme

substrate: tRNAArg


substrate_name: ATP

substrate: ATP


substrate_name: RNA microhelix

substrate: RNA microhelix


substrate_name: Pro

substrate: Pro


substrate_name: gamma-thiaproline

substrate: gamma-thiaproline


substrate_name: Cys

substrate: Cys


substrate_name: diphosphate

substrate: diphosphate


mutation_signature: truncated DELTANhcArgRS / truncated DELTANhcArgRS

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

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

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


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

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


substrate_name: L-arginine

substrate: L-arginine


substrate_name: His

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

substrate: His


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


proof_lines:
cytoplasmic
ATP, , mitochondrial, aminoacylation
mitochondrial


substrate_name: 2'-deoxyadenosine 5'-triphosphate

substrate: 2'-deoxyadenosine 5'-triphosphate


substrate_name: 3'-Deoxyadenosine 5'-triphosphate

substrate: 3'-Deoxyadenosine 5'-triphosphate


substrate_name: L-tyrosine

proof_lines:
wild-type mtPheRS
wild-type ctPheRS

substrate: L-tyrosine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: tRNAHis

substrate: tRNAHis


substrate_name: tRNAGly

substrate: tRNAGly


substrate_name: Gly

substrate: Gly


organism: Streptococcus pneumoniae

substrate_name: tRNAPhe

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

substrate: tRNAPhe


organism: Borreliella burgdorferi

substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-proline

substrate: L-proline


organism: Saccharomyces pastorianus

substrate_name: tRNAArgIII

proof_lines:
aminoacylation
Arg, , ATP-diphosphate exchange

substrate: tRNAArgIII


substrate_name: Arg

substrate: Arg


organism: Vigna radiata var. radiata

substrate_name: selenocysteine

substrate: selenocysteine


substrate_name: Cys

substrate: Cys


substrate_name: 2-aminobutyric acid

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

substrate: 2-aminobutyric acid


organism: Cricetulus sp.

substrate_name: tRNAArg

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

substrate: tRNAArg


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


organism: Escherichia coli

substrate_name: ATP

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

substrate: ATP


substrate_name: Glu

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

substrate: Glu


proof_lines: 3-thiaproline, , ATP-diphosphate exchange


organism: Thermus thermophilus

substrate_name: tRNAGlu

assay_conditions_summary: pH 7.5; 338.15 K; cofactor ATP

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

substrate: tRNAGlu


substrate_name: L-Glu

substrate: L-Glu


substrate_name: 2'-deoxyadenosine 5'-triphosphate

substrate: 2'-deoxyadenosine 5'-triphosphate


organism: Glycine max

substrate_name: L-arginine

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

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

substrate: L-arginine


substrate_name: L-canavanine

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

substrate: L-canavanine


organism: Geobacillus stearothermophilus

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


substrate_name: Phe

substrate: Phe


organism: Methanothermobacter thermautotrophicus

assay_conditions_summary: pH 7.2; 333.15 K; cofactor ATP

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


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

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


organism: Homo sapiens

substrate_name: L-alanine

substrate: L-alanine


organism: Mus musculus


substrate_name: Unknown

substrate: Unknown


organism: Oryctolagus cuniculus

substrate_name: tRNAHisII

proof_lines: unfractionated substrate from rabbit liver or rabbit reticulocyte tRNAHisI

substrate: tRNAHisII


substrate_name: L-His

substrate: L-His


organism: Phaseolus vulgaris


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

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

row_label: hcArgRS aminoacylation activity prose

table_label: ACS full text Results prose


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

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


organism: Plasmodium falciparum

substrate_name: tRNAGln

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

substrate: tRNAGln


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


organism: Rhodopseudomonas palustris

substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-proline

substrate: L-proline


organism: Saccharomyces cerevisiae


enzyme_display_name: threonine--tRNA ligase

substrate_name: tRNAThr

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

enzyme: threonine--tRNA ligase

substrate: tRNAThr


substrate_name: tRNAHis

substrate: tRNAHis


substrate_name: tRNAGly

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

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

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

substrate: tRNAGly


substrate_name: glycine

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

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

substrate: glycine


proof_lines: pH and temperature not specified in the publication


substrate_name: L-glutamine

substrate: L-glutamine


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


substrate_name: L-phenylalanine

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

substrate: L-phenylalanine


substrate_name: tubercidin 5'-triphosphate

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

substrate: tubercidin 5'-triphosphate


substrate_name: ATP

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

substrate: ATP


enzyme_display_name: UniProt Q8PWY1

organism: Methanosarcina mazei

substrate_name: N-acetyl-L-lysine

source_db: skid

source_license: CC BY-NC-ND 4.0

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

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

enzyme: UniProt Q8PWY1

substrate: N-acetyl-L-lysine

source: skid


organism: Staphylococcus aureus

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


assay_conditions_summary: pH 7.9; 295.15 K; cofactor ATP


substrate_name: tRNAGlu mutant C36G

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

substrate: tRNAGlu mutant C36G


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


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

substrate_name: D-lactate

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

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

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

substrate: D-lactate


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


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


substrate_name: D-Ala

substrate: D-Ala


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


enzyme_display_name: glutamate--tRNA(Gln) ligase

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

enzyme: glutamate--tRNA(Gln) ligase


substrate_name: L-Glu

substrate: L-Glu


enzyme_display_name: pyrrolysine--tRNA(Pyl) ligase

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

enzyme: pyrrolysine--tRNA(Pyl) ligase


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


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


substrate_name: L-glutamate

substrate: L-glutamate


enzyme_display_name: aspartate--tRNA(Asn) ligase

organism: Halalkalibacterium halodurans

substrate_name: tRNAAsn

enzyme: aspartate--tRNA(Asn) ligase

substrate: tRNAAsn


organism: Thermosynechococcus vestitus

substrate_name: tRNAGln

substrate: tRNAGln


organism: Bacillus subtilis

proof_lines:
homologous tRNAGln
homologous tRNAGlu
tRNAGln from E. coli


organism: Enterococcus faecalis

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

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


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


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

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


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

substrate_name: L-aspartate (at 37 degrees Celsius)

