substrate_name: benzyl alcohol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Benzyl Alcohol; columns Km (mM), Kcat, Kcat/Km; cells 4.57, 23.5, 5.14

raw_value_unit_evidence: Benzyl Alcohol: Km=4.57 mM; kcat=23.5 s^-1; kcat/Km=5.14 s^-1 mM^-1

row_label: Benzyl Alcohol

substrate: benzyl alcohol


enzyme_display_name: alcohol O-acetyltransferase

organism: Fragaria x ananassa

substrate_name: butanol

source_db: oed

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.

smiles: CCCCO

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Butanol; columns Km (mM), Kcat, Kcat/Km; cells 2.34, 21.5, 9.1

row_label: Butanol

data_origin: experimental

enzyme: alcohol O-acetyltransferase

substrate: butanol

status: corrected

source: oed


substrate_name: cinnamyl alcohol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Cinnamyl Alcohol; columns Km (mM), Kcat, Kcat/Km; cells 2.03, 1480, 727

raw_value_unit_evidence: Cinnamyl Alcohol: Km=2.03 mM; kcat=1480 s^-1; kcat/Km=727 s^-1 mM^-1

row_label: Cinnamyl Alcohol

substrate: cinnamyl alcohol


substrate_name: ethanol

smiles: CCO

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Ethanol; columns Km (mM), Kcat, Kcat/Km; cells 4.35, 7.5, 1.7

row_label: Ethanol

substrate: ethanol


substrate_name: eugenol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Eugenol; columns Km (mM), Kcat, Kcat/Km; cells 3.78, 548.5, 150

row_label: Eugenol

substrate: eugenol


substrate_name: geraniol

smiles: CC(C)=CCC/C(C)=C/CO

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Geraniol; columns Km (mM), Kcat, Kcat/Km; cells 2.04, 370.5, 180

row_label: Geraniol

substrate: geraniol


substrate_name: Heptanol

smiles: CCCCCCCO

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Heptanol; columns Km (mM), Kcat, Kcat/Km; cells 2.71, 170, 62

raw_value_unit_evidence: Heptanol: Km=2.71 mM; kcat=170 s^-1; kcat/Km=62 s^-1 mM^-1

row_label: Heptanol

substrate: Heptanol


substrate_name: Hexanol

smiles: CCCCCCO

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Hexanol; columns Km (mM), Kcat, Kcat/Km; cells 1.53, 483, 314

row_label: Hexanol

substrate: Hexanol


enzyme_display_name: quinate O-hydroxycinnamoyltransferase

organism: Solanum tuberosum

substrate_name: CoA

source_db: brenda

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

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

assay_conditions_summary: cofactor CoA

enzyme: quinate O-hydroxycinnamoyltransferase

substrate: CoA

status: unverified

source: brenda


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


substrate_name: chlorogenic acid

substrate: chlorogenic acid


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


substrate_name: quinate

substrate: quinate


organism: Bambusa multiplex


assay_conditions_summary: pH 8; 313.15 K; cofactor CoA


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

organism: Pseudomonas aeruginosa

substrate_name: gentamicin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y146F to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 6.5; cofactor CoA

column_label: Table 3; row Y146F; columns kcat (s^-1), kcat/Km (s^-1 uM^-1), Km (uM).

normalized_value_unit_evidence: Normalized paper values: kcat=4.33 s^-1; kcat/Km=510 s^-1 mM^-1; Km=0.0085 mM. Export values: Km=0.0085 mM; kcat=4.33 s^-1; kcat/Km=509.412 s^-1 mM^-1.

table_label: Table 3

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: gentamicin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y64F to reconstruct the assayed variant sequence.

column_label: Table 3; row Y64F; columns kcat (s^-1), kcat/Km (s^-1 uM^-1), Km (uM).

normalized_value_unit_evidence: Normalized paper values: kcat=12.5 s^-1; kcat/Km=870 s^-1 mM^-1; Km=0.0143 mM. Export values: Km=0.0143 mM; kcat=12.5 s^-1; kcat/Km=874.126 s^-1 mM^-1.


substrate_name: neomycin (at pH 6.5 and 22 degrees Celsius)

source_db: uniprot

verification_status: verified

column_label: Table 4. Kinetic parameters for antibiotics; row Neomycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.0066 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Neomycin: kcat 6.15 s^-1; Km 6.6 uM (0.0066 mM); kcat/Km 0.93 s^-1 uM^-1 (930.0 s^-1 mM^-1).

row_label: Neomycin

status: verified

source: uniprot


substrate_name: paromomycin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Paromomycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.0067 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Paromomycin: kcat 5.52 s^-1; Km 6.7 uM (0.0067 mM); kcat/Km 0.82 s^-1 uM^-1 (820.0 s^-1 mM^-1).

row_label: Paromomycin


substrate_name: ribostamycin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Ribostamycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.0079 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Ribostamycin: kcat 5.38 s^-1; Km 7.9 uM (0.0079 mM); kcat/Km 0.68 s^-1 uM^-1 (680.0 s^-1 mM^-1).

row_label: Ribostamycin


substrate_name: sisomicin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Sisomicin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.0109 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Sisomicin: kcat 10.48 s^-1; Km 10.9 uM (0.0109 mM); kcat/Km 0.97 s^-1 uM^-1 (970.0 s^-1 mM^-1).

row_label: Sisomicin


substrate_name: gentamicin (at pH 6.5 and 22 degrees Celsius)

column_label: PDF Table 4. Kinetic parameters for antibiotics row Gentamicin; Km normalized_value=0.0101 normalized_unit=mM.

raw_value_unit_evidence: Km raw_value=10.1 raw_unit=uM.

row_label: Gentamicin


substrate_name: kanamycin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Kanamycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.007 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Kanamycin: kcat 4.45 s^-1; Km 7 uM (0.007 mM); kcat/Km 0.63 s^-1 uM^-1 (630.0 s^-1 mM^-1).

row_label: Kanamycin


substrate_name: tobramycin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Tobramycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Tobramycin: kcat 5.68 s^-1; Km 6.6 uM (0.0066 mM); kcat/Km 0.86 s^-1 uM^-1 (860.0 s^-1 mM^-1).

row_label: Tobramycin


organism: Nicotiana tabacum

assay_conditions_summary: pH 6.6; 303.15 K; cofactor CoA

proof_lines:
pH 6.6, 30°C, cosubstrate: shikimate
pH 6.6, 30°C, cosubstrate: quinate


substrate_name: p-Coumaroyl-CoA

proof_lines:
pH 6.6, 30°C, cosubstrate: quinate
pH 6.6, 30°C, cosubstrate: shikimate

substrate: p-Coumaroyl-CoA


substrate_name: shikimate

proof_lines: pH 6.6, 30°C, cosubstrate: p-coumaroyl-CoA

substrate: shikimate


organism: Lonicera japonica

assay_conditions_summary: 303.15 K; cofactor CoA

proof_lines: cosubstrate 4-coumaroyl-CoA, pH not specified in the publication, 30°C


proof_lines: cosubstrate CoA, pH not specified in the publication, 30°C


proof_lines: cosubstrate quinate, pH not specified in the publication, 30°C


organism: Taraxacum antungense

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


organism: Cichorium endivia

substrate_name: coumaroyl-CoA

substrate: coumaroyl-CoA


organism: Marchantia paleacea


assay_conditions_summary: pH 6.5; 303.15 K; cofactor CoA


enzyme_display_name: trihydroxystilbene synthase

organism: Cannabis sativa

enzyme: trihydroxystilbene synthase


substrate_name: Dihydrocaffeoyl-CoA

substrate: Dihydrocaffeoyl-CoA


organism: Rattus norvegicus

substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


organism: Pinus strobus

assay_conditions_summary: pH 4; 303.15 K; cofactor CoA


substrate_name: Unknown

proof_lines:
pH 4.0, 30°C, uncompetitive inhibition
pH 4.0, 30°C, competitive inhibition


organism: Plagiochasma appendiculatum


substrate_name: quinate


organism: Homo sapiens

substrate_name: HIV1 Nef protein N-terminal peptide

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

substrate: HIV1 Nef protein N-terminal peptide


organism: Solanum lycopersicum

substrate_name: glucaric acid

substrate: glucaric acid


substrate_name: chlorogenic acid


organism: Secale cereale

substrate_name: feruloyl-CoA


organism: Pinus massoniana

assay_conditions_summary: pH 4; cofactor CoA

column_label: Table 3; P. massoniana column; rows kcat (min^-1), Km (uM), and kcat/Km (M^-1 s^-1)

row_label: P. massoniana stilbene synthase


assay_conditions_summary: pH 7.9; 298.15 K; cofactor CoA


proof_lines:
with coumaroyl-CoA
with caffeoyl-CoA


enzyme_display_name: 6-deoxyerythronolide-B synthase

organism: Saccharopolyspora erythraea

substrate_name: propanoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S315A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; cofactor CoA

proof_lines: mutant S315A, pH 7.2, temperature not specified in the publication

enzyme: 6-deoxyerythronolide-B synthase

substrate: propanoyl-CoA


organism: uncultured archaeon

substrate_name: formylmethanofuran

substrate: formylmethanofuran


enzyme_display_name: UniProt P30419

source_db: skid

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

sequence_source: multiple

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines: kcat is 0.41 sec(-1) with tetradecanoyl-CoA as substrate.

source_databases_merged: skid uniprot

enzyme: UniProt P30419

source: skid


substrate_name: caffeoyl-CoA

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

assay_conditions_summary: pH 7.5; cofactor CoA

substrate: caffeoyl-CoA


column_label: Official Thieme full-text HTML Figure 5 caption, panel a, reports caffeoyl-CoA Km=293.6 uM and Vmax=79.0 nkat/mg; required metric for this row is Km only.

normalized_value_unit_evidence: Km 0.2936 mM; matches exported Km 0.2936 mM.

raw_value_unit_evidence: Fig. 5 panel a: Km 293.6 uM and Vmax 79.0 nkat/mg for caffeoyl-CoA.

row_label: Varying caffeoyl-CoA / recombinant HQT

table_label: Fig. 5


kcat_over_km_origin: calculated

proof_lines: cosubstrate caffeoyl-CoA, pH not specified in the publication, 30°C


assay_conditions_summary: pH 7; cofactor CoA

column_label: Results section prose, right column, journal page 747: tobacco HQT Km for quinate 871 +/- 53 uM.

raw_value_unit_evidence: Results prose reports tobacco HQT Km for quinate as 871 +/- 53 uM.

row_label: Tobacco HQT; quinate Km

table_label: Results prose, journal page 747


organism: Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)

substrate: Unknown


enzyme_display_name: Formyltransferase/hydrolase complex subunit D

organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)


proof_lines:
pH 7.4, 37°C, isozyme NMT2
pH 7.9-8.0, 25°C, isozyme NMT2


organism: Leishmania major

substrate_name: Myristoyl-CoA; Glycylpeptide

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

substrate: Myristoyl-CoA; Glycylpeptide


organism: Plasmodium vivax

substrate_name: peptide pp60src(2-16)

