organism: Vigna radiata var. radiata

substrate_name: p-coumaroyltartronic acid

substrate: p-coumaroyltartronic acid


substrate_name: caffeoyltartronic acid

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

substrate: caffeoyltartronic acid

status: unverified

source: brenda


substrate_name: CoA

assay_conditions_summary: cofactor CoA

proof_lines:
+ p-coumaroyltartronic acid
+ caffeoyltartronic acid

substrate: CoA


substrate_name: feruloyltartronic acid

substrate: feruloyltartronic acid


organism: Oryctolagus cuniculus

substrate_name: acetyl-CoA

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

substrate: acetyl-CoA


organism: Rattus norvegicus

assay_conditions_summary: pH 8.4; 296.15 K; cofactor CoA


organism: Homo sapiens

substrate_name: S-benzyl-L-cysteine

protein_accession_database: UniProt

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

data_origin: experimental

source_databases_merged: brenda uniprot

substrate: S-benzyl-L-cysteine


enzyme_display_name: Formyltransferase/hydrolase complex subunit D

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

source_db: uniprot

verification_status: verified

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

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

raw_value_unit_evidence: 30 uM

table_label: Abstract/prose apparent Km values

status: verified

source: uniprot


substrate_name: formyl-MFR

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

raw_value_unit_evidence: 50 uM

row_label: formylMFR

enzyme: Formyltransferase/hydrolase complex subunit D

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


enzyme_display_name: Alcohol O-acetyltransferase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: acetyl-CoA (for acetyltransferase activity)

enzyme: Alcohol O-acetyltransferase 1


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


enzyme_display_name: deacetylvindoline O-acetyltransferase

organism: Catharanthus roseus

substrate_name: Deacetylvindoline; Acetyl-CoA

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

sequence_source: multiple

source_databases_merged: sabio_rk brenda uniprot

enzyme: deacetylvindoline O-acetyltransferase

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

km_display: Not reported

ki_unit: mM

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: 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

source_db: oed

verification_status: corrected

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

status: corrected

source: oed


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


assay_conditions_summary: pH 7; cofactor 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_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt C5XXB7

substrate: shikimate

source: skid


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

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

enzyme: UniProt R9RYW2


enzyme_display_name: UniProt P14743

organism: Saccharomyces cerevisiae

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

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

source_databases_merged: skid uniprot

enzyme: UniProt P14743


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Salmonella enterica

substrate_name: tobramycin

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

enzyme: aminoglycoside 6'-N-acetyltransferase

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

substrate_name: acetyl-CoA

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

substrate: acetyl-CoA


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.

mutation_type: substitution

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.


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


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


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.


kcat_over_km_origin: calculated

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

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

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


organism: Acinetobacter baumannii

substrate_name: gentamicin

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

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.


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

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


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

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

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

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

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


assay_conditions_summary: pH 7; cofactor CoA

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

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


substrate_name: isovaleryl-CoA

column_label: Table 1 row Isovaleryl-CoA, Triketide pyrone Km column: 99.1 uM.

raw_value_unit_evidence: Table 1 row Isovaleryl-CoA under Triketide pyrone: Km 99.1 uM.

row_label: Isovaleryl-CoA / Triketide pyrone

substrate: isovaleryl-CoA


substrate_name: octanoyl-CoA

column_label: Table 1 row Octanoyl-CoA, Triketide pyrone Km column: 81.7 uM.

raw_value_unit_evidence: Table 1 row Octanoyl-CoA under Triketide pyrone: Km 81.7 uM.

row_label: Octanoyl-CoA / Triketide pyrone

substrate: octanoyl-CoA


assay_conditions_summary: pH 6.5; buffer and no single assay pH numeral; cofactor CoA

column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS2'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 1.76; column 'Km (uM)' = 2.3; column 'kcat/Km (M^-1 s^-1)' = 12,716; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 10.0.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS2', salicoyl-CoA group: kcat = 1.76 min^-1; Km = 2.3 uM; printed kcat/Km = 12,716 M^-1 s^-1.

row_label: Table 2, isoenzyme row 'BIS2', salicoyl-CoA starter-substrate block (the three columns headed kcat (min^-1), Km (uM) and kcat/Km (M^-1 s^-1) under the salicoyl-CoA group head)


column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS3'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 2.22; column 'Km (uM)' = 3.2; column 'kcat/Km (M^-1 s^-1)' = 11,486; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 10.1.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS3', salicoyl-CoA group: kcat = 2.22 min^-1; Km = 3.2 uM; printed kcat/Km = 11,486 M^-1 s^-1.

row_label: Table 2, isoenzyme row 'BIS3', salicoyl-CoA starter-substrate block (the three columns headed kcat (min^-1), Km (uM) and kcat/Km (M^-1 s^-1) under the salicoyl-CoA group head)


substrate_name: malonyl-CoA

assay_conditions_summary: pH 6.5; cofactor CoA

proof_lines: kcat is 0.89 min(-1) with benzoyl-CoA as substrate. kcat is 1.76 min(-1) with salicoyl-CoA as substrate.