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

substrate: L-aspartate (at 37 degrees Celsius)


substrate_name: ATP (at 37 degrees Celsius)

substrate: ATP (at 37 degrees Celsius)


organism: Escherichia coli

assay_conditions_summary: pH 8; cofactor ATP

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


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


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Chlamydia trachomatis

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

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

sequence_source: multiple

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


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

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

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


substrate_name: tRNA(Glu)

substrate: tRNA(Glu)


enzyme_display_name: serine--tRNA ligase

organism: Methanothermobacter thermautotrophicus

substrate_name: tRNASer

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

enzyme: serine--tRNA ligase

substrate: tRNASer


substrate_name: tRNAArg

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

substrate: tRNAArg


organism: Mycobacterium tuberculosis

substrate_name: ATP

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: tRNAGlu

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

substrate: tRNAGlu


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

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


organism: Desulfitobacterium hafniense

substrate_name: tRNAPyl

substrate: tRNAPyl


substrate_name: more

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

substrate: more


organism: Methanosarcina barkeri

substrate_name: L-Pyrrolysine; ATP

source_databases_merged: sabio_rk brenda uniprot

substrate: L-Pyrrolysine; ATP


enzyme_display_name: O-phosphoserine--tRNA ligase

organism: Methanocaldococcus jannaschii

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

assay_conditions_summary: pH 6; 333.15 K; cofactor ATP

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

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

enzyme: O-phosphoserine--tRNA ligase

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


substrate_name: tRNACys

substrate: tRNACys


enzyme_display_name: asparagine--tRNA ligase

organism: Escherichia coli (strain K12)

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

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

row_label: WT enzyme / ATP substrate

table_label: FEBS Letters PDF p.164 Table 1

enzyme: asparagine--tRNA ligase


organism: Deinococcus radiodurans

substrate_name: tRNAAsp

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

substrate: tRNAAsp


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


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


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


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

substrate_name: tRNA(Asp)

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

substrate: tRNA(Asp)


organism: Helicobacter pylori (strain ATCC 700392 / 26695)

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


organism: Methanosarcina mazei

substrate_name: O-phospho-L-threonine

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

assay_conditions_summary: pH 7.5; 310.15 K; buffer containing 6 mM ATP; cofactor ATP

column_label: Table 2 (Steady-state kinetic parameters for aminoacylation WT SepRS), amino acid column 'Phosphothreonine'; metric row 'Km (amino acid) (mM)' = 8.4; metric row 'kcat (s^-1)' = 5.4 x 10^-3; metric row 'kcat/Km (amino acid) (s^-1 M^-1)' = 0.64. The same column carries one further printed cell, metric row 'Plateau aminoacylation (%)' = 27.2.

normalized_value_unit_evidence: Km: printed cell 8.4 mM; already in mM, no unit conversion applies; the exported value is 8.4 mM. kcat: printed cell 5.4 x 10^-3 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.0054 s^(-1). kcat/Km: printed cell 0.64 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 0.00064 s^(-1)*mM^(-1), while the exported kcat_over_km 0.0006428571428571428 s^(-1)*mM^(-1) is the full-precision quotient 0.0054 / 8.4 of the same two printed cells, which the printed efficiency cell reproduces at its own printed precision.

raw_value_unit_evidence: Table 2, amino acid column 'Phosphothreonine': Km = 8.4 mM; kcat = 5.4 x 10^-3 s^-1; printed kcat/Km = 0.64 s^-1 M^-1.

row_label: Table 2, amino acid column 'Phosphothreonine' (the printed kcat, Km (amino acid) and kcat/Km cells of that column)

table_label: Table 2: Steady-state kinetic parameters for aminoacylation WT SepRS (J. Biol. Chem. 2008, 283(32):21997-22006)

substrate: O-phospho-L-threonine


column_label: Table 1 (ATP-PPi exchange kinetics), amino acid column 'phosphothreonine (WT)'; metric row 'Km (amino acid) (mM)' = 2.2; metric row 'kcat (s^-1)' = 1.4 x 10^-2; metric row 'kcat/Km (s^-1 M^-1)' = 6.4.

normalized_value_unit_evidence: Km: printed cell 2.2 mM; already in mM, no unit conversion applies; the exported value is 2.2 mM. kcat: printed cell 1.4 x 10^-2 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.014 s^(-1). kcat/Km: printed cell 6.4 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 0.0064 s^(-1)*mM^(-1), while the exported kcat_over_km 0.006363636363636363 s^(-1)*mM^(-1) is the full-precision quotient 0.014 / 2.2 of the same two printed cells, which the printed efficiency cell reproduces at its own printed precision.

raw_value_unit_evidence: Table 1, amino acid column 'phosphothreonine (WT)': Km = 2.2 mM; kcat = 1.4 x 10^-2 s^-1; printed kcat/Km = 6.4 s^-1 M^-1.

row_label: Table 1, amino acid column 'phosphothreonine (WT)' (the printed kcat, Km (amino acid) and kcat/Km cells of that column)

table_label: Table 1: ATP-PPi exchange kinetics (J. Biol. Chem. 2008, 283(32):21997-22006)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0F8NI45 and applied mutation signature T307S to reconstruct the assayed variant sequence.

column_label: Table 1 (ATP-PPi exchange kinetics), amino acid column 'phosphothreonine (T307S)'; metric row 'Km (amino acid) (mM)' = 0.93; metric row 'kcat (s^-1)' = 2.1 x 10^-2; metric row 'kcat/Km (s^-1 M^-1)' = 22.6.

normalized_value_unit_evidence: Km: printed cell 0.93 mM; already in mM, no unit conversion applies; the exported value is 0.93 mM. kcat: printed cell 2.1 x 10^-2 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.021 s^(-1). kcat/Km: printed cell 22.6 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 0.022600000000000002 s^(-1)*mM^(-1), while the exported kcat_over_km 0.02258064516129032 s^(-1)*mM^(-1) is the full-precision quotient 0.021 / 0.93 of the same two printed cells, which the printed efficiency cell reproduces at its own printed precision.

raw_value_unit_evidence: Table 1, amino acid column 'phosphothreonine (T307S)': Km = 0.93 mM; kcat = 2.1 x 10^-2 s^-1; printed kcat/Km = 22.6 s^-1 M^-1.