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

substrate: peptide pp60src(2-16)


organism: Trypanosoma brucei

substrate_name: Glycylpeptide; Myristoyl-CoA

substrate: Glycylpeptide; Myristoyl-CoA


substrate_name: coumaroylquinate

substrate: coumaroylquinate


organism: Vitis vinifera

column_label: Table 3; V. vinifera column; rows kcat (min^-1), Km (uM), and kcat/Km (M^-1 s^-1)

row_label: V. vinifera stilbene synthase


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Acinetobacter baumannii

substrate_name: 2'-N-ethyl netilmicin

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / 2'-N-ethyl netilmicin; organism mapping Acinetobacter baumannii

normalized_value_unit_evidence: Normalized evidence: kcat=0.098 s^-1; km/S0.5=0.049 mM; kcat_over_km=2 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / 2'-N-ethyl netilmicin; kcat 0.098 s^-1; S0.5 49.0 ± 5.9 μM (normalized km 0.049 mM); kcat/S0.5 2.00 x10^3 M^-1 s^-1 (normalized kcat_over_km 2 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ih / 2'-N-ethyl netilmicin

table_label: ACS Infectious Diseases 2016 Table 1

enzyme: aminoglycoside 6'-N-acetyltransferase

substrate: 2'-N-ethyl netilmicin


substrate_name: amikacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / amikacin; organism mapping Acinetobacter baumannii; kcat_over_km paper=4.98 s^-1 mM^-1; export=4.97991967871486 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.496 s^-1; km/S0.5=0.0996 mM; kcat_over_km=4.98 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / amikacin; kcat 0.496 s^-1; S0.5 99.6 ± 12.5 μM (normalized km 0.0996 mM); kcat/S0.5 4.98 x10^3 M^-1 s^-1 (normalized kcat_over_km 4.98 s^-1 mM^-1).

row_label: AAC(6′)-Ih / amikacin

substrate: amikacin


substrate_name: arbekacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / arbekacin; organism mapping Acinetobacter baumannii; kcat_over_km paper=3.56 s^-1 mM^-1; export=3.5593220338983054 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.021 s^-1; km/S0.5=0.0059 mM; kcat_over_km=3.56 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / arbekacin; kcat 0.021 s^-1; S0.5 5.9 ± 0.8 μM (normalized km 0.0059 mM); kcat/S0.5 3.56 x10^3 M^-1 s^-1 (normalized kcat_over_km 3.56 s^-1 mM^-1).

row_label: AAC(6′)-Ih / arbekacin

substrate: arbekacin


substrate_name: butirosin A

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / butirosin A; organism mapping Acinetobacter baumannii; kcat_over_km paper=5.23 s^-1 mM^-1; export=5.231481481481481 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.113 s^-1; km/S0.5=0.0216 mM; kcat_over_km=5.23 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / butirosin A; kcat 0.113 s^-1; S0.5 21.6 ± 2.4 μM (normalized km 0.0216 mM); kcat/S0.5 5.23 x10^3 M^-1 s^-1 (normalized kcat_over_km 5.23 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ih / butirosin A

substrate: butirosin A


substrate_name: dibekacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / dibekacin; organism mapping Acinetobacter baumannii; kcat_over_km paper=4.08 s^-1 mM^-1; export=4.081632653061225 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.04 s^-1; km/S0.5=0.0098 mM; kcat_over_km=4.08 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / dibekacin; kcat 0.040 s^-1; S0.5 9.8 ± 1.4 μM (normalized km 0.0098 mM); kcat/S0.5 4.08 x10^3 M^-1 s^-1 (normalized kcat_over_km 4.08 s^-1 mM^-1).

row_label: AAC(6′)-Ih / dibekacin

substrate: dibekacin


substrate_name: gentamicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / gentamicin; organism mapping Acinetobacter baumannii; kcat_over_km paper=1.84 s^-1 mM^-1; export=1.8390804597701151 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.016 s^-1; km/S0.5=0.0087 mM; kcat_over_km=1.84 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / gentamicin; kcat 0.016 s^-1; S0.5 8.7 ± 3.1 μM (normalized km 0.0087 mM); kcat/S0.5 1.84 x10^3 M^-1 s^-1 (normalized kcat_over_km 1.84 s^-1 mM^-1).

row_label: AAC(6′)-Ih / gentamicin

substrate: gentamicin


substrate_name: isepamicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / isepamicin; organism mapping Acinetobacter baumannii; kcat_over_km paper=5.59 s^-1 mM^-1; export=5.585585585585585 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.62 s^-1; km/S0.5=0.111 mM; kcat_over_km=5.59 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / isepamicin; kcat 0.620 s^-1; S0.5 111 ± 13 μM (normalized km 0.111 mM); kcat/S0.5 5.59 x10^3 M^-1 s^-1 (normalized kcat_over_km 5.59 s^-1 mM^-1).

row_label: AAC(6′)-Ih / isepamicin

substrate: isepamicin


substrate_name: kanamycin B

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / kanamycin B; organism mapping Acinetobacter baumannii

normalized_value_unit_evidence: Normalized evidence: kcat=0.06 s^-1; km/S0.5=0.012 mM; kcat_over_km=5 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / kanamycin B; kcat 0.060 s^-1; S0.5 12.0 ± 1.1 μM (normalized km 0.012 mM); kcat/S0.5 5.00 x10^3 M^-1 s^-1 (normalized kcat_over_km 5 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ih / kanamycin B

substrate: kanamycin B


substrate_name: neomycin C

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / neomycin C; organism mapping Acinetobacter baumannii; kcat_over_km paper=7.59 s^-1 mM^-1; export=7.594936708860758 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.06 s^-1; km/S0.5=0.0079 mM; kcat_over_km=7.59 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / neomycin C; kcat 0.060 s^-1; S0.5 7.9 ± 1.0 μM (normalized km 0.0079 mM); kcat/S0.5 7.59 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.59 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ih / neomycin C

substrate: neomycin C


substrate_name: ribostamycin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / ribostamycin; organism mapping Acinetobacter baumannii; kcat paper=0.044 s^-1; export=0.04 s^-1; kcat_over_km paper=7.1 s^-1 mM^-1; export=6.451612903225807 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.044 s^-1; km/S0.5=0.0062 mM; kcat_over_km=7.1 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / ribostamycin; kcat 0.044 s^-1; S0.5 6.2 ± 1.5 μM (normalized km 0.0062 mM); kcat/S0.5 7.10 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.1 s^-1 mM^-1).

row_label: AAC(6′)-Ih / ribostamycin

substrate: ribostamycin


substrate_name: sisomicin

column_label: Table 1, AAC(6′)-Ih sisomicin row, exact Hill-equation cells kcat 0.051 s^-1; S0.5 10.5 ± 0.8 μM; kcat/S0.5 4.86 × 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat=0.051 s^(-1); S0.5=0.0105 mM in the current km slot; independently printed kcat/S0.5=4.86 s^(-1)*mM^(-1).

raw_value_unit_evidence: AAC(6′)-Ih / Acinetobacter baumannii / sisomicin source-bound cells: kcat 0.051 s^-1; S0.5 10.5 ± 0.8 μM; catalytic efficiency reported as kcat/S0.5 4.86 × 10^3 M^-1 s^-1.

row_label: AAC(6′)-Ih / sisomicin

table_label: Table 1. Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation.

substrate: sisomicin


substrate_name: tobramicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / tobramicin; organism mapping Acinetobacter baumannii; kcat_over_km paper=7.59 s^-1 mM^-1; export=7.586206896551724 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.022 s^-1; km/S0.5=0.0029 mM; kcat_over_km=7.59 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / tobramicin; kcat 0.022 s^-1; S0.5 2.9 ± 1.0 μM (normalized km 0.0029 mM); kcat/S0.5 7.59 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.59 s^-1 mM^-1).

row_label: AAC(6′)-Ih / tobramicin

substrate: tobramicin


organism: Serratia marcescens

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: acetyl-CoA


column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / AMK.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; AMK

table_label: Table 1, steady-state kinetic characterization of ANT(3\)-Ii/AAC(6')-IId"


column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / GEN.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; GEN


substrate_name: kanamycin

substrate: kanamycin


substrate_name: neomycin

column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / NEO.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; NEO

substrate: neomycin


substrate_name: netilmicin

column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / NET.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; NET

substrate: netilmicin


column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / RIB.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; RIB


column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / SIS.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; SIS


substrate_name: tobramycin

substrate: tobramycin


enzyme_display_name: aminoglycoside N(3)-acetyltransferase

organism: Pseudomonas aeruginosa

substrate_name: kanamycin A

enzyme: aminoglycoside N(3)-acetyltransferase

substrate: kanamycin A


substrate_name: sisomycin

substrate: sisomycin


substrate_name: myristoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature K107E/K252E to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Lys107Glu/Lys252Glu'; column 'Km (uM)' = 51; column 'kcat (s-1)' = 1.33; column 'kcat/Km (s-1.M-1)' = 25,848; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.33 s^-1; already in s^-1, so no unit conversion applies; the exported value is 1.33 s^(-1). Km: printed Table 1 cell 51 uM; 51 / 1000 = 0.051 mM; the exported value is 0.051 mM. kcat/Km: printed Table 1 cell 25,848 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 25,848 / 1000 = 25.848 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Lys107Glu/Lys252Glu': Km = 51 uM; kcat = 1.33 s^-1; printed kcat/Km = 25,848 s^-1.M^-1.