proof_lines: kcat is 1.02 min(-1) with benzoyl-CoA as substrate. kcat is 2.22 min(-1) with salicoyl-CoA as substrate.


enzyme_display_name: 4-hydroxycoumarin synthase 2

enzyme: 4-hydroxycoumarin synthase 2


enzyme_display_name: 4-hydroxycoumarin synthase 1

enzyme: 4-hydroxycoumarin synthase 1


column_label: Table I BAS WT row, malonyl-CoA columns kcat, Km, and kcat/Km: 1780 +/- 59 x10^-3 min^-1; 23.3 +/- 2.2 uM; 1273 s^-1 M^-1.

raw_value_unit_evidence: BAS WT malonyl-CoA row: kcat 1780 +/- 59 x10^-3 min^-1; Km 23.3 +/- 2.2 uM; independently printed kcat/Km 1273 s^-1 M^-1.

row_label: BAS WT

table_label: Table I. Steady state kinetic parameters for enzyme reactions


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D232A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row D232A; 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F41A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row F41A; 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H239A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row H239A; 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H276A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row H276A; 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K194A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row K194A; 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K46A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row K46A; 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N233A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row N233A; 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q236A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row Q236A; 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R293A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row R293A; 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.


column_label: PMCID PMC2435086 Table 4; row Wild type; 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.

raw_value_unit_evidence: Table 4 row Wild type: kcat 23+/-1 s^-1; KM, UDP-3-O-(R-3-OHC14)-GlcN 2.5+/-0.3 uM.

row_label: Wild type


proof_lines: pH 8.0, 30°C, recombinant wild-type enzyme


proof_lines: kcat is 1.79 min(-1) with 4-coumaroyl-CoA as substrate (at pH 8 and 30 degrees Celsius).


substrate_name: N-methylanthraniloyl-CoA

proof_lines: pH 8.0, temperature not specified in the publication

substrate: N-methylanthraniloyl-CoA


substrate_name: D-phenylalanyl-CoA

substrate: D-phenylalanyl-CoA


substrate_name: Hexanoyl-CoA; Malonyl-CoA

substrate: Hexanoyl-CoA; Malonyl-CoA


substrate_name: Malonyl-CoA; 2-Hydroxybenzoyl-CoA

assay_conditions_summary: buffer and no single assay pH numeral; cofactor CoA

table_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25)

substrate: Malonyl-CoA; 2-Hydroxybenzoyl-CoA


substrate_name: 2-Hydroxybenzoyl-CoA; Malonyl-CoA

substrate: 2-Hydroxybenzoyl-CoA; Malonyl-CoA


enzyme_display_name: Polyketide synthase 4

substrate_name: p-coumaryl CoA

enzyme: Polyketide synthase 4

substrate: p-coumaryl CoA


column_label: Table 3. Kinetic parameters; row VioB O7 / SH-CoA table row resolved by adjacent prose as acetyl-CoA variable-substrate assay; column kcat /s; metric kcat; normalized value 21.6 s^-1 | Table 3. Kinetic parameters and adjacent prose; row VioB O7 / acetyl-CoA variable-substrate assay; column Km (uM); metric km; normalized value 0.554 mM | Table 3. Kinetic parameters; row VioB O7 / acetyl-CoA variable-substrate assay; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 38.98916967509025 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=21.6 normalized_unit=s^-1; km normalized_value=0.554 normalized_unit=mM; kcat_over_km normalized_value=38.98916967509025 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=21.6 raw_unit=s^-1; km raw_value=554 raw_unit=uM; kcat_over_km raw_value=21.6/0.554 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km evidence

table_label: Table 3. Kinetic parameters

substrate: acetyl-CoA


column_label: Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column kcat /s; metric kcat; normalized value 155.3 s^-1 | Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column Km (uM); metric km; normalized value 0.142 mM | Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 1093.6619718309862 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=155.3 normalized_unit=s^-1; km normalized_value=0.142 normalized_unit=mM; kcat_over_km normalized_value=1093.6619718309862 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=155.3 raw_unit=s^-1; km raw_value=142 raw_unit=uM; kcat_over_km raw_value=155.3/0.142 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells

row_label: VioB O7 / dTDP-D-Qui4N


organism: Strongylocentrotus purpuratus

assay_conditions_summary: pH 8; 296.15 K; cofactor CoA

substrate: malonyl-CoA


assay_conditions_summary: pH 7.7; 295.15 K; cofactor CoA

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

row_label: Phenyl ethanol


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

row_label: Acetyl-CoA


column_label: Table I row Benzyl alcohol footnote d columns Km, Kcat, Kcat/Km

row_label: Benzyl alcohol

substrate: benzyl alcohol


enzyme_display_name: UniProt Q9Y7D1

organism: Aspergillus terreus

enzyme: UniProt Q9Y7D1


organism: Streptomyces coelicolor

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y224M with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature Y224L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y224C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y224F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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

assay_conditions_summary: pH 7.4; buffer 100 mM Tris-HCl; cofactor CoA

proof_lines: wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C


assay_conditions_summary: pH 5.5; 303.15 K; cofactor CoA

column_label: Table 1 row Isovaleryl-CoA, Triketide pyrone columns: Km 99.1 uM, kcat 0.585 min^-1, kcat/Km 98.4 s^-1 M^-1.

