substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

substrate: octanoic acid


enzyme_display_name: medium-chain acyl-CoA ligase

organism: Mycobacterium avium

substrate_name: decanoic acid

source_db: uniprot

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.

smiles: CCCCCCCCCC(=O)O

assay_conditions_summary: cofactor CoA

data_origin: experimental

enzyme: medium-chain acyl-CoA ligase

substrate: decanoic acid

source: uniprot


substrate_name: dodecanoic acid

smiles: CCCCCCCCCCCC(=O)O

substrate: dodecanoic acid


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

organism: Rattus norvegicus

substrate_name: linoleate

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

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

substrate: linoleate


substrate_name: arachidonate

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

substrate: arachidonate


substrate_name: stearate

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

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: stearate


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

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

substrate_name: ATP

assay_conditions_summary: cofactor ATP

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

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

substrate: ATP


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

organism: Thermus thermophilus

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


substrate_name: GTP

substrate: GTP


substrate_name: succinate

substrate: succinate


substrate_name: CoA

substrate: CoA


organism: Plasmodium knowlesi

substrate_name: palmitate

source_db: brenda

verification_status: verified

smiles: CCCCCCCCCCCCCCCC(=O)O

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

status: verified

source: brenda


substrate_name: oleate

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

substrate: oleate


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)


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: ADP

substrate: ADP


enzyme_display_name: acetate--CoA ligase

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

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

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

enzyme: acetate--CoA ligase


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


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

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


organism: Lathyrus oleraceus

substrate_name: acetyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

substrate: acetyl-CoA


substrate_name: ATP

substrate: ATP


verification_status: unverified

status: unverified


substrate_name: CoA

substrate: CoA


substrate_name: palmitate

substrate: palmitate


substrate_name: oleate

substrate: oleate


substrate_name: arachidonate

substrate: arachidonate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


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

smiles: CCCCCC(=O)[O-]

substrate: hexanoate


substrate_name: octanoate

smiles: CCCCCCCC(=O)[O-]

substrate: octanoate


substrate_name: isobutyrate

substrate: isobutyrate


organism: Bos taurus

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

source_db: oed

verification_status: corrected

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

status: corrected

source: oed


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


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

kcat_over_km_origin: calculated

sequence_source: multiple

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

source_databases_merged: brenda uniprot

enzyme: olefin beta-lactone synthetase

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


organism: Stenotrophomonas maltophilia (strain K279a)


organism: Homo sapiens

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: ATP


substrate_name: GTP

substrate: GTP


substrate_name: palmitic acid (at pH 7.5)

substrate: palmitic acid (at pH 7.5)


organism: Sus scrofa

source_db: skid

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

source: skid


organism: Arabidopsis thaliana

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

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

mutation_type: substitution

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

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

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

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

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


organism: Rattus norvegicus

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


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: CCCCCCCC(=O)[O-]


smiles: CCCCCC(=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: 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


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

substrate: hexanoate


substrate_name: Heptanoate

substrate: Heptanoate


substrate_name: Oleate

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

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

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


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


organism: Columba livia

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: 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_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

substrate: 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

km_display: Not reported

ki_unit: mM

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


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


organism: Penicillium chrysogenum

assay_conditions_summary: pH 8; cofactor ATP

column_label: Results prose on printed page 5476 states hyperbolic behavior for ATP, CoA, and acetate, with Km values 17, 0.18, and 6.8 mM, respectively.

raw_value_unit_evidence: The Results prose lists ATP, CoA, and acetate, with Km values 17, 0.18, and 6.8 mM in that order.

row_label: CoA in ATP-CoA-acetate Km sentence

table_label: Results prose p5476/PDF p3


row_label: acetate in ATP-CoA-acetate Km sentence


substrate_name: ATP

row_label: ATP in ATP-CoA-acetate Km sentence

substrate: ATP


organism: Ovis aries


substrate_name: Butyrate

substrate: Butyrate


substrate_name: propanoate

substrate: propanoate


organism: Saccharomyces cerevisiae

column_label: Table II forward reaction maps Km to 18.3 uM CoA under oleate held constant at 50 uM.

raw_value_unit_evidence: Km raw_value=18.3 raw_unit=uM CoA

row_label: Km / 18.3 uM CoA

table_label: PMID 17604220 PMC Table II


column_label: Table II forward reaction maps Km to 51.6 uM ATP under oleate held constant at 50 uM.

raw_value_unit_evidence: Km raw_value=51.6 raw_unit=uM ATP

row_label: Km / 51.6 uM ATP


substrate_name: oleate

assay_conditions_summary: pH 8

proof_lines: in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 30°C

substrate: oleate


organism: Sus scrofa

substrate_name: Octanoate

smiles: CCCCCCCC(=O)[O-]

assay_conditions_summary: cofactor CoA

substrate: Octanoate


organism: Dunaliella tertiolecta

substrate_name: potassium acetate

substrate: potassium acetate


substrate_name: Sodium acetate

substrate: Sodium acetate


organism: Drosophila melanogaster

substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

substrate: lauric acid


substrate_name: linoleic acid

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

substrate: linoleic acid


organism: Salmonella enterica

proof_lines: mutant L641P, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant G266S, pH not specified in the publication, temperature not specified in the publication


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


organism: Geobacillus thermodenitrificans

substrate_name: caproate

smiles: CCCCCC(=O)[O-]

substrate: caproate


substrate_name: palmitate

substrate: palmitate


assay_conditions_summary: pH 6.7; buffer notes and an unresolved EC+organism candidate pool; cofactor ATP

proof_lines:
in Tris buffer, pH 6.7, 200 mM K+
in Pipes buffer, pH 6.7, 200 mM K+
Tris buffer, pH 8.3, 200 mM K+


assay_conditions_summary: pH 6.7; buffer notes and an unresolved EC+organism candidate pool; cofactor CoA

proof_lines:
CoA
pH 6.7, 200 mM K+
CoA, in Tris buffer, pH 8.3, 200 mM K+


assay_conditions_summary: cofactor ATP

proof_lines: synthesis of adenosine 5?-tetraphosphate


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: tripolyphosphate

substrate: tripolyphosphate


proof_lines:
enzyme form pI 6.4
enzyme form pI 5.8
enzyme forms pI 6.2 and pI 6.0


substrate_name: GTP

proof_lines:
enzyme form pI 6.4
enzyme form 6.0
enzyme forms pI 6.2, pI 5.9 and pI 5.8

substrate: GTP


substrate_name: succinate

proof_lines:
enzyme form pI 6.4
enzyme forms pI 5.9 and pI 5.8
enzyme form pI 6.0

substrate: succinate


substrate_name: CoA

substrate: CoA


organism: Glycine max

proof_lines:
immobilized enzyme
soluble enzyme


organism: Methanothrix soehngenii


substrate_name: acetate

substrate: acetate


substrate_name: fluoroacetate

substrate: fluoroacetate


assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


organism: Caulobacter vibrioides

substrate_name: octadecanoate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: octadecanoate


organism: Bos taurus

assay_conditions_summary: pH 6.7; buffer Tris; cofactor CoA

proof_lines:
in Tris buffer, pH 6.7, 200 mM K+
in Pipes buffer, pH 6.7, 200 mM K+


