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


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

organism: Entamoeba histolytica

substrate_name: ATP

source_db: brenda

verification_status: corrected

ki_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.

assay_conditions_summary: cofactor ATP

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

data_origin: experimental

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

substrate: ATP

status: corrected

source: brenda


substrate_name: CoA

assay_conditions_summary: cofactor CoA

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.

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)

substrate: CoA


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

substrate_name: ADP (at 80 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

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

assay_conditions_summary: cofactor ADP

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: ADP (at 80 degrees Celsius)

source: uniprot


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_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)


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


enzyme_display_name: 4-coumarate--CoA ligase

organism: Physcomitrium patens

verification_status: verified

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

enzyme: 4-coumarate--CoA ligase

status: verified


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_name: acetate

substrate: acetate


substrate_name: phenylacetate

substrate: phenylacetate


substrate_name: ATP

substrate: ATP


substrate_name: CoA

substrate: CoA


substrate_name: acetyl-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_name: ADP

substrate: ADP


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: oxalate--CoA ligase

organism: Medicago truncatula

substrate_name: oxalate

assay_conditions_summary: pH 8

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

enzyme: oxalate--CoA ligase

substrate: oxalate


organism: Arabidopsis thaliana

substrate_name: 4-Coumarate; Coenzyme A; ATP

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

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

assay_conditions_summary: pH 8; 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-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


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


enzyme_display_name: cholate--CoA ligase

organism: Rattus norvegicus

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

enzyme: cholate--CoA ligase


organism: Nicotiana tabacum

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O24146 and applied mutation signature T193A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

column_label: Table 3: Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid (Structure 2015, volume 23, issue 11, pages 2032-2042); printed column heads KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 3, variant row T193A; column KM (uM) = 2.9; column kcat (s^-1) = 0.996; column kcat/KM (M^-1 s^-1) = 3.434 x 10^5. captured primary segment: T193A | 4-Coumaric Acid | Km 2.9 uM | kcat 0.996 s^-1 | kcat/Km 3.434 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 cell 2.9 uM; 2.9 / 1000 = 0.0029 mM. kcat: printed Table 3 cell 0.996 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 0.996 s^(-1). kcat/Km: printed Table 3 cell 3.434 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 343.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.996 / 0.0029 = 343.448275862069 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row T193A: KM = 2.9 uM; kcat = 0.996 s^-1; printed kcat/KM = 3.434 x 10^5 M^-1 s^-1.

row_label: Table 3, variant row T193A


substrate_name: sinapinate

source_db: skid

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

sequence_source: multiple

proof_lines: kcat is 3.978 sec(-1) with (E)-4-coumarate as substrate (PubMed:26412334). kcat is 2.652 sec(-1) with (E)-caffeate as substrate (PubMed:26412334). kcat is 3.576 sec(-1) with (E)-ferulate as substrate (PubMed:26412334). kcat is 0.018 sec(-1)

source_databases_merged: skid uniprot

substrate: sinapinate

source: skid


substrate_name: caffeate

column_label: Table 2: Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates (Structure 2015, volume 23, issue 11, pages 2032-2042); printed column heads KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, substrate row Caffeic Acid; column KM (uM) = 1.0; column kcat (s^-1) = 2.652; column kcat/KM (M^-1 s^-1) = 2.652 x 10^6. captured primary segment: Nt4CL2 | Caffeic Acid | Km 1.0 uM | kcat 2.652 s^-1 | kcat/Km 2.652 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 1.0 uM; 1.0 / 1000 = 0.001 mM. kcat: printed Table 2 cell 2.652 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 2.652 s^(-1). kcat/Km: printed Table 2 cell 2.652 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 2652.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.652 / 0.001 = 2652.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row Caffeic Acid: KM = 1.0 uM; kcat = 2.652 s^-1; printed kcat/KM = 2.652 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row Caffeic Acid

substrate: caffeate


substrate_name: ferulate

column_label: Table 2: Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates (Structure 2015, volume 23, issue 11, pages 2032-2042); printed column heads KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, substrate row Ferulic Acid; column KM (uM) = 2.9; column kcat (s^-1) = 3.576; column kcat/KM (M^-1 s^-1) = 1.233 x 10^6. captured primary segment: Nt4CL2 | Ferulic Acid | Km 2.9 uM | kcat 3.576 s^-1 | kcat/Km 1.233 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 2.9 uM; 2.9 / 1000 = 0.0029 mM. kcat: printed Table 2 cell 3.576 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 3.576 s^(-1). kcat/Km: printed Table 2 cell 1.233 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 1233.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.576 / 0.0029 = 1233.103448275862 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row Ferulic Acid: KM = 2.9 uM; kcat = 3.576 s^-1; printed kcat/KM = 1.233 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row Ferulic Acid

substrate: ferulate


organism: Anthoceros agrestis

substrate_name: isoferulate

kcat_over_km_origin: calculated

proof_lines:
isoform 4CL_1, at pH 7.0 and 40°C
isoform 4CL_2, at pH 7.0 and 40°C

substrate: isoferulate


substrate_name: CoA

assay_conditions_summary: pH 7; 313.15 K; cofactor CoA

substrate: CoA


substrate_name: cinnamate

assay_conditions_summary: pH 7; cofactor ATP

column_label: Table 1 Kinetic data for Aa4CL_1 (a) and Aa4CL_2 (b). Table 1 panel (b), substrate row 'Cinnamic acid', enzyme column Aa4CL_2; column 'Km (uM)' = 216.7; column 'Kcat (1/s)' = 1.8; column 'kcat/Km (1/s mM)' = 8.1.

normalized_value_unit_evidence: Km: printed cell 216.7 uM; 216.7 / 1000 = 0.2167 mM; the exported value is 0.2167 mM. kcat: printed cell 1.8 in the column headed 'Kcat (1/s)'; 1/s is s^(-1), no conversion; the exported value is 1.8 s^(-1). kcat/Km: printed cell 8.1 in the column headed 'kcat/Km (1/s mM)'; 1/s mM is s^(-1)*mM^(-1), no conversion; the exported value is 8.306414397784955 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1 panel (b), substrate row 'Cinnamic acid', enzyme column Aa4CL_2: Km = 216.7 uM; Kcat = 1.8 1/s; printed kcat/Km = 8.1 1/s mM.

substrate: cinnamate


substrate_name: ATP

assay_conditions_summary: pH 7; 313.15 K; cofactor ATP

substrate: ATP


organism: Plagiochasma appendiculatum


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M247Y/A251S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M247Y/A251S, at pH 7.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M247Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A251S to reconstruct the assayed variant sequence.


organism: Oryza sativa subsp. japonica

substrate_name: Unknown

km_display: Not reported

proof_lines: kcat is 0.37 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 0.49 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 0.52 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 0.41 min(-1) with ferulate

substrate: Unknown


proof_lines: kcat is 1.02 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 2.88 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 0.84 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 2.04 min(-1) with ferulate


proof_lines: kcat is 10.92 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 17.1 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 15.3 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 17.94 min(-1) with ferulat


proof_lines: kcat is 1.28 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 2.82 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 2.16 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 1.92 min(-1) with ferulate


proof_lines: kcat is 1.13 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 2.37 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 2.67 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 2.31 min(-1) with ferulate


substrate_name: adenosine 5'-tetraphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M293P/K320L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: reverse reaction, M293P/K320L mutant enzyme, pH 7.0, 30°C

substrate: adenosine 5'-tetraphosphate


organism: Glycine max


substrate_name: phosphate

assay_conditions_summary: pH 7.3; cofactor ATP

proof_lines: with propionyl-CoA as cosubstrate, at pH 7.3 and 37°C

proof_lines: with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C

substrate: phosphate


substrate_name: ADP

substrate: ADP


substrate_name: GDP

assay_conditions_summary: pH 7.3; 310.15 K; cofactor CoA

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, acetyl-CoA as acyl substrate, varied-substrate row 'GDP'; column 'Km (mM)' = 1.9 ± 0.14; column 'kcat (s^-1)' = 170 ± 5.2; column 'kcat/Km (s^-1 mM^-1)' = 90 ± 8.3. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.9 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.9 mM; the exported value is 1.9 mM. kcat: printed Table 1 cell 170 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 170.0 s^(-1); the exported value is 170.0 s^(-1). kcat/Km: printed Table 1 cell 90 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 90.0 s^(-1)*mM^(-1); the exported value is 89.47368421052632 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate GDP: Km = 1.9 ± 0.14 mM; kcat = 170 ± 5.2 s^-1; printed kcat/Km = 90 ± 8.3 s^-1 mM^-1.