normalized_value_unit_evidence: Km 0.0991 mM; kcat 0.00975 s^-1; kcat/Km 0.0984 s^-1 mM^-1 from explicit paper column; source kcat and Km are rounded.

raw_value_unit_evidence: Table 1 row Isovaleryl-CoA under Triketide pyrone: Km 99.1 uM; kcat 0.585 min^-1; kcat/Km 98.4 s^-1 M^-1.


substrate_name: Hexanoyl-CoA

substrate: Hexanoyl-CoA


substrate_name: Octanoyl-CoA

column_label: Table 1 row Octanoyl-CoA, Triketide pyrone columns: Km 81.7 uM, kcat 0.525 min^-1, kcat/Km 107 s^-1 M^-1.

normalized_value_unit_evidence: Km 0.0817 mM; kcat 0.00875 s^-1; kcat/Km 0.107 s^-1 mM^-1 from explicit paper column; source values are rounded.

raw_value_unit_evidence: Table 1 row Octanoyl-CoA under Triketide pyrone: Km 81.7 uM; kcat 0.525 min^-1; kcat/Km 107 s^-1 M^-1.

substrate: Octanoyl-CoA


substrate_name: butanoyl-CoA

column_label: Table 1 row Butyryl-CoA, Triketide pyrone columns: Km 88.9 uM, kcat 0.719 min^-1, kcat/Km 134 s^-1 M^-1.

normalized_value_unit_evidence: Km 0.0889 mM; kcat 0.011983333333333334 s^-1; kcat/Km 0.134 s^-1 mM^-1 from explicit paper column; source values are rounded.

raw_value_unit_evidence: Table 1 row Butyryl-CoA under Triketide pyrone: Km 88.9 uM; kcat 0.719 min^-1; kcat/Km 134 s^-1 M^-1.

substrate: butanoyl-CoA


enzyme_display_name: UniProt B0VHH0

organism: Candidatus Cloacimonas acidaminovorans

substrate_name: acetyl-CoA

enzyme: UniProt B0VHH0


enzyme_display_name: 2-heptyl-4(1H)-quinolone synthase subunit PqsC

organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: octanoyl-CoA (in the presence of PqsB)

substrate: octanoyl-CoA (in the presence of PqsB)


substrate_name: 2-ABA (in the presence of PqsB)

enzyme: 2-heptyl-4(1H)-quinolone synthase subunit PqsC

substrate: 2-ABA (in the presence of PqsB)


enzyme_display_name: methanol O-anthraniloyltransferase

organism: Vitis labrusca

substrate_name: methanol

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme

proof_lines: pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, 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: methanol O-anthraniloyltransferase

substrate: methanol


substrate_name: anthraniloyl-CoA

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

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

substrate: anthraniloyl-CoA


enzyme_display_name: Methanol O-anthraniloyltransferase

substrate_name: benzoyl-CoA (with native enzyme, in the presence of benzyl alcohol)

assay_conditions_summary: cofactor CoA

enzyme: Methanol O-anthraniloyltransferase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C171S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; buffer 100 mM Tris-HCl; cofactor CoA

proof_lines: mutant enzyme C171S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C184S with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C184S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C


enzyme_display_name: 3,5-dihydroxyphenylacetyl-CoA synthase

organism: Amycolatopsis mediterranei

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

assay_conditions_summary: pH 7.5; 297.15 K; cofactor CoA

enzyme: 3,5-dihydroxyphenylacetyl-CoA synthase


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


enzyme_display_name: spermidine disinapoyl transferase

organism: Arabidopsis thaliana

substrate_name: putrescine

smiles: C(CCN)CN

assay_conditions_summary: pH 7.3; 303.15 K; buffer vitro forward-reaction assay in 0.1 M Tris-HCl; cofactor CoA