substrate_name: Unknown

assay_conditions_summary: pH 8.5; cofactor CoA

substrate: Unknown


substrate_name: Acrylate

substrate: Acrylate


enzyme_display_name: phenylalanine--tRNA ligase

organism: Enterococcus faecalis

substrate_name: L-Phe

enzyme: phenylalanine--tRNA ligase

substrate: L-Phe


enzyme_display_name: arginine--tRNA ligase

organism: Escherichia coli

substrate_name: L-arginine

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

proof_lines: aminoacylation reaction, 4-fluorotryptophan-labeled enzyme

enzyme: arginine--tRNA ligase

substrate: L-arginine


enzyme_display_name: glutamate--tRNA ligase

substrate_name: tRNAGlu

enzyme: glutamate--tRNA ligase

substrate: tRNAGlu


enzyme_display_name: UniProt Q941M3

organism: Populus tomentosa

substrate_name: cinnamate

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q941M3

substrate: cinnamate


substrate_name: ferulate

substrate: ferulate


substrate_name: caffeate

substrate: caffeate


enzyme_display_name: 6-carboxyhexanoate-CoA ligase

organism: Ectopseudomonas mendocina

enzyme: 6-carboxyhexanoate-CoA ligase


organism: Priestia megaterium

substrate_name: heptanedioate

substrate: heptanedioate


enzyme_display_name: UniProt O67575

organism: Aquifex aeolicus

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

enzyme: UniProt O67575


enzyme_display_name: UniProt P53559

organism: Bacillus subtilis

enzyme: UniProt P53559


substrate_name: Glutarate

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

substrate: Glutarate


substrate_name: suberate

substrate: suberate


substrate_name: adipate

substrate: adipate


substrate_name: Octanoate

substrate: Octanoate


substrate_name: Heptanoate

smiles: CCCCCCC(=O)[O-]

substrate: Heptanoate


substrate_name: benzofuranylalanine

substrate: benzofuranylalanine


enzyme_display_name: proline--tRNA ligase

substrate_name: ATP

enzyme: proline--tRNA ligase

substrate: ATP


substrate_name: Butyrate

smiles: CCCC(=O)[O-]

substrate: Butyrate


enzyme_display_name: glutamine--tRNA ligase

substrate_name: Gln

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

proof_lines:
reaction with mutant tRNAGln G36U
reaction with mutant tRNAGln U35A

enzyme: glutamine--tRNA ligase

substrate: Gln


enzyme_display_name: 4-coumarate--CoA ligase

organism: Arabidopsis thaliana

substrate_name: 4-Coumarate; Coenzyme A; ATP

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

enzyme: 4-coumarate--CoA ligase

substrate: 4-Coumarate; Coenzyme A; ATP


substrate_name: Coenzyme A; ATP; Sinapate

substrate: Coenzyme A; ATP; Sinapate


organism: Pueraria montana var. lobata

assay_conditions_summary: pH 7.8; 295.15 K; cofactor CoA


substrate_name: trans-cinnamate

substrate: trans-cinnamate


organism: Sorbus aucuparia

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA


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

organism: Pyrococcus furiosus

substrate_name: Phosphate; ADP; Acetyl-CoA

assay_conditions_summary: cofactor ADP

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

substrate: Phosphate; ADP; Acetyl-CoA


substrate_name: ADP; Acetyl-CoA; Phosphate

substrate: ADP; Acetyl-CoA; Phosphate


substrate_name: Isobutanoate

assay_conditions_summary: pH 8.4; 353.15 K; cofactor ADP

substrate: Isobutanoate


substrate_name: GTP

substrate: GTP


substrate_name: ADP; Phosphate; Acetyl-CoA

substrate: ADP; Phosphate; Acetyl-CoA


substrate_name: ADP

substrate: ADP


substrate_name: phenylacetic acid

substrate: phenylacetic acid


substrate_name: Acetyl-CoA

substrate: Acetyl-CoA


substrate_name: Acetate

smiles: CC(=O)O

substrate: Acetate


substrate_name: GDP

substrate: GDP


substrate_name: Phosphate

smiles: O=P(O)(O)O

substrate: Phosphate


substrate_name: Phenylacetyl-CoA

substrate: Phenylacetyl-CoA


substrate_name: Phosphate; Acetyl-CoA; ADP

substrate: Phosphate; Acetyl-CoA; ADP


substrate_name: ATP

assay_conditions_summary: pH 8.4; 353.15 K; cofactor ATP

substrate: ATP


substrate_name: Coenzyme A

substrate: Coenzyme A


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: isobutyryl-CoA

proof_lines:
isoenzyme ACS II
GTP, isoenzyme ACS I
isoenzyme ACS I

substrate: isobutyryl-CoA


proof_lines:
isoenzyme ACS II
isoenzyme ACS I


substrate_name: Isobutyrate

substrate: Isobutyrate


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: CoA

proof_lines:
isoenzyme ACS I
isoenzyme ACS II

substrate: CoA


substrate_name: indoleacetate

substrate: indoleacetate


substrate_name: acetate

substrate: acetate


substrate_name: phenylacetate

substrate: phenylacetate


substrate_name: ADP

substrate: ADP


substrate_name: phosphate

substrate: phosphate


substrate_name: GTP

substrate: GTP


organism: Thermococcus kodakarensis

assay_conditions_summary: pH 6.5; 328.15 K; cofactor ADP


assay_conditions_summary: pH 6.5; 328.15 K; cofactor ATP


substrate_name: CoASH

proof_lines:
isoenzyme 2
isoenzyme 1

substrate: CoASH


substrate_name: sinapoate

substrate: sinapoate


proof_lines:
isoenzyme 1
isoenzyme 2


proof_lines:
isoenzyme 2
3-coumarate, , isoenzyme 1


substrate_name: isoferulate

proof_lines:
3,4-dimethoxycinnamate, , isoenzyme 1
isoenzyme 2

substrate: isoferulate


organism: Chloroflexus aurantiacus

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ADP

proof_lines: in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55°C


assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP


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

organism: Rattus norvegicus

substrate_name: Octanoate

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

substrate: Octanoate


substrate_name: Butyrate

substrate: Butyrate


substrate_name: oleate

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

substrate: oleate


substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitate


assay_conditions_summary: cofactor CoA


enzyme_display_name: biotin--CoA ligase

organism: Mycoplana sp.

enzyme: biotin--CoA ligase


substrate_name: (+/-)-dethiobiotin

substrate: (+/-)-dethiobiotin


substrate_name: (+)-biotin

substrate: (+)-biotin


substrate_name: DL-actithiazic acid

substrate: DL-actithiazic acid


substrate_name: ATP

substrate: ATP


organism: Piper nigrum

substrate_name: cinnamate

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: cinnamate


substrate_name: ferulate

proof_lines:
isoform 4CL1, at pH 7.5 and 25°C
isoform 4CL3, at pH 7.5 and 25°C

substrate: ferulate


substrate_name: piperate

substrate: piperate


organism: Oryza sativa

proof_lines: pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl1

proof_lines: pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl5

proof_lines: pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl2


proof_lines: pH 7.5, temperature not specified in the publication, recombinant isozyme Os4Cl4