table_label: Table 1: Apparent kinetic parameters for EhACD in each direction of the reaction (Eukaryotic Cell 2014, volume 13, number 12, page 1533)

substrate: GDP


substrate_name: GTP

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetyl-CoA-forming direction, acetate as acyl substrate, varied-substrate row 'GTP'; column 'Km (mM)' = 10 ± 0.1; column 'kcat (s^-1)' = 180 ± 1.6; column 'kcat/Km (s^-1 mM^-1)' = 18 ± 0.1. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 10 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 10.0 mM; the exported value is 10.0 mM. kcat: printed Table 1 cell 180 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 180.0 s^(-1); the exported value is 180.0 s^(-1). kcat/Km: printed Table 1 cell 18 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 18.0 s^(-1)*mM^(-1); the exported value is 18.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetyl-CoA-forming direction, acetate as acyl substrate, varied substrate GTP: Km = 10 ± 0.1 mM; kcat = 180 ± 1.6 s^-1; printed kcat/Km = 18 ± 0.1 s^-1 mM^-1.

substrate: GTP


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

proof_lines:
pH 7.0, 37°C, recombinant enzyme
at pH 6.0 and 37°C
at pH 7.0 and 37°C

substrate: acetyl-CoA


substrate_name: acetate

proof_lines:
at pH 6.0 and 37°C
pH 6.0, 37°C, recombinant enzyme
at pH 7.0 and 37°C

substrate: acetate


assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

proof_lines: with propionate as cosubstrate, at pH 7.3 and 37°C

proof_lines: with acetate as cosubstrate, at pH 7.3 and 37°C


proof_lines:
M293P/K320L mutant enzyme
M293P/K320L mutant enzyme, pH 7.0, 30°C


proof_lines: kcat is 0.472 sec(-1) with trans-cinnamic acid as substrate (PubMed:22649270). kcat is 0.248 sec(-1) with 4-coumaric acid as substrate (PubMed:22649270). kcat is 0.238 sec(-1) with caffeic acid as substrate (PubMed:22649270). kcat is 0.458


organism: Homo sapiens


enzyme_display_name: 6-carboxyhexanoate--CoA ligase

organism: Bacillus subtilis

substrate_name: Octanoate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y211F to reconstruct the assayed variant sequence.

smiles: CCCCCCCC(=O)[O-]

proof_lines: mutant Y211F, pH and temperature not specified in the publication

enzyme: 6-carboxyhexanoate--CoA ligase

substrate: Octanoate


substrate_name: Heptanoate

smiles: CCCCCCC(=O)[O-]

substrate: Heptanoate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: malate--CoA ligase

organism: Sus scrofa

enzyme: malate--CoA ligase


substrate_name: tetradecanoate

smiles: CCCCCCCCCCCCCC(=O)[O-]

proof_lines: kcat is 0.43 sec(-1) with tetradecanoate as substrate (PubMed:18267944). kcat is 0.7 sec(-1) with trans-cinnamate as substrate (PubMed:24838974). kcat is 2.1 sec(-1) with p-coumarate as substrate (PubMed:24838974). kcat is 3.6 sec(-1) with

substrate: tetradecanoate


organism: Entamoeba histolytica

substrate_name: propionyl-CoA

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ADP

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, propionyl-CoA as acyl substrate, varied-substrate row 'Propionyl-CoA'; column 'Km (mM)' = 0.032 ± 0.002; column 'kcat (s^-1)' = 21 ± 0.6; column 'kcat/Km (s^-1 mM^-1)' = 650 ± 63. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.032 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.032 mM; the exported value is 0.032 mM. kcat: printed Table 1 cell 21 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 21.0 s^(-1); the exported value is 21.0 s^(-1). kcat/Km: printed Table 1 cell 650 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 650.0 s^(-1)*mM^(-1); the exported value is 656.25 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, propionyl-CoA as acyl substrate, varied substrate Propionyl-CoA: Km = 0.032 ± 0.002 mM; kcat = 21 ± 0.6 s^-1; printed kcat/Km = 650 ± 63 s^-1 mM^-1.

substrate: propionyl-CoA


substrate_name: propionate

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetyl-CoA-forming direction, propionate as acyl substrate, varied-substrate row 'Propionate'; column 'Km (mM)' = 29 ± 1.4; column 'kcat (s^-1)' = 190 ± 1.5; column 'kcat/Km (s^-1 mM^-1)' = 6.3 ± 0.3. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 29 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 29.0 mM; the exported value is 29.0 mM. kcat: printed Table 1 cell 190 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 190.0 s^(-1); the exported value is 190.0 s^(-1). kcat/Km: printed Table 1 cell 6.3 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 6.3 s^(-1)*mM^(-1); the exported value is 6.551724137931035 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetyl-CoA-forming direction, propionate as acyl substrate, varied substrate Propionate: Km = 29 ± 1.4 mM; kcat = 190 ± 1.5 s^-1; printed kcat/Km = 6.3 ± 0.3 s^-1 mM^-1.

substrate: propionate


source_db: oed

smiles: CC(=O)O

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetyl-CoA-forming direction, acetate as acyl substrate, varied-substrate row 'Acetate'; column 'Km (mM)' = 14 ± 0.6; column 'kcat (s^-1)' = 240 ± 2.7; column 'kcat/Km (s^-1 mM^-1)' = 16 ± 0.5. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 14 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 14.0 mM; the exported value is 14.0 mM. kcat: printed Table 1 cell 240 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 240.0 s^(-1); the exported value is 240.0 s^(-1). kcat/Km: printed Table 1 cell 16 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 16.0 s^(-1)*mM^(-1); the exported value is 17.142857142857142 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetyl-CoA-forming direction, acetate as acyl substrate, varied substrate Acetate: Km = 14 ± 0.6 mM; kcat = 240 ± 2.7 s^-1; printed kcat/Km = 16 ± 0.5 s^-1 mM^-1.

source: oed


column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, acetyl-CoA as acyl substrate, varied-substrate row 'Acetyl-CoA'; column 'Km (mM)' = 0.04 ± 0.001; column 'kcat (s^-1)' = 110 ± 1.6; column 'kcat/Km (s^-1 mM^-1)' = 2,600 ± 370. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.04 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.04 mM; the exported value is 0.04 mM. kcat: printed Table 1 cell 110 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 110.0 s^(-1); the exported value is 110.0 s^(-1). kcat/Km: printed Table 1 cell 2,600 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 2600.0 s^(-1)*mM^(-1); the exported value is 2750.0 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate Acetyl-CoA: Km = 0.04 ± 0.001 mM; kcat = 110 ± 1.6 s^-1; printed kcat/Km = 2,600 ± 370 s^-1 mM^-1.


column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, acetyl-CoA as acyl substrate, varied-substrate row 'ADP'; column 'Km (mM)' = 1.6 ± 0.15; column 'kcat (s^-1)' = 140 ± 1.2; column 'kcat/Km (s^-1 mM^-1)' = 89 ± 7.9. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.6 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.6 mM; the exported value is 1.6 mM. kcat: printed Table 1 cell 140 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 140.0 s^(-1); the exported value is 140.0 s^(-1). kcat/Km: printed Table 1 cell 89 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 89.0 s^(-1)*mM^(-1); the exported value is 87.5 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate ADP: Km = 1.6 ± 0.15 mM; kcat = 140 ± 1.2 s^-1; printed kcat/Km = 89 ± 7.9 s^-1 mM^-1.


column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetyl-CoA-forming direction, acetate as acyl substrate, varied-substrate row 'ATP'; column 'Km (mM)' = 12 ± 0.4; column 'kcat (s^-1)' = 320 ± 4.4; column 'kcat/Km (s^-1 mM^-1)' = 27 ± 0.7. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 12 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 12.0 mM; the exported value is 12.0 mM. kcat: printed Table 1 cell 320 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 320.0 s^(-1); the exported value is 320.0 s^(-1). kcat/Km: printed Table 1 cell 27 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 27.0 s^(-1)*mM^(-1); the exported value is 26.666666666666668 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetyl-CoA-forming direction, acetate as acyl substrate, varied substrate ATP: Km = 12 ± 0.4 mM; kcat = 320 ± 4.4 s^-1; printed kcat/Km = 27 ± 0.7 s^-1 mM^-1.


row_label: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate GDP


column_label: TABLE 1. Apparent kinetic parameters for EhACD in each direction of the reaction. TABLE 1, Acetyl-CoA-forming direction, varied substrate GTP; column 'Km (mM)' = 10; column 'kcat (s^-1)' = 180; column 'kcat/Km (s^-1 mM^-1)' = 18.

normalized_value_unit_evidence: Km: printed cell 10 mM converts to 10.0 mM; the exported value is 10.0 mM. kcat: printed cell 180 s^-1 converts to 180.0 s^(-1); the exported value is 180.0 s^(-1). kcat/Km: printed cell 18 s^-1 mM^-1 converts to 18.0 s^(-1)*mM^(-1); the exported value is 18.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 1. Apparent kinetic parameters for EhACD in each direction of the reaction. TABLE 1, Acetyl-CoA-forming direction, varied substrate GTP: Km = 10 mM; kcat = 180 s^-1; printed kcat/Km = 18 s^-1 mM^-1.