table_label: Table 1: Catalytic parameters for HsNMT1 and related mutants using MyrCoA (Nature Communications 2020, 11:1132)

substrate: myristoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature V181A to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Val181Ala'; column 'Km (uM)' = 20; column 'kcat (s-1)' = 0.36; column 'kcat/Km (s-1.M-1)' = 18,541; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.36 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.36 s^(-1). Km: printed Table 1 cell 20 uM; 20 / 1000 = 0.02 mM; the exported value is 0.02 mM. kcat/Km: printed Table 1 cell 18,541 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 18,541 / 1000 = 18.541 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Val181Ala': Km = 20 uM; kcat = 0.36 s^-1; printed kcat/Km = 18,541 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Val181Ala'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature V181L to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Val181Leu'; column 'Km (uM)' = 54; column 'kcat (s-1)' = 0.33; column 'kcat/Km (s-1.M-1)' = 6172; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.33 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.33 s^(-1). Km: printed Table 1 cell 54 uM; 54 / 1000 = 0.054 mM; the exported value is 0.054 mM. kcat/Km: printed Table 1 cell 6172 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6172 / 1000 = 6.172 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Val181Leu': Km = 54 uM; kcat = 0.33 s^-1; printed kcat/Km = 6172 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Val181Leu'


column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Wild-type'; column 'Km (uM)' = 18; column 'kcat (s-1)' = 0.41; column 'kcat/Km (s-1.M-1)' = 23,502; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.41 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.41 s^(-1). Km: printed Table 1 cell 18 uM; 18 / 1000 = 0.018 mM; the exported value is 0.018 mM. kcat/Km: printed Table 1 cell 23,502 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 23,502 / 1000 = 23.502 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Wild-type': Km = 18 uM; kcat = 0.41 s^-1; printed kcat/Km = 23,502 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Wild-type'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature Y180A to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Tyr180Ala'; column 'Km (uM)' = 765; column 'kcat (s-1)' = 0.16; column 'kcat/Km (s-1.M-1)' = 206; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.16 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.16 s^(-1). Km: printed Table 1 cell 765 uM; 765 / 1000 = 0.765 mM; the exported value is 0.765 mM. kcat/Km: printed Table 1 cell 206 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 206 / 1000 = 0.206 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Tyr180Ala': Km = 765 uM; kcat = 0.16 s^-1; printed kcat/Km = 206 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Tyr180Ala'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature Y180F/N246A to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Tyr180Phe/Asn246Ala'; column 'Km (uM)' = 33; column 'kcat (s-1)' = 0.68; column 'kcat/Km (s-1.M-1)' = 20,924; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.68 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.68 s^(-1). Km: printed Table 1 cell 33 uM; 33 / 1000 = 0.033 mM; the exported value is 0.033 mM. kcat/Km: printed Table 1 cell 20,924 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 20,924 / 1000 = 20.924 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Tyr180Phe/Asn246Ala': Km = 33 uM; kcat = 0.68 s^-1; printed kcat/Km = 20,924 s^-1.M^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature Y192A to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Tyr192Ala'; column 'Km (uM)' = 187; column 'kcat (s-1)' = 0.93; column 'kcat/Km (s-1.M-1)' = 4960; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.93 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.93 s^(-1). Km: printed Table 1 cell 187 uM; 187 / 1000 = 0.187 mM; the exported value is 0.187 mM. kcat/Km: printed Table 1 cell 4960 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4960 / 1000 = 4.96 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Tyr192Ala': Km = 187 uM; kcat = 0.93 s^-1; printed kcat/Km = 4960 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Tyr192Ala'


organism: Acinetobacter haemolyticus

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / 2'-N-ethylnetilmicin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=5.3 s^-1 mM^-1; export=5.300546448087432 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.097 s^-1; km/S0.5=0.0183 mM; kcat_over_km=5.3 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / 2'-N-ethylnetilmicin; kcat 0.097 s^-1; S0.5 18.3 ± 1.5 μM (normalized km 0.0183 mM); kcat/S0.5 5.30 x10^3 M^-1 s^-1 (normalized kcat_over_km 5.3 s^-1 mM^-1).

row_label: AAC(6′)-Ig / 2'-N-ethylnetilmicin


substrate_name: amikacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / amikacin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=7.44 s^-1 mM^-1; export=7.437641723356009 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.328 s^-1; km/S0.5=0.0441 mM; kcat_over_km=7.44 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / amikacin; kcat 0.328 s^-1; S0.5 44.1 ± 5.6 μM (normalized km 0.0441 mM); kcat/S0.5 7.44 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.44 s^-1 mM^-1).

row_label: AAC(6′)-Ig / amikacin

substrate: amikacin


substrate_name: arbekacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / arbekacin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=5.54 s^-1 mM^-1; export=5.539568345323741 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.077 s^-1; km/S0.5=0.0139 mM; kcat_over_km=5.54 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / arbekacin; kcat 0.077 s^-1; S0.5 13.9 ± 1.1 μM (normalized km 0.0139 mM); kcat/S0.5 5.54 x10^3 M^-1 s^-1 (normalized kcat_over_km 5.54 s^-1 mM^-1).

row_label: AAC(6′)-Ig / arbekacin

substrate: arbekacin


substrate_name: butirosin A

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / butirosin A; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=6.18 s^-1 mM^-1; export=6.184971098265896 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.107 s^-1; km/S0.5=0.0173 mM; kcat_over_km=6.18 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / butirosin A; kcat 0.107 s^-1; S0.5 17.3 ± 2.8 μM (normalized km 0.0173 mM); kcat/S0.5 6.18 x10^3 M^-1 s^-1 (normalized kcat_over_km 6.18 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ig / butirosin A

substrate: butirosin A


substrate_name: dibekacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / dibekacin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=4.9 s^-1 mM^-1; export=4.903474903474904 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.127 s^-1; km/S0.5=0.0259 mM; kcat_over_km=4.9 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / dibekacin; kcat 0.127 s^-1; S0.5 25.9 ± 2.5 μM (normalized km 0.0259 mM); kcat/S0.5 4.90 x10^3 M^-1 s^-1 (normalized kcat_over_km 4.9 s^-1 mM^-1).

row_label: AAC(6′)-Ig / dibekacin

substrate: dibekacin


substrate_name: gentamicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / gentamicin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=3.13 s^-1 mM^-1; export=3.125 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.055 s^-1; km/S0.5=0.0176 mM; kcat_over_km=3.13 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / gentamicin; kcat 0.055 s^-1; S0.5 17.6 ± 2.7 μM (normalized km 0.0176 mM); kcat/S0.5 3.13 x10^3 M^-1 s^-1 (normalized kcat_over_km 3.13 s^-1 mM^-1); note: substrate row label carries footnote d.

row_label: AAC(6′)-Ig / gentamicin

substrate: gentamicin


substrate_name: isepamicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / isepamicin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=7.49 s^-1 mM^-1; export=7.490384615384616 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.779 s^-1; km/S0.5=0.104 mM; kcat_over_km=7.49 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / isepamicin; kcat 0.779 s^-1; S0.5 104 ± 15 μM (normalized km 0.104 mM); kcat/S0.5 7.49 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.49 s^-1 mM^-1).

row_label: AAC(6′)-Ig / isepamicin

substrate: isepamicin


substrate_name: kanamycin B

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / kanamycin B; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=6.24 s^-1 mM^-1; export=6.241379310344827 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.181 s^-1; km/S0.5=0.029 mM; kcat_over_km=6.24 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / kanamycin B; kcat 0.181 s^-1; S0.5 29.0 ± 3.4 μM (normalized km 0.029 mM); kcat/S0.5 6.24 x10^3 M^-1 s^-1 (normalized kcat_over_km 6.24 s^-1 mM^-1).

row_label: AAC(6′)-Ig / kanamycin B

substrate: kanamycin B


substrate_name: neomycin C

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / neomycin C; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=7.7 s^-1 mM^-1; export=7.702702702702703 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.057 s^-1; km/S0.5=0.0074 mM; kcat_over_km=7.7 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / neomycin C; kcat 0.057 s^-1; S0.5 7.4 ± 0.5 μM (normalized km 0.0074 mM); kcat/S0.5 7.70 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.7 s^-1 mM^-1).

row_label: AAC(6′)-Ig / neomycin C

substrate: neomycin C


substrate_name: ribostamycin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / ribostamycin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=6.1 s^-1 mM^-1; export=6.101694915254237 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.072 s^-1; km/S0.5=0.0118 mM; kcat_over_km=6.1 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / ribostamycin; kcat 0.072 s^-1; S0.5 11.8 ± 1.7 μM (normalized km 0.0118 mM); kcat/S0.5 6.10 x10^3 M^-1 s^-1 (normalized kcat_over_km 6.1 s^-1 mM^-1).

row_label: AAC(6′)-Ig / ribostamycin

substrate: ribostamycin


substrate_name: sisomicin

column_label: Table 1, AAC(6′)-Ig sisomicin row, exact Hill-equation cells kcat 0.130 s^-1; S0.5 16.8 ± 2.0 μM; kcat/S0.5 7.74 × 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat=0.130 s^(-1); S0.5=0.0168 mM in the current km slot; independently printed kcat/S0.5=7.74 s^(-1)*mM^(-1).

raw_value_unit_evidence: AAC(6′)-Ig / Acinetobacter haemolyticus / sisomicin source-bound cells: kcat 0.130 s^-1; S0.5 16.8 ± 2.0 μM; catalytic efficiency reported as kcat/S0.5 7.74 × 10^3 M^-1 s^-1.

row_label: AAC(6′)-Ig / sisomicin

substrate: sisomicin


substrate_name: tobramicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / tobramicin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=3.86 s^-1 mM^-1; export=3.863636363636364 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.085 s^-1; km/S0.5=0.022 mM; kcat_over_km=3.86 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / tobramicin; kcat 0.085 s^-1; S0.5 22.0 ± 2.9 μM (normalized km 0.022 mM); kcat/S0.5 3.86 x10^3 M^-1 s^-1 (normalized kcat_over_km 3.86 s^-1 mM^-1).

row_label: AAC(6′)-Ig / tobramicin

substrate: tobramicin


organism: Fragaria x ananassa

substrate_name: methanol

smiles: CO

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Methanol; columns Km (mM), Kcat, Kcat/Km; cells 4.05, 18.5, 4.5

row_label: Methanol

substrate: methanol


substrate_name: octanol

smiles: CCCCCCCCO

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Octanol; columns Km (mM), Kcat, Kcat/Km; cells 2.23, 466, 208

row_label: Octanol

substrate: octanol


substrate_name: pentanol

smiles: CCCCCO

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Pentanol; columns Km (mM), Kcat, Kcat/Km; cells 5.78, 407, 71

raw_value_unit_evidence: Pentanol: Km=5.78 mM; kcat=407 s^-1; kcat/Km=71 s^-1 mM^-1

row_label: Pentanol

substrate: pentanol


substrate_name: propanol

smiles: CCCO

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Propanol; columns Km (mM), Kcat, Kcat/Km; cells 2.4, 17.5, 7.2

raw_value_unit_evidence: Propanol: Km=2.4 mM; kcat=17.5 s^-1; kcat/Km=7.2 s^-1 mM^-1

row_label: Propanol

substrate: propanol


enzyme_display_name: deacetylvindoline O-acetyltransferase

organism: Catharanthus roseus

substrate_name: vindoline

enzyme: deacetylvindoline O-acetyltransferase

substrate: vindoline


organism: Methylorubrum extorquens

column_label: Abstract/prose reports apparent Km for H4MPT = 30 uM.

raw_value_unit_evidence: 30 uM

table_label: Abstract/prose apparent Km values


substrate_name: formylmethanofuran

column_label: Abstract/prose reports apparent Km for formylMFR = 50 uM.