row_label: Table 1, amino acid column 'phosphothreonine (T307S)' (the printed kcat, Km (amino acid) and kcat/Km cells of that column)


substrate_name: O-phospho-L-serine

substrate: O-phospho-L-serine


column_label: Table 1 (ATP-PPi exchange kinetics), amino acid column 'Phosphoserine (WT)'; metric row 'Km (amino acid) (mM)' = 0.27; metric row 'kcat (s^-1)' = 10.6; metric row 'kcat/Km (s^-1 M^-1)' = 3.9 x 10^4.

normalized_value_unit_evidence: Km: printed cell 0.27 mM; already in mM, no unit conversion applies; the exported value is 0.27 mM. kcat: printed cell 10.6 s^-1; already in s^-1, no unit conversion applies; the exported value is 10.6 s^(-1). kcat/Km: printed cell 3.9 x 10^4 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 39.0 s^(-1)*mM^(-1), while the exported kcat_over_km 39.25925925925925 s^(-1)*mM^(-1) is the full-precision quotient 10.6 / 0.27 of the same two printed cells, which the printed efficiency cell reproduces at its own printed precision.

raw_value_unit_evidence: Table 1, amino acid column 'Phosphoserine (WT)': Km = 0.27 mM; kcat = 10.6 s^-1; printed kcat/Km = 3.9 x 10^4 s^-1 M^-1.

row_label: Table 1, amino acid column 'Phosphoserine (WT)' (the printed kcat, Km (amino acid) and kcat/Km cells of that column)


column_label: Table 1 (ATP-PPi exchange kinetics), amino acid column 'Phosphoserine (T307S)'; metric row 'Km (amino acid) (mM)' = 0.15; metric row 'kcat (s^-1)' = 11.2; metric row 'kcat/Km (s^-1 M^-1)' = 7.5 x 10^4.

normalized_value_unit_evidence: Km: printed cell 0.15 mM; already in mM, no unit conversion applies; the exported value is 0.15 mM. kcat: printed cell 11.2 s^-1; already in s^-1, no unit conversion applies; the exported value is 11.2 s^(-1). kcat/Km: printed cell 7.5 x 10^4 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 75.0 s^(-1)*mM^(-1), while the exported kcat_over_km 74.66666666666667 s^(-1)*mM^(-1) is the full-precision quotient 11.2 / 0.15 of the same two printed cells, which the printed efficiency cell reproduces at its own printed precision.

raw_value_unit_evidence: Table 1, amino acid column 'Phosphoserine (T307S)': Km = 0.15 mM; kcat = 11.2 s^-1; printed kcat/Km = 7.5 x 10^4 s^-1 M^-1.

row_label: Table 1, amino acid column 'Phosphoserine (T307S)' (the printed kcat, Km (amino acid) and kcat/Km cells of that column)


substrate_name: asparagine

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

raw_value_unit_evidence: Km raw_value=15.3 uM raw_unit=uM

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

substrate: asparagine


substrate_name: N-acetyl-L-lysine

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

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

substrate: N-acetyl-L-lysine


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

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


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


substrate_name: Asn

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

substrate: Asn


proof_lines: mutant Y426F, , ATP-diphosphate exchange


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


substrate_name: L-Pyrrolysine

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

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

substrate: L-Pyrrolysine


organism: Vigna radiata var. radiata

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


proof_lines:
tRNA esterification
ATP-diphosphate exchange


substrate_name: isoasparagine

substrate: isoasparagine


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


organism: Cricetulus griseus

substrate_name: tRNAAsn

substrate: tRNAAsn


substrate_name: L-pyrrolysine

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

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

substrate: L-pyrrolysine


organism: Enterococcus faecium

substrate_name: D-lactate

source_databases_merged: brenda uniprot

substrate: D-lactate


substrate_name: D-Ala

substrate: D-Ala


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


organism: Helicobacter pylori


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


organism: Thermus thermophilus


substrate_name: aspartate

substrate: aspartate


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Archaeoglobus fulgidus

substrate_name: tRNACys

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

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

substrate: tRNACys


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


organism: Plasmodium falciparum

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


substrate_name: L-asparagine

substrate: L-asparagine


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


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-Glu

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

substrate: L-Glu


organism: Escherichia coli

assay_conditions_summary: 310.15 K; cofactor ATP

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

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


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


substrate_name: Unknown

proof_lines:
versus ATP
versus L-Phe

substrate: Unknown


organism: Bacillus subtilis


organism: Bombyx mori

proof_lines:
aminoacylation
tRNA2Gly, , aminoacylation
substrate from liver


organism: Bdellovibrio bacteriovorus


enzyme_display_name: proline--tRNA ligase

organism: Bos taurus

enzyme: proline--tRNA ligase


substrate_name: Phe

substrate: Phe


organism: Cricetulus sp.

