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


enzyme_display_name: acetate--CoA ligase

substrate_name: acetate

source_db: brenda

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

row_label: acetate in ATP-CoA-acetate Km sentence

data_origin: experimental

enzyme: acetate--CoA ligase

substrate: acetate

status: verified

source: brenda


substrate_name: ATP

row_label: ATP in ATP-CoA-acetate Km sentence

substrate: ATP


organism: Ovis aries

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

assay_conditions_summary: cofactor ATP


substrate_name: Butyrate

smiles: CCCC(=O)[O-]

substrate: Butyrate


substrate_name: propanoate

substrate: propanoate


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

organism: Saccharomyces cerevisiae

substrate_name: CoA

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

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

substrate: CoA


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

verification_status: unverified

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

assay_conditions_summary: pH 8

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

substrate: oleate

status: unverified


enzyme_display_name: medium-chain acyl-CoA ligase

organism: Sus scrofa

substrate_name: Octanoate

smiles: CCCCCCCC(=O)[O-]

assay_conditions_summary: cofactor CoA

enzyme: medium-chain acyl-CoA ligase

substrate: Octanoate


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


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

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

mutation_type: substitution

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

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitate


organism: Bos taurus

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+


proof_lines: synthesis of adenosine 5?-tetraphosphate


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: tripolyphosphate

substrate: tripolyphosphate


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

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

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


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


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

organism: Rattus norvegicus

substrate_name: ATP

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

substrate: ATP


organism: Glycine max

proof_lines:
immobilized enzyme
soluble enzyme


organism: Methanothrix soehngenii


substrate_name: acetate

substrate: acetate


substrate_name: propanoate

substrate: propanoate


substrate_name: fluoroacetate

substrate: fluoroacetate


organism: Homo sapiens

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


organism: Caulobacter vibrioides

substrate_name: octadecanoate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: octadecanoate


substrate_name: CoA

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: CoA


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_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q941M3

substrate: cinnamate

source: skid


substrate_name: ferulate

substrate: ferulate


substrate_name: caffeate

substrate: caffeate


enzyme_display_name: 6-carboxyhexanoate-CoA ligase

organism: Ectopseudomonas mendocina

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

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

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

source_db: oed

assay_conditions_summary: pH 7.8; 295.15 K; cofactor CoA

source: oed


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

substrate: oleate


substrate_name: palmitate

substrate: palmitate


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

assay_conditions_summary: cofactor 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

assay_conditions_summary: cofactor CoA

substrate: CoA


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


verification_status: corrected

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)

status: corrected


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)


kcat_over_km_origin: calculated

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

source_db: uniprot

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)

source: uniprot


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.


sequence_source: multiple

source_databases_merged: brenda uniprot


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


column_label: Table 2 | WT EhACD | varied substrate Acetate | acetyl-CoA-forming direction | kinetic-assay pH not reported; temperature not reported | kcat 233 ± 2.7 s^-1 | Km 14 ± 0.61 mM | kcat/Km 16 ± 1 mM^-1 s^-1

normalized_value_unit_evidence: kcat=233 s^(-1); km=14 mM; kcat_over_km=16 s^(-1)*mM^(-1). Each central value is copied from a separate printed paper cell; no scale conversion is needed.

row_label: WT EhACD / Acetate

table_label: Table 2: apparent kinetic parameters of the His533 variants in the acetyl-CoA-forming direction


column_label: Table 2 | WT EhACD | varied substrate ATP | acetyl-CoA-forming direction | kinetic-assay pH not reported; temperature not reported | kcat 320 ± 4.4 s^-1 | Km 12 ± 0.4 mM | kcat/Km 27 ± 1 mM^-1 s^-1

normalized_value_unit_evidence: kcat=320 s^(-1); km=12 mM; kcat_over_km=27 s^(-1)*mM^(-1). Each central value is copied from a separate printed paper cell; no scale conversion is needed.

row_label: WT EhACD / ATP


column_label: Table 2 (Apparent kinetic parameters of the His533 variants in the acetyl-CoA forming direction), varied-substrate block CoA, enzyme row WT; column kcat (s-1) = 328; column Km (mM) = 0.20; column kcat/Km (mM-1 s-1) = 1100.

normalized_value_unit_evidence: kcat: printed Table 2 cell 328 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 328.0 s^(-1). Km: printed Table 2 cell 0.20 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.2 mM. kcat/Km: printed Table 2 cell 1100 mM-1 s-1; the printed efficiency column is already per mM per second, so no unit conversion applies and the paper value is 1100.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acetyl-CoA forming direction, varied substrate CoA, enzyme row WT: kcat = 328 s-1; Km = 0.20 mM; printed kcat/Km = 1100 mM-1 s-1.