raw_value_unit_evidence: 50 uM

row_label: formylMFR

substrate: formylmethanofuran


enzyme_display_name: Alcohol O-acetyltransferase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: butyryl-CoA (for thioesterase activity)

assay_conditions_summary: buffer in vitro; cofactor CoA

column_label: Main text states KM was 25+/-1 uM for butyryl-CoA; Supplementary Table 1 row Butyryl reports KM 25+/-1 under wild-type Atf1p.

raw_value_unit_evidence: KM 25+/-1 uM for butyryl-CoA; supplement row Butyryl under Atf1p wild-type

row_label: Atf1p wild-type; Butyryl

table_label: Supplementary Table 1. Kinetic data from coupled enzyme assays; main text Biochemical assays of Atf1p.

enzyme: Alcohol O-acetyltransferase 1

substrate: butyryl-CoA (for thioesterase activity)


substrate_name: hexanoyl-CoA (for thioesterase activity)

column_label: Main text states KM was 12+/-3 uM for hexanoyl-CoA; Supplementary Table 1 row Hexanoyl reports KM 12+/-3 under wild-type Atf1p.

raw_value_unit_evidence: KM 12+/-3 uM for hexanoyl-CoA; supplement row Hexanoyl under Atf1p wild-type

row_label: Atf1p wild-type; Hexanoyl


substrate_name: octanoyl-CoA (for thioesterase activity)

column_label: Main text states KM was 3+/-1 uM for octanoyl-CoA; Supplementary Table 1 row Octanoyl reports KM 3+/-1 under wild-type Atf1p.

raw_value_unit_evidence: KM 3+/-1 uM for octanoyl-CoA; supplement row Octanoyl under Atf1p wild-type

row_label: Atf1p wild-type; Octanoyl


organism: Rattus norvegicus

substrate_name: S-acetyl-CoA

assay_conditions_summary: cofactor CoA

column_label: Primary PDF page 520 Properties prose gives S-Acetyl coenzyme A apparent Km 26 uM; converted to 0.026 mM.

normalized_value_unit_evidence: apparent Km 0.026 mM

raw_value_unit_evidence: Page 520 prose: S-Acetyl coenzyme A serves as acetyl donor with an apparent Km of 26 uM (Vm = 420 nmol min^-1) in an otherwise standard assay system

table_label: ScienceDirect PDF page 520 Properties prose

substrate: S-acetyl-CoA


substrate_name: S-butyl-L-cysteine

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

column_label: Primary PDF page 519 Table II row S-Butyl-L-cysteine has Ks (uM) value 63; converted to 0.063 mM.

normalized_value_unit_evidence: apparent Km/Ks 0.063 mM

raw_value_unit_evidence: Table II row S-Butyl-L-cysteine, column Ks (uM): 63; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: S-Butyl-L-cysteine

table_label: ScienceDirect PDF page 519 Table II, Substrate Specificity of Cysteine S-Conjugate N-Acetyltransferase

substrate: S-butyl-L-cysteine


substrate_name: S-Benzyl-L-cysteine

column_label: Primary PDF page 519 Table II row S-Benzyl-L-cysteine has Ks (uM) value 140; converted to 0.14 mM.

normalized_value_unit_evidence: apparent Km/Ks 0.14 mM

raw_value_unit_evidence: Table II row S-Benzyl-L-cysteine, column Ks (uM): 140; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: S-Benzyl-L-cysteine

substrate: S-Benzyl-L-cysteine


substrate_name: S-propyl-L-cysteine

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

column_label: Primary PDF page 519 Table II row S-Propyl-L-cysteine has Ks (uM) value 670; converted to 0.67 mM.

normalized_value_unit_evidence: apparent Km/Ks 0.67 mM

raw_value_unit_evidence: Table II row S-Propyl-L-cysteine, column Ks (uM): 670; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: S-Propyl-L-cysteine

substrate: S-propyl-L-cysteine


substrate_name: O-benzyl-L-serine

column_label: Primary PDF page 519 Table II row O-benzyl-L-serine has Ks (uM) value 2600; converted to 2.6 mM.

normalized_value_unit_evidence: apparent Km/Ks 2.6 mM

raw_value_unit_evidence: Table II row O-benzyl-L-serine, column Ks (uM): 2600; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: O-benzyl-L-serine

substrate: O-benzyl-L-serine


substrate_name: S-ethyl-L-cysteine

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

column_label: Primary PDF page 519 Table II row S-Ethyl-L-cysteine has Ks (uM) value 7100; converted to 7.1 mM.

normalized_value_unit_evidence: apparent Km/Ks 7.1 mM

raw_value_unit_evidence: Table II row S-Ethyl-L-cysteine, column Ks (uM): 7100; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: S-Ethyl-L-cysteine

substrate: S-ethyl-L-cysteine


substrate_name: N-formylmethanofuran

column_label: The abstract reports Km for CHO-MFR was 50 microM at the optimal salt concentration and 65 degrees C.

raw_value_unit_evidence: Km raw_value=50 microM raw_unit=microM

row_label: Prose segment: CHO-MFR Km

table_label: PubMed PMID 1483480 abstract

substrate: N-formylmethanofuran


column_label: The abstract reports Km for H4MPT was 100 microM at the optimal salt concentration and 65 degrees C.

raw_value_unit_evidence: Km raw_value=100 microM raw_unit=microM

row_label: Prose segment: H4MPT Km


substrate_name: N-furfurylformamide

verification_status: disputed

substrate: N-furfurylformamide

status: disputed


organism: Raphanus sativus


organism: Corynebacterium striatum

substrate_name: acetyl-CoA

assay_conditions_summary: pH 6; 310.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: dibekacin

substrate: dibekacin


substrate_name: kanamycin B

substrate: kanamycin B


organism: Vigna radiata var. radiata

substrate_name: p-coumaroyltartronic acid

substrate: p-coumaroyltartronic acid


substrate_name: caffeoyltartronic acid

substrate: caffeoyltartronic acid


substrate_name: CoA

proof_lines:
+ p-coumaroyltartronic acid
+ caffeoyltartronic acid

substrate: CoA


substrate_name: feruloyltartronic acid

substrate: feruloyltartronic acid


organism: Oryctolagus cuniculus

proof_lines:
apparent Km for subcellular fraction R
apparent Km for subcellular fraction P3


assay_conditions_summary: pH 8.4; 296.15 K; cofactor CoA


organism: Homo sapiens

substrate_name: S-benzyl-L-cysteine

source_databases_merged: brenda uniprot

substrate: S-benzyl-L-cysteine


organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)

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

enzyme: Formyltransferase/hydrolase complex subunit D


substrate_name: formyl-MFR

substrate: formyl-MFR


enzyme_display_name: Alpha-tubulin N-acetyltransferase 1

proof_lines: kcat is 2.2 h(-1) for the acetylation of polymerized tubulin (microtubules), 0.35 h(-1) for the acetylation of free tubulin, and 1.47 h(-1)with acetyl-CoA as substrate.

enzyme: Alpha-tubulin N-acetyltransferase 1


substrate_name: acetyl-CoA (for acetyltransferase activity)


substrate_name: isoamyl alcohol (for acetyltransferase activity)

smiles: CC(C)CCO


enzyme_display_name: N(6)-hydroxylysine O-acetyltransferase

organism: Escherichia coli

enzyme: N(6)-hydroxylysine O-acetyltransferase


substrate_name: Deacetylvindoline; Acetyl-CoA

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

source_databases_merged: sabio_rk brenda uniprot

substrate: Deacetylvindoline; Acetyl-CoA


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


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


substrate_name: N-methylhydroxylamine

smiles: CNO

substrate: N-methylhydroxylamine


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


enzyme_display_name: alpha-tubulin N-acetyltransferase

organism: Chlamydomonas reinhardtii

substrate_name: Unknown

enzyme: alpha-tubulin N-acetyltransferase

substrate: Unknown


substrate_name: free alpha-tubulin

substrate: free alpha-tubulin


assay_conditions_summary: buffer HEPES in in Tris-HCl; cofactor CoA

proof_lines: kinetic properties concerning the enzyme reaction are discussed


enzyme_display_name: Alcohol O-acetyltransferase 2

substrate_name: pregnenolone

enzyme: Alcohol O-acetyltransferase 2

substrate: pregnenolone


substrate_name: acetyl-CoA


substrate_name: deacetylvindoline

column_label: Abstract reports purified DAT possessed Km values of 6.5 microM and 1.3 microM for acetylcoenzyme A and deacetylvindoline, respectively.

raw_value_unit_evidence: Km raw_value=1.3 microM raw_unit=microM

row_label: Catharanthus roseus DAT / deacetylvindoline

table_label: PubMed XML abstract PMID 2350183

substrate: deacetylvindoline


organism: Trypanosoma brucei

substrate_name: Glycylpeptide

smiles: NCC(=O)NCC(=O)NCC(=O)O

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

column_label: Table 1; row CAP5.5 (TbNMT block); column Km (uM) raw 11.3 +/- 1.41; column kcat (s^-1) raw 18.2; column kcat/Km (uM^-1 s^-1) raw 1.61.

normalized_value_unit_evidence: kcat 18.2 s^-1 = 18.2 s^-1 (no conversion). Km 11.3 uM = 11.3/1000 = 0.0113 mM, which the catalog carries rounded to 0.011 mM. kcat/Km 1.61 uM^-1 s^-1 = 1.61 x 1000 = 1610 s^-1 mM^-1 (1 uM^-1 = 1000 mM^-1); the catalog's 1654.55 is 18.2/0.011 recomputed from that rounded Km, agreeing with the paper's printed 1.61 within its rounding.

row_label: TbNMT / CAP5.5 peptide

table_label: Table 1. Peptide and myristoyl-CoA kinetic parameters for LmNMT and TbNMT

substrate: Glycylpeptide


substrate_name: myristoyl-CoA

column_label: Table 1; row Myristoyl-CoA, TbNMT block; column Km (uM) raw 1.78 +/- 0.40; column kcat (s^-1) raw 76.8; column kcat/Km (uM^-1 s^-1) raw 43.2.

row_label: TbNMT / Myristoyl-CoA

substrate: myristoyl-CoA


substrate: acetyl-CoA


proof_lines:
HGSNAT
Ac-CoA
acetylated products


organism: Leishmania major

column_label: Table 1; row ARL1 (LmNMT block); column Km (uM) raw 110 +/- 33; column kcat (s^-1) raw 24.00; column kcat/Km (uM^-1 s^-1) raw 0.219.

normalized_value_unit_evidence: kcat 24.00 s^-1 = 24.0 s^-1 (no conversion). Km 110 uM = 110/1000 = 0.110 mM. kcat/Km 0.219 uM^-1 s^-1 = 0.219 x 1000 = 219 s^-1 mM^-1 (1 uM^-1 = 1000 mM^-1). The catalog's 218.18 s^-1 mM^-1 is 24/0.11 recomputed from the rounded Km and agrees with the paper's printed 0.219 within its three-significant-figure rounding.