substrate_name: tRNAArg

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

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

substrate: tRNAArg


enzyme_display_name: glycine--tRNA ligase

substrate_name: Gly

enzyme: glycine--tRNA ligase

substrate: Gly


organism: Triticum aestivum

substrate_name: tRNAGlu

proof_lines: enzyme forms GluRSC and GluRSP, aminoacylation

substrate: tRNAGlu


substrate_name: Glu

proof_lines: enzyme forms GluRSP and GluRSE, aminoacylation

substrate: Glu


organism: Chlamydomonas reinhardtii


substrate_name: L-alanine

substrate: L-alanine


enzyme_display_name: UniProt Q9VCC6

organism: Drosophila melanogaster

substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

enzyme: UniProt Q9VCC6

substrate: lauric acid


substrate_name: linoleic acid

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

substrate: linoleic acid


enzyme_display_name: UniProt Q9P2R7

organism: Homo sapiens

substrate_name: succinate

enzyme: UniProt Q9P2R7

substrate: succinate


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

organism: Blastocystis hominis

substrate_name: GTP

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

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

substrate: GTP


assay_conditions_summary: pH 7.4; 294.15 K; cofactor ATP


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


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


enzyme_display_name: acetate--CoA ligase

organism: Pyrococcus furiosus

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 353.15 K; cofactor ADP

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

enzyme: acetate--CoA ligase

substrate: acetyl-CoA


substrate_name: CoA

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ADP

substrate: CoA


substrate_name: ADP

substrate: ADP


substrate_name: ATP

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP

substrate: ATP


substrate_name: phosphate

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

substrate: phosphate


substrate_name: acetate

substrate: acetate


substrate_name: ATP; Coenzyme A; Acetate

assay_conditions_summary: cofactor CoA

substrate: ATP; Coenzyme A; Acetate


organism: Saccharomyces cerevisiae

substrate_name: Coenzyme A; ATP; Acetate

substrate: Coenzyme A; ATP; Acetate


substrate_name: Coenzyme A; ATP; Acrylate

substrate: Coenzyme A; ATP; Acrylate


organism: Columba livia

substrate_name: GTP; Succinate; Coenzyme A

substrate: GTP; Succinate; Coenzyme A


substrate_name: Succinyl-CoA; GDP; Phosphate

substrate: Succinyl-CoA; GDP; Phosphate


organism: Sus scrofa


substrate_name: GTP; Coenzyme A; Succinate

substrate: GTP; Coenzyme A; Succinate


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

organism: Thermococcus kodakarensis

assay_conditions_summary: 328.15 K; cofactor CoA

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


assay_conditions_summary: 328.15 K; cofactor ADP


assay_conditions_summary: 328.15 K; cofactor ATP


organism: Alcanivorax borkumensis

substrate_name: Itaconate

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

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

substrate: Itaconate


substrate_name: L-malate

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ADP

substrate: L-malate


substrate_name: D-Malate

substrate: D-Malate


substrate_name: Succinyl-CoA; ADP; Phosphate

substrate: Succinyl-CoA; ADP; Phosphate


substrate_name: Coenzyme A; Succinate; ATP

substrate: Coenzyme A; Succinate; ATP


organism: Escherichia coli K-12

substrate_name: succinate

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

substrate: succinate


organism: Calliphoridae

substrate_name: coenzyme A

substrate: coenzyme A


substrate_name: succinyl-CoA

substrate: succinyl-CoA


substrate_name: ADP

assay_conditions_summary: cofactor ADP

substrate: ADP


substrate_name: ATP

substrate: ATP


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


substrate_name: CoA

substrate: CoA


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

organism: Rattus norvegicus

substrate_name: oleate

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

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

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

substrate: oleate


substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

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

substrate: palmitate


enzyme_display_name: medium-chain acyl-CoA ligase

organism: Pseudomonas aeruginosa

enzyme: medium-chain acyl-CoA ligase


organism: Aedes togoi

substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Nipponoluciola cruciata

substrate_name: lauric acid

substrate: lauric acid


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

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


substrate_name: arachidonate

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

substrate: arachidonate


organism: Advenella mimigardefordensis

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

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

row_label: SucCD Am / CoA

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


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

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

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

row_label: SucCD Am / Itaconate


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

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

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

row_label: SucCD Am / L-malate


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

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

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

row_label: SucCD Am / D-malate


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

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

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

row_label: SucCD Am / Succinate


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

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

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

row_label: SucCD Am / 3SP


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

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

row_label: SucCD Am / ATP


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

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

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

row_label: SucCD AboHis / Succinate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

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


organism: Methanosarcina acetivorans


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

substrate_name: butyrate

smiles: CCCC(=O)[O-]

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

substrate: butyrate


substrate_name: propionate

substrate: propionate


substrate_name: valerate

smiles: CCCCC(=O)[O-]

substrate: valerate


substrate_name: acetate

substrate: acetate


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


organism: Penicillium chrysogenum

substrate_name: phenylacetate

assay_conditions_summary: pH 8.5; cofactor ATP

substrate: phenylacetate


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

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


substrate_name: Phenoxyacetate

substrate: Phenoxyacetate


substrate_name: trans-cinnamic acid

substrate: trans-cinnamic acid


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: myristic acid


substrate_name: propionic acid

smiles: CCC(=O)O

substrate: propionic acid


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

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

assay_conditions_summary: pH 8; cofactor CoA

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

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


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

assay_conditions_summary: pH 8


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

assay_conditions_summary: pH 8; cofactor ATP

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


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

assay_conditions_summary: pH 7.3; cofactor CoA

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


organism: Populus trichocarpa

substrate_name: Sodium acetate

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

substrate: Sodium acetate


substrate_name: CoA

assay_conditions_summary: pH 7.4; cofactor CoA

substrate: CoA


substrate_name: palmitate

substrate: palmitate


substrate_name: oleate

substrate: oleate


substrate_name: arachidonate


substrate_name: ATP

assay_conditions_summary: pH 7.4; cofactor ATP

substrate: ATP


substrate_name: butyrate


substrate_name: propionate


substrate_name: valerate


substrate_name: acetate


organism: Arabidopsis thaliana

substrate_name: 16-hydroxypalmitic acid

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

substrate: 16-hydroxypalmitic acid


organism: Bacillus brevis

substrate_name: ATP; Coenzyme A; Phenylalanine

assay_conditions_summary: cofactor ATP

substrate: ATP; Coenzyme A; Phenylalanine


substrate_name: Coenzyme A; ATP; Tyrosine

substrate: Coenzyme A; ATP; Tyrosine


substrate_name: Coenzyme A; Phenylalanine; ATP

substrate: Coenzyme A; Phenylalanine; ATP


organism: Bacillus subtilis

substrate_name: Coenzyme A; ATP; D-Alanine

substrate: Coenzyme A; ATP; D-Alanine


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

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


substrate_name: Acetate; Coenzyme A; ATP

substrate: Acetate; Coenzyme A; ATP


organism: Escherichia coli

substrate_name: Acetate; ATP; Coenzyme A

substrate: Acetate; ATP; Coenzyme A


organism: Methanothrix thermoacetophila


organism: Saccharomyces cerevisiae

substrate_name: Coenzyme A; Acetate; ATP

substrate: Coenzyme A; Acetate; ATP


organism: Salmonella enterica

substrate_name: Propanoate; Coenzyme A; ATP

substrate: Propanoate; Coenzyme A; ATP


organism: Bos taurus

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

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


organism: Chromochloris zofingiensis

substrate_name: Sodium acetate


substrate_name: potassium acetate

substrate: potassium acetate


organism: Lathyrus oleraceus

substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens


organism: Mycobacterium avium


organism: Rattus norvegicus


substrate_name: ATP; Coenzyme A; Palmitate

substrate: ATP; Coenzyme A; Palmitate


substrate_name: ATP; Palmitate; Coenzyme A

substrate: ATP; Palmitate; Coenzyme A


substrate_name: Palmitate; Coenzyme A; ATP

substrate: Palmitate; Coenzyme A; ATP


substrate_name: ATP; Benzoate; Coenzyme A

substrate: ATP; Benzoate; Coenzyme A


substrate_name: Coenzyme A; Palmitate; ATP

substrate: Coenzyme A; Palmitate; ATP


substrate_name: Coenzyme A; Hexanoate; ATP

substrate: Coenzyme A; Hexanoate; ATP


substrate_name: ATP; Coenzyme A; Hexanoate

substrate: ATP; Coenzyme A; Hexanoate


substrate_name: Coenzyme A; Octanoate; ATP

substrate: Coenzyme A; Octanoate; ATP


organism: Sus scrofa


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

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


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: Coenzyme A; ATP; Palmitate