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

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, acetyl-CoA as acyl substrate, varied-substrate row 'Phosphate'; column 'Km (mM)' = 1.8 ± 0.18; column 'kcat (s^-1)' = 120 ± 7.8; column 'kcat/Km (s^-1 mM^-1)' = 65 ± 2.3. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.8 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.8 mM; the exported value is 1.8 mM. kcat: printed Table 1 cell 120 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 120.0 s^(-1); the exported value is 120.0 s^(-1). kcat/Km: printed Table 1 cell 65 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 65.0 s^(-1)*mM^(-1); the exported value is 66.66666666666667 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate Phosphate: Km = 1.8 ± 0.18 mM; kcat = 120 ± 7.8 s^-1; printed kcat/Km = 65 ± 2.3 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature H237A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row H237A / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); H237A / 4-coumaric acid: kcat 1.98 +/- 0.078 s^-1; Km 143.4 +/- 17.8 uM; kcat/Km (1.381 +/- 0.054) x 10^4 M^-1 s^-1. Normalized directly by unit conversion to kcat=1.98 s^-1; Km=0.1434 mM; kcat/Km=13.81 s^-1*mM^-1.

row_label: H237A / 4-coumaric acid


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature K197A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row K197A / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); K197A / 4-coumaric acid: kcat 7.11 +/- 0.252 s^-1; Km 13.9 +/- 1.8 uM; kcat/Km (5.115 +/- 0.181) x 10^5 M^-1 s^-1. Normalized directly by unit conversion to kcat=7.11 s^-1; Km=0.0139 mM; kcat/Km=511.5 s^-1*mM^-1.

row_label: K197A / 4-coumaric acid


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature K443A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic parameters of Nt4CL2 mutants; row K443A / 4-coumarate; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 3. Kinetic parameters of Nt4CL2 mutants, row K443A / 4-coumarate: Km 0.9 +/- 0.2 uM; kcat 1.470 +/- 0.096 s^-1; kcat/Km (1.633 +/- 0.107) x 10^6 M^-1 s^-1.

row_label: K443A / 4-coumarate


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M344A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

status: unverified


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature R435A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic parameters of Nt4CL2 mutants; row R435A / 4-coumarate; Km, kcat, and kcat/Km columns.

row_label: R435A / 4-coumarate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T193A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row T193A / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); T193A / 4-coumaric acid: kcat 0.996 +/- 0.036 s^-1; Km 2.9 +/- 0.3 uM; kcat/Km (3.434 +/- 0.124) x 10^5 M^-1 s^-1. Normalized directly by unit conversion to kcat=0.996 s^-1; Km=0.0029 mM; kcat/Km=343.4 s^-1*mM^-1.

row_label: T193A / 4-coumaric acid


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T336A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row T336A / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); T336A / 4-coumaric acid: kcat 0.282 +/- 0.012 s^-1; Km 5.1 +/- 1.0 uM; kcat/Km (5.529 +/- 0.235) x 10^4 M^-1 s^-1. Normalized directly by unit conversion to kcat=0.282 s^-1; Km=0.0051 mM; kcat/Km=55.29 s^-1*mM^-1.

row_label: T336A / 4-coumaric acid


column_label: Table 2. Kinetic parameters of Nt4CL2; row Nt4CL2 wild type / 4-coumarate; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2. Kinetic parameters of Nt4CL2, row Nt4CL2 wild type / 4-coumarate: Km 1.5 +/- 0.4 uM; kcat 3.978 +/- 0.252 s^-1; kcat/Km (2.652 +/- 0.168) x 10^6 M^-1 s^-1.

row_label: Nt4CL2 wild type / 4-coumarate

table_label: Table 2. Kinetic parameters of Nt4CL2


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature Y239A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic parameters of Nt4CL2 mutants; row Y239A / 4-coumarate; Km, kcat, and kcat/Km columns.

row_label: Y239A / 4-coumarate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y239F to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row Y239F / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Y239F / 4-coumaric acid: kcat 4.47 +/- 0.096 s^-1; Km 6.9 +/- 0.6 uM; kcat/Km (6.478 +/- 0.139) x 10^5 M^-1 s^-1. Normalized directly by unit conversion to kcat=4.47 s^-1; Km=0.0069 mM; kcat/Km=647.8 s^-1*mM^-1.

row_label: Y239F / 4-coumaric acid


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

row_label: Table 1, acetyl-CoA-forming direction, propionate as acyl substrate, varied substrate Propionate


column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, propionyl-CoA as acyl substrate, varied-substrate row 'Propionyl-CoA'; column 'Km (mM)' = 0.032 ± 0.002; column 'kcat (s^-1)' = 21 ± 0.6; column 'kcat/Km (s^-1 mM^-1)' = 650 ± 63. Table 1 prints no further kinetic column.

row_label: Table 1, acetate-forming direction, propionyl-CoA as acyl substrate, varied substrate Propionyl-CoA


substrate_name: caffeate

substrate: caffeate


substrate_name: ferulate

substrate: ferulate


assay_conditions_summary: pH 6; 310.15 K; cofactor CoA


assay_conditions_summary: pH 7; 310.15 K; cofactor ADP


assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


substrate_name: CoA

substrate: CoA


organism: Columba livia

substrate_name: succinate (for A-SCS)

assay_conditions_summary: cofactor ATP

substrate: succinate (for A-SCS)


substrate_name: CoA (for A-SCS)

substrate: CoA (for A-SCS)


substrate_name: succinyl-CoA (for A-SCS)

substrate: succinyl-CoA (for A-SCS)


substrate_name: phosphate (for A-SCS)

substrate: phosphate (for A-SCS)


substrate_name: ATP

substrate: ATP


substrate_name: ADP

substrate: ADP


column_label: Table 2. Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates; row Caffeic Acid / wild type; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Caffeic Acid / wild type: kcat 2.652 +/- 0.162 s^-1; Km 1.0 +/- 0.2 uM; kcat/Km (2.652 +/- 0.162) x 10^6 M^-1 s^-1. Normalized directly by unit conversion to kcat=2.652 s^-1; Km=0.001 mM; kcat/Km=2652.0 s^-1*mM^-1.

row_label: Caffeic Acid / wild type


column_label: Table 2. Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates; row Ferulic Acid / wild type; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Ferulic Acid / wild type: kcat 3.576 +/- 0.132 s^-1; Km 2.9 +/- 0.4 uM; kcat/Km (1.233 +/- 0.046) x 10^6 M^-1 s^-1. Normalized directly by unit conversion to kcat=3.576 s^-1; Km=0.0029 mM; kcat/Km=1233.0 s^-1*mM^-1.

row_label: Ferulic Acid / wild type


substrate_name: sinapinate

column_label: Table 2. Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates; row Sinapinic Acid / wild type; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Sinapinic Acid / wild type: kcat 0.018 +/- 0.000 s^-1; Km 1321.9 +/- 103.9 uM; kcat/Km 13.617 +/- 0.000 M^-1 s^-1. Normalized directly by unit conversion to kcat=0.018 s^-1; Km=1.3219 mM; kcat/Km=0.013617 s^-1*mM^-1.

row_label: Sinapinic Acid / wild type

substrate: sinapinate


organism: Solanum lycopersicum

substrate_name: oxalate

assay_conditions_summary: pH 8

proof_lines: isoform AAE3-1, at pH 8.0, temperature not specified in the publication

substrate: oxalate


organism: Ocimum tenuiflorum


substrate_name: trans-cinnamate

substrate: trans-cinnamate


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

substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: phosphate

substrate: phosphate


organism: Lysinibacillus sphaericus

substrate_name: CoASH

assay_conditions_summary: cofactor CoA

column_label: PMID 1445232 abstract; substrate CoASH; metric apparent Km; raw value 33 microM; normalized value 0.033 mM.

normalized_value_unit_evidence: 33 microM normalized to 0.033 mM.

raw_value_unit_evidence: Abstract reports apparent Km for CoASH = 33 microM.

row_label: pimeloyl-CoA synthase / CoASH apparent Km

table_label: Open PMC/PubMed abstract prose (PMID 1445232)

substrate: CoASH


substrate_name: pimelate

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

column_label: PMID 1445232 abstract; substrate pimelate; metric apparent Km; raw value 145 microM; normalized value 0.145 mM.