row_label: LmNMT / ARL1 peptide


column_label: Table 1; row Myristoyl-CoA, LmNMT block; column Km (uM) raw 1.37 +/- 0.29; column kcat (s^-1) raw 23.60; column kcat/Km (uM^-1 s^-1) raw 17.22.

row_label: LmNMT / Myristoyl-CoA


organism: Arabidopsis thaliana

substrate_name: myristoyl-CoA, in the presence of CPK3

substrate: myristoyl-CoA, in the presence of CPK3


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


enzyme_display_name: UniProt C5XXB7

organism: Sorghum bicolor

substrate_name: shikimate

source_license: CC BY-NC-ND 4.0

enzyme: UniProt C5XXB7

substrate: shikimate


enzyme_display_name: UniProt E8ZAP2

organism: Coleus scutellarioides

substrate_name: sinapoyl-CoA

enzyme: UniProt E8ZAP2

substrate: sinapoyl-CoA


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


substrate_name: cinnamoyl-CoA

substrate: cinnamoyl-CoA


enzyme_display_name: UniProt R9RYW2

organism: Panicum virgatum

enzyme: UniProt R9RYW2


enzyme_display_name: UniProt P14743

organism: Saccharomyces cerevisiae

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

enzyme: UniProt P14743


organism: Salmonella enterica

substrate_name: tobramycin

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

substrate: tobramycin


substrate_name: malonyl-CoA

proof_lines: reaction with tobramycin, wild-type enzyme

substrate: malonyl-CoA


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: butyryl-CoA

substrate: butyryl-CoA


enzyme_display_name: Fatty acid synthase

column_label: Overall reaction block; WT row; K ACET column; Km raw value 7 +/- 3 uM.

raw_value_unit_evidence: WT overall reaction row reports K ACET = 7 +/- 3 uM.

row_label: WT, Overall reaction; metric columns kcat, K NADPH, K MAL, K ACET, kcat/K columns

table_label: PMID 16215233, Table 3: Kinetic evaluation of wild-type, K1699A, and K1699Q HFAS

enzyme: Fatty acid synthase


column_label: Overall reaction block; WT row; K MAL column; Km raw value 6 +/- 2 uM.

raw_value_unit_evidence: WT overall reaction row reports K MAL = 6 +/- 2 uM.


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

column_label: Overall reaction block; WT row; K NADPH column; Km raw value 5 +/- 1 uM.

raw_value_unit_evidence: WT overall reaction row reports K NADPH = 5 +/- 1 uM.

substrate: NADPH


substrate_name: butanoyl-CoA

column_label: Prose results on scanned p. 8696; acyl primer specificity sentence; butyryl-CoA/butanoyl-CoA Km raw value 4 uM.

raw_value_unit_evidence: Scanned PNAS p. 8696 prose states that human FAS prefers butyryl-CoA (Km = 4 uM) over acetyl-CoA.

row_label: Human FAS acyl primer specificity; butyryl-CoA (synonym of butanoyl-CoA) compared with acetyl-CoA

table_label: PMID 7567999, scanned PNAS p. 8696 prose: Purification and Properties of Human FAS

substrate: butanoyl-CoA


enzyme_display_name: fatty-acid synthase system

substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P49327 and applied mutation signature K1699A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

column_label: TABLE THREE overall reaction block, enzyme row K1699A; columns kcat (min^-1), KACET (uM) and kcat/KACET (uM^-1 min^-1); kcat cell = 19 min^-1; KACET cell = 7 uM; kcat/KACET cell = 3; author manuscript page 15 (PDF page 15). captured primary segment: acetyl-CoA | K1699A HFAS, the site-directed K1699A mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE overall reaction block, enzyme row K1699A: Km ACET 7 uM | kcat 19 min^-1 | kcat/Km ACET printed cell 3 under the column head kcat/KACET (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE overall reaction block, enzyme row K1699A: KACET = 7 uM; kcat = 19 min^-1; printed kcat/KACET = 3 uM^-1 min^-1.

table_label: TABLE THREE (kinetic evaluation of the wild-type and Lys-1699 mutant HFAS enzymes), overall reaction block; printed column heads enzyme | kcat (min^-1) | KNADPH (uM) | KMAL (uM) | KACET (uM) | kcat/KNADPH (uM^-1 min^-1) | kcat/KMAL (uM^-1 min^-1) | kcat/KACET (uM^-1 min^-1)

enzyme: fatty-acid synthase system

substrate: Acetyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K1699Q with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


column_label: Official PMC Table 3 section T3; row label WT | overall reaction | acetyl-CoA; metric columns kcat, K_ACET, kcat/K_ACET

raw_value_unit_evidence: Table 3 row WT | overall reaction | acetyl-CoA; columns kcat, K_ACET, kcat/K_ACET: kcat 160 +/- 15 min^-1; K value 7 +/- 3 uM; explicit kcat/K value 23 +/- 12 uM^-1 min^-1.

row_label: WT | overall reaction | acetyl-CoA

table_label: TABLE THREE. Kinetic evaluation of wild-type, K1699A, and K1699Q HFAS


substrate_name: Malonyl-CoA

column_label: TABLE THREE overall reaction block, enzyme row K1699A; columns kcat (min^-1), KMAL (uM) and kcat/KMAL (uM^-1 min^-1); kcat cell = 19 min^-1; KMAL cell = 3.0 uM; kcat/KMAL cell = 6; author manuscript page 15 (PDF page 15). captured primary segment: malonyl-CoA | K1699A HFAS, the site-directed K1699A mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE overall reaction block, enzyme row K1699A: Km MAL 3.0 uM | kcat 19 min^-1 | kcat/Km MAL printed cell 6 under the column head kcat/KMAL (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE overall reaction block, enzyme row K1699A: KMAL = 3.0 uM; kcat = 19 min^-1; printed kcat/KMAL = 6 uM^-1 min^-1.

substrate: Malonyl-CoA


column_label: Official PMC Table 3 section T3; row label WT | overall reaction | malonyl-CoA; metric columns kcat, K_MAL, kcat/K_MAL

raw_value_unit_evidence: Table 3 row WT | overall reaction | malonyl-CoA; columns kcat, K_MAL, kcat/K_MAL: kcat 160 +/- 15 min^-1; K value 6 +/- 2 uM; explicit kcat/K value 27 +/- 11 uM^-1 min^-1.

row_label: WT | overall reaction | malonyl-CoA


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: TABLE THREE overall reaction block, enzyme row K1699A; columns kcat (min^-1), KNADPH (uM) and kcat/KNADPH (uM^-1 min^-1); kcat cell = 19 min^-1; KNADPH cell = 370 uM; kcat/KNADPH cell = 0.05; author manuscript page 15 (PDF page 15). captured primary segment: NADPH | K1699A HFAS, the site-directed K1699A mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE overall reaction block, enzyme row K1699A: Km NADPH 370 uM | kcat 19 min^-1 | kcat/Km NADPH printed cell 0.05 under the column head kcat/KNADPH (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE overall reaction block, enzyme row K1699A: KNADPH = 370 uM; kcat = 19 min^-1; printed kcat/KNADPH = 0.05 uM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P49327 and applied mutation signature K1699Q with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

column_label: TABLE THREE overall reaction block, enzyme row K1699Q; columns kcat (min^-1), KNADPH (uM) and kcat/KNADPH (uM^-1 min^-1); kcat cell = 18 min^-1; KNADPH cell = 400 uM; kcat/KNADPH cell = 0.05; author manuscript page 15 (PDF page 15). captured primary segment: NADPH | K1699Q HFAS, the site-directed K1699Q mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE overall reaction block, enzyme row K1699Q: Km NADPH 400 uM | kcat 18 min^-1 | kcat/Km NADPH printed cell 0.05 under the column head kcat/KNADPH (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE overall reaction block, enzyme row K1699Q: KNADPH = 400 uM; kcat = 18 min^-1; printed kcat/KNADPH = 0.05 uM^-1 min^-1.


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

column_label: Official PMC Table 3 section T3; row label WT | overall reaction | NADPH; metric columns kcat, K_NADPH, kcat/K_NADPH

raw_value_unit_evidence: Table 3 row WT | overall reaction | NADPH; columns kcat, K_NADPH, kcat/K_NADPH: kcat 160 +/- 15 min^-1; K value 5 +/- 1 uM; explicit kcat/K value 32 +/- 9 uM^-1 min^-1.

row_label: WT | overall reaction | NADPH


enzyme_display_name: UniProt P19096

organism: Mus musculus

assay_conditions_summary: 298.15 K; cofactor CoA

proof_lines: native substrates, acetyl- and malonyl-CoA

enzyme: UniProt P19096


substrate_name: acetyl-CoA

proof_lines: malonyl/acetyltransferase (MAT) of murine FAS


organism: Enterococcus sp.

substrate_name: fortimicin A

substrate: fortimicin A


substrate_name: paromomycin

substrate: paromomycin


substrate_name: neamine

substrate: neamine


substrate_name: kanamycin A

substrate: kanamycin A


substrate: acetyl-CoA


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


proof_lines:
pH 7.5, 37°C, wild-type AAC(6')-Ie
pH 7.5, 37°C,wild-type AAC(6')-Ie


substrate_name: netilmicin

substrate: netilmicin


substrate_name: sisomicin

substrate: sisomicin


substrate_name: neomycin C

substrate: neomycin C


proof_lines: reaction with tobramycin, mutant enzyme C109A


substrate_name: dibekacin

substrate: dibekacin


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: amikacin

substrate: amikacin


substrate_name: tobramycin

substrate: tobramycin


proof_lines: reaction with tobramycin, mutant enzyme C109A/C70A


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: neomycin A

substrate: neomycin A


enzyme_display_name: shikimate O-hydroxycinnamoyltransferase

organism: Cichorium endivia

substrate_name: shikimate

enzyme: shikimate O-hydroxycinnamoyltransferase

substrate: shikimate


substrate_name: CoA

substrate: CoA


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

proof_lines: pH 7.0, 30°C, with 2,3-dihydroxybenzoate


substrate_name: sinapoyl-CoA

substrate: sinapoyl-CoA


substrate_name: cinnamoyl-CoA

substrate: cinnamoyl-CoA


proof_lines:
pH 7.0, 30°C, with 4-coumaroyl-CoA
pH 7.0, 30°C, with caffeoyl-CoA


proof_lines:
pH 7.0, 30°C, with 4-coumaroyl-CoA
pH 7.0, 30°C, with cinnamoyl-CoA
pH 7.0, 30°C, with caffeoyl-CoA


proof_lines:
pH 7.0, 30°C, with caffeoyl-CoA
pH 7.0, 30°C, with 4-coumaroyl-CoA


organism: Equisetum arvense


organism: Taraxacum antungense


substrate_name: quinate

substrate: quinate


organism: Marchantia paleacea


assay_conditions_summary: pH 6.5; 303.15 K; cofactor CoA


organism: Amaranthus cruentus


substrate_name: isocitric acid

proof_lines:
second substrate caffeoyl-CoA
second substrate p-coumaroyl-CoA
second substrate feruloyl-CoA

substrate: isocitric acid


organism: Phoenix dactylifera


organism: Oryza sativa


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


organism: Secale cereale


proof_lines:
with 4-coumaroyl-CoA
with caffeoyl-CoA


organism: Plagiochasma appendiculatum


organism: Raphanus sativus


substrate_name: galactarate

substrate: galactarate


enzyme_display_name: glucarate O-hydroxycinnamoyltransferase

enzyme: glucarate O-hydroxycinnamoyltransferase


substrate_name: glucarate

substrate: glucarate


enzyme_display_name: UniProt A5U161

organism: Mycobacterium tuberculosis

enzyme: UniProt A5U161


substrate_name: n-propionyl-CoA

substrate: n-propionyl-CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


enzyme_display_name: Name not preserved

substrate_name: alpha-D-glucosamine 1-phosphate

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.6
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: Name not preserved

substrate: alpha-D-glucosamine 1-phosphate


organism: Bacillus subtilis

substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C380A to reconstruct the assayed variant sequence.