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Forward reaction, Acyl acceptor row Putrescine; the turnover number 0.3 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 236.9 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 0.3 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.3 s^(-1). Km: printed cell 236.9 uM; 1 uM is 0.001 mM, so 236.9 / 1000 = 0.2369 mM; the paper value is 0.2369 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 1.2663571127057829 s^(-1)*mM^(-1) is not a printed value; it is the quotient 0.3 / 0.2369 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Forward reaction, Acyl acceptor row Putrescine: kcat = 0.3 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 236.9 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

source_databases_merged: brenda skid uniprot

enzyme: spermidine disinapoyl transferase

substrate: putrescine


substrate_name: sinapoyl-CoA

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Forward reaction, Acyl donor row Sinapoyl-CoA; the turnover number 5.1 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 8.3 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 5.1 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 5.1 s^(-1). Km: printed cell 8.3 uM; 1 uM is 0.001 mM, so 8.3 / 1000 = 0.0083 mM; the paper value is 0.0083 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 614.4578313253012 s^(-1)*mM^(-1) is not a printed value; it is the quotient 5.1 / 0.0083 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Forward reaction, Acyl donor row Sinapoyl-CoA: kcat = 5.1 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 8.3 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

substrate: sinapoyl-CoA


substrate_name: spermidine

smiles: C(CCNCCCN)CN

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Forward reaction, Acyl acceptor row Spermidine; the turnover number 5.6 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 37.4 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 5.6 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 5.6 s^(-1). Km: printed cell 37.4 uM; 1 uM is 0.001 mM, so 37.4 / 1000 = 0.0374 mM; the paper value is 0.0374 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 149.7326203208556 s^(-1)*mM^(-1) is not a printed value; it is the quotient 5.6 / 0.0374 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Forward reaction, Acyl acceptor row Spermidine: kcat = 5.6 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 37.4 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

substrate: spermidine


assay_conditions_summary: pH 7.3; 303.15 K; buffer 0.1 M Tris-HCl; cofactor CoA

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Reverse reaction, row Disinapoyl spermidine; the turnover number 37.8 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 34.6 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 37.8 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 37.8 s^(-1). Km: printed cell 34.6 uM; 1 uM is 0.001 mM, so 34.6 / 1000 = 0.0346 mM; the paper value is 0.0346 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 1092.4855491329479 s^(-1)*mM^(-1) is not a printed value; it is the quotient 37.8 / 0.0346 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Reverse reaction, row Disinapoyl spermidine: kcat = 37.8 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 34.6 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.


substrate_name: CoA

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Reverse reaction, row CoA; the turnover number 39.6 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 83.6 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 39.6 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 39.6 s^(-1). Km: printed cell 83.6 uM; 1 uM is 0.001 mM, so 83.6 / 1000 = 0.0836 mM; the paper value is 0.0836 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 473.68421052631584 s^(-1)*mM^(-1) is not a printed value; it is the quotient 39.6 / 0.0836 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Reverse reaction, row CoA: kcat = 39.6 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 83.6 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

row_label: Table 1, Reverse reaction, row CoA

substrate: CoA


enzyme_display_name: phloroglucinol synthase

organism: Pseudomonas fluorescens

substrate_name: malonyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y256R/A289R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y256R/A289R, pH and temperature not specified in the publication

enzyme: phloroglucinol synthase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K210L/Y256R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K210L/Y256R, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A289R with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A289R, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y256R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y256R, pH and temperature not specified in the publication


enzyme_display_name: spermidine dicoumaroyl transferase

column_label: Table 2: Kinetics of Recombinant At2g25150 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 2, Acyl acceptor row Spermidine; the turnover number 3.1 s^-1 comes from the kcat (s^-1) column of Table 2 and the Michaelis constant 52.7 uM comes from the Km (uM) column of Table 2. Table 2 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 3.1 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 3.1 s^(-1). Km: printed cell 52.7 uM; 1 uM is 0.001 mM, so 52.7 / 1000 = 0.0527 mM; the paper value is 0.0527 mM. kcat/Km: Table 2 prints no kcat/Km cell for this measurement, so the exported 58.82352941176471 s^(-1)*mM^(-1) is not a printed value; it is the quotient 3.1 / 0.0527 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, Acyl acceptor row Spermidine: kcat = 3.1 s^-1 (printed column the kcat (s^-1) column of Table 2); Km = 52.7 uM (printed column the Km (uM) column of Table 2). Table 2 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

row_label: Table 2, Acyl acceptor row Spermidine

enzyme: spermidine dicoumaroyl transferase


column_label: Table 2: Kinetics of Recombinant At2g25150 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 2, Acyl donor row Coumaroyl-CoA; the turnover number 3.4 s^-1 comes from the kcat (s^-1) column of Table 2 and the Michaelis constant 10.6 uM comes from the Km (uM) column of Table 2. Table 2 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 3.4 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 3.4 s^(-1). Km: printed cell 10.6 uM; 1 uM is 0.001 mM, so 10.6 / 1000 = 0.0106 mM; the paper value is 0.0106 mM. kcat/Km: Table 2 prints no kcat/Km cell for this measurement, so the exported 320.75471698113205 s^(-1)*mM^(-1) is not a printed value; it is the quotient 3.4 / 0.0106 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, Acyl donor row Coumaroyl-CoA: kcat = 3.4 s^-1 (printed column the kcat (s^-1) column of Table 2); Km = 10.6 uM (printed column the Km (uM) column of Table 2). Table 2 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

row_label: Table 2, Acyl donor row Coumaroyl-CoA


organism: Streptomyces griseus

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

proof_lines: in 100 mM Tris-HCl (pH 7.5), 1 mM EDTA, 1 mM 2-mercaptoethanol, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S82G to reconstruct the assayed variant sequence.