substrate_name: caffeate

substrate: caffeate


substrate_name: sinapate

substrate: sinapate


organism: Physcomitrium patens


enzyme_display_name: cholate--CoA ligase

organism: Ophiodon elongatus

substrate_name: lithocholate

enzyme: cholate--CoA ligase

substrate: lithocholate


substrate_name: cholate

substrate: cholate


substrate_name: deoxycholate

substrate: deoxycholate


substrate_name: chenodeoxycholate

substrate: chenodeoxycholate


enzyme_display_name: oxalate--CoA ligase

substrate_name: oxalate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

enzyme: oxalate--CoA ligase

substrate: oxalate


organism: Glycine max

proof_lines:
4CL3
isoenzyme 2
isoenzyme 1


proof_lines:
isoenzyme 2
isoenzyme 1
4CL3


organism: Populus x canadensis

proof_lines:
isoenzyme II
isoenzyme III
5-hydroxyferulate


proof_lines:
isoenzyme II
isoenzyme III
ferulate, , isoenzyme I


substrate_name: sinapoate

substrate: sinapoate


organism: Forsythia suspensa

substrate_name: CoA

substrate: CoA


assay_conditions_summary: cofactor ATP


organism: Giardia duodenalis

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: ADP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

substrate: ADP


substrate_name: phosphate

substrate: phosphate


organism: Pyrobaculum aerophilum

substrate_name: isobutyryl-CoA

assay_conditions_summary: pH 6.5; 358.15 K; cofactor CoA

substrate: isobutyryl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


organism: Erythrina crista-galli


organism: Ruta graveolens

assay_conditions_summary: pH 7.8; 305.15 K; cofactor CoA

proof_lines:
isozyme 4CL2, at pH 7.8 and 32°C
isozyme 4CL1, pH 7.8, 32°C


substrate_name: cinnamate

substrate: cinnamate


substrate_name: dADP

substrate: dADP


organism: Salix babylonica

substrate_name: ferulate

substrate: ferulate


organism: Phycomyces blakesleeanus

substrate_name: acetate

proof_lines:
30°C, isoenzyme ACS1
pH 8.0, 37°C, isoenzyme ACS2

substrate: acetate


substrate_name: propionate

proof_lines:
pH 8.0, 37°C, isoenzyme ACS2
30°C, isoenzyme ACS1

substrate: propionate


proof_lines:
4CL1
isoenzyme 1
isoenzyme 2


organism: Eubacterium sp.


substrate_name: ATP

substrate: ATP


organism: unidentified archaeon

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: at pH 8.0, temperature not specified in the publication


organism: Cavia porcellus

substrate_name: cholate

substrate: cholate


organism: Entamoeba histolytica

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H533E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H533E, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NAT4 and applied mutation signature H533D to reconstruct the assayed variant sequence.

column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block Acetate, enzyme variant row His533Asp; column kcat (s-1) = 0.18; column Km (mM) = 0.31; column kcat/Km (mM-1 s-1) = 0.59.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.18 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.18 s^(-1). Km: printed Table 2 cell 0.31 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.31 mM. kcat/Km: printed Table 2 cell 0.59 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 0.59 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate Acetate, enzyme variant row His533Asp, which is the H533D variant this catalog row carries: kcat = 0.18 s-1; Km = 0.31 mM; printed kcat/Km = 0.59 mM-1 s-1.

table_label: Table 2: Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction (FEBS Lett. 2017, 591(4):603-612); printed column heads Varied Substrate | Enzyme Variant | kcat (s-1) | Km (mM) | kcat/Km (mM-1 s-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NAT4 and applied mutation signature H533E to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block Pi, enzyme variant row His533Glu; column kcat (s-1) = 0.22; column Km (mM) = 0.18; column kcat/Km (mM-1 s-1) = 1.3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.22 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.22 s^(-1). Km: printed Table 1 cell 0.18 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.18 mM. kcat/Km: printed Table 1 cell 1.3 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 1.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate Pi, enzyme variant row His533Glu, which is the H533E variant this catalog row carries: kcat = 0.22 s-1; Km = 0.18 mM; printed kcat/Km = 1.3 mM-1 s-1.

table_label: Table 1: Apparent kinetic parameters of the His533 variants in the acetate-forming direction (FEBS Lett. 2017, 591(4):603-612); printed column heads Varied Substrate | Enzyme Variant | kcat (s-1) | Km (mM) | kcat/Km (mM-1 s-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H533D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H533D, pH and temperature not specified in the publication


column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block Acetate, enzyme variant row His533Glu; column kcat (s-1) = 0.26; column Km (mM) = 0.40; column kcat/Km (mM-1 s-1) = 0.67.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.26 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.26 s^(-1). Km: printed Table 2 cell 0.40 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.4 mM. kcat/Km: printed Table 2 cell 0.67 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 0.67 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate Acetate, enzyme variant row His533Glu, which is the H533E variant this catalog row carries: kcat = 0.26 s-1; Km = 0.40 mM; printed kcat/Km = 0.67 mM-1 s-1.


column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block CoA, enzyme variant row His533Glu; column kcat (s-1) = 0.27; column Km (mM) = 0.26; column kcat/Km (mM-1 s-1) = 1.1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.27 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.27 s^(-1). Km: printed Table 2 cell 0.26 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.26 mM. kcat/Km: printed Table 2 cell 1.1 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 1.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate CoA, enzyme variant row His533Glu, which is the H533E variant this catalog row carries: kcat = 0.27 s-1; Km = 0.26 mM; printed kcat/Km = 1.1 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H533Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H533Q, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NAT4 and applied mutation signature H533N to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block Acetyl-CoA, enzyme variant row His533Asn; column kcat (s-1) = 1.4; column Km (mM) = 0.015; column kcat/Km (mM-1 s-1) = 92.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.4 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.4 s^(-1). Km: printed Table 1 cell 0.015 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.015 mM. kcat/Km: printed Table 1 cell 92 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 92.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate Acetyl-CoA, enzyme variant row His533Asn, which is the H533N variant this catalog row carries: kcat = 1.4 s-1; Km = 0.015 mM; printed kcat/Km = 92 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H533N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H533N, pH and temperature not specified in the publication


column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block Pi, enzyme variant row His533Asn; column kcat (s-1) = 1.5; column Km (mM) = 0.94; column kcat/Km (mM-1 s-1) = 1.7.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.5 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.5 s^(-1). Km: printed Table 1 cell 0.94 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.94 mM. kcat/Km: printed Table 1 cell 1.7 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 1.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate Pi, enzyme variant row His533Asn, which is the H533N variant this catalog row carries: kcat = 1.5 s-1; Km = 0.94 mM; printed kcat/Km = 1.7 mM-1 s-1.


column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block Acetate, enzyme variant row His533Asn; column kcat (s-1) = 1.5; column Km (mM) = 0.76; column kcat/Km (mM-1 s-1) = 1.9.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.5 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.5 s^(-1). Km: printed Table 2 cell 0.76 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.76 mM. kcat/Km: printed Table 2 cell 1.9 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 1.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate Acetate, enzyme variant row His533Asn, which is the H533N variant this catalog row carries: kcat = 1.5 s-1; Km = 0.76 mM; printed kcat/Km = 1.9 mM-1 s-1.


column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block ADP, enzyme variant row His533Asp; column kcat (s-1) = 1.7; column Km (mM) = 0.60; column kcat/Km (mM-1 s-1) = 2.9.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.7 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.7 s^(-1). Km: printed Table 1 cell 0.60 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.6 mM. kcat/Km: printed Table 1 cell 2.9 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 2.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate ADP, enzyme variant row His533Asp, which is the H533D variant this catalog row carries: kcat = 1.7 s-1; Km = 0.60 mM; printed kcat/Km = 2.9 mM-1 s-1.