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C380A/C405S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C405A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C405S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V385C/C405S to reconstruct the assayed variant sequence.


substrate_name: glucarolactone

substrate: glucarolactone


organism: Populus x canadensis

substrate_name: shikimate

proof_lines: pH 8.0, 37°C, recombinant GST-tagged enzyme, with 4-coumaroyl-CoA

substrate: shikimate


proof_lines: pH 8.0, 37°C, recombinant GST-tagged enzyme, with shikimate

proof_lines: pH 8.0, 37°C, recombinant GST-tagged enzyme, with quinate


organism: Arabidopsis thaliana

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: vinorine synthase

organism: Rauvolfia serpentina

enzyme: vinorine synthase


organism: Vitis vinifera


organism: Sorghum bicolor

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y40A to reconstruct the assayed variant sequence.

proof_lines: mutant Y40A, pH 6.5, temperature not specified in the publication


proof_lines: wild-type, pH 6.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S38A to reconstruct the assayed variant sequence.

proof_lines: mutant S38A, pH 6.5, temperature not specified in the publication


organism: Leptospira interrogans

source_databases_merged: brenda skid


organism: Nicotiana tabacum

substrate_name: 4-Coumaroyl-CoA; Shikimate

substrate: 4-Coumaroyl-CoA; Shikimate


enzyme_display_name: acridone synthase

organism: Huperzia serrata

enzyme: acridone synthase


enzyme_display_name: taxadien-5alpha-ol O-acetyltransferase

organism: Taxus canadensis

enzyme: taxadien-5alpha-ol O-acetyltransferase


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Acinetobacter baumannii

substrate_name: gentamicin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.84, pH 8.0, 37°C

enzyme: aminoglycoside 6'-N-acetyltransferase

substrate: gentamicin


substrate_name: arbekacin

proof_lines: kcat/S 0.5 value, Hill coefficient 2.5, pH 8.0, 37°C

substrate: arbekacin


substrate_name: tobramicin

proof_lines: kcat/S 0.5 value, Hill coefficient 2.12, pH 8.0, 37°C

substrate: tobramicin


substrate_name: dibekacin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.42, pH 8.0, 37°C

substrate: dibekacin


substrate_name: ribostamycin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.92, pH 8.0, 37°C

substrate: ribostamycin


substrate_name: sisomicin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.93, pH 8.0, 37°C

substrate: sisomicin


substrate_name: kanamycin B

proof_lines: kcat/S 0.5 value, Hill coefficient 2.30, pH 8.0, 37°C

substrate: kanamycin B


substrate_name: neomycin C

proof_lines: kcat/S 0.5 value, Hill coefficient 2.05, pH 8.0, 37°C

substrate: neomycin C


substrate_name: 2'-N-ethyl netilmicin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.39, pH 8.0, 37°C

substrate: 2'-N-ethyl netilmicin


substrate_name: butirosin A

proof_lines: kcat/S 0.5 value, Hill coefficient 2.03, pH 8.0, 37°C

substrate: butirosin A


substrate_name: amikacin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.26, pH 8.0, 37°C

substrate: amikacin


substrate_name: isepamicin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.48, pH 8.0, 37°C

substrate: isepamicin


organism: Ruta graveolens

substrate_name: N-methylanthraniloyl-CoA

proof_lines:
partially purified enzyme
isozyme I
isozyme II

substrate: N-methylanthraniloyl-CoA


substrate_name: caffeoyl-CoA

assay_conditions_summary: pH 6.6; cofactor CoA

column_label: Table II, Kinetic parameters of recombinant HCT; row=Caffeoyl-CoA; saturating substrate=Shikimate; metric column=Km [uM].

raw_value_unit_evidence: Table II row Caffeoyl-CoA with saturating Shikimate: Km 50 +/- 20 uM; Vmax 15 +/- 5 picokatals/mg; Vmax/Km 0.3.

row_label: Varying substrate Caffeoyl-CoA; saturating substrate Shikimate

table_label: Table II

substrate: caffeoyl-CoA


substrate_name: quinate

substrate: quinate


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


substrate_name: shikimate

column_label: Table II, Kinetic parameters of recombinant HCT; row=Shikimate; saturating substrate=p-Coumaroyl-CoA; metric column=Km [uM].

raw_value_unit_evidence: Table II row Shikimate with saturating p-Coumaroyl-CoA: Km 750 +/- 100 uM; Vmax 140 +/- 20 picokatals/mg; Vmax/Km 0.19.

row_label: Varying substrate Shikimate; saturating substrate p-Coumaroyl-CoA

substrate: shikimate


substrate_name: malonyl-CoA

proof_lines:
isozyme II
isozyme I
partially purified enzyme

substrate: malonyl-CoA


enzyme_display_name: UniProt K9MST3

organism: Malus domestica

substrate_name: benzoyl-CoA

enzyme: UniProt K9MST3

substrate: benzoyl-CoA


enzyme_display_name: 10-hydroxytaxane O-acetyltransferase

organism: Taxus cuspidata

substrate_name: acetyl-CoA

enzyme: 10-hydroxytaxane O-acetyltransferase

substrate: acetyl-CoA


organism: Rauvolfia serpentina x Rhazya stricta

substrate_name: gardneral

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C149A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

substrate: gardneral


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S29A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N293A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S413A to reconstruct the assayed variant sequence.


substrate_name: vinorine

substrate: vinorine


assay_conditions_summary: pH 7; cofactor CoA


substrate_name: CoA

substrate: CoA


proof_lines: Except vinorine, no other acetylated alkaloids are deacetylated by the reverse reaction.


enzyme_display_name: pseudotropine acyltransferase

organism: Datura stramonium

substrate_name: tigloyl-CoA

enzyme: pseudotropine acyltransferase

substrate: tigloyl-CoA


column_label: Table 3 row p-coumaroyl-CoA reports Vmax=187, Km=4.04 uM, Vmax/Km=46.28.

raw_value_unit_evidence: Km raw_value=4.04 raw_unit=uM

row_label: p-coumaroyl-CoA

table_label: ScienceDirect full-text Table 3: Kinetic properties of the recombinant AtHST used in this study


proof_lines:
AtHST
p-coumaroyl-CoA
protocatechuic acid


column_label: Table 3 row Shikimate reports Vmax=187, Km=213 uM, Vmax/Km=0.878.

raw_value_unit_evidence: Km raw_value=213 raw_unit=uM

row_label: Shikimate


column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row o-Coumaroyl-CoA; kcat column raw 0.02 min^-1; Km column raw 20.5 uM; kcat/Km column raw 19.5 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: paper_kcat normalized_value=0.000333333 normalized_unit=s^-1; paper_Km normalized_value=0.0205 normalized_unit=mM; paper_kcat/Km normalized_value=0.0195 normalized_unit=s^-1*mM^-1; export_kcat normalized_value=0.0003 normalized_unit=s^-1; export_Km normalized_value=0.021 normalized_unit=mM; export_kcat/Km normalized_value=0.014285714285714284 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.02 raw_unit=min^-1; Km raw_value=20.5 raw_unit=uM; kcat/Km raw_value=19.5 raw_unit=M^-1 s^-1

row_label: o-Coumaroyl-CoA


column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row m-Coumaroyl-CoA; kcat column raw 0.08 min^-1; Km column raw 14.7 uM; kcat/Km column raw 89.6 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: paper_kcat normalized_value=0.00133333 normalized_unit=s^-1; paper_Km normalized_value=0.0147 normalized_unit=mM; paper_kcat/Km normalized_value=0.0896 normalized_unit=s^-1*mM^-1; export_kcat normalized_value=0.001 normalized_unit=s^-1; export_Km normalized_value=0.015 normalized_unit=mM; export_kcat/Km normalized_value=0.06666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.08 raw_unit=min^-1; Km raw_value=14.7 raw_unit=uM; kcat/Km raw_value=89.6 raw_unit=M^-1 s^-1

row_label: m-Coumaroyl-CoA


column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row p-Coumaroyl-CoA; kcat column raw 0.02 min^-1; Km column raw 16.3 uM; kcat/Km column raw 20.4 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: kcat normalized_value=0.0003 normalized_unit=s^-1; Km normalized_value=0.016 normalized_unit=mM; kcat/Km normalized_value=0.01875 normalized_unit=s^-1*mM^-1; printed_kcat/Km_normalized_value=0.0204 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.02 raw_unit=min^-1; Km raw_value=16.3 raw_unit=uM; kcat/Km raw_value=20.4 raw_unit=M^-1 s^-1

row_label: p-Coumaroyl-CoA


column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row 4-Methylcinnamoyl-CoA; kcat column raw 0.01 min^-1; Km column raw 9.5 uM; kcat/Km column raw 24.6 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: kcat normalized_value=0.0002 normalized_unit=s^-1; Km normalized_value=0.009 normalized_unit=mM; kcat/Km normalized_value=0.022222222222222227 normalized_unit=s^-1*mM^-1; printed_kcat/Km_normalized_value=0.0246 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.01 raw_unit=min^-1; Km raw_value=9.5 raw_unit=uM; kcat/Km raw_value=24.6 raw_unit=M^-1 s^-1


substrate_name: Benzoyl-CoA

column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row Benzoyl-CoA; kcat column raw 0.55 min^-1; Km column raw 15.6 uM; kcat/Km column raw 590 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: kcat normalized_value=0.009 normalized_unit=s^-1; Km normalized_value=0.016 normalized_unit=mM; kcat/Km normalized_value=0.5625 normalized_unit=s^-1*mM^-1; printed_kcat/Km_normalized_value=0.59 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.55 raw_unit=min^-1; Km raw_value=15.6 raw_unit=uM; kcat/Km raw_value=590 raw_unit=M^-1 s^-1