column_label: Official PMC HTML Table 2, row S82G, columns Km (S)-KAH, kcat, and kcat/Km ((S)-KAH), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.13 normalized_unit=s^-1; km normalized_value=1.181 normalized_unit=mM; kcat_over_km normalized_value=0.1 normalized_unit=s^-1 mM^-1.

table_label: Table 2. Steady-state kinetic analysis of Kce and point mutants


column_label: Official PMC HTML Table 2, row S82G, columns Km AcCoA, kcat, and kcat/Km (AcCoA), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.13 normalized_unit=s^-1; km normalized_value=0.046 normalized_unit=mM; kcat_over_km normalized_value=2.8 normalized_unit=s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E143Q to reconstruct the assayed variant sequence.

column_label: Official PMC HTML Table 2, row E143Q, columns Km (S)-KAH, kcat, and kcat/Km ((S)-KAH), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.32 normalized_unit=s^-1; km normalized_value=0.442 normalized_unit=mM; kcat_over_km normalized_value=0.7 normalized_unit=s^-1 mM^-1.


column_label: Official PMC HTML Table 2, row E143Q, columns Km AcCoA, kcat, and kcat/Km (AcCoA), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.32 normalized_unit=s^-1; km normalized_value=0.012 normalized_unit=mM; kcat_over_km normalized_value=26.7 normalized_unit=s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E143G to reconstruct the assayed variant sequence.

column_label: Official PMC HTML Table 2, row E143G, columns Km (S)-KAH, kcat, and kcat/Km ((S)-KAH), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.37 normalized_unit=s^-1; km normalized_value=0.921 normalized_unit=mM; kcat_over_km normalized_value=0.4 normalized_unit=s^-1 mM^-1.


column_label: Official PMC HTML Table 2, row E143G, columns Km AcCoA, kcat, and kcat/Km (AcCoA), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.37 normalized_unit=s^-1; km normalized_value=0.024 normalized_unit=mM; kcat_over_km normalized_value=15.4 normalized_unit=s^-1 mM^-1.


column_label: Official PMC HTML Table 2, row Wild type, columns Km (S)-KAH, kcat, and kcat/Km ((S)-KAH), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=2.69 normalized_unit=s^-1; km normalized_value=0.208 normalized_unit=mM; kcat_over_km normalized_value=12.9 normalized_unit=s^-1 mM^-1.


column_label: Official PMC HTML Table 2, row Wild type, columns Km AcCoA, kcat, and kcat/Km (AcCoA), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=2.69 normalized_unit=s^-1; km normalized_value=0.012 normalized_unit=mM; kcat_over_km normalized_value=224.2 normalized_unit=s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y224L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


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


substrate_name: Methanol; Anthraniloyl-CoA

substrate: Methanol; Anthraniloyl-CoA


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

substrate_name: 5 malonyl-CoA

proof_lines: kcat is 0.48 min(-1) for THN synthase activity with THN as substrate.

substrate: 5 malonyl-CoA


enzyme_display_name: Spermidine sinapoyl-CoA acyltransferase

substrate_name: disinapoyl-spermidine (with CoA as cosubstrate, at 30 degrees Celsius)

proof_lines: kcat is 5.1 sec(-1) with sinapoyl-CoA as substrate (in the presence of spermidine as the acyl acceptor). kcat is 5.6 sec(-1) with spermidine as substrate (in the presence of sinapoyl-CoA as the acyl donor). kcat is 0.3 sec(-1) with putresci

enzyme: Spermidine sinapoyl-CoA acyltransferase


organism: Amycolatopsis orientalis

proof_lines: kcat is 1 min(-1) for transferase activity with malonyl-CoA as substrate.


organism: Amycolatopsis balhimycina

proof_lines: kcat is 0.81 min(-1) for transferase activity with malonyl-CoA as substrate.


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

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


smiles: CC/C=C\CCO

assay_conditions_summary: pH 7.7; 298.15 K; cofactor CoA


substrate: acetyl-CoA


enzyme_display_name: 3-keto-5-aminohexanoate cleavage enzyme

organism: Cloacimonas acidaminovorans (strain Evry)

substrate_name: KAH

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

column_label: Official PMC HTML Table 2, row Wild type, column Km (S)-KAH, HTML lines 1798-1880.

raw_value_unit_evidence: Table 2 row Wild type, Km (S)-KAH column = 0.208 +/- 0.032 mM.

enzyme: 3-keto-5-aminohexanoate cleavage enzyme

substrate: KAH


substrate_name: acetoacetate

proof_lines: kcat is 2.69 sec(-1) for 3-keto-5-aminohexanoate cleavage.

substrate: acetoacetate


enzyme_display_name: Phloroglucinol synthase

organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)

column_label: PMID 15826166 primary JACS prose, purified PhlD enzymology segment, malonyl-CoA Km = 5.6 uM.