normalized_value_unit_evidence: 145 microM normalized to 0.145 mM.

raw_value_unit_evidence: Abstract reports apparent Km for pimelate = 145 microM.

row_label: pimeloyl-CoA synthase / pimelate apparent Km

substrate: pimelate


column_label: PMID 1445232 abstract; paper substrate ATP.Mg2-; package substrate ATP; metric apparent Km; raw value 170 microM; normalized value 0.17 mM.

normalized_value_unit_evidence: 170 microM normalized to 0.17 mM.

raw_value_unit_evidence: Abstract reports apparent Km for ATP.Mg2- = 170 microM.

row_label: pimeloyl-CoA synthase / ATP.Mg2- apparent Km


organism: Arabidopsis thaliana

column_label: Official PMC Table 1 row '4-Coumarate', column 'Km, uM': 432

raw_value_unit_evidence: Km column reports 432 uM

table_label: Table 1. Kinetic properties of At4CL4 in vitro


column_label: Official PMC Table 1 row 'Caffeate', column 'Km, uM': 186

raw_value_unit_evidence: Km column reports 186 uM

row_label: Caffeate


column_label: Official PMC Table 1 row 'Ferulate', column 'Km, uM': 26

raw_value_unit_evidence: Km column reports 26 uM

row_label: Ferulate


substrate_name: sinapate

column_label: Official PMC Table 1 row 'Sinapate', column 'Km, uM': 20

raw_value_unit_evidence: Km column reports 20 uM

row_label: Sinapate

substrate: sinapate


organism: Clostridium scindens (strain JCM 10418 / VPI 12708)

substrate_name: cholate

substrate: cholate


organism: Acetobacterium woodii


substrate_name: caffeate

assay_conditions_summary: pH 7

substrate: caffeate


organism: Vigna umbellata

assay_conditions_summary: pH 4.5; cofactor CoA

column_label: Abstract reports recombinant VuAAE3 protein has specific activity against oxalate, with Km = 121+/-8.2 microM and Vmax of 7.7+/-0.88 micromol min-1 mg-1 protein.

raw_value_unit_evidence: Km raw_value=121+/-8.2 microM raw_unit=microM

row_label: recombinant Vigna umbellata VuAAE3 / oxalate

table_label: PubMed XML abstract PMID 27650448


organism: Lathyrus oleraceus

substrate_name: CoA

substrate: CoA


column_label: Figure 4A and Kinetic Studies prose report hBACS cholate Km 2.8 uM.

raw_value_unit_evidence: Km raw_value=2.8 raw_unit=uM

row_label: hBACS / cholate

table_label: Figure 4 - Kinetic analysis / Kinetic Studies prose


substrate_name: hexadecanoate (palmitate)

smiles: CCCCCCCCCCCCCCCC(=O)[O-]

substrate: hexadecanoate (palmitate)


organism: Pyrococcus furiosus

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

assay_conditions_summary: pH 6.5; 328.15 K; cofactor ADP

proof_lines: pH 6.5, 55°C, recombinant wild-type enzyme


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

proof_lines:
pH 6.5, 55°C, mutant enzyme H257Dalpha
pH 6.5, 55°C, mutant enzyme E217Dalpha


proof_lines:
pH 6.5, 55°C, mutant enzyme E217Dalpha
pH 6.5, 55°C, mutant enzyme H257Dalpha


assay_conditions_summary: pH 6.5; 328.15 K; cofactor ATP


substrate_name: acetate

substrate: acetate


substrate_name: succinate

substrate: succinate


organism: Rattus norvegicus

substrate_name: chenodeoxycholic acid

substrate: chenodeoxycholic acid


organism: Nicotiana tabacum


substrate_name: ferulate

substrate: ferulate


organism: Petroselinum crispum

substrate_name: Coenzyme A; 4-Coumarate; ATP

substrate: Coenzyme A; 4-Coumarate; ATP


substrate_name: isoferulate

substrate: isoferulate


substrate_name: cinnamate

substrate: cinnamate


organism: Bacillus subtilis

substrate_name: azelate

proof_lines: pH and temperature not specified in the publication

substrate: azelate


substrate_name: suberate

substrate: suberate


substrate_name: Glutarate

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

substrate: Glutarate


substrate_name: adipate

substrate: adipate


substrate_name: ATP

substrate: ATP


proof_lines: recombinant wild-type enzyme, pH 7.8, 30°C


organism: Haloarcula marismortui

substrate_name: ADP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

substrate: ADP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: phosphate

substrate: phosphate


organism: Solanum tuberosum


substrate_name: caffeate

substrate: caffeate


substrate_name: p-methoxycinnamate

substrate: p-methoxycinnamate


organism: Thermococcus kodakarensis

substrate_name: thioglycolate

substrate: thioglycolate


substrate_name: phenylacetate

substrate: phenylacetate


substrate_name: acetate

substrate: acetate


substrate_name: Isobutyrate

substrate: Isobutyrate


substrate_name: CoA

substrate: CoA


organism: Pinus taeda

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

proof_lines: isoform 4CL1, pH and temperature not specified in the publication


substrate_name: ferulate

substrate: ferulate


substrate_name: cinnamate

substrate: cinnamate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K457S to reconstruct the assayed variant sequence.

column_label: Table 2; row Lys457/Ser; column Km caffeate (uM); raw cell 5.

normalized_value_unit_evidence: Km caffeate: 5 uM = 0.005 mM.

raw_value_unit_evidence: Table 2 row Lys457/Ser, Km caffeate column: 5 uM; all values are averages of three independent determinations.

table_label: Table 2 | Enzymatic properties of heterologously expressed At4CL2 variants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K211S to reconstruct the assayed variant sequence.

column_label: Table 2; row Lys211/Ser; column Km caffeate (uM); raw cell 14.

normalized_value_unit_evidence: Km caffeate: 14 uM = 0.014 mM.

raw_value_unit_evidence: Table 2 row Lys211/Ser, Km caffeate column: 14 uM; all values are averages of three independent determinations.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C403A to reconstruct the assayed variant sequence.

column_label: Table 2; row Cys403/Ala; column Km caffeate (uM); raw cell 18.

normalized_value_unit_evidence: Km caffeate: 18 uM = 0.018 mM.

raw_value_unit_evidence: Table 2 row Cys403/Ala, Km caffeate column: 18 uM; all values are averages of three independent determinations.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E401Q to reconstruct the assayed variant sequence.

column_label: Table 2; row Glu401/Gln; column Km caffeate (uM); raw cell 28.

normalized_value_unit_evidence: Km caffeate: 28 uM = 0.028 mM.

raw_value_unit_evidence: Table 2 row Glu401/Gln, Km caffeate column: 28 uM; all values are averages of three independent determinations.


column_label: Table 2; row Lys457/Ser; column Km ATP (uM); raw cell 29.

raw_value_unit_evidence: Table 2 row Lys457/Ser, Km ATP column: 29 uM; all values are averages of three independent determinations.


column_label: Table 2; row Lys211/Ser; column Km ATP (uM); raw cell 151.

raw_value_unit_evidence: Table 2 row Lys211/Ser, Km ATP column: 151 uM; all values are averages of three independent determinations.


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

column_label: Table 2; Wild-type row; column Km ATP (uM); raw cell 163. The Cys403/Ala row contains 173.

normalized_value_unit_evidence: Paper Km ATP: 163 uM = 0.163 mM; current value is 0.173 mM.

raw_value_unit_evidence: Table 2 Wild-type row, Km ATP column: 163 uM; 173 uM belongs to the Cys403/Ala row; all values are averages of three independent determinations.

row_label: Wild-type


column_label: Table 2; row Glu401/Gln; column Km ATP (uM); raw cell 240.

raw_value_unit_evidence: Table 2 row Glu401/Gln, Km ATP column: 240 uM; all values are averages of three independent determinations.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R449Q to reconstruct the assayed variant sequence.


column_label: Table 2; row Arg449/Gln; column Km ATP (uM); raw cell 1507.

raw_value_unit_evidence: Table 2 row Arg449/Gln, Km ATP column: 1507 uM; all values are averages of three independent determinations.