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

proof_lines: kcat is 203 sec(-1) for ADP. kcat is 411 sec(-1) for GDP. kcat is 182 sec(-1) for phosphate. kcat is 157 sec(-1) for acetyl-CoA. kcat is 121 sec(-1) for isobutyryl-CoA. kcat is 82 sec(-1) for ATP. kcat is 121 sec(-1) for GTP. kcat is 73 sec


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: ADP (at 80 degrees Celsius)


substrate: GDP (at 80 degrees Celsius)


substrate: phosphate (at 80 degrees Celsius)


substrate: acetyl-CoA (at 80 degrees Celsius)


substrate: isobutyryl-CoA (at 80 degrees Celsius)


organism: Physcomitrium patens

column_label: Table 2; row label: 4-coumarate; column labels: Km (uM) under Pp4CL1, specific activity relative Vmax under Pp4CL1, and relative Vmax/Km under Pp4CL1; raw Km 4 uM; normalized Km 0.004 mM; accession identity B7SB99 maps to Pp4CL1 via UniProt EMBL accession in the paper.

normalized_value_unit_evidence: Km=0.004 mM after converting 4 uM from Table 2.

raw_value_unit_evidence: Table 2; substrate 4-coumarate; Pp4CL1 Km = 4 uM; relative Vmax = 100; relative Vmax/Km = 25.97 uM^-1.

row_label: Substrate row: 4-coumarate; isoform/column block: Pp4CL1 (B7SB99); metric column: Km (uM); relative Vmax and relative Vmax/Km columns also present.

table_label: Table 2. Kinetic properties of P. patens Pp4CL1-3 in vitro


column_label: Table 2; row label: 4-coumarate; column labels: Km (uM) under Pp4CL2, specific activity relative Vmax under Pp4CL2, and relative Vmax/Km under Pp4CL2; raw Km 16 uM; normalized Km 0.016 mM; accession identity B7SBA0 maps to Pp4CL2 via UniProt EMBL accession in the paper.

normalized_value_unit_evidence: Km=0.016 mM after converting 16 uM from Table 2.

raw_value_unit_evidence: Table 2; substrate 4-coumarate; Pp4CL2 Km = 16 uM; relative Vmax = 100; relative Vmax/Km = 6.25 uM^-1.

row_label: Substrate row: 4-coumarate; isoform/column block: Pp4CL2 (B7SBA0); metric column: Km (uM); relative Vmax and relative Vmax/Km columns also present.


substrate_name: caffeate

column_label: Table 2; row label: caffeate; column labels: Km (uM) under Pp4CL1, specific activity relative Vmax under Pp4CL1, and relative Vmax/Km under Pp4CL1; raw Km 25 uM; normalized Km 0.025 mM; accession identity B7SB99 maps to Pp4CL1 via UniProt EMBL accession in the paper.

normalized_value_unit_evidence: Km=0.025 mM after converting 25 uM from Table 2.

raw_value_unit_evidence: Table 2; substrate caffeate; Pp4CL1 Km = 25 uM; relative Vmax = 24; relative Vmax/Km = 0.9 uM^-1.

row_label: Substrate row: caffeate; isoform/column block: Pp4CL1 (B7SB99); metric column: Km (uM); relative Vmax and relative Vmax/Km columns also present.

substrate: caffeate


column_label: Table 2; row label: caffeate; column labels: Km (uM) under Pp4CL2, specific activity relative Vmax under Pp4CL2, and relative Vmax/Km under Pp4CL2; raw Km 45 uM; normalized Km 0.045 mM; accession identity B7SBA0 maps to Pp4CL2 via UniProt EMBL accession in the paper.

normalized_value_unit_evidence: Km=0.045 mM after converting 45 uM from Table 2.