column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block Pi, enzyme variant row His533Asp; column kcat (s-1) = 1.7; column Km (mM) = 0.25; column kcat/Km (mM-1 s-1) = 7.3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.7 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.7 s^(-1). Km: printed Table 1 cell 0.25 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.25 mM. kcat/Km: printed Table 1 cell 7.3 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 7.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate Pi, enzyme variant row His533Asp, which is the H533D variant this catalog row carries: kcat = 1.7 s-1; Km = 0.25 mM; printed kcat/Km = 7.3 mM-1 s-1.


column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block CoA, enzyme variant row His533Asn; column kcat (s-1) = 2.0; column Km (mM) = 0.08; column kcat/Km (mM-1 s-1) = 26.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.0 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 2.0 s^(-1). Km: printed Table 2 cell 0.08 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.08 mM. kcat/Km: printed Table 2 cell 26 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 26.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate CoA, enzyme variant row His533Asn, which is the H533N variant this catalog row carries: kcat = 2.0 s-1; Km = 0.08 mM; printed kcat/Km = 26 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H533A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H533A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NAT4 and applied mutation signature H533K to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block Acetyl-CoA, enzyme variant row His533Lys; column kcat (s-1) = 2.4; column Km (mM) = 0.030; column kcat/Km (mM-1 s-1) = 79.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.4 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 2.4 s^(-1). Km: printed Table 1 cell 0.030 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.03 mM. kcat/Km: printed Table 1 cell 79 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 79.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate Acetyl-CoA, enzyme variant row His533Lys, which is the H533K variant this catalog row carries: kcat = 2.4 s-1; Km = 0.030 mM; printed kcat/Km = 79 mM-1 s-1.


organism: Escherichia coli

substrate_name: tRNAArg

proof_lines:
argS1 mutant, pH 7.5, 37°C
aminoacylation, mutant enzyme

substrate: tRNAArg


organism: Oryza sativa subsp. japonica

assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL3'; substrate row 'Cinnamate'; column 'Km (uM)' = 28.2; column 'Vmax (pkat mg^-1)' = 3010; column 'Kcat (min^-1)' = 10.92; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 6458.

normalized_value_unit_evidence: Km: printed Table I cell 28.2 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 28.2 / 1000 = 0.0282 mM; the exported value is 0.0282 mM. kcat: printed Table I cell 10.92 min^-1 (the Kcat column header prints 'min^-1'); 10.92 / 60 = 0.182 s^(-1); the exported value is 10.92 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 6458 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 6458 / 1000 = 6.458 s^(-1)*mM^(-1); the exported value is 387.2340425531915 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL3', substrate row 'Cinnamate': Km = 28.2 uM; Vmax = 3010 pkat mg^-1; Kcat = 10.92 min^-1; printed Kenz = Kcat/Km = 6458 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL3', substrate row 'Cinnamate' (catalog accession Q6ETN3)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL3'; substrate row '4-Coumarate'; column 'Km (uM)' = 4.9; column 'Vmax (pkat mg^-1)' = 4700; column 'Kcat (min^-1)' = 17.10; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 58521.

normalized_value_unit_evidence: Km: printed Table I cell 4.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 4.9 / 1000 = 0.004900000000000001 mM; the exported value is 0.004900000000000001 mM. kcat: printed Table I cell 17.10 min^-1 (the Kcat column header prints 'min^-1'); 17.10 / 60 = 0.28500000000000003 s^(-1); the exported value is 17.1 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 58521 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 58521 / 1000 = 58.521 s^(-1)*mM^(-1); the exported value is 3489.7959183673465 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL3', substrate row '4-Coumarate': Km = 4.9 uM; Vmax = 4700 pkat mg^-1; Kcat = 17.10 min^-1; printed Kenz = Kcat/Km = 58521 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL3', substrate row '4-Coumarate' (catalog accession Q6ETN3)


substrate_name: caffeate

column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL3'; substrate row 'Caffeate'; column 'Km (uM)' = 10.9; column 'Vmax (pkat mg^-1)' = 4210; column 'Kcat (min^-1)' = 15.30; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 23330.

normalized_value_unit_evidence: Km: printed Table I cell 10.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 10.9 / 1000 = 0.0109 mM; the exported value is 0.0109 mM. kcat: printed Table I cell 15.30 min^-1 (the Kcat column header prints 'min^-1'); 15.30 / 60 = 0.255 s^(-1); the exported value is 15.3 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 23330 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 23330 / 1000 = 23.33 s^(-1)*mM^(-1); the exported value is 1403.6697247706422 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL3', substrate row 'Caffeate': Km = 10.9 uM; Vmax = 4210 pkat mg^-1; Kcat = 15.30 min^-1; printed Kenz = Kcat/Km = 23330 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL3', substrate row 'Caffeate' (catalog accession Q6ETN3)

substrate: caffeate


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL3'; substrate row 'Ferulate'; column 'Km (uM)' = 3.5; column 'Vmax (pkat mg^-1)' = 4930; column 'Kcat (min^-1)' = 17.94; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 84943.

normalized_value_unit_evidence: Km: printed Table I cell 3.5 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 3.5 / 1000 = 0.0035 mM; the exported value is 0.0035 mM. kcat: printed Table I cell 17.94 min^-1 (the Kcat column header prints 'min^-1'); 17.94 / 60 = 0.29900000000000004 s^(-1); the exported value is 17.94 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 84943 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 84943 / 1000 = 84.943 s^(-1)*mM^(-1); the exported value is 5125.714285714286 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL3', substrate row 'Ferulate': Km = 3.5 uM; Vmax = 4930 pkat mg^-1; Kcat = 17.94 min^-1; printed Kenz = Kcat/Km = 84943 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL3', substrate row 'Ferulate' (catalog accession Q6ETN3)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Cinnamate'; column 'Km (uM)' = 54.4; column 'Vmax (pkat mg^-1)' = 300; column 'Kcat (min^-1)' = 1.02; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 312.

normalized_value_unit_evidence: Km: printed Table I cell 54.4 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 54.4 / 1000 = 0.0544 mM; the exported value is 0.0544 mM. kcat: printed Table I cell 1.02 min^-1 (the Kcat column header prints 'min^-1'); 1.02 / 60 = 0.017 s^(-1); the exported value is 1.02 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 312 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 312 / 1000 = 0.312 s^(-1)*mM^(-1); the exported value is 18.75 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Cinnamate': Km = 54.4 uM; Vmax = 300 pkat mg^-1; Kcat = 1.02 min^-1; printed Kenz = Kcat/Km = 312 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Cinnamate' (catalog accession Q6ZAC1)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row '4-Coumarate'; column 'Km (uM)' = 10.3; column 'Vmax (pkat mg^-1)' = 830; column 'Kcat (min^-1)' = 2.88; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 4660.

normalized_value_unit_evidence: Km: printed Table I cell 10.3 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 10.3 / 1000 = 0.0103 mM; the exported value is 0.0103 mM. kcat: printed Table I cell 2.88 min^-1 (the Kcat column header prints 'min^-1'); 2.88 / 60 = 0.048 s^(-1); the exported value is 2.88 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 4660 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 4660 / 1000 = 4.66 s^(-1)*mM^(-1); the exported value is 279.6116504854369 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row '4-Coumarate': Km = 10.3 uM; Vmax = 830 pkat mg^-1; Kcat = 2.88 min^-1; printed Kenz = Kcat/Km = 4660 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row '4-Coumarate' (catalog accession Q6ZAC1)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Caffeate'; column 'Km (uM)' = 26.1; column 'Vmax (pkat mg^-1)' = 240; column 'Kcat (min^-1)' = 0.84; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 535.