row_label: Benzoyl-CoA

substrate: Benzoyl-CoA


substrate_name: Cinnamoyl-CoA

column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row Cinnamoyl-CoA; kcat column raw 0.07 min^-1; Km column raw 10.2 uM; kcat/Km column raw 106 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: kcat normalized_value=0.001 normalized_unit=s^-1; Km normalized_value=0.01 normalized_unit=mM; kcat/Km normalized_value=0.1 normalized_unit=s^-1*mM^-1; printed_kcat/Km_normalized_value=0.106 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.07 raw_unit=min^-1; Km raw_value=10.2 raw_unit=uM; kcat/Km raw_value=106 raw_unit=M^-1 s^-1

row_label: Cinnamoyl-CoA

substrate: Cinnamoyl-CoA


substrate_name: Feruloyl-CoA

column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row Feruloyl-CoA; kcat column raw 0.01 min^-1; Km column raw 16.7 uM; kcat/Km column raw 15 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: paper_kcat normalized_value=0.000166667 normalized_unit=s^-1; paper_Km normalized_value=0.0167 normalized_unit=mM; paper_kcat/Km normalized_value=0.015 normalized_unit=s^-1*mM^-1; export_kcat normalized_value=0.0002 normalized_unit=s^-1; export_Km normalized_value=0.017 normalized_unit=mM; export_kcat/Km normalized_value=0.011764705882352941 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.01 raw_unit=min^-1; Km raw_value=16.7 raw_unit=uM; kcat/Km raw_value=15 raw_unit=M^-1 s^-1

row_label: Feruloyl-CoA

substrate: Feruloyl-CoA


substrate_name: Hexanoyl-CoA

column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row Hexanoyl-CoA; kcat column raw 1.59 min^-1; Km column raw 3.8 uM; kcat/Km column raw 6970 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: kcat normalized_value=0.026 normalized_unit=s^-1; Km normalized_value=0.004 normalized_unit=mM; kcat/Km normalized_value=6.5 normalized_unit=s^-1*mM^-1; printed_kcat/Km_normalized_value=6.97 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.59 raw_unit=min^-1; Km raw_value=3.8 raw_unit=uM; kcat/Km raw_value=6970 raw_unit=M^-1 s^-1

row_label: Hexanoyl-CoA

substrate: Hexanoyl-CoA


substrate_name: N-Methylanthraniloyl-CoA

column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row N-methylanthraniloyl-CoA; kcat column raw 0.68 min^-1; Km column raw 29.4 uM; kcat/Km column raw 386 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: kcat normalized_value=0.011 normalized_unit=s^-1; Km normalized_value=0.029 normalized_unit=mM; kcat/Km normalized_value=0.3793103448275862 normalized_unit=s^-1*mM^-1; printed_kcat/Km_normalized_value=0.386 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.68 raw_unit=min^-1; Km raw_value=29.4 raw_unit=uM; kcat/Km raw_value=386 raw_unit=M^-1 s^-1

row_label: N-methylanthraniloyl-CoA

substrate: N-Methylanthraniloyl-CoA


substrate_name: n-Valeryl-CoA

column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row Valeryl-CoA; kcat column raw 0.11 min^-1; Km column raw 9.9 uM; kcat/Km column raw 180 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: kcat normalized_value=0.002 normalized_unit=s^-1; Km normalized_value=0.01 normalized_unit=mM; kcat/Km normalized_value=0.2 normalized_unit=s^-1*mM^-1; printed_kcat/Km_normalized_value=0.18 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.11 raw_unit=min^-1; Km raw_value=9.9 raw_unit=uM; kcat/Km raw_value=180 raw_unit=M^-1 s^-1

row_label: Valeryl-CoA

substrate: n-Valeryl-CoA


enzyme_display_name: Vinorine synthase

enzyme: Vinorine synthase


column_label: The abstract reports Km values of 4.2 and 5.5 microM for taxadienol and acetyl CoA, respectively.

raw_value_unit_evidence: Km raw_value=4.2 microM raw_unit=microM

row_label: Prose segment: taxadienol Km

table_label: PubMed PMID 10190984 abstract


raw_value_unit_evidence: Km raw_value=5.5 microM raw_unit=microM

row_label: Prose segment: acetyl CoA Km


substrate_name: Octanoyl-CoA

column_label: Table 2. Steady-state kinetic parameters for ACS; ACS column group; row Octanoyl-CoA; kcat column raw 0.78 min^-1; Km column raw 3.9 uM; kcat/Km column raw 3340 M^-1 s^-1; footnote states units are min^-1, uM, and M^-1*s^-1 respectively, values are means (n=3) with standard errors less than 15%.

normalized_value_unit_evidence: kcat normalized_value=0.013 normalized_unit=s^-1; Km normalized_value=0.004 normalized_unit=mM; kcat/Km normalized_value=3.25 normalized_unit=s^-1*mM^-1; printed_kcat/Km_normalized_value=3.34 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.78 raw_unit=min^-1; Km raw_value=3.9 raw_unit=uM; kcat/Km raw_value=3340 raw_unit=M^-1 s^-1

row_label: Octanoyl-CoA

substrate: Octanoyl-CoA


substrate_name: Phenylacetyl-CoA

column_label: Table 2. Steady-state kinetic parameters; ACS column group; row Phenylacetyl-CoA; kcat column raw 0.59 min^-1; Km column raw 4.9 uM; kcat/Km column raw 2,010 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 0.59 min^-1 / 60 = 0.009833 s^-1, carried at the export precision as normalized_value=0.01 normalized_unit=s^-1; Km 4.9 uM / 1000 = 0.004900 mM, carried at the export precision as normalized_value=0.005 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 2.0 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 2,010 M^-1 s^-1 normalizes to 2.01 s^-1*mM^-1 (deviation 0.5%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, ACS column group, row Phenylacetyl-CoA: kcat raw_value=0.59 raw_unit=min^-1; Km raw_value=4.9 raw_unit=uM; kcat/Km raw_value=2,010 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: ACS column group | Phenylacetyl-CoA

substrate: Phenylacetyl-CoA


substrate_name: heptanoyl-CoA

column_label: Table 2. Steady-state kinetic parameters; ACS column group; row Heptanoyl-CoA; kcat column raw 1.06 min^-1; Km column raw 4.4 uM; kcat/Km column raw 4,020 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 1.06 min^-1 / 60 = 0.017667 s^-1, carried at the export precision as normalized_value=0.018 normalized_unit=s^-1; Km 4.4 uM / 1000 = 0.004400 mM, carried at the export precision as normalized_value=0.004 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 4.5 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 4,020 M^-1 s^-1 normalizes to 4.02 s^-1*mM^-1 (deviation 11.9%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, ACS column group, row Heptanoyl-CoA: kcat raw_value=1.06 raw_unit=min^-1; Km raw_value=4.4 raw_unit=uM; kcat/Km raw_value=4,020 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: ACS column group | Heptanoyl-CoA

substrate: heptanoyl-CoA


substrate_name: phenylpropionyl-CoA

column_label: Table 2. Steady-state kinetic parameters; ACS column group; row 3-Phenylpropionyl-CoA; kcat column raw 1.62 min^-1; Km column raw 30.0 uM; kcat/Km column raw 900 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 1.62 min^-1 / 60 = 0.027000 s^-1, carried at the export precision as normalized_value=0.027 normalized_unit=s^-1; Km 30.0 uM / 1000 = 0.030000 mM, carried at the export precision as normalized_value=0.03 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 0.9 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 900 M^-1 s^-1 normalizes to 0.9 s^-1*mM^-1 (deviation 0.0%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, ACS column group, row 3-Phenylpropionyl-CoA: kcat raw_value=1.62 raw_unit=min^-1; Km raw_value=30.0 raw_unit=uM; kcat/Km raw_value=900 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: ACS column group | 3-Phenylpropionyl-CoA

substrate: phenylpropionyl-CoA


substrate_name: N-Methylanthraniloyl-CoA; Malonyl-CoA

substrate: N-Methylanthraniloyl-CoA; Malonyl-CoA


organism: Citrus x microcarpa

column_label: Table 1 columns Km, kcat, and kcat/Km for row C. microcarpa ACS under 4-Coumaroyl-CoA with product Naringenin.

normalized_value_unit_evidence: Km normalized_value=0.0136 normalized_unit=mM; kcat normalized_value=0.113 normalized_unit=s^-1; kcat/Km explicit_table_normalized_value=8.333 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=13.6 +/- 3.1 raw_unit=uM; kcat raw_value=6.8 +/- 2.2 raw_unit=min^-1; kcat/Km raw_value=500 raw_unit=min^-1 mM^-1

row_label: 4-Coumaroyl-CoA / C. microcarpa ACS / Product Naringenin

table_label: Table 1. Steady-state kinetic parameters of C. microcarpa QNS and ACS


column_label: Table 1 columns Km, kcat, and kcat/Km for row C. microcarpa ACS under N-methylanthraniloyl-CoA with product Quinolone.

normalized_value_unit_evidence: Km normalized_value=0.0374 normalized_unit=mM; kcat normalized_value=0.0667 normalized_unit=s^-1; kcat/Km explicit_table_normalized_value=1.95 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=37.4 +/- 2.4 raw_unit=uM; kcat raw_value=4.0 +/- 0.6 raw_unit=min^-1; kcat/Km raw_value=117 raw_unit=min^-1 mM^-1

row_label: N-methylanthraniloyl-CoA / C. microcarpa ACS / Product Quinolone


enzyme_display_name: acetoin dehydrogenase system

organism: Saccharolobus solfataricus

substrate_name: acetoin

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

enzyme: acetoin dehydrogenase system

substrate: acetoin


enzyme_display_name: glycine N-phenylacetyltransferase

organism: Homo sapiens

substrate_name: L-glutamine

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

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

enzyme: glycine N-phenylacetyltransferase

substrate: L-glutamine


organism: Pseudomonas aeruginosa


substrate_name: diacetyl

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

substrate: diacetyl


enzyme_display_name: benzyl alcohol O-benzoyltransferase

organism: Vitis labrusca

substrate_name: benzoyl-CoA

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, native enzyme

proof_lines: pH 7.5, 20-22°C, cosubstrate: benzyl alcohol, recombinant enzyme

proof_lines: kcat is 0.045 sec(-1) with benzoyl-CoA as substrate (with native enzyme). kcat is 0.022 sec(-1) with anthraniloyl-CoA as substrate (with native enzyme). kcat is 0.0035 sec(-1) with methanol as substrate (with native enzyme). kcat is 0.045 s

enzyme: benzyl alcohol O-benzoyltransferase

substrate: benzoyl-CoA


enzyme_display_name: Methanol O-anthraniloyltransferase

substrate_name: anthraniloyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: Methanol O-anthraniloyltransferase

substrate: anthraniloyl-CoA


substrate_name: methanol

smiles: CO

substrate: methanol


enzyme_display_name: acetoacetyl-CoA synthase

organism: Streptomyces sp.