raw_value_unit_evidence: Table 2; substrate caffeate; Pp4CL2 Km = 45 uM; relative Vmax = 46; relative Vmax/Km = 1.0 uM^-1.

row_label: Substrate row: caffeate; isoform/column block: Pp4CL2 (B7SBA0); metric column: Km (uM); relative Vmax and relative Vmax/Km columns also present.


substrate_name: cinnamate

column_label: Table 2; row label: cinnamate; column labels: Km (uM) under Pp4CL1, specific activity relative Vmax under Pp4CL1, and relative Vmax/Km under Pp4CL1; raw Km 50 uM; normalized Km 0.05 mM; accession identity B7SB99 maps to Pp4CL1 via UniProt EMBL accession in the paper.

normalized_value_unit_evidence: Km=0.05 mM after converting 50 uM from Table 2.

raw_value_unit_evidence: Table 2; substrate cinnamate; Pp4CL1 Km = 50 uM; relative Vmax = 61; relative Vmax/Km = 1.19 uM^-1.

row_label: Substrate row: cinnamate; isoform/column block: Pp4CL1 (B7SB99); metric column: Km (uM); relative Vmax and relative Vmax/Km columns also present.

substrate: cinnamate


column_label: Table 2; row label: cinnamate; column labels: Km (uM) under Pp4CL2, specific activity relative Vmax under Pp4CL2, and relative Vmax/Km under Pp4CL2; raw Km 66 uM; normalized Km 0.066 mM; accession identity B7SBA0 maps to Pp4CL2 via UniProt EMBL accession in the paper.

normalized_value_unit_evidence: Km=0.066 mM after converting 66 uM from Table 2.

raw_value_unit_evidence: Table 2; substrate cinnamate; Pp4CL2 Km = 66 uM; relative Vmax = 59; relative Vmax/Km = 0.89 uM^-1.

row_label: Substrate row: cinnamate; isoform/column block: Pp4CL2 (B7SBA0); metric column: Km (uM); relative Vmax and relative Vmax/Km columns also present.


substrate_name: ferulate

column_label: Table 2; row label: ferulate; column labels: Km (uM) under Pp4CL2, specific activity relative Vmax under Pp4CL2, and relative Vmax/Km under Pp4CL2; raw Km 73 uM; normalized Km 0.073 mM; accession identity B7SBA0 maps to Pp4CL2 via UniProt EMBL accession in the paper.

normalized_value_unit_evidence: Km=0.073 mM after converting 73 uM from Table 2.

raw_value_unit_evidence: Table 2; substrate ferulate; Pp4CL2 Km = 73 uM; relative Vmax = 108; relative Vmax/Km = 1.4 uM^-1.

row_label: Substrate row: ferulate; isoform/column block: Pp4CL2 (B7SBA0); metric column: Km (uM); relative Vmax and relative Vmax/Km columns also present.

substrate: ferulate


column_label: Table 2; row label: ferulate; column labels: Km (uM) under Pp4CL1, specific activity relative Vmax under Pp4CL1, and relative Vmax/Km under Pp4CL1; raw Km 187 uM; normalized Km 0.187 mM; accession identity B7SB99 maps to Pp4CL1 via UniProt EMBL accession in the paper.

normalized_value_unit_evidence: Km=0.187 mM after converting 187 uM from Table 2.

raw_value_unit_evidence: Table 2; substrate ferulate; Pp4CL1 Km = 187 uM; relative Vmax = 114; relative Vmax/Km = 0.61 uM^-1.

row_label: Substrate row: ferulate; isoform/column block: Pp4CL1 (B7SB99); metric column: Km (uM); relative Vmax and relative Vmax/Km columns also present.