normalized_value_unit_evidence: Km: printed Table I cell 26.1 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 26.1 / 1000 = 0.0261 mM; the exported value is 0.0261 mM. kcat: printed Table I cell 0.84 min^-1 (the Kcat column header prints 'min^-1'); 0.84 / 60 = 0.014 s^(-1); the exported value is 0.84 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 535 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 535 / 1000 = 0.535 s^(-1)*mM^(-1); the exported value is 32.183908045977006 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Caffeate': Km = 26.1 uM; Vmax = 240 pkat mg^-1; Kcat = 0.84 min^-1; printed Kenz = Kcat/Km = 535 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Caffeate' (catalog accession Q6ZAC1)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Ferulate'; column 'Km (uM)' = 6.9; column 'Vmax (pkat mg^-1)' = 590; column 'Kcat (min^-1)' = 2.04; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 4871.

normalized_value_unit_evidence: Km: printed Table I cell 6.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 6.9 / 1000 = 0.006900000000000001 mM; the exported value is 0.006900000000000001 mM. kcat: printed Table I cell 2.04 min^-1 (the Kcat column header prints 'min^-1'); 2.04 / 60 = 0.034 s^(-1); the exported value is 2.04 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 4871 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 4871 / 1000 = 4.871 s^(-1)*mM^(-1); the exported value is 295.65217391304344 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Ferulate': Km = 6.9 uM; Vmax = 590 pkat mg^-1; Kcat = 2.04 min^-1; printed Kenz = Kcat/Km = 4871 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Ferulate' (catalog accession Q6ZAC1)


substrate_name: sinapate

column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Sinapate'; column 'Km (uM)' = 58.9; column 'Vmax (pkat mg^-1)' = 920; column 'Kcat (min^-1)' = 3.18; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 899.

normalized_value_unit_evidence: Km: printed Table I cell 58.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 58.9 / 1000 = 0.0589 mM; the exported value is 0.0589 mM. kcat: printed Table I cell 3.18 min^-1 (the Kcat column header prints 'min^-1'); 3.18 / 60 = 0.053000000000000005 s^(-1); the exported value is 3.18 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 899 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 899 / 1000 = 0.899 s^(-1)*mM^(-1); the exported value is 53.98981324278438 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Sinapate': Km = 58.9 uM; Vmax = 920 pkat mg^-1; Kcat = 3.18 min^-1; printed Kenz = Kcat/Km = 899 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Sinapate' (catalog accession Q6ZAC1)

substrate: sinapate


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row 'Cinnamate'; column 'Km (uM)' = 9.4; column 'Vmax (pkat mg^-1)' = 100; column 'Kcat (min^-1)' = 0.37; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 663.

normalized_value_unit_evidence: Km: printed Table I cell 9.4 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 9.4 / 1000 = 0.0094 mM; the exported value is 0.0094 mM. kcat: printed Table I cell 0.37 min^-1 (the Kcat column header prints 'min^-1'); 0.37 / 60 = 0.006166666666666667 s^(-1); the exported value is 0.37 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 663 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 663 / 1000 = 0.663 s^(-1)*mM^(-1); the exported value is 39.36170212765957 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row 'Cinnamate': Km = 9.4 uM; Vmax = 100 pkat mg^-1; Kcat = 0.37 min^-1; printed Kenz = Kcat/Km = 663 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row 'Cinnamate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row '4-Coumarate'; column 'Km (uM)' = 11.9; column 'Vmax (pkat mg^-1)' = 130; column 'Kcat (min^-1)' = 0.49; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 681.

normalized_value_unit_evidence: Km: printed Table I cell 11.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 11.9 / 1000 = 0.0119 mM; the exported value is 0.0119 mM. kcat: printed Table I cell 0.49 min^-1 (the Kcat column header prints 'min^-1'); 0.49 / 60 = 0.008166666666666666 s^(-1); the exported value is 0.49 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 681 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 681 / 1000 = 0.681 s^(-1)*mM^(-1); the exported value is 41.17647058823529 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row '4-Coumarate': Km = 11.9 uM; Vmax = 130 pkat mg^-1; Kcat = 0.49 min^-1; printed Kenz = Kcat/Km = 681 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row '4-Coumarate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row 'Caffeate'; column 'Km (uM)' = 29.3; column 'Vmax (pkat mg^-1)' = 140; column 'Kcat (min^-1)' = 0.52; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 296.

normalized_value_unit_evidence: Km: printed Table I cell 29.3 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 29.3 / 1000 = 0.0293 mM; the exported value is 0.0293 mM. kcat: printed Table I cell 0.52 min^-1 (the Kcat column header prints 'min^-1'); 0.52 / 60 = 0.008666666666666666 s^(-1); the exported value is 0.52 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 296 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 296 / 1000 = 0.296 s^(-1)*mM^(-1); the exported value is 17.747440273037544 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row 'Caffeate': Km = 29.3 uM; Vmax = 140 pkat mg^-1; Kcat = 0.52 min^-1; printed Kenz = Kcat/Km = 296 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row 'Caffeate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row 'Ferulate'; column 'Km (uM)' = 8.3; column 'Vmax (pkat mg^-1)' = 110; column 'Kcat (min^-1)' = 0.41; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 824.

normalized_value_unit_evidence: Km: printed Table I cell 8.3 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 8.3 / 1000 = 0.0083 mM; the exported value is 0.0083 mM. kcat: printed Table I cell 0.41 min^-1 (the Kcat column header prints 'min^-1'); 0.41 / 60 = 0.006833333333333333 s^(-1); the exported value is 0.41 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 824 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 824 / 1000 = 0.824 s^(-1)*mM^(-1); the exported value is 49.39759036144578 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row 'Ferulate': Km = 8.3 uM; Vmax = 110 pkat mg^-1; Kcat = 0.41 min^-1; printed Kenz = Kcat/Km = 824 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row 'Ferulate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row 'Cinnamate'; column 'Km (uM)' = 21.7; column 'Vmax (pkat mg^-1)' = 299; column 'Kcat (min^-1)' = 1.13; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 867.

normalized_value_unit_evidence: Km: printed Table I cell 21.7 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 21.7 / 1000 = 0.0217 mM; the exported value is 0.0217 mM. kcat: printed Table I cell 1.13 min^-1 (the Kcat column header prints 'min^-1'); 1.13 / 60 = 0.01883333333333333 s^(-1); the exported value is 1.13 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 867 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 867 / 1000 = 0.867 s^(-1)*mM^(-1); the exported value is 52.073732718894 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row 'Cinnamate': Km = 21.7 uM; Vmax = 299 pkat mg^-1; Kcat = 1.13 min^-1; printed Kenz = Kcat/Km = 867 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row 'Cinnamate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row '4-Coumarate'; column 'Km (uM)' = 16.8; column 'Vmax (pkat mg^-1)' = 629; column 'Kcat (min^-1)' = 2.37; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 2351.