assay_conditions_summary: cofactor CoA

substrate: Coenzyme A; ATP; Palmitate


substrate_name: Palmitate; ATP; Coenzyme A

substrate: Palmitate; ATP; Coenzyme A


substrate_name: palmitate

substrate: palmitate


substrate_name: ATP (Isoform 1)

substrate: ATP (Isoform 1)


substrate_name: CoA (Isoform 1)

substrate: CoA (Isoform 1)


substrate_name: palmitate (Isoform 1)

substrate: palmitate (Isoform 1)


substrate_name: oleate (Isoform 1)

substrate: oleate (Isoform 1)


substrate_name: arachidonate (Isoform 1)

substrate: arachidonate (Isoform 1)


substrate_name: benzoate

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

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

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

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

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

substrate: benzoate


substrate_name: butyrate

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

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

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

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

substrate: butyrate


substrate_name: decanoate

smiles: CCCCCCCCCC(=O)[O-]

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

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

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

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

substrate: decanoate


substrate_name: hexanoate

smiles: CCCCCC(=O)[O-]

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

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

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

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

substrate: hexanoate


substrate_name: laurate

smiles: CCCCCCCCCCCC(=O)[O-]

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

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

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

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

substrate: laurate


substrate_name: phenylacetate

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

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

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

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

substrate: phenylacetate


substrate_name: salicylate

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

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

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

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

substrate: salicylate


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

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

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

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


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

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

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

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


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

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

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

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


substrate_name: ATP

substrate: ATP


substrate_name: CoA

substrate: CoA


substrate_name: oleate

substrate: oleate


substrate_name: arachidonate

substrate: arachidonate


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


substrate_name: succinate

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

substrate: succinate


substrate_name: dodecanoate

substrate: dodecanoate


substrate_name: Octanoate

smiles: CCCCCCCC(=O)[O-]

substrate: Octanoate


substrate_name: Decanoate

substrate: Decanoate


substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

substrate: octanoic acid


substrate_name: decanoic acid

smiles: CCCCCCCCCC(=O)O

substrate: decanoic acid


substrate_name: dodecanoic acid

smiles: CCCCCCCCCCCC(=O)O

substrate: dodecanoic acid


substrate_name: linoleate

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

substrate: linoleate


substrate_name: stearate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: stearate


organism: Thermus thermophilus


substrate_name: GTP

substrate: GTP


organism: Plasmodium knowlesi

substrate_name: palmitate

column_label: Abstract reports fatty-acid Km values ranging from 11 microM for palmitate to 59 microM for arachidonate.

raw_value_unit_evidence: Km raw_value=11 microM raw_unit=microM

row_label: Plasmodium knowlesi acyl-CoA synthetase / palmitate

table_label: PubMed XML abstract PMID 3334857

substrate: palmitate


smiles: CCCCCCCCC=CCCCCCCCC(=O)O


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


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

raw_value_unit_evidence: Km raw_value=59 microM raw_unit=microM

row_label: Plasmodium knowlesi acyl-CoA synthetase / arachidonate


substrate_name: stearate (when expressed in bacteria)

substrate: stearate (when expressed in bacteria)


substrate_name: oleate (when expressed in bacteria)

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

substrate: oleate (when expressed in bacteria)


substrate_name: linoleate (when expressed in bacteria)

substrate: linoleate (when expressed in bacteria)


substrate_name: arachidonate (when expressed in bacteria)

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


column_label: Table 2 row F-ACSL3; column 18:0 stearate; Km column group.

raw_value_unit_evidence: Table 2 reports Km 3.1 +/- 0.2 uM for F-ACSL3; 18:0 (18:0 stearate).

table_label: Table 2: Km values from overexpressed ACSL isoforms in bacteria with various substrates


column_label: Table 2 row F-ACSL3; column 18:2 linoleate; Km column group.

raw_value_unit_evidence: Table 2 reports Km 7.3 +/- 0.6 uM for F-ACSL3; 18:2 (18:2 linoleate).


column_label: Table 2 row F-ACSL4; column 18:0 stearate; Km column group.

raw_value_unit_evidence: Table 2 reports Km 2.9 +/- 0.2 uM for F-ACSL4; 18:0 (18:0 stearate).


column_label: Table 2 row F-ACSL4; column 18:2 linoleate; Km column group.

raw_value_unit_evidence: Table 2 reports Km 4.0 +/- 0.6 uM for F-ACSL4; 18:2 (18:2 linoleate).


column_label: Table 2 row F-ACSL1; column 18:0 stearate; Km column group.

raw_value_unit_evidence: Table 2 reports Km 6.6 +/- 0.7 uM for F-ACSL1; 18:0 (18:0 stearate).


column_label: Table 2 row F-ACSL1; column 18:1 oleate; Km column group.

raw_value_unit_evidence: Table 2 reports Km 6.7 +/- 1.4 uM for F-ACSL1; 18:1 (18:1 oleate).


organism: Columba livia

substrate_name: succinate (for A-SCS)

substrate: succinate (for A-SCS)


substrate_name: CoA (for A-SCS)

substrate: CoA (for A-SCS)


substrate_name: succinyl-CoA (for A-SCS)

substrate: succinyl-CoA (for A-SCS)


substrate_name: phosphate (for A-SCS)

substrate: phosphate (for A-SCS)


substrate_name: ATP

substrate: ATP


substrate_name: ADP

substrate: ADP


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: ATP (at pH 7.5 and at 37 degrees Celsius)


substrate_name: CoA (at pH 7.5 and at 37 degrees Celsius)


substrate_name: acetate (at pH 7.5 and at 37 degrees Celsius)


substrate_name: propionate (at pH 7.5 and at 37 degrees Celsius)


substrate_name: glycine (at pH 7.5 and at 37 degrees Celsius)