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

substrate_name: phenylacetyl-CoA

proof_lines: kcat is 2.3 sec(-1) for phenylacetyl-CoA. kcat is 1.84 sec(-1) for acetate. kcat is 3.45 sec(-1) for indole-3-acetate. kcat is 3 sec(-1) for phenylacetate. kcat is 3 sec(-1) for ATP. kcat is 2.9 sec(-1) for CoA.

substrate: phenylacetyl-CoA


substrate: acetate


substrate_name: phenylacetate

substrate: phenylacetate


substrate: ATP


substrate: CoA


proof_lines: kcat is 95 sec(-1) for acetyl-CoA. kcat is 70 sec(-1) for ADP. kcat is 58 sec(-1) for phosphate. kcat is 138 sec(-1) for acetate. kcat is 11.5 sec(-1) for phenylacetate. kcat is 150 sec(-1) for ATP. kcat is 110 sec(-1) for CoA.

substrate: acetyl-CoA


substrate: ADP


substrate: phosphate


organism: Medicago truncatula

substrate_name: oxalate

assay_conditions_summary: pH 8

substrate: oxalate


substrate_name: 4-Coumarate; Coenzyme A; ATP

substrate: 4-Coumarate; Coenzyme A; ATP


substrate_name: ATP; 4-Coumarate; Coenzyme A

substrate: ATP; 4-Coumarate; Coenzyme A


substrate_name: ATP; Coenzyme A; 3,4-Dihydroxy-trans-cinnamate


substrate_name: Coenzyme A; ATP; 4-Coumarate

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

substrate: Coenzyme A; ATP; 4-Coumarate


organism: Archaeoglobus fulgidus

substrate_name: Phosphate; ADP; Acetyl-CoA

substrate: Phosphate; ADP; Acetyl-CoA


organism: Petunia hybrida

substrate_name: trans-cinnamic acid

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-CNL', substrate (acid) row 't-Cinnamic'; column 'Km (uM)' prints 285.7; column 'Vmax (pkat mg^-1)' prints 7401.7; column 'kcat (s^-1)' prints 0.472; column 'kcat/Km (mM^-1 s^-1)' prints 1.82; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.472 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.472 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 285.7 uM; 285.7 / 1000 = 0.2857 mM; the exported value is 0.2857 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 1.82 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 1.82 s^-1 mM^-1. The exported ratio 1.6520826041302064 s^(-1)*mM^(-1) is the quotient 0.472 / 0.2857 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 1.82 and kcat and Km are unchanged.

substrate: trans-cinnamic acid


substrate_name: 4-coumaric acid

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-CNL', substrate (acid) row '4-Coumaric'; column 'Km (uM)' prints 550.4; column 'Vmax (pkat mg^-1)' prints 3890.7; column 'kcat (s^-1)' prints 0.248; column 'kcat/Km (mM^-1 s^-1)' prints 0.512; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.248 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.248 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 550.4 uM; 550.4 / 1000 = 0.5504 mM; the exported value is 0.5504 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 0.512 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 0.512 s^-1 mM^-1. The exported ratio 0.45058139534883723 s^(-1)*mM^(-1) is the quotient 0.248 / 0.5504 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 0.512 and kcat and Km are unchanged.

substrate: 4-coumaric acid


substrate_name: caffeic acid

column_label: Table 1. Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins. Enzyme block 'Ph-CNL', substrate row 'Caffeic'; column 'Km (uM)' = 1042.4; column 'kcat (s^-1)' = 0.238; column 'kcat/Km (mM^-1 s^-1)' = 0.232.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.238 s^-1; the table already reports kcat in s^-1, so no conversion is applied and the value is 0.238 s^(-1). Km: printed Table 1 cell 1042.4 uM; converted at 1 uM = 0.001 mM the value is 1.0424 mM. kcat/Km: the paper prints its own Table 1 cell 0.232 mM^-1 s^-1; the table already reports kcat/Km in mM^-1 s^-1, so no conversion is applied and the printed cell is 0.232 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme block 'Ph-CNL', substrate row 'Caffeic': Km = 1042.4 uM; kcat = 0.238 s^-1; printed kcat/Km = 0.232 mM^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription, enzyme block 'Ph-CNL', substrate row 'Caffeic'

substrate: caffeic acid


substrate_name: CoA

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-CNL', substrate (acid) row 'CoA'; column 'Km (uM)' prints 775.2; column 'Vmax (pkat mg^-1)' prints 7179.7; column 'kcat (s^-1)' prints 0.458; column 'kcat/Km (mM^-1 s^-1)' prints 0.607; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.458 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.458 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 775.2 uM; 775.2 / 1000 = 0.7752 mM; the exported value is 0.7752000000000001 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 0.607 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 0.607 s^-1 mM^-1. The exported ratio 0.5908152734778122 s^(-1)*mM^(-1) is the quotient 0.458 / 0.7752000000000001 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 0.607 and kcat and Km are unchanged.