normalized_value_unit_evidence: Km: printed Table I cell 16.8 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 16.8 / 1000 = 0.016800000000000002 mM; the exported value is 0.016800000000000002 mM. kcat: printed Table I cell 2.37 min^-1 (the Kcat column header prints 'min^-1'); 2.37 / 60 = 0.0395 s^(-1); the exported value is 2.37 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 2351 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 2351 / 1000 = 2.351 s^(-1)*mM^(-1); the exported value is 141.07142857142856 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row '4-Coumarate': Km = 16.8 uM; Vmax = 629 pkat mg^-1; Kcat = 2.37 min^-1; printed Kenz = Kcat/Km = 2351 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row '4-Coumarate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row 'Caffeate'; column 'Km (uM)' = 27.6; column 'Vmax (pkat mg^-1)' = 708; column 'Kcat (min^-1)' = 2.67; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 1612.

normalized_value_unit_evidence: Km: printed Table I cell 27.6 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 27.6 / 1000 = 0.027600000000000003 mM; the exported value is 0.0216 mM. kcat: printed Table I cell 2.67 min^-1 (the Kcat column header prints 'min^-1'); 2.67 / 60 = 0.0445 s^(-1); the exported value is 2.67 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 1612 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 1612 / 1000 = 1.612 s^(-1)*mM^(-1); the exported value is 123.6111111111111 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row 'Caffeate': Km = 27.6 uM; Vmax = 708 pkat mg^-1; Kcat = 2.67 min^-1; printed Kenz = Kcat/Km = 1612 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row 'Caffeate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row 'Ferulate'; column 'Km (uM)' = 2.2; column 'Vmax (pkat mg^-1)' = 613; column 'Kcat (min^-1)' = 2.31; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 17295.

normalized_value_unit_evidence: Km: printed Table I cell 2.2 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 2.2 / 1000 = 0.0022 mM; the exported value is 0.0022 mM. kcat: printed Table I cell 2.31 min^-1 (the Kcat column header prints 'min^-1'); 2.31 / 60 = 0.0385 s^(-1); the exported value is 2.31 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 17295 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 17295 / 1000 = 17.295 s^(-1)*mM^(-1); the exported value is 1050.0 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row 'Ferulate': Km = 2.2 uM; Vmax = 613 pkat mg^-1; Kcat = 2.31 min^-1; printed Kenz = Kcat/Km = 17295 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row 'Ferulate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL4'; substrate row 'Cinnamate'; column 'Km (uM)' = 15.7; column 'Vmax (pkat mg^-1)' = 350; column 'Kcat (min^-1)' = 1.28; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 1361.

normalized_value_unit_evidence: Km: printed Table I cell 15.7 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 15.7 / 1000 = 0.0157 mM; the exported value is 0.0157 mM. kcat: printed Table I cell 1.28 min^-1 (the Kcat column header prints 'min^-1'); 1.28 / 60 = 0.021333333333333333 s^(-1); the exported value is 1.28 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 1361 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 1361 / 1000 = 1.361 s^(-1)*mM^(-1); the exported value is 81.52866242038218 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL4', substrate row 'Cinnamate': Km = 15.7 uM; Vmax = 350 pkat mg^-1; Kcat = 1.28 min^-1; printed Kenz = Kcat/Km = 1361 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL4', substrate row 'Cinnamate' (catalog accession Q67W82)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL4'; substrate row '4-Coumarate'; column 'Km (uM)' = 3.9; column 'Vmax (pkat mg^-1)' = 770; column 'Kcat (min^-1)' = 2.82; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 12176.

normalized_value_unit_evidence: Km: printed Table I cell 3.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 3.9 / 1000 = 0.0039 mM; the exported value is 0.0039 mM. kcat: printed Table I cell 2.82 min^-1 (the Kcat column header prints 'min^-1'); 2.82 / 60 = 0.047 s^(-1); the exported value is 2.82 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 12176 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 12176 / 1000 = 12.176 s^(-1)*mM^(-1); the exported value is 723.0769230769231 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL4', substrate row '4-Coumarate': Km = 3.9 uM; Vmax = 770 pkat mg^-1; Kcat = 2.82 min^-1; printed Kenz = Kcat/Km = 12176 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL4', substrate row '4-Coumarate' (catalog accession Q67W82)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL4'; substrate row 'Caffeate'; column 'Km (uM)' = 5.8; column 'Vmax (pkat mg^-1)' = 590; column 'Kcat (min^-1)' = 2.16; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 6206.

normalized_value_unit_evidence: Km: printed Table I cell 5.8 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 5.8 / 1000 = 0.0058 mM; the exported value is 0.0058 mM. kcat: printed Table I cell 2.16 min^-1 (the Kcat column header prints 'min^-1'); 2.16 / 60 = 0.036000000000000004 s^(-1); the exported value is 2.16 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 6206 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 6206 / 1000 = 6.206 s^(-1)*mM^(-1); the exported value is 372.4137931034483 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL4', substrate row 'Caffeate': Km = 5.8 uM; Vmax = 590 pkat mg^-1; Kcat = 2.16 min^-1; printed Kenz = Kcat/Km = 6206 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL4', substrate row 'Caffeate' (catalog accession Q67W82)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL4'; substrate row 'Ferulate'; column 'Km (uM)' = 4.6; column 'Vmax (pkat mg^-1)' = 520; column 'Kcat (min^-1)' = 1.92; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 6956.

normalized_value_unit_evidence: Km: printed Table I cell 4.6 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 4.6 / 1000 = 0.0046 mM; the exported value is 0.0046 mM. kcat: printed Table I cell 1.92 min^-1 (the Kcat column header prints 'min^-1'); 1.92 / 60 = 0.032 s^(-1); the exported value is 1.92 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 6956 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 6956 / 1000 = 6.956 s^(-1)*mM^(-1); the exported value is 417.39130434782606 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL4', substrate row 'Ferulate': Km = 4.6 uM; Vmax = 520 pkat mg^-1; Kcat = 1.92 min^-1; printed Kenz = Kcat/Km = 6956 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL4', substrate row 'Ferulate' (catalog accession Q67W82)


organism: Thermococcus kodakarensis

substrate_name: Isobutyrate

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

substrate: Isobutyrate


substrate_name: CoA

substrate: CoA


substrate_name: thioglycolate

smiles: O=C(O)CS

substrate: thioglycolate


organism: Arabidopsis thaliana

substrate_name: trans-cinnamate

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 't-Cinnamate': column 'K_m (uM)' = 112; column 'k_cat (s^-1)' = 0.7; column 'k_cat/K_m (s^-1 mM^-1)' = 6.

normalized_value_unit_evidence: K_m: printed Table 2 cell 112 uM; 1 uM is 0.001 mM, so 112 / 1000 = 0.112 mM, and the exported value is 0.112 mM. k_cat: printed Table 2 cell 0.7 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.7 s^(-1). k_cat/K_m: printed Table 2 cell 6 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 6.0 s^-1 mM^-1. Quotient disclosure for this row: 0.7 / 0.112 = 6.249999999999999 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 't-Cinnamate': K_m = 112 uM; k_cat = 0.7 s^-1; printed k_cat/K_m = 6 s^-1 mM^-1.