substrate_name: Malonyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, 30°C, reaction with acetyl-CoA and malonyl-CoA

proof_lines: pH 8.0, 30°C, reaction with malonyl-CoA, without acetyl-CoA

enzyme: acetoacetyl-CoA synthase

substrate: Malonyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Bos taurus

substrate_name: glycine

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

proof_lines: cosubstrate phenylacetyl-CoA, pH 8.0, 30°C

proof_lines: cosubstrate 2,4-dichlorophenoxyacetyl-CoA pH 8.0, 30°C

substrate: glycine


substrate_name: benzyl alcohol

assay_conditions_summary: pH 7.7; cofactor CoA

column_label: Prose section: Characterizaton of the Activities of the Proteins Encoded by Tobacco HSR201 cDNA and by Another BEBT-Related cDNA from Arabidopsis states the HSR201 protein had BEBT activity with Km values for benzoyl CoA and benzyl alcohol of 35 and 19 microM, respectively.

raw_value_unit_evidence: Km raw_value=19 raw_unit=microM

row_label: HSR201 protein; benzyl alcohol

substrate: benzyl alcohol


raw_value_unit_evidence: Km raw_value=35 raw_unit=microM

row_label: HSR201 protein; benzoyl CoA

table_label: Prose section: Characterizaton of the Activities of the Proteins Encoded by Tobacco HSR201 cDNA and by Another BEBT-Related cDNA from Arabidopsis


organism: Petunia x hybrida

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

proof_lines: pH 7.7, 22°C, cosubstrate: benzyl alcohol


column_label: Table I row Acetyl-CoA columns Km, Kcat, Kcat/Km

row_label: Acetyl-CoA

table_label: Table I


column_label: Table I row Phenyl ethanol footnote e columns Km, Kcat, Kcat/Km

row_label: Phenyl ethanol


column_label: Table I row Benzoyl-CoA footnote b columns Km, Kcat, Kcat/Km

row_label: Benzoyl-CoA


enzyme_display_name: acetoin dehydrogenase

organism: Pelobacter carbinolicus

substrate_name: 2,6-Dichloroindophenol; H2O; Acetoin

enzyme: acetoin dehydrogenase

substrate: 2,6-Dichloroindophenol; H2O; Acetoin


organism: Populus trichocarpa


substrate_name: 3-Hydroxybenzyl alcohol

substrate: 3-Hydroxybenzyl alcohol


substrate_name: salicyl alcohol

substrate: salicyl alcohol


enzyme_display_name: (Z)-3-hexen-1-ol acetyltransferase

organism: Arabidopsis thaliana

smiles: CCCCCCCCO

proof_lines: pH 7.7, 25°C, recombinant His6-tagged enzyme

enzyme: (Z)-3-hexen-1-ol acetyltransferase


proof_lines: pH 7.7, 25°C, native enzyme, partially purified


organism: Aneurinibacillus thermoaerophilus

assay_conditions_summary: pH 7.4; cofactor CoA

column_label: Main text FdtC kinetic paragraph names acetyl-CoA second and gives second Km/kcat values respectively.

normalized_value_unit_evidence: Km 0.061 mM; kcat 3.1 s^-1; kcat/Km 50.81967213114754 s^-1 mM^-1 derived from paper values

row_label: acetyl-CoA

table_label: Main text - FdtC Catalyzes the Transfer of an Acetyl Group to dTDP-d-Fucp3N


enzyme_display_name: UniProt Q94FV7

organism: Rheum palmatum

substrate_name: malonyl-CoA

enzyme: UniProt Q94FV7

substrate: malonyl-CoA


enzyme_display_name: benzalacetone synthase

organism: Rubus idaeus

enzyme: benzalacetone synthase


enzyme_display_name: Benzyl alcohol O-benzoyltransferase

organism: Petunia hybrida

proof_lines: kcat is 4.4 sec(-1) with acetyl-CoA as substrate (PubMed:15286288). kcat is 57.1 sec(-1) with benzoyl-CoA as substrate (in the presence of benzyl alcohol) (PubMed:15286288). kcat is 81.3 sec(-1) with benzoyl-CoA as substrate (in the presenc

enzyme: Benzyl alcohol O-benzoyltransferase


substrate_name: benzoyl-CoA (in the presence of benzyl alcohol)


substrate_name: benzyl alcohol (in the presence of acetyl-CoA)


substrate_name: phenyl ethanol (in the presence of benzoyl-CoA)


organism: Escherichia coli


substrate_name: Leaf alcohol; Acetyl-CoA

assay_conditions_summary: pH 7.7; 298.15 K; cofactor CoA

substrate: Leaf alcohol; Acetyl-CoA


substrate_name: Unknown

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

proof_lines: kcat is 4.4 sec(-1) with acetyl-CoA as substrate (PubMed:15286288).

proof_lines: kcat is 57.1 sec(-1) with benzoyl-CoA as substrate (in the presence of benzyl alcohol) (PubMed:15286288).

proof_lines: kcat is 81.3 sec(-1) with benzoyl-CoA as substrate (in the presence of phenyl alcohol) (PubMed:15286288).

substrate: Unknown


proof_lines: kcat is 2.3 sec(-1) with dTDP-D-Fucp3N as substrate.

proof_lines: kcat is 3.1 sec(-1) with acetyl-CoA as substrate.


enzyme_display_name: tRNAMet cytidine acetyltransferase

substrate_name: H2O; ATP

assay_conditions_summary: cofactor ATP

enzyme: tRNAMet cytidine acetyltransferase

substrate: H2O; ATP


substrate_name: Acetyl-CoA; Malonyl-CoA

substrate: Acetyl-CoA; Malonyl-CoA


organism: Clarkia breweri

substrate_name: Benzyl alcohol; Benzoyl-CoA

substrate: Benzyl alcohol; Benzoyl-CoA


organism: Nicotiana tabacum


substrate_name: Benzoyl-CoA; Benzyl alcohol

substrate: Benzoyl-CoA; Benzyl alcohol


enzyme_display_name: 4-hydroxycoumarin synthase

organism: Sorbus aucuparia

assay_conditions_summary: pH 6.5; 308.15 K; cofactor CoA

enzyme: 4-hydroxycoumarin synthase


proof_lines: cosubstrate benzyl alcohol, pH 7.0, 30°C

proof_lines: cosubstrate salicyl alcohol, pH 7.0, 30°C


proof_lines:
cosubstrate acetyl-CoA, pH 7.0, 30°C
cosubstrate benzoyl-CoA, pH 7.0, 30°C


substrate_name: benzoyl-CoA

proof_lines: cosubstrate 3-hydroxybenzyl alcohol, pH 7.0, 30°C

substrate: benzoyl-CoA


substrate_name: cinnamoyl-CoA

assay_conditions_summary: pH 7.7; buffer Paper metric evidence: table label: Table II; cofactor CoA

column_label: Table II row 'Cinnamoyl CoA (with benzyl alcohol)' has columns Km=464 microM, Kcat=0.4 s^-1, and Kcat/Km=0.9 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.464 normalized_unit=mM; Kcat normalized_value=0.4 normalized_unit=s^-1; Kcat/Km normalized_value=0.9 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=464 raw_unit=microM; Kcat raw_value=0.4 raw_unit=s^-1; Kcat/Km raw_value=0.9 raw_unit=s^-1*mM^-1

row_label: Cinnamoyl CoA (with benzyl alcohol)

table_label: Table II. Kinetic parameters of BEBT

substrate: cinnamoyl-CoA


substrate_name: acetyl-CoA

column_label: Table II row 'Acetyl CoA (with benzyl alcohol)' has columns Km=818 microM, Kcat=17.5 s^-1, and Kcat/Km=21.5 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.818 normalized_unit=mM; Kcat normalized_value=17.5 normalized_unit=s^-1; Kcat/Km normalized_value=21.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=818 raw_unit=microM; Kcat raw_value=17.5 raw_unit=s^-1; Kcat/Km raw_value=21.5 raw_unit=s^-1*mM^-1

row_label: Acetyl CoA (with benzyl alcohol)


substrate_name: cinnamyl alcohol

column_label: Table II row 'Cinnamyl alcohol (with benzoyl CoA)' has columns Km=97.8 microM, Kcat=4.6 s^-1, and Kcat/Km=47.2 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0978 normalized_unit=mM; Kcat normalized_value=4.6 normalized_unit=s^-1; Kcat/Km normalized_value=47.2 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=97.8 raw_unit=microM; Kcat raw_value=4.6 raw_unit=s^-1; Kcat/Km raw_value=47.2 raw_unit=s^-1*mM^-1

row_label: Cinnamyl alcohol (with benzoyl CoA)

substrate: cinnamyl alcohol


substrate_name: benzyl alcohol

column_label: Table II row 'Benzyl alcohol (with benzoyl CoA)' has columns Km=46.8 microM, Kcat=4.0 s^-1, and Kcat/Km=85.2 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0468 normalized_unit=mM; Kcat normalized_value=4.0 normalized_unit=s^-1; Kcat/Km normalized_value=85.2 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=46.8 raw_unit=microM; Kcat raw_value=4.0 raw_unit=s^-1; Kcat/Km raw_value=85.2 raw_unit=s^-1*mM^-1

row_label: Benzyl alcohol (with benzoyl CoA)


column_label: Table II row 'Benzoyl CoA (with benzyl alcohol)' has columns Km=20.5 microM, Kcat=2.5 s^-1, and Kcat/Km=124.0 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0205 normalized_unit=mM; Kcat normalized_value=2.5 normalized_unit=s^-1; Kcat/Km normalized_value=124.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=20.5 raw_unit=microM; Kcat raw_value=2.5 raw_unit=s^-1; Kcat/Km raw_value=124.0 raw_unit=s^-1*mM^-1

row_label: Benzoyl CoA (with benzyl alcohol)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y47A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row Y47A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.

table_label: Table 4. Steady-State Kinetic Parameters for Selected EcLpxD Mutants


enzyme_display_name: 3,5,7-trioxododecanoyl-CoA synthase

organism: Cannabis sativa

substrate_name: hexanoyl-CoA

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

column_label: Table 1 row Hexanoyl-CoA, Triketide pyrone Km column: 60.8 uM.

raw_value_unit_evidence: Table 1 row Hexanoyl-CoA under Triketide pyrone: Km 60.8 uM.

row_label: Hexanoyl-CoA / Triketide pyrone

table_label: Table 1

enzyme: 3,5,7-trioxododecanoyl-CoA synthase

substrate: hexanoyl-CoA


substrate_name: butyryl-CoA

column_label: Table 1 row Butyryl-CoA, Triketide pyrone Km column: 88.9 uM.

raw_value_unit_evidence: Table 1 row Butyryl-CoA under Triketide pyrone: Km 88.9 uM.

row_label: Butyryl-CoA / Triketide pyrone

substrate: butyryl-CoA