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


substrate_name: GTP


substrate_name: GDP

substrate: GDP


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

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


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


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


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

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


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

smiles: CCCC(=O)[O-]


organism: Mus musculus

substrate_name: acetate

substrate: acetate


substrate_name: propionate

substrate: propionate


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: ATP


substrate_name: CoA

substrate: CoA


substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitate


substrate_name: oleate

substrate: oleate


substrate_name: arachidonate

substrate: arachidonate


substrate_name: butyrate

substrate: butyrate


column_label: PubMed abstract reports recombinant ACSS3 propionate Km = 0.19 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=0.19 mM raw_unit=mM

row_label: Prose segment: recombinant ACSS3 propionate

table_label: PubMed PMID 28003429 abstract


substrate_name: hexanoate

substrate: hexanoate


substrate_name: octanoate

substrate: octanoate


substrate_name: isobutyrate

substrate: isobutyrate


substrate_name: (R)-lipoate with ATP as phosphate donor

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


substrate_name: ATP (with hexanoate as substrate)

substrate: ATP (with hexanoate as substrate)


substrate_name: stearate (when expressed in bacteria)

substrate: stearate (when expressed in bacteria)


substrate_name: linoleate (when expressed in bacteria)

substrate: linoleate (when expressed in bacteria)


organism: Methanosarcina acetivorans

assay_conditions_summary: pH 7.5; 328.15 K; cofactor CoA

column_label: Primary paper Table 2 row 2-Methylbutyrate reports Km (mM) = 8.92 +/- 0.51, kcat (s^-1) = 1.58 +/- 0.07, and kcat/Km (s^-1 mM^-1) = 0.18 +/- 0.002.

normalized_value_unit_evidence: Km normalized_value=8.92 normalized_unit=mM; kcat normalized_value=1.58 normalized_unit=s^-1; kcat/Km table_normalized_value=0.18 normalized_unit=s^-1 mM^-1; CatLog computed ratio=1.58/8.92=0.17713004484304934.

raw_value_unit_evidence: Table 2 row 2-Methylbutyrate: Km raw_value=8.92 +/- 0.51 raw_unit=mM; kcat raw_value=1.58 +/- 0.07 raw_unit=s^-1; kcat/Km raw_value=0.18 +/- 0.002 raw_unit=s^-1 mM^-1.

table_label: Table 2: Kinetic parameters for acyl-CoA formation in the presence of 2-methylbutyrate


assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP

normalized_value_unit_evidence: Km normalized_value=4.21 normalized_unit=mM; kcat normalized_value=1.94 normalized_unit=s^-1; kcat/Km table_normalized_value=0.46 normalized_unit=s^-1 mM^-1; CatLog computed ratio=1.94/4.21=0.46080760095011875.

raw_value_unit_evidence: Table 2 row ATP: Km raw_value=4.21 +/- 0.11 raw_unit=mM; kcat raw_value=1.94 +/- 0.02 raw_unit=s^-1; kcat/Km raw_value=0.46 +/- 0.006 raw_unit=s^-1 mM^-1.

row_label: ATP

substrate: ATP


normalized_value_unit_evidence: Km normalized_value=4.09 normalized_unit=mM; kcat normalized_value=2.15 normalized_unit=s^-1; kcat/Km table_normalized_value=0.53 normalized_unit=s^-1 mM^-1; CatLog computed ratio=2.15/4.09=0.5256723716381418.

raw_value_unit_evidence: Table 2 row CoA: Km raw_value=4.09 +/- 0.45 raw_unit=mM; kcat raw_value=2.15 +/- 0.10 raw_unit=s^-1; kcat/Km raw_value=0.53 +/- 0.030 raw_unit=s^-1 mM^-1.

row_label: CoA


substrate_name: myristate

smiles: CCCCCCCCCCCCCC(=O)[O-]

substrate: myristate


enzyme_display_name: olefin beta-lactone synthetase

organism: Stenotrophomonas maltophilia

substrate_name: (2S,3R)-2-hexyl-3-hydroxydecanoic acid

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

enzyme: olefin beta-lactone synthetase

substrate: (2S,3R)-2-hexyl-3-hydroxydecanoic acid


organism: Stenotrophomonas maltophilia (strain K279a)


substrate_name: hexadecanoate (palmitate)

smiles: CCCCCCCCCCCCCCCC(=O)[O-]

substrate: hexadecanoate (palmitate)


substrate_name: cholate

substrate: cholate


organism: Escherichia coli (strain K12)

substrate_name: ATP (at pH 8.5 and 37 degrees Celsius)

substrate: ATP (at pH 8.5 and 37 degrees Celsius)


substrate_name: CoA (at pH 8.5 and 37 degrees Celsius)

substrate: CoA (at pH 8.5 and 37 degrees Celsius)


substrate_name: acetate (at pH 8.5 and 37 degrees Celsius)


substrate_name: (9Z)-octadecenoate (oleate)

smiles: CCCCCCCCCCCCCCCC=CC(=O)[O-]

substrate: (9Z)-octadecenoate (oleate)


substrate_name: succinate

proof_lines: kcat is 2684 min(-1) with ATP as substrate and 1471 min(-1) with GTP as substrate.

substrate: succinate


substrate_name: CoA

substrate: CoA


substrate_name: ATP


substrate_name: GTP

substrate: GTP


substrate_name: palmitic acid (at pH 7.5)

substrate: palmitic acid (at pH 7.5)