table_label: Table 2: Kinetic Properties of Recombinant At4g19010 (The Plant Cell 2014, volume 26, number 5, pages 1938-1948); printed column heads K_m (uM), k_cat (s^-1) and k_cat/K_m (s^-1 mM^-1)

substrate: trans-cinnamate


substrate_name: p-coumarate

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 'p-Coumarate': column 'K_m (uM)' = 125; column 'k_cat (s^-1)' = 2.1; column 'k_cat/K_m (s^-1 mM^-1)' = 17.

normalized_value_unit_evidence: K_m: printed Table 2 cell 125 uM; 1 uM is 0.001 mM, so 125 / 1000 = 0.125 mM, and the exported value is 0.125 mM. k_cat: printed Table 2 cell 2.1 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 2.1 s^(-1). k_cat/K_m: printed Table 2 cell 17 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 17.0 s^-1 mM^-1. Quotient disclosure for this row: 2.1 / 0.125 = 16.8 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 'p-Coumarate': K_m = 125 uM; k_cat = 2.1 s^-1; printed k_cat/K_m = 17 s^-1 mM^-1.

substrate: p-coumarate


column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 'Ferulate': column 'K_m (uM)' = 113; column 'k_cat (s^-1)' = 3.6; column 'k_cat/K_m (s^-1 mM^-1)' = 32.

normalized_value_unit_evidence: K_m: printed Table 2 cell 113 uM; 1 uM is 0.001 mM, so 113 / 1000 = 0.113 mM, and the exported value is 0.113 mM. k_cat: printed Table 2 cell 3.6 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 3.6 s^(-1). k_cat/K_m: printed Table 2 cell 32 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 32.0 s^-1 mM^-1. Quotient disclosure for this row: 3.6 / 0.113 = 31.858407079646017 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 'Ferulate': K_m = 113 uM; k_cat = 3.6 s^-1; printed k_cat/K_m = 32 s^-1 mM^-1.


column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 'Caffeate': column 'K_m (uM)' = 85; column 'k_cat (s^-1)' = 2.4; column 'k_cat/K_m (s^-1 mM^-1)' = 28.

normalized_value_unit_evidence: K_m: printed Table 2 cell 85 uM; 1 uM is 0.001 mM, so 85 / 1000 = 0.085 mM, and the exported value is 0.085 mM. k_cat: printed Table 2 cell 2.4 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 2.4 s^(-1). k_cat/K_m: printed Table 2 cell 28 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 28.0 s^-1 mM^-1. Quotient disclosure for this row: 2.4 / 0.085 = 28.235294117647054 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 'Caffeate': K_m = 85 uM; k_cat = 2.4 s^-1; printed k_cat/K_m = 28 s^-1 mM^-1.


column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row '4-Hydroxybenzoate': column 'K_m (uM)' = 67; column 'k_cat (s^-1)' = 0.01; column 'k_cat/K_m (s^-1 mM^-1)' = 0.15.

normalized_value_unit_evidence: K_m: printed Table 2 cell 67 uM; 1 uM is 0.001 mM, so 67 / 1000 = 0.067 mM, and the exported value is 0.067 mM. k_cat: printed Table 2 cell 0.01 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.01 s^(-1). k_cat/K_m: printed Table 2 cell 0.15 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 0.15 s^-1 mM^-1. Quotient disclosure for this row: 0.01 / 0.067 = 0.14925373134328357 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row '4-Hydroxybenzoate': K_m = 67 uM; k_cat = 0.01 s^-1; printed k_cat/K_m = 0.15 s^-1 mM^-1.


organism: Populus tomentosa

proof_lines: isoform 4CL3, pH and temperature not specified in the publication


proof_lines: isoform 4CL4, pH and temperature not specified in the publication


organism: Solanum lycopersicum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F269L/K415T with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q274H with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: phenylacetyl-CoA (at 80 degrees Celsius)

proof_lines: kcat is 115 sec(-1) for ADP. kcat is 21 sec(-1) for GDP. kcat is 117 sec(-1) for phosphate. kcat is 42 sec(-1) for acetyl-CoA. kcat is 8 sec(-1) for isobutyryl-CoA. kcat is 138 sec(-1) for phenylacetyl-CoA. kcat is 68 sec(-1) for ATP. kcat


substrate_name: ATP (at 80 degrees Celsius)

substrate: ATP (at 80 degrees Celsius)


substrate_name: GTP (at 80 degrees Celsius)

substrate: GTP (at 80 degrees Celsius)


substrate_name: CoA (at 80 degrees Celsius)

substrate: CoA (at 80 degrees Celsius)


substrate_name: acetate (at 80 degrees Celsius)

substrate: acetate (at 80 degrees Celsius)


substrate_name: isobutyrate (at 80 degrees Celsius)

substrate: isobutyrate (at 80 degrees Celsius)


substrate_name: indoleacetate (at 80 degrees Celsius)

substrate: indoleacetate (at 80 degrees Celsius)


substrate_name: phenylacetate (at 80 degrees Celsius)

substrate: phenylacetate (at 80 degrees Celsius)


substrate_name: ADP (at 80 degrees Celsius)

assay_conditions_summary: cofactor ADP

substrate: ADP (at 80 degrees Celsius)


substrate_name: GDP (at 80 degrees Celsius)

substrate: GDP (at 80 degrees Celsius)


substrate_name: phosphate (at 80 degrees Celsius)

substrate: phosphate (at 80 degrees Celsius)


substrate_name: acetyl-CoA (at 80 degrees Celsius)

substrate: acetyl-CoA (at 80 degrees Celsius)


substrate_name: isobutyryl-CoA (at 80 degrees Celsius)

substrate: isobutyryl-CoA (at 80 degrees Celsius)


substrate: phenylacetyl-CoA (at 80 degrees Celsius)


substrate_name: ADP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NAT4 and applied mutation signature H533Q to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block ADP, enzyme variant row His533Gln; column kcat (s-1) = 2.5; column Km (mM) = 1.28; column kcat/Km (mM-1 s-1) = 1.9.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.5 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 2.5 s^(-1). Km: printed Table 1 cell 1.28 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 1.28 mM. kcat/Km: printed Table 1 cell 1.9 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 1.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate ADP, enzyme variant row His533Gln, which is the H533Q variant this catalog row carries: kcat = 2.5 s-1; Km = 1.28 mM; printed kcat/Km = 1.9 mM-1 s-1.

substrate: ADP


substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NAT4 and applied mutation signature H533A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block Acetyl-CoA, enzyme variant row His533Ala; column kcat (s-1) = 2.7; column Km (mM) = 0.010; column kcat/Km (mM-1 s-1) = 266.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.7 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 2.7 s^(-1). Km: printed Table 1 cell 0.010 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.01 mM. kcat/Km: printed Table 1 cell 266 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 266.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate Acetyl-CoA, enzyme variant row His533Ala, which is the H533A variant this catalog row carries: kcat = 2.7 s-1; Km = 0.010 mM; printed kcat/Km = 266 mM-1 s-1.

substrate: acetyl-CoA


column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block ADP, enzyme variant row His533Ala; column kcat (s-1) = 2.8; column Km (mM) = 0.41; column kcat/Km (mM-1 s-1) = 6.9.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.8 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 2.8 s^(-1). Km: printed Table 1 cell 0.41 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.41 mM. kcat/Km: printed Table 1 cell 6.9 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 6.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate ADP, enzyme variant row His533Ala, which is the H533A variant this catalog row carries: kcat = 2.8 s-1; Km = 0.41 mM; printed kcat/Km = 6.9 mM-1 s-1.