organism: Haloferax volcanii

assay_conditions_summary: pH 7.5; 315.15 K; cofactor ADP


assay_conditions_summary: pH 7.5; 315.15 K; cofactor ATP


organism: Populus tomentosa

proof_lines: isoform 4CL2, pH and temperature not specified in the publication

proof_lines: isoform 4CL5, pH and temperature not specified in the publication


organism: Sorbus aucuparia

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA


organism: Pueraria montana var. lobata

substrate_name: trans-cinnamate

substrate: trans-cinnamate


organism: Populus trichocarpa

proof_lines:
isoform 4Cl4, at pH 7.0 and 30°C
isoform 4Cl5, at pH 7.0 and 30°C


organism: Arabidopsis thaliana


organism: Lysinibacillus sphaericus


substrate_name: heptanedioate

substrate: heptanedioate


organism: Halococcus saccharolyticus

assay_conditions_summary: pH 9; 310.15 K; cofactor ADP


assay_conditions_summary: pH 9; 310.15 K; cofactor ATP


organism: Populus trichocarpa x Populus deltoides


organism: Populus tremuloides


proof_lines: 4CL1 with 4-coumarate as substrate, pH 7.5, 30°C


assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines:
wild-type enzyme, pH 7.0, 30°C
wild type


proof_lines:
wild-type enzyme, pH 7.0, 30°C
wild-type enzyme


organism: Aquifex aeolicus


organism: Rattus norvegicus

substrate_name: chenodeoxycholate

proof_lines: native recombinant enzyme expressed in Sf9 microsomes

substrate: chenodeoxycholate


substrate_name: oxalate

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, temperature not specified in the publication

substrate: oxalate


assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

proof_lines:
wild-type enzyme
wild-type enzyme, pH 7.0, 30°C
wild type


enzyme_display_name: glutamine--tRNA ligase

organism: Escherichia coli

substrate_name: L-glutamine

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

proof_lines:
reaction with tRNA(2'H)Gln
Gln

enzyme: glutamine--tRNA ligase

substrate: L-glutamine


organism: Corynebacterium amycolatum

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, 30°C, fusion protein CaBioWF. 8-amino-7-oxononanoic acid synthase, i.e. AON synthase, encoded by BioF. ATP-dependent, pimeloyl-CoA synthetase, i.e. PCAS, encoded by BioW


organism: Camellia sinensis var. sinensis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines:
isoform 4CL1, at pH 7.5 and 30°C
isoform 4CL2, at pH 7.5 and 30°C


proof_lines:
isoform 4CL2, at pH 7.5 and 30°C
isoform 4CL1, at pH 7.5 and 30°C


enzyme_display_name: proline--tRNA ligase

substrate_name: L-proline

enzyme: proline--tRNA ligase

substrate: L-proline


enzyme_display_name: arginine--tRNA ligase

substrate_name: tRNAArg(ACG)

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

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

proof_lines: transfer RNA isoacceptor for arginine UCU

enzyme: arginine--tRNA ligase

substrate: tRNAArg(ACG)


enzyme_display_name: cysteine--tRNA ligase

substrate_name: L-cysteine

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

enzyme: cysteine--tRNA ligase

substrate: L-cysteine


enzyme_display_name: glutamate--tRNA ligase

substrate_name: tRNAGlu

proof_lines: pH 7.2, 37°C, recombinant His-tagged enzyme

enzyme: glutamate--tRNA ligase

substrate: tRNAGlu


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

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
versus glutamine
pH 7.0, 37°C
pH 7.2, 37°C, versus L-glutamine

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


enzyme_display_name: phenylalanine--tRNA ligase

organism: Gallus gallus

substrate_name: 2'-deoxyadenosine 5'-triphosphate

enzyme: phenylalanine--tRNA ligase

substrate: 2'-deoxyadenosine 5'-triphosphate


enzyme_display_name: glycine--tRNA ligase

proof_lines:
acceptor stem mutant substrate
mutant substrate

enzyme: glycine--tRNA ligase


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Geobacillus stearothermophilus

assay_conditions_summary: pH 8; 328.15 K; cofactor ATP

proof_lines: ATP-diphosphate exchange reaction, pH 8, 55°C


enzyme_display_name: propionate--CoA ligase

organism: Ralstonia solanacearum

substrate_name: Acrylate

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

enzyme: propionate--CoA ligase

substrate: Acrylate


proof_lines:
pH 8.0, 37°C
37°C, pH 8.0, cosubstrate: propanoate


substrate_name: Butyrate

smiles: CCCC(=O)[O-]

substrate: Butyrate


substrate_name: propionate

substrate: propionate


substrate_name: CoA

substrate: CoA


substrate_name: acetate

substrate: acetate


substrate_name: L-Cysteinyl-tRNACys

proof_lines:
steady-state
pH 7.0, 37°C

substrate: L-Cysteinyl-tRNACys


organism: Rhodotorula glutinis

substrate_name: linoleic acid

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

substrate: linoleic acid


substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

substrate: oleic acid


substrate_name: stearic acid

smiles: CCCCCCCCCCCCCCCCCC(=O)O

substrate: stearic acid


substrate_name: palmitic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitic acid


enzyme_display_name: [citrate (pro-3S)-lyase] ligase

organism: Clostridium sphenoides

substrate_name: ATP; Citrate (pro-3S)-lyase (thiol form); Acetate

enzyme: [citrate (pro-3S)-lyase] ligase


enzyme_display_name: acetoacetate--CoA ligase

organism: Zoogloea ramigera

substrate_name: Coenzyme A; Acetoacetate; ATP

enzyme: acetoacetate--CoA ligase

substrate: Coenzyme A; Acetoacetate; ATP


substrate_name: acetoacetate

substrate: acetoacetate


organism: Synechococcus elongatus


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

substrate_name: hexanoic acid

smiles: CCCCCC(=O)O

assay_conditions_summary: pH 7.8; 298.15 K; buffer that applies to every line of the table; cofactor ATP

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Hexanoic acid (C6)'; column 'Km (uM)' = 129; column 'kcat (min^-1)' = 0.11; column 'kcat/Km (uM^-1 min^-1)' = 0.0008. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 129 uM; 1 uM is one thousandth of 1 mM, so 129 / 1000 = 0.129 mM; the exported value is 0.129 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 0.11 min^-1; the printed head is per minute, so 0.11 / 60 = 0.0018333333333333333 s^(-1); the proposed kcat is 0.0018333333333333333 s^(-1). kcat/Km: printed Table 2 cell 0.0008 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.0008 times 1000 divided by 60 = 0.013333333333333334 s^(-1)*mM^(-1); the proposed kcat/Km is 0.013333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Hexanoic acid (C6)': Km cell = 129 uM; kcat cell = 0.11 min^-1; printed kcat/Km cell = 0.0008 uM^-1 min^-1.

table_label: Table 2: acyl chain length selectivity and kinetic parameters of FadD33 (J. Biol. Chem. 2013, 288(39):28116-28125), PDF page 5 of 10; printed column heads Enzyme/Substrate, Km (uM), kcat (min^-1) and kcat/Km (uM^-1 min^-1)

substrate: hexanoic acid


substrate_name: decanoic acid

smiles: CCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Decanoic acid (C10)'; column 'Km (uM)' = 121; column 'kcat (min^-1)' = 1.5; column 'kcat/Km (uM^-1 min^-1)' = 0.012. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 121 uM; 1 uM is one thousandth of 1 mM, so 121 / 1000 = 0.121 mM; the exported value is 0.121 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 1.5 min^-1; the printed head is per minute, so 1.5 / 60 = 0.025 s^(-1); the proposed kcat is 0.025 s^(-1). kcat/Km: printed Table 2 cell 0.012 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.012 times 1000 divided by 60 = 0.2 s^(-1)*mM^(-1); the proposed kcat/Km is 0.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Decanoic acid (C10)': Km cell = 121 uM; kcat cell = 1.5 min^-1; printed kcat/Km cell = 0.012 uM^-1 min^-1.

substrate: decanoic acid


substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Lauric acid (C12)'; column 'Km (uM)' = 21; column 'kcat (min^-1)' = 2.4; column 'kcat/Km (uM^-1 min^-1)' = 0.110. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 21 uM; 1 uM is one thousandth of 1 mM, so 21 / 1000 = 0.021 mM; the exported value is 0.021 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 2.4 min^-1; the printed head is per minute, so 2.4 / 60 = 0.04 s^(-1); the proposed kcat is 0.04 s^(-1). kcat/Km: printed Table 2 cell 0.110 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.110 times 1000 divided by 60 = 1.8333333333333335 s^(-1)*mM^(-1); the proposed kcat/Km is 1.8333333333333335 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Lauric acid (C12)': Km cell = 21 uM; kcat cell = 2.4 min^-1; printed kcat/Km cell = 0.110 uM^-1 min^-1.