raw_value_unit_evidence: Primary prose reports a Km = 5.6 uM for malonyl-CoA and a kcat = 10 min-1 determined for PhlD.

row_label: Purified PhlD / malonyl-CoA

table_label: Primary prose enzymology section in PMID 15826166

enzyme: Phloroglucinol synthase

substrate: malonyl-CoA


organism: Salmonella enterica subsp. enterica serovar Typhimurium

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C


substrate_name: 4-aminobutylphosphonic acid

smiles: C(CCP(=O)(O)O)CN

substrate: 4-aminobutylphosphonic acid


substrate_name: 1-aminobutyl phosphonic acid

substrate: 1-aminobutyl phosphonic acid


substrate_name: (aminomethyl)phosphonate

substrate: (aminomethyl)phosphonate


substrate_name: 2-aminoethyl phosphonic acid

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

substrate: 2-aminoethyl phosphonic acid


substrate_name: acetyl-CoA


substrate_name: (S)-1-aminoethylphosphonic acid

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

substrate: (S)-1-aminoethylphosphonic acid


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: 2-aminoethanesulfonic acid

substrate: 2-aminoethanesulfonic acid


substrate_name: 2-aminoethanesulfinic acid

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

substrate: 2-aminoethanesulfinic acid


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

substrate_name: 3-aminopropylphosphonate (in the presence of Ni(2+))

proof_lines: kcat is 13.1 sec(-1) for the acetylation of (S)-1AEP. kcat is 14.7 sec(-1) for the propionylation of (S)-1AEP. kcat is 0.4 sec(-1) for the malonylation of (S)-1AEP. kcat is 7.0 sec(-1) for the acetylation of aminomethylphosphonate. kcat is


organism: Mycobacterium tuberculosis

proof_lines: kcat is 0.12 min(-1) with trehalose-2-sulfate-2'-palmitate as substrate.


organism: Mycobacterium marinum

substrate_name: glycosyl-phenolphthiocerol

substrate: glycosyl-phenolphthiocerol


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: mycoserosate acylated to mas protein

substrate: mycoserosate acylated to mas protein


organism: Papaver somniferum


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


enzyme_display_name: 4-hydroxycoumarin synthase

organism: Sorbus aucuparia

assay_conditions_summary: pH 7; 308.15 K; buffer and no single assay pH numeral; cofactor CoA

column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS2'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 1.76; column 'Km (uM)' = 2.3; column 'kcat/Km (M^-1 s^-1)' = 12,716; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 10.0.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS2', salicoyl-CoA group: kcat = 1.76 min^-1; Km = 2.3 uM; printed kcat/Km = 12,716 M^-1 s^-1.

enzyme: 4-hydroxycoumarin synthase


column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS3'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 2.22; column 'Km (uM)' = 3.2; column 'kcat/Km (M^-1 s^-1)' = 11,486; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 10.1.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS3', salicoyl-CoA group: kcat = 2.22 min^-1; Km = 3.2 uM; printed kcat/Km = 11,486 M^-1 s^-1.


column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS1'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 0.27; column 'Km (uM)' = 0.8; column 'kcat/Km (M^-1 s^-1)' = 5,625; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 6.2.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS1', salicoyl-CoA group: kcat = 0.27 min^-1; Km = 0.8 uM; printed kcat/Km = 5,625 M^-1 s^-1.

row_label: Table 2, isoenzyme row 'BIS1', salicoyl-CoA starter-substrate block (the three columns headed kcat (min^-1), Km (uM) and kcat/Km (M^-1 s^-1) under the salicoyl-CoA group head)


organism: Aneurinibacillus thermoaerophilus

assay_conditions_summary: pH 7.4; cofactor CoA

column_label: Main text FdtC kinetic paragraph names dTDP-d-Fucp3N first and gives first Km/kcat values respectively.

normalized_value_unit_evidence: Km 0.0667 mM; kcat 2.3 s^-1; kcat/Km 34.48275862068966 s^-1 mM^-1 derived from paper values


assay_conditions_summary: pH 7.4; 310.15 K; 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


enzyme_display_name: tRNA(Met) cytidine acetyltransferase TmcA

organism: Escherichia coli (strain K12)

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: GTP

enzyme: tRNA(Met) cytidine acetyltransferase TmcA

substrate: GTP


organism: Vitis labrusca

substrate_name: anthraniloyl-CoA

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

substrate: anthraniloyl-CoA


substrate_name: methanol

substrate: methanol


smiles: CCCCCCCCCCC(C)O


substrate_name: lauroyl-CoA

substrate: lauroyl-CoA


organism: Escherichia coli

substrate_name: Acetyl-CoA

column_label: Table 3. Kinetic parameters; row VioB O7 / SH-CoA table row resolved by adjacent prose as acetyl-CoA variable-substrate assay; column kcat /s; metric kcat; normalized value 21.6 s^-1 | Table 3. Kinetic parameters and adjacent prose; row VioB O7 / acetyl-CoA variable-substrate assay; column Km (uM); metric km; normalized value 0.554 mM | Table 3. Kinetic parameters; row VioB O7 / acetyl-CoA variable-substrate assay; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 38.98916967509025 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=21.6 normalized_unit=s^-1; km normalized_value=0.554 normalized_unit=mM; kcat_over_km normalized_value=38.98916967509025 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=21.6 raw_unit=s^-1; km raw_value=554 raw_unit=uM; kcat_over_km raw_value=21.6/0.554 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km evidence