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

assay_conditions_summary: pH 7.4; 294.15 K; cofactor CoA

source_databases_merged: skid uniprot


organism: Arabidopsis thaliana

smiles: CCC(C)CC(=O)[O-]

assay_conditions_summary: pH 7.5; 310.15 K; buffer Tris-HCl; cofactor CoA

proof_lines: mutant enzyme T324G, purified with Tris-HCl buffer, at pH 7.5 and 37°C


substrate_name: Butyrate

substrate: Butyrate


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


substrate_name: Isobutyrate

substrate: Isobutyrate


proof_lines: mutant enzyme T324V, purified with Tris-HCl buffer, at pH 7.5 and 37°C


substrate_name: acetate

assay_conditions_summary: pH 7.5; 310.15 K; buffer HEPES; cofactor CoA

proof_lines: mutant enzyme T324G/V399A/W427G, purified with HEPES buffer, at pH 7.5 and 37°C

substrate: acetate


substrate_name: propionate

proof_lines: wild type enzyme, purified with Tris-HCl buffer, at pH 7.5 and 37°C

substrate: propionate


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

proof_lines: mutant enzyme I323A/V399A/W427G, purified with HEPES buffer, at pH 7.5 and 37°C


proof_lines: mutant enzyme W427S, purified with HEPES buffer, at pH 7.5 and 37°C


substrate_name: valerate

smiles: CCCCC(=O)[O-]

proof_lines: mutant enzyme I323A/V399G/W427G, purified with HEPES buffer, at pH 7.5 and 37°C

substrate: valerate


substrate_name: Heptanoate

smiles: CCCCCCC(=O)[O-]

substrate: Heptanoate


proof_lines: wild type enzyme, purified with HEPES buffer, at pH 7.5 and 37°C


proof_lines: mutant enzyme W427V, purified with HEPES buffer, at pH 7.5 and 37°C


proof_lines: mutant enzyme V399A, purified with Tris-HCl buffer, at pH 7.5 and 37°C


substrate_name: hexanoate

smiles: CCCCCC(=O)[O-]

assay_conditions_summary: pH 7.5; 310.15 K; buffer HEPES; cofactor ATP

substrate: hexanoate


assay_conditions_summary: pH 7.5; 310.15 K; buffer Tris-HCl; cofactor ATP


substrate_name: Octanoate

smiles: CCCCCCCC(=O)[O-]

proof_lines: mutant enzyme V399A/W427G, purified with Tris-HCl buffer, at pH 7.5 and 37°C

substrate: Octanoate


proof_lines: mutant enzyme W427G, purified with Tris-HCl buffer, at pH 7.5 and 37°C


column_label: Table 2 row [Formate] 0 mM, column Kmapp (mM): 0.76 +/- 0.19.

raw_value_unit_evidence: Table 2 reports Kmapp 0.76 +/- 0.19 mM for succinate; Results text says Km for succinate in the absence of formate is 0.76 +/- 0.19 mM.

row_label: Pig GTPSCS, 0 mM formate / wild-type succinate kinetics

table_label: Table 2 and Results text


assay_conditions_summary: pH 7.5; 310.15 K; buffer Tris-HCl


assay_conditions_summary: pH 7.5; 310.15 K; buffer HEPES


proof_lines: mutant enzyme T324S/V399A/W427G, purified with HEPES buffer, at pH 7.5 and 37°C


proof_lines: mutant enzyme W427A, purified with HEPES buffer, at pH 7.5 and 37°C


proof_lines: mutant enzyme W427F, purified with HEPES buffer, at pH 7.5 and 37°C


substrate_name: chenodeoxycholic acid

column_label: ScienceDirect HTML, Discussion prose, row rBAL activity for CDCA expressed in Sf9 cell microsomes, column apparent Km.

raw_value_unit_evidence: Discussion prose rBAL activity for CDCA expressed in Sf9 cell microsomes apparent Km: 32 uM

table_label: Discussion prose

substrate: chenodeoxycholic acid


substrate_name: butyrate

substrate: butyrate


proof_lines: mutant enzyme W427H, purified with HEPES buffer, at pH 7.5 and 37°C


organism: Methanothermobacter thermautotrophicus

assay_conditions_summary: 338.15 K; cofactor CoA


assay_conditions_summary: 338.15 K; cofactor ATP

substrate: ATP


organism: Brassica napus

smiles: CCCCC=CCCCCCCCC(=O)O

assay_conditions_summary: pH 8.5; 303.15 K; cofactor CoA


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


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


substrate_name: tetradecanoate

substrate: tetradecanoate


substrate_name: hexadecanoate

substrate: hexadecanoate


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


substrate_name: (6Z,12Z, 15Z)-octadecatrienoate

substrate: (6Z,12Z, 15Z)-octadecatrienoate


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


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


smiles: CCCCCCCCCCCC=CCCCCC(=O)[O-]


substrate_name: octadecanoate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: octadecanoate


substrate_name: dodecanoate

smiles: CCCCCCCCCCCC(=O)[O-]

substrate: dodecanoate


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


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


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


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


smiles: CCCC(=O)[O-]


smiles: CCCCCCC(=O)[O-]


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


smiles: CCCCC(=O)[O-]


proof_lines:
65°C, wild-type enzyme
pH 7.0, 65°C, wild-type enzyme


organism: Salmonella enterica

substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP


substrate_name: CoA

assay_conditions_summary: pH 7.5; cofactor CoA

substrate: CoA


assay_conditions_summary: pH 7; 338.15 K; cofactor ATP


assay_conditions_summary: pH 7; 338.15 K; cofactor CoA


proof_lines:
pH pH 7.0, 65°C, mutant enzyme T499A
pH 7.0, 65°C, mutant enzyme T499A


proof_lines:
pH 7.0, 65°C, wild-type enzyme
65°C, wild-type enzyme


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: mutant S291Y, at 37°C, in 175 mM Tris-HCl, at pH 7.4


proof_lines: wild type enzyme, at 37°C, in 175 mM Tris-HCl, at pH 7.4


proof_lines: mutant Q525K, at 37°C, in 175 mM Tris-HCl at pH 7.4


proof_lines: mutant L399M, at 37°C, in 175 mM Tris-HCl at pH 7.4


substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitate


proof_lines: mutant S291Y, at 37°C, in 175 mM Tris-HCl at pH 7.4


proof_lines: wild type enzyme, at 37°C, in 175 mM Tris-HCl at pH 7.4


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


proof_lines: mutant Q525K, at 37°C, in 175 mM Tris-HCl, at pH 7.4


organism: Escherichia coli

substrate_name: Undecanoate

smiles: CCCCCCCCCCC(=O)O

assay_conditions_summary: cofactor CoA

substrate: Undecanoate


substrate_name: palmitoleate

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

substrate: palmitoleate


substrate_name: Pentadecanoate

smiles: CCCCCCCCCCCCCCC(=O)[O-]

substrate: Pentadecanoate


substrate_name: tridecanoate

smiles: CCCCCCCCCCCCC(=O)[O-]