assay_conditions_summary: pH 8.5; buffer 50 mM Tris/K phosphate/Na citrate; cofactor CoA

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 't-Cinnamic'; column 'Km (uM)' prints 149.4; column 'Vmax (pkat mg^-1)' prints 14680; column 'kcat (s^-1)' prints 0.847; column 'kcat/Km (mM^-1 s^-1)' prints 6.43; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.847 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.847 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 149.4 uM; 149.4 / 1000 = 0.1494 mM; the exported value is 0.1494 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 6.43 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 6.43 s^-1 mM^-1. The exported ratio 5.669344042838018 s^(-1)*mM^(-1) is the quotient 0.847 / 0.1494 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 6.43 and kcat and Km are unchanged.


column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row '4-Coumaric'; column 'Km (uM)' prints 16.4; column 'Vmax (pkat mg^-1)' prints 25797; column 'kcat (s^-1)' prints 1.488; column 'kcat/Km (mM^-1 s^-1)' prints 84.32; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.488 s^-1; already in s^-1, no unit conversion applies; the exported value is 1.488 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 16.4 uM; 16.4 / 1000 = 0.0164 mM; the exported value is 0.016399999999999998 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 84.32 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 84.32 s^-1 mM^-1. The exported ratio 90.73170731707319 s^(-1)*mM^(-1) is the quotient 1.488 / 0.016399999999999998 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 84.32 and kcat and Km are unchanged.


column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 'Caffeic'; column 'Km (uM)' prints 47.8; column 'Vmax (pkat mg^-1)' prints 63200; column 'kcat (s^-1)' prints 3.645; column 'kcat/Km (mM^-1 s^-1)' prints 70.14; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.645 s^-1; already in s^-1, no unit conversion applies; the exported value is 3.645 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 47.8 uM; 47.8 / 1000 = 0.0478 mM; the exported value is 0.047799999999999995 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 70.14 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 70.14 s^-1 mM^-1. The exported ratio 76.25523012552301 s^(-1)*mM^(-1) is the quotient 3.645 / 0.047799999999999995 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 70.14 and kcat and Km are unchanged.


substrate_name: ferulic acid

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 'Ferulic'; column 'Km (uM)' prints 15.2; column 'Vmax (pkat mg^-1)' prints 41377; column 'kcat (s^-1)' prints 2.39; column 'kcat/Km (mM^-1 s^-1)' prints 145.37; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.39 s^-1; already in s^-1, no unit conversion applies; the exported value is 2.39 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 15.2 uM; 15.2 / 1000 = 0.0152 mM; the exported value is 0.0152 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 145.37 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 145.37 s^-1 mM^-1. The exported ratio 157.23684210526318 s^(-1)*mM^(-1) is the quotient 2.39 / 0.0152 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 145.37 and kcat and Km are unchanged.

substrate: ferulic acid


substrate_name: benzoic acid

proof_lines: kcat is 0.847 sec(-1) with trans-cinnamic acid as substrate (PubMed:22649270). kcat is 1.488 sec(-1) with 4-coumaric acid as substrate (PubMed:22649270). kcat is 3.645 sec(-1) with caffeic acid as substrate (PubMed:22649270). kcat is 2.39 s

substrate: benzoic acid


column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 'CoA'; column 'Km (uM)' prints 9.9; column 'Vmax (pkat mg^-1)' prints 8451; column 'kcat (s^-1)' prints 0.487; column 'kcat/Km (mM^-1 s^-1)' prints 49.46; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.487 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.487 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 9.9 uM; 9.9 / 1000 = 0.0099 mM; the exported value is 0.0099 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 49.46 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 49.46 s^-1 mM^-1. The exported ratio 49.19191919191918 s^(-1)*mM^(-1) is the quotient 0.487 / 0.0099 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 49.46 and kcat and Km are unchanged.


organism: Methanocaldococcus jannaschii

substrate_name: Acetyl-CoA; Phosphate; ADP

substrate: Acetyl-CoA; Phosphate; ADP


organism: Rattus norvegicus

substrate_name: 3alpha,7alpha,12alpha-Trihydroxy-5beta-cholestanoate; ATP; Coenzyme A