substrate: lauric acid


column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Palmitic acid (C16)'; column 'Km (uM)' = 1.9; column 'kcat (min^-1)' = 4.2; column 'kcat/Km (uM^-1 min^-1)' = 2.3. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.9 uM; 1 uM is one thousandth of 1 mM, so 1.9 / 1000 = 0.0019 mM; the exported value is 0.0019 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 4.2 min^-1; the printed head is per minute, so 4.2 / 60 = 0.07 s^(-1); the proposed kcat is 0.07 s^(-1). kcat/Km: printed Table 2 cell 2.3 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 2.3 times 1000 divided by 60 = 38.333333333333336 s^(-1)*mM^(-1); the proposed kcat/Km is 38.333333333333336 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Palmitic acid (C16)': Km cell = 1.9 uM; kcat cell = 4.2 min^-1; printed kcat/Km cell = 2.3 uM^-1 min^-1.


substrate_name: ATP

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'ATP'; column 'Km (uM)' = 15; column 'kcat (min^-1)' = 1.3; column 'kcat/Km (uM^-1 min^-1)' = 0.085. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 15 uM; 1 uM is one thousandth of 1 mM, so 15 / 1000 = 0.015 mM; the exported value is 0.015 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 1.3 min^-1; the printed head is per minute, so 1.3 / 60 = 0.021666666666666667 s^(-1); the proposed kcat is 0.021666666666666667 s^(-1). kcat/Km: printed Table 2 cell 0.085 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.085 times 1000 divided by 60 = 1.416666666666667 s^(-1)*mM^(-1); the proposed kcat/Km is 1.416666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'ATP': Km cell = 15 uM; kcat cell = 1.3 min^-1; printed kcat/Km cell = 0.085 uM^-1 min^-1.


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

substrate_name: butyrate

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

substrate: butyrate


substrate_name: valerate

smiles: CCCCC(=O)[O-]

substrate: valerate


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


substrate_name: propionate


organism: Sulfurisphaera tokodaii

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


assay_conditions_summary: pH 8.4; 338.15 K; cofactor ATP

substrate: ATP


substrate_name: decanoate

smiles: CCCCCCCCCC(=O)[O-]

proof_lines: kcat is 16.1 min(-1) with decanoate as substrate (PubMed:23364516). kcat is 11.2 min(-1) with dodecanoate as substrate (PubMed:23364516). kcat is 4.2 min(-1) with tetradecanoate as substrate (PubMed:23364516).

substrate: decanoate


substrate_name: dodecanoate

smiles: CCCCCCCCCCCC(=O)[O-]

substrate: dodecanoate


substrate_name: tetradecanoate

smiles: CCCCCCCCCCCCCC(=O)[O-]

substrate: tetradecanoate


organism: Humulus lupulus

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 18.3 min(-1) with 2-methylpropanoate as substrate (PubMed:23300257). kcat is 10.5 min(-1) with 2-methylbutanoate as substrate (PubMed:23300257). kcat is 167 min(-1) with CoA as substrate (PubMed:23300257).


substrate_name: CoA

substrate: CoA


organism: Vibrio harveyi

substrate_name: palmitoleic acid

smiles: CCCCCCC=CCCCCCCCC(=O)O

substrate: palmitoleic acid


substrate_name: Unknown

substrate: Unknown


substrate_name: MbtL-holo

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'MbtL-holo'; column 'Km (uM)' = 106; column 'kcat (min^-1)' = 2.0; column 'kcat/Km (uM^-1 min^-1)' = 0.018. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 106 uM; 1 uM is one thousandth of 1 mM, so 106 / 1000 = 0.106 mM; the exported value is 0.106 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 2.0 min^-1; the printed head is per minute, so 2.0 / 60 = 0.03333333333333333 s^(-1); the proposed kcat is 0.03333333333333333 s^(-1). kcat/Km: printed Table 2 cell 0.018 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.018 times 1000 divided by 60 = 0.3 s^(-1)*mM^(-1); the proposed kcat/Km is 0.3 s^(-1)*mM^(-1). The live catalog row for this substrate holds no kcat/Km value, so the printed efficiency cell is recorded here as evidence only.

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'MbtL-holo': Km cell = 106 uM; kcat cell = 2.0 min^-1; printed kcat/Km cell = 0.018 uM^-1 min^-1.

substrate: MbtL-holo


organism: Lacrimispora sphenoides

substrate_name: citrate lyase

substrate: citrate lyase


organism: Rubrivivax gelatinosus


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.150 min(-1) with dodecanoate as substrate (PubMed:19477415). kcat is 2.04 min(-1) with dodecanoate as substrate (PubMed:26900152). kcat is 0.123 min(-1) with tetradecanoate as substrate (PubMed:19477415). kcat is 0.98 min(-1) with


substrate_name: hexadecanoate

smiles: CCCCCCCCCCCCCCCC(=O)[O-]

substrate: hexadecanoate


enzyme_display_name: arachidonate--CoA ligase

organism: Homo sapiens

enzyme: arachidonate--CoA ligase


organism: Rattus norvegicus


substrate_name: palmitate

substrate: palmitate


substrate_name: oleate

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

substrate: oleate


substrate_name: arachidonate

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

substrate: arachidonate


organism: Mycobacterium marinum (strain ATCC BAA-535 / M)

proof_lines: kcat is 1.51 min(-1) with dodecanoate as substrate (PubMed:26900152). kcat is 0.69 min(-1) with tetradecanoate as substrate (PubMed:26900152).


substrate_name: Acetoacetate; ATP; Coenzyme A

column_label: Results paragraph immediately after Fig. 4; metric Km for acetoacetate; prose/figure-associated evidence, not a table cell

normalized_value_unit_evidence: Km 0.07 mM

raw_value_unit_evidence: The measured K,n of the enzyme for acetoacetate was 70 Am, with the concentrations of the other substrates being 50 wlvl CoA and 1.25 mm ATP. OCR renders micro-units as A/wlvl/mm in this extraction; interpreted as 70 uM, 50 uM CoA, and 1.25 mM ATP from context.

row_label: rat liver cytosolic acetoacetyl-CoA synthetase; acetoacetate varied

table_label: Results/Fig. 4 prose

substrate: Acetoacetate; ATP; Coenzyme A


substrate_name: Coenzyme A; Acetate; ATP

substrate: Coenzyme A; Acetate; ATP


substrate_name: acyl-carrier protein

substrate: acyl-carrier protein


substrate_name: arachidonate (Isoform 1)

substrate: arachidonate (Isoform 1)


substrate_name: acetate

substrate: acetate


substrate_name: butyrate

smiles: CCCC(=O)[O-]

substrate: butyrate


substrate_name: propionate

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

raw_value_unit_evidence: Km raw_value=0.19 mM raw_unit=mM

row_label: Prose segment: recombinant ACSS3 propionate

table_label: PubMed PMID 28003429 abstract

substrate: propionate


organism: Mus musculus


organism: Chloroflexus aurantiacus


substrate_name: NADPH

assay_conditions_summary: pH 7.8; 328.15 K; cofactor NADPH

column_label: The Catalytic Properties section reports apparent Km values for 3-hydroxypropionate, NADPH, ATP, and CoA; NADPH maps to the second value, 10 uM.

raw_value_unit_evidence: NADPH apparent Km 10 uM

row_label: NADPH

table_label: ScienceDirect full-text Results prose: Catalytic Properties of Propionyl-CoA Synthase

substrate: NADPH


substrate_name: CoA

assay_conditions_summary: pH 7.8; 328.15 K; cofactor CoA

column_label: The Catalytic Properties section reports apparent Km values for 3-hydroxypropionate, NADPH, ATP, and CoA; CoA maps to the fourth value, 10 uM.

raw_value_unit_evidence: CoA apparent Km 10 uM

row_label: CoA

substrate: CoA


substrate_name: ATP

assay_conditions_summary: pH 7.8; 328.15 K; cofactor ATP

column_label: The Catalytic Properties section reports apparent Km values for 3-hydroxypropionate, NADPH, ATP, and CoA; ATP maps to the third value, 50 uM.

raw_value_unit_evidence: ATP apparent Km 50 uM

row_label: ATP

substrate: ATP


substrate_name: ATP (Isoform 1)

substrate: ATP (Isoform 1)


substrate_name: CoA (Isoform 1)

substrate: CoA (Isoform 1)


substrate_name: palmitate (Isoform 1)

substrate: palmitate (Isoform 1)


substrate_name: oleate (Isoform 1)

substrate: oleate (Isoform 1)


substrate_name: linoleate (when expressed in bacteria)

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

substrate: linoleate (when expressed in bacteria)


substrate_name: arachidonate (when expressed in bacteria)


substrate_name: stearate (when expreesed in bacteria)