substrate: Acetyl-CoA


column_label: Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column kcat /s; metric kcat; normalized value 155.3 s^-1 | Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column Km (uM); metric km; normalized value 0.142 mM | Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 1093.6619718309862 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=155.3 normalized_unit=s^-1; km normalized_value=0.142 normalized_unit=mM; kcat_over_km normalized_value=1093.6619718309862 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=155.3 raw_unit=s^-1; km raw_value=142 raw_unit=uM; kcat_over_km raw_value=155.3/0.142 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


enzyme_display_name: benzalacetone synthase

organism: Rubus idaeus

substrate_name: malonyl-CoA

assay_conditions_summary: pH 9.5; cofactor CoA

proof_lines:
pH 9.5, 35°C
at pH 9.5 and 50°C
pH 8.0, 30°C

enzyme: benzalacetone synthase

substrate: malonyl-CoA


enzyme_display_name: benzyl alcohol O-benzoyltransferase

substrate_name: benzoyl-CoA

assay_conditions_summary: pH 7.5; 295.15 K; buffer 50 mM Tris-HCl pH 7; cofactor CoA

column_label: Table 2, Benzoyl-CoA (with benzyl alcohol) row, native purified protein N columns: Km 11.80 uM; kcat 0.045 s^-1; specificity 3.81. Footnote: N = native purified protein from mature grape; R = recombinant purified protein from E. coli.

normalized_value_unit_evidence: Paper Km 11.80 uM converts to 0.01180 mM; paper kcat is 0.045 s^-1; the printed specificity value is 3.81 s^-1 mM^-1. The export specificity value is 3.8135593220338984 s^-1 mM^-1 and does not exactly equal the printed value.

raw_value_unit_evidence: Table 2 native-protein columns report benzoyl-CoA Km = 11.80 uM, kcat = 0.045 s^-1, and specificity = 3.81 with benzyl alcohol. The footnote defines N as native purified protein from mature grape.

row_label: Benzoyl-CoA (with benzyl alcohol)

table_label: Primary-paper Table 2: Kinetic parameters of AMAT

enzyme: benzyl alcohol O-benzoyltransferase

substrate: benzoyl-CoA


organism: Rheum palmatum

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

column_label: PMID 12724310/JBC Table I, BAS WT row, 4-Coumaroyl-CoA column group: kcat = 1790 +/- 54 x 10^-3 min^-1, Km = 10.0 +/- 2.1 uM, kcat/Km = 2963 s^-1 M^-1.

raw_value_unit_evidence: Table I reports kcat = 1790 +/- 54 x 10^-3 min^-1, Km = 10.0 +/- 2.1 uM, and kcat/Km = 2963 s^-1 M^-1 for BAS WT with 4-coumaroyl-CoA.

row_label: BAS WT / Benzalacetone / pH optimum 8.0 / 4-Coumaroyl-CoA

table_label: JBC 2003 Table I. Steady state kinetic parameters for enzyme reactions


column_label: PMID 12724310 Table I, BAS WT row, Malonyl-CoA column group: kcat = 1780 +/- 59 x 10^-3 min^-1, Km = 23.3 +/- 2.2 uM, kcat/Km = 1273 s^-1 M^-1.

raw_value_unit_evidence: Table I reports kcat = 1780 +/- 59 x 10^-3 min^-1, Km = 23.3 +/- 2.2 uM, and kcat/Km = 1273 s^-1 M^-1 for BAS WT with malonyl-CoA.

row_label: BAS WT / Benzalacetone / pH optimum 8.0 / malonyl-CoA


organism: Pseudomonas fluorescens

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

column_label: PMID 16931521 abstract and Kinetics/Stability prose, PhlD / malonyl-CoA: kcat = 24 +/- 4 min^-1, Km = 13 +/- 1 uM, kcat/Km = 1883 mM^-1 min^-1.

raw_value_unit_evidence: Paper reports kcat = 24 +/- 4 min^-1, Km = 13 +/- 1 uM, and kcat/Km = 1883 mM^-1 min^-1 for PhlD with malonyl-CoA.

row_label: PhlD / malonyl-CoA

table_label: Abstract and Kinetics/Stability prose


organism: Clarkia breweri

assay_conditions_summary: pH 7.7; 295.15 K; cofactor CoA


organism: Streptomyces coelicolor

assay_conditions_summary: pH 7.5; cofactor CoA

column_label: Page 513, Kinetic parameters for THN formation: recombinant wild-type S. coelicolor THNS kcat 0.48 +/- 0.03 min^-1 and Km 3.58 +/- 0.85 uM for malonyl-CoA-to-THN formation.