substrate_name: phosphate

column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block Pi, enzyme variant row His533Lys; column kcat (s-1) = 3.1; column Km (mM) = 3.25; column kcat/Km (mM-1 s-1) = 0.97.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.1 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 3.1 s^(-1). Km: printed Table 1 cell 3.25 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 3.25 mM. kcat/Km: printed Table 1 cell 0.97 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 0.97 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate Pi, enzyme variant row His533Lys, which is the H533K variant this catalog row carries: kcat = 3.1 s-1; Km = 3.25 mM; printed kcat/Km = 0.97 mM-1 s-1.

substrate: phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H533K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H533K, pH and temperature not specified in the publication


substrate_name: acetate

column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block Acetate, enzyme variant row His533Ala; column kcat (s-1) = 3.3; column Km (mM) = 0.68; column kcat/Km (mM-1 s-1) = 4.8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.3 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 3.3 s^(-1). Km: printed Table 2 cell 0.68 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.68 mM. kcat/Km: printed Table 2 cell 4.8 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 4.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate Acetate, enzyme variant row His533Ala, which is the H533A variant this catalog row carries: kcat = 3.3 s-1; Km = 0.68 mM; printed kcat/Km = 4.8 mM-1 s-1.

substrate: acetate


substrate_name: ATP

column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block ATP, enzyme variant row His533Ala; column kcat (s-1) = 3.3; column Km (mM) = 2.2; column kcat/Km (mM-1 s-1) = 1.6.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.3 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 3.3 s^(-1). Km: printed Table 2 cell 2.2 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 2.2 mM. kcat/Km: printed Table 2 cell 1.6 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 1.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate ATP, enzyme variant row His533Ala, which is the H533A variant this catalog row carries: kcat = 3.3 s-1; Km = 2.2 mM; printed kcat/Km = 1.6 mM-1 s-1.

substrate: ATP


column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block Acetate, enzyme variant row His533Lys; column kcat (s-1) = 3.4; column Km (mM) = 0.84; column kcat/Km (mM-1 s-1) = 4.1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.4 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 3.4 s^(-1). Km: printed Table 2 cell 0.84 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.84 mM. kcat/Km: printed Table 2 cell 4.1 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 4.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate Acetate, enzyme variant row His533Lys, which is the H533K variant this catalog row carries: kcat = 3.4 s-1; Km = 0.84 mM; printed kcat/Km = 4.1 mM-1 s-1.


column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block ATP, enzyme variant row His533Lys; column kcat (s-1) = 3.7; column Km (mM) = 1.7; column kcat/Km (mM-1 s-1) = 2.4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.7 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 3.7 s^(-1). Km: printed Table 2 cell 1.7 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 1.7 mM. kcat/Km: printed Table 2 cell 2.4 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 2.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate ATP, enzyme variant row His533Lys, which is the H533K variant this catalog row carries: kcat = 3.7 s-1; Km = 1.7 mM; printed kcat/Km = 2.4 mM-1 s-1.


substrate_name: CoA

substrate: CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H533R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H533R, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NAT4 and applied mutation signature H533R to reconstruct the assayed variant sequence.

column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block ATP, enzyme variant row His533Arg; column kcat (s-1) = 6.6; column Km (mM) = 2.5; column kcat/Km (mM-1 s-1) = 2.7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 6.6 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 6.6 s^(-1). Km: printed Table 2 cell 2.5 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 2.5 mM. kcat/Km: printed Table 2 cell 2.7 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 2.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate ATP, enzyme variant row His533Arg, which is the H533R variant this catalog row carries: kcat = 6.6 s-1; Km = 2.5 mM; printed kcat/Km = 2.7 mM-1 s-1.


column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block Pi, enzyme variant row His533Arg; column kcat (s-1) = 14; column Km (mM) = 0.15; column kcat/Km (mM-1 s-1) = 95.

normalized_value_unit_evidence: kcat: printed Table 1 cell 14 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 14.0 s^(-1). Km: printed Table 1 cell 0.15 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.15 mM. kcat/Km: printed Table 1 cell 95 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 95.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate Pi, enzyme variant row His533Arg, which is the H533R variant this catalog row carries: kcat = 14 s-1; Km = 0.15 mM; printed kcat/Km = 95 mM-1 s-1.


column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block Acetyl-CoA, enzyme variant row His533Arg; column kcat (s-1) = 18; column Km (mM) = 0.016; column kcat/Km (mM-1 s-1) = 1115.

normalized_value_unit_evidence: kcat: printed Table 1 cell 18 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 18.0 s^(-1). Km: printed Table 1 cell 0.016 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.016 mM. kcat/Km: printed Table 1 cell 1115 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 1115.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate Acetyl-CoA, enzyme variant row His533Arg, which is the H533R variant this catalog row carries: kcat = 18 s-1; Km = 0.016 mM; printed kcat/Km = 1115 mM-1 s-1.


column_label: Table 1 (Apparent kinetic parameters of the His533 variants in the acetate-forming direction), varied-substrate block ADP, enzyme variant row His533Arg; column kcat (s-1) = 20; column Km (mM) = 0.64; column kcat/Km (mM-1 s-1) = 32.

normalized_value_unit_evidence: kcat: printed Table 1 cell 20 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 20.0 s^(-1). Km: printed Table 1 cell 0.64 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.64 mM. kcat/Km: printed Table 1 cell 32 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 32.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetate-forming direction, varied substrate ADP, enzyme variant row His533Arg, which is the H533R variant this catalog row carries: kcat = 20 s-1; Km = 0.64 mM; printed kcat/Km = 32 mM-1 s-1.


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

column_label: Table 1 | WT EhACD | varied substrate Acetyl-CoA | acetate-forming direction | kinetic-assay pH not reported; temperature not reported | kcat 111 ± 2 s^-1 | Km 0.043 ± 0.005 mM | kcat/Km 2600 ± 371 mM^-1 s^-1

normalized_value_unit_evidence: kcat=111 s^(-1); km=0.043 mM; kcat_over_km=2600 s^(-1)*mM^(-1). Each central value is copied from a separate printed paper cell; no scale conversion is needed.

row_label: WT EhACD / Acetyl-CoA

table_label: Table 1: apparent kinetic parameters of the His533 variants in the acetate-forming direction


column_label: Table 1 | WT EhACD | varied substrate Pi | acetate-forming direction | kinetic-assay pH not reported; temperature not reported | kcat 115 ± 8 s^-1 | Km 1.77 ± 0.18 mM | kcat/Km 65 ± 2 mM^-1 s^-1

normalized_value_unit_evidence: kcat=115 s^(-1); km=1.77 mM; kcat_over_km=65 s^(-1)*mM^(-1). Each central value is copied from a separate printed paper cell; no scale conversion is needed.

row_label: WT EhACD / Pi


column_label: Table 1 | WT EhACD | varied substrate ADP | acetate-forming direction | kinetic-assay pH not reported; temperature not reported | kcat 138 ± 1 s^-1 | Km 1.56 ± 0.15 mM | kcat/Km 89 ± 8 mM^-1 s^-1

normalized_value_unit_evidence: kcat=138 s^(-1); km=1.56 mM; kcat_over_km=89 s^(-1)*mM^(-1). Each central value is copied from a separate printed paper cell; no scale conversion is needed.

row_label: WT EhACD / ADP