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: stearate (when expreesed in bacteria)


substrate_name: linoleate (when expreesed in bacteria)

substrate: linoleate (when expreesed in bacteria)


substrate_name: stearate

substrate: stearate


substrate_name: oleate

substrate: oleate


substrate_name: linoleate

substrate: linoleate


substrate_name: arachidonate

substrate: arachidonate


substrate_name: butyrate


substrate_name: isobutyrate

substrate: isobutyrate


column_label: Abstract reports reaction rates for ATP, acetate and citrate lyase followed Michaelis-Menten kinetics with Km values 0.14 mM, 5 mM and 37 nM respectively.

raw_value_unit_evidence: Km raw_value=0.14 mM raw_unit=mM

row_label: Rhodopseudomonas/Rubrivivax citrate lyase ligase / ATP

table_label: PubMed XML abstract PMID 7128585


substrate_name: acetate

raw_value_unit_evidence: Km raw_value=5 mM raw_unit=mM

row_label: Rhodopseudomonas/Rubrivivax citrate lyase ligase / acetate

substrate: acetate


organism: Ralstonia solanacearum


substrate_name: Coenzyme A

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

substrate: Coenzyme A


substrate_name: hexadecanoate (palmitate)

substrate: hexadecanoate (palmitate)


substrate_name: palmitic acid (at pH 7.5)

substrate: palmitic acid (at pH 7.5)


substrate_name: (9Z)-octadecenoate (oleate)

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

substrate: (9Z)-octadecenoate (oleate)


column_label: Table I row Km value (mM) for acetate reports 66 for active CL-ligase.

raw_value_unit_evidence: Km raw_value=66 mM raw_unit=mM

row_label: Active CL-ligase from C. sphenoides / acetate

table_label: Table I, PMID 2512994 PDF


substrate_name: ATP

substrate: ATP


organism: Salmonella enterica

substrate_name: ATP; Coenzyme A; Propanoate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: ATP; Coenzyme A; Propanoate


substrate_name: Butyrate

substrate: Butyrate


substrate_name: CoA

proof_lines:
pH 8.0, 37°C
45°C, pH 7.0, cosubstrate: propanoate
pH 7.5, 37°C

substrate: CoA


substrate_name: Acrylate

substrate: Acrylate


proof_lines:
pH 8.0, 37°C
45°C, pH 7.0: cosubstrate: propanoate
pH 7.5, 37°C


substrate_name: propionate

substrate: propionate


organism: Escherichia coli

substrate_name: stearic acid

smiles: CCCCCCCCCCCCCCCCCC(=O)O

substrate: stearic acid


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: myristic acid


substrate_name: palmitoleic acid

proof_lines: cis-vaccenic acid, oleic acid, linoleic acid

substrate: palmitoleic acid


substrate_name: lauric acid

substrate: lauric acid


substrate_name: Decanoic acid

smiles: CCCCCCCCCC(=O)O

substrate: Decanoic acid


substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

substrate: octanoic acid


organism: Metallosphaera sedula

assay_conditions_summary: pH 8.4; 318.15 K; cofactor CoA

proof_lines: pH 8.4, 45°C, coupled spectrophotometric assay


substrate_name: propanoate

substrate: propanoate


substrate_name: arachidonate

substrate: arachidonate


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


substrate_name: palmitic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitic acid


substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

substrate: oleic acid


substrate_name: acetoacetate

substrate: acetoacetate


substrate_name: ATP

substrate: ATP


organism: Klebsiella aerogenes


substrate_name: acetyl adenylate

substrate: acetyl adenylate


substrate_name: acetate

substrate: acetate


substrate_name: CoA

substrate: CoA


organism: Oryctolagus cuniculus


organism: Streptomyces lividans


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


sequence_source: UniProtKB/Swiss-Prot A0A0G2K047

assay_conditions_summary: pH 8; cofactor ATP


substrate_name: Butyrate

substrate: Butyrate


organism: Bos taurus

proof_lines:
mammary gland enzyme, cow
cow liver enzyme


organism: Cavia porcellus


substrate_name: propionyl-AMP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

substrate: propionyl-AMP


substrate_name: diphosphate

substrate: diphosphate


proof_lines:
cow liver enzyme
mammary gland enzyme, cow


proof_lines:
ATP, propanoate
mamary gland enzyme, cow,
cow liver enzyme


organism: Geobacillus stearothermophilus

substrate_name: L-arginine

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

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

substrate: L-arginine


organism: Glycine max

substrate_name: tRNAArg(ACG)

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

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

substrate: tRNAArg(ACG)


substrate_name: E. coli acyl-carrier protein

proof_lines: fatty acids with shorter chain length than 12

substrate: E. coli acyl-carrier protein


organism: Haemophilus influenzae

substrate_name: L-Phe

substrate: L-Phe


organism: Sinorhizobium meliloti


organism: Homo sapiens

substrate_name: tRNAGlu

substrate: tRNAGlu


substrate_name: sinapate

substrate: sinapate


substrate_name: propanoate

substrate: propanoate


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Helicobacter pylori

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


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

substrate_name: succinate

assay_conditions_summary: pH 8; 310.15 K; cofactor ADP

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

substrate: succinate


enzyme_display_name: beta-phosphoglucomutase

organism: Lactobacillus delbrueckii subsp. lactis

substrate_name: beta-D-glucose 1-phosphate

enzyme: beta-phosphoglucomutase

substrate: beta-D-glucose 1-phosphate


enzyme_display_name: DNA 3'-5' helicase

organism: Lathyrus oleraceus

proof_lines: pH 8.0, 37°C, inhibition of DNA helicase activity

proof_lines: pH 8.0, 37°C, inhibition of ATPase activity

enzyme: DNA 3'-5' helicase


enzyme_display_name: glutamine synthetase

enzyme: glutamine synthetase


enzyme_display_name: glucose-6-phosphate isomerase

substrate_name: glucose 6-phosphate

enzyme: glucose-6-phosphate isomerase

substrate: glucose 6-phosphate


enzyme_display_name: oxalate--CoA ligase

organism: Glycine soja

substrate_name: oxalate

assay_conditions_summary: pH 8; cofactor CoA

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

enzyme: oxalate--CoA ligase

substrate: oxalate


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Latilactobacillus sakei

substrate_name: L-cysteine

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

proof_lines: pH 10.0, 35°C, recombinant His-tagged enzyme

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cysteine


substrate_name: ATP

assay_conditions_summary: pH 5.12; 310.15 K; cofactor ATP

proof_lines:
ATP-diphosphate exchange, pH 5.12, 37°C
ATP-diphosphate exchange, 17°C, pH 7.5
ATP-diphosphate exchange, 19°C, pH 7.5

substrate: ATP


enzyme_display_name: peptidylprolyl isomerase

organism: Legionella pneumophila

enzyme: peptidylprolyl isomerase


enzyme_display_name: lactoylglutathione lyase

organism: Leishmania donovani

substrate_name: reduced trypanothione

proof_lines: recombinant enzyme, pH 7.2, room temperature

enzyme: lactoylglutathione lyase

substrate: reduced trypanothione


substrate_name: L-phenylalanine

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

substrate: L-phenylalanine


enzyme_display_name: DNA topoisomerase (ATP-hydrolyzing)

assay_conditions_summary: cofactor ATP

proof_lines: recombinant 116 kDa mutant, ATP hydrolysis activity, in presence of DNA

proof_lines: recombinant 116 kDa mutant, ATP hydrolysis activity, in absence of DNA

enzyme: DNA topoisomerase (ATP-hydrolyzing)


organism: Lathyrus sativus

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA


organism: Leishmania major

substrate_name: alpha-D-glucose 1-phosphate

proof_lines: pH and temperature not specified in the publication

substrate: alpha-D-glucose 1-phosphate


substrate_name: L-glutamate

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

substrate: L-glutamate


organism: Levilactobacillus brevis


enzyme_display_name: L-arabinose isomerase

substrate_name: L-arabinose

enzyme: L-arabinose isomerase

substrate: L-arabinose


organism: Leishmania mexicana mexicana

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: triose-phosphate isomerase

organism: Leishmania mexicana

enzyme: triose-phosphate isomerase


enzyme_display_name: glutamate racemase

organism: Limosilactobacillus fermentum

substrate_name: D-Glu

enzyme: glutamate racemase

substrate: D-Glu


enzyme_display_name: coproporphyrin ferrochelatase

organism: Listeria monocytogenes

enzyme: coproporphyrin ferrochelatase


enzyme_display_name: serine racemase

organism: Macrostomum lignano

substrate_name: D-serine

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

enzyme: serine racemase

substrate: D-serine


substrate_name: D-glyceraldehyde 3-phosphate

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

substrate: D-glyceraldehyde 3-phosphate


organism: Malus domestica

substrate_name: L-arginine

substrate: L-arginine


enzyme_display_name: maltose epimerase

substrate_name: beta-maltose

enzyme: maltose epimerase

substrate: beta-maltose


substrate_name: (R,S)-S-adenosylmethionine

substrate: (R,S)-S-adenosylmethionine


organism: Mesocricetus auratus


enzyme_display_name: UDP-glucose 4-epimerase

organism: Magallana gigas

substrate_name: UDP-alpha-D-galactose

enzyme: UDP-glucose 4-epimerase

substrate: UDP-alpha-D-galactose


organism: Manihot esculenta

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication


organism: Methanococcus maripaludis

substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Methanocaldococcus jannaschii