substrate: tridecanoate


substrate_name: heptadecanoate

smiles: CCCCCCCCCCCCCCCCC(=O)[O-]

substrate: heptadecanoate


substrate_name: hexanoate

smiles: CCCCCC(=O)[O-]

substrate: hexanoate


substrate_name: Heptanoate

substrate: Heptanoate


substrate_name: Oleate

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

substrate: Oleate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: stearate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

proof_lines:
acyl-CoA synthetase-4.6
acyl-CoA synthetase-5.6
acyl-CoA synthetase-5.0

substrate: stearate


substrate_name: myristate

smiles: CCCCCCCCCCCCCC(=O)[O-]

substrate: myristate


substrate_name: laurate

smiles: CCCCCCCCCCCC(=O)[O-]

proof_lines:
acyl-CoA synthetase-5.6
acyl-CoA synthetase-4.6
acyl-CoA synthetase-5.0

substrate: laurate


substrate_name: Octanoate

smiles: CCCCCCCC(=O)[O-]

substrate: Octanoate


substrate_name: Decanoate

smiles: CCCCCCCCCC(=O)[O-]

proof_lines:
acyl-CoA synthetase-5.0
acyl-CoA synthetase-4.6
acyl-CoA synthetase-5.6

substrate: Decanoate


assay_conditions_summary: cofactor ATP

proof_lines:
acyl-CoA synthetase-5.6
nonanoate
acyl-CoA synthetase-5.0

substrate: ATP


proof_lines:
acyl-CoA synthetase-5.6
acyl-CoA synthetase-5.0
acyl-CoA synthetase-4.6


organism: Paecilomyces variotii


substrate_name: Butyrate

smiles: CCCC(=O)[O-]

substrate: Butyrate


substrate_name: pentanoate

smiles: CCCCC(=O)O

substrate: pentanoate


substrate_name: Isopentanoate

substrate: Isopentanoate


substrate_name: Isobutyrate

substrate: Isobutyrate


substrate_name: propionate

substrate: propionate


substrate_name: CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


substrate_name: ADP

assay_conditions_summary: pH 8; 303.15 K; cofactor ADP

substrate: ADP


substrate_name: phosphate

substrate: phosphate


substrate_name: succinate

substrate: succinate


organism: Pigeon

substrate_name: GDP

substrate: GDP


substrate_name: GTP

substrate: GTP


organism: Escherichia coli K-12

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ADP


substrate_name: D-malate

substrate: D-malate


substrate_name: Itaconate

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

substrate: Itaconate


substrate_name: L-malate

substrate: L-malate


assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP


organism: Yarrowia lipolytica


substrate_name: dephospho-CoA

substrate: dephospho-CoA


substrate: ATP


substrate_name: pantetheine

smiles: CC(C)(CO)C(C(=O)NCCC(=O)NCCS)O

substrate: pantetheine


smiles: CC(C)(COP(=O)(O)O)C(C(=O)NCCC(=O)NCCS)O


organism: Archaeoglobus fulgidus

substrate_name: Butyrate

substrate: Butyrate


substrate_name: acetate

substrate: acetate


organism: Alcanivorax borkumensis


organism: Acetobacter aceti


substrate_name: propanoate

substrate: propanoate


assay_conditions_summary: pH 8; 298.15 K; cofactor CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Bradyrhizobium japonicum


substrate_name: CoA

substrate: CoA


substrate_name: dATP

substrate: dATP


organism: Advenella mimigardefordensis


proof_lines:
recombinant enzyme, pH 7.4, 30°C
pH 7.4, 30°C, recombinant sucCD


substrate_name: ATP


organism: Plasmodium falciparum

proof_lines: recombinant wild type enzyme, at pH 7.4 and 37°C


proof_lines: mutant enzyme D95E/Y164D, at pH 7.4 and 37°C


substrate_name: propionate

substrate: propionate


proof_lines: mutant enzyme C123ALPHAA, apparent value

proof_lines: mutant enzyme C123ALPHAV, apparent value

proof_lines: mutant enzyme C123ALPHAS, apparent value


organism: Mus musculus

substrate_name: n-tetracosanoic acid

smiles: CCCCCCCCCCCCCCCCCCCCCCCC(=O)O

substrate: n-tetracosanoic acid


substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitate


organism: Cereibacter sphaeroides


substrate_name: Acrylate

substrate: Acrylate


enzyme_display_name: L-3-cyanoalanine synthase

organism: Spinacia oleracea

substrate_name: NaCN

enzyme: L-3-cyanoalanine synthase

substrate: NaCN


assay_conditions_summary: cofactor ADP


substrate_name: succinate

substrate: succinate


organism: Bos taurus

substrate_name: benzoate

substrate: benzoate


substrate_name: GTP

proof_lines:
pH 7.4, 22°C, mutant enzyme E197betaQ
pH 7.4, 22°C, mutant enzyme E208alphaQ
pH 7.4, 22°C, mutant enzyme E208alphaD

substrate: GTP


assay_conditions_summary: pH 7.4; 295.15 K; cofactor ATP

proof_lines:
pH 7.4, 22°C, mutant enzyme E208alphaQ
pH 7.4, 22°C, mutant enzyme E197betaQ
pH 7.4, 22°C, mutant enzyme E197betaD


assay_conditions_summary: pH 7.4; 295.15 K; cofactor CoA

proof_lines:
pH 7.4, 22°C, mutant enzyme E208alphaQ
pH 7.4, 22°C, mutant enzyme E197betaQ
pH 7.4, 22°C, mutant enzyme E208alphaD


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

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


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


substrate_name: Unknown

substrate: Unknown


organism: Methanothrix thermoacetophila

assay_conditions_summary: pH 7.5; 328.15 K; cofactor CoA


assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP

substrate: ATP


organism: Homo sapiens


organism: Rattus norvegicus


substrate_name: linolenate

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

substrate: linolenate


substrate_name: palmitoleate

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

substrate: palmitoleate


substrate_name: linoleate

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

substrate: linoleate


organism: Nitrosomonas europaea


organism: Pseudomonas aeruginosa


substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

substrate: oleic acid


substrate_name: coenzyme A

substrate: coenzyme A


organism: Oryctolagus cuniculus

substrate_name: CoA

substrate: CoA


substrate_name: acetate

substrate: acetate