enzyme_display_name: lysine 2,3-aminomutase

substrate_name: L-lysine

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

enzyme: lysine 2,3-aminomutase

substrate: L-lysine


enzyme_display_name: lysine--tRNA ligase

substrate_name: Escherichia coli tRNALys CNBr-treated

enzyme: lysine--tRNA ligase

substrate: Escherichia coli tRNALys CNBr-treated


enzyme_display_name: serine--tRNA ligase

organism: Methanosarcina barkeri

substrate_name: tRNASer(GGA)

proof_lines:
pH 7.2, 37°C, bacterial type SerRS
pH 7.2, 37°C, methanogenic SerRS
methanogenic type seryl-tRNA synthetase

enzyme: serine--tRNA ligase

substrate: tRNASer(GGA)


enzyme_display_name: arachidonate--CoA ligase

organism: Rattus norvegicus

substrate_name: CoA

proof_lines:
pH 8, 37°C, 70-day-old rats
pH 8, 37°C, 10-day-old rats

enzyme: arachidonate--CoA ligase

substrate: CoA


substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: L-serine

substrate: L-serine


organism: Metallosphaera sedula

assay_conditions_summary: pH 7.9; 348.15 K; cofactor CoA


enzyme_display_name: O-phosphoserine--tRNA ligase

substrate_name: tRNACys

enzyme: O-phosphoserine--tRNA ligase

substrate: tRNACys


enzyme_display_name: proline--tRNA ligase

organism: Methanothermobacter thermautotrophicus

substrate_name: tRNAPro

proof_lines: presence of bovine serum albumine, 50°C, pH 7.5

proof_lines: presence of leucyl-tRNA synthetase, 50°C, pH 7.5

enzyme: proline--tRNA ligase

substrate: tRNAPro


enzyme_display_name: glutamate--tRNA ligase

substrate_name: tRNAGln(UUG)

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

enzyme: glutamate--tRNA ligase

substrate: tRNAGln(UUG)


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

substrate_name: isopentenyl diphosphate

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

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: D-cysteine desulfhydrase

organism: Methylorubrum extorquens

substrate_name: D-cysteine

enzyme: D-cysteine desulfhydrase

substrate: D-cysteine


enzyme_display_name: methylmalonyl-CoA mutase

assay_conditions_summary: 310.15 K; cofactor CoA

proof_lines: presence of P-loop GTPase MeaB and GDP, 37°C

enzyme: methylmalonyl-CoA mutase


enzyme_display_name: methionine gamma-lyase

organism: Micromonospora echinospora

substrate_name: L-methionine

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

enzyme: methionine gamma-lyase

substrate: L-methionine


enzyme_display_name: medium-chain acyl-CoA ligase

organism: Mus musculus

substrate_name: Unknown

enzyme: medium-chain acyl-CoA ligase

substrate: Unknown


enzyme_display_name: pyrrolysine--tRNA(Pyl) ligase

organism: Methanosarcina thermophila

substrate_name: more

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

enzyme: pyrrolysine--tRNA(Pyl) ligase

substrate: more


enzyme_display_name: prostaglandin-D synthase

proof_lines: in the presence of 500 mM guanidinium hydrochloride

enzyme: prostaglandin-D synthase


enzyme_display_name: serine racemase

substrate_name: L-aspartate

enzyme: serine racemase

substrate: L-aspartate


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: protoporphyrin IX

proof_lines: mutant P255G, under strictly anaerobic conditions

enzyme: protoporphyrin ferrochelatase

substrate: protoporphyrin IX


enzyme_display_name: glutamine synthetase

enzyme: glutamine synthetase


enzyme_display_name: lactoylglutathione lyase

proof_lines: inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30°C

proof_lines: inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics from 0.5 to 2 microM, competitive inhibition, pH 7.0, 30°C

enzyme: lactoylglutathione lyase


proof_lines: pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction

proof_lines: pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction


enzyme_display_name: plus-end-directed kinesin ATPase

proof_lines: recombinant K888 mutants S175A and S175D, pH and temperature not specified in the publication

enzyme: plus-end-directed kinesin ATPase


enzyme_display_name: peptidylprolyl isomerase

sequence_source: UniProtKB FASTA (Q9QUR7)

enzyme: peptidylprolyl isomerase


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: cysteine-S-conjugate beta-lyase

enzyme: cysteine-S-conjugate beta-lyase


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

substrate_name: oleate

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

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: at pH 7.5, temperature not specified in the publication

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

substrate: oleate


enzyme_display_name: alanine racemase

organism: Mycobacterium avium

substrate_name: D-Ala

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

enzyme: alanine racemase

substrate: D-Ala


substrate_name: arachidonate

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

substrate: arachidonate


assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines: KHC, at 25°C, pH not specified in the publication

proof_lines: KIF16B, at 25°C, pH not specified in the publication

proof_lines: KIF13B, at 25°C, pH not specified in the publication


organism: Mycobacterium tuberculosis

substrate_name: (R)-pantoate

substrate: (R)-pantoate


organism: Mimosa pudica

substrate_name: cystathionine

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

substrate: cystathionine


enzyme_display_name: triose-phosphate isomerase

substrate_name: D-glyceraldehyde 3-phosphate

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: adenylate cyclase

substrate_name: ATP

proof_lines: recombinant adenylyl cclase, in the presence of Mn2+

proof_lines: recombinant adenylyl cclase, in the presence of Mg2+

enzyme: adenylate cyclase

substrate: ATP


enzyme_display_name: ribose-5-phosphate isomerase

substrate_name: D-ribose 5-phosphate

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate


enzyme_display_name: DNA 3'-5' helicase

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5, in presence of 1 mM Ni2+
pH 7.5, in presence of 1 mM Mn2+
pH 7.5, in presence of 1 mM Co2+

enzyme: DNA 3'-5' helicase


proof_lines: pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate


enzyme_display_name: chorismate mutase

substrate_name: chorismate

enzyme: chorismate mutase

substrate: chorismate


enzyme_display_name: alpha-methylacyl-CoA racemase

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: recombinant six-His tagged enzyme, 50 mM Tris-HCl, 0.2% octyl-beta-D-glucopyranoside, pH 8.0 at 37°C

proof_lines: recombinant enzyme, 50 mM Tris-HCl, 0.2% octyl-beta-D-glucopyranoside, pH 8.0 at 37°C

enzyme: alpha-methylacyl-CoA racemase


proof_lines: 4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid shows the most potent inhibition with Ki value of 0.0057 mM against MtCM

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: UDP-galactopyranose mutase

proof_lines:
under reducing conditions
pH 7.5, 37°C, recombinant enzyme
under non-reducing (native) conditions

enzyme: UDP-galactopyranose mutase


enzyme_display_name: 3-oxocholest-4-en-26-oate--CoA ligase

enzyme: 3-oxocholest-4-en-26-oate--CoA ligase


substrate_name: (R)-pristanoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: (R)-pristanoyl-CoA


enzyme_display_name: o-succinylbenzoate--CoA ligase

proof_lines: versus ATP, pH and temperature not specified in the publication

proof_lines: versus 2-succinylbenzoate, pH and temperature not specified in the publication

enzyme: o-succinylbenzoate--CoA ligase


enzyme_display_name: coproporphyrin ferrochelatase

substrate_name: coproporphyrin III

enzyme: coproporphyrin ferrochelatase

substrate: coproporphyrin III


substrate_name: dihydroxyacetone phosphate

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

substrate: dihydroxyacetone phosphate


organism: Bacillus anthracis

proof_lines: pH 7.5, temperature not specified in the publication

proof_lines: kcat is 7.1 min(-1) with 3,4-DHBA as substrate. kcat is 9.1 min(-1) with ATP as substrate.

source_databases_merged: brenda uniprot


organism: Nitrosopumilus maritimus (strain SCM1)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: UniProt P14900

organism: Escherichia coli

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P14900


enzyme_display_name: UniProt P9WJL3

enzyme: UniProt P9WJL3


substrate_name: meso-diaminopimelic acid

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

substrate: meso-diaminopimelic acid