row_label: wild-type THNS malonyl-CoA measurement

table_label: page 513, Kinetic parameters for THN formation


substrate_name: acetyl-CoA (in the presence of Ni(2+))

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA (in the presence of Ni(2+))


substrate_name: propionyl-CoA (in the presence of Ni(2+))


substrate_name: malonyl-CoA (in the presence of Ni(2+))

substrate: malonyl-CoA (in the presence of Ni(2+))


substrate_name: aminomethylphosphonate (in the presence of Ni(2+))


substrate_name: 2-aminoethylphosphonate (in the presence of Ni(2+))


substrate_name: (S)-1-aminoethylphosphonate (in the presence of Ni(2+))


substrate_name: 2-aminoethanesulfonate (in the presence of Ni(2+))


substrate_name: 2-aminoethanesulfinate (in the presence of Ni(2+))


enzyme_display_name: chlorogenate caffeoyltransferase

organism: Solanum lycopersicum

substrate_name: chlorogenic acid

enzyme: chlorogenate caffeoyltransferase

substrate: chlorogenic acid


organism: Ipomoea batatas

substrate_name: chlorogenate

substrate: chlorogenate


enzyme_display_name: 2-amino-4-oxopentanoate thiolase

organism: Pelosinus propionicus

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

proof_lines: pH 7.5, 22°C, recombinant His-tagged enzyme, calculated by BRENDA

enzyme: 2-amino-4-oxopentanoate thiolase


organism: Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M)

substrate_name: acetyl-CoA

column_label: Official Nature Chemical Biology Supplementary Information PDF, Supplementary Table 6a, row BKACE_274 / acetylCoA, column KM (uM), raw value 252 +/- 37.

normalized_value_unit_evidence: 252 uM acetylCoA = 0.252 mM, matching exported Km 0.252 mM.

raw_value_unit_evidence: Supplementary Table 6a reports BKACE_274 acetylCoA KM (uM) = 252 +/- 37.

row_label: BKACE_274 (BKACE G1), acetylCoA, footnote q

table_label: Supplementary Table 6a: Enzymatic kinetics assays

substrate: acetyl-CoA


enzyme_display_name: 2-amino-4-ketopentanoate thiolase alpha subunit

organism: Unknown prokaryotic organism

substrate_name: CoA

column_label: Table 1 row AKPT / CoA-SH column Km

row_label: AKPT / CoA-SH

substrate: CoA


substrate_name: AKP

column_label: Table 1 row AKPT / AKP column Km

row_label: AKPT / AKP

enzyme: 2-amino-4-ketopentanoate thiolase alpha subunit

substrate: AKP


enzyme_display_name: 2-amino-4-ketopentanoate thiolase beta subunit


enzyme: 2-amino-4-ketopentanoate thiolase beta subunit


organism: Taxus sp.

proof_lines: with 3'-N-debenzoyltaxol as cosubstrate, at pH 7.5 and 31°C

proof_lines: with N-debenzoyl-2'-deoxytaxol as cosubstrate, at pH 7.5 and 31°C


organism: Taxus cuspidata

substrate_name: baccatin III

proof_lines: pH and temperature not specified in the publication

substrate: baccatin III


organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

substrate_name: beta-ketoglutarate

column_label: Official Nature Chemical Biology Supplementary Information PDF, Supplementary Table 6a, row BKACE_378 / beta-ketoglutarate, column KM (uM), raw value 1350 +/- 470.

normalized_value_unit_evidence: 1350 uM beta-ketoglutarate = 1.35 mM, matching exported Km 1.35 mM.

raw_value_unit_evidence: Supplementary Table 6a reports BKACE_378 beta-ketoglutarate KM (uM) = 1350 +/- 470.

row_label: BKACE_378 (BKACE G4), beta-ketoglutarate, footnote h

substrate: beta-ketoglutarate


substrate_name: beta-ketohexanoate

proof_lines: kcat is 0.97 sec(-1) with acetyl-CoA as substrate. kcat is 0.03 sec(-1) with beta-keto-5-aminohexanoate as substrate.

substrate: beta-ketohexanoate


organism: Pseudomonas aeruginosa

substrate_name: Malonyl-CoA; Anthraniloyl-CoA

substrate: Malonyl-CoA; Anthraniloyl-CoA


enzyme_display_name: ethanol O-acetyltransferase

organism: Wickerhamomyces anomalus

substrate_name: Ethanol; Acetyl-CoA

enzyme: ethanol O-acetyltransferase

substrate: Ethanol; Acetyl-CoA


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: 1-aminobutyl phosphonic acid

smiles: CCCC(N)P(=O)(O)O

column_label: Table 1 part B; row 1-aminobutyl phosphonic acid; column Km (mM) raw value 12.5; column kcat (s^-1) raw value 1; column kcat/Km (M^-1 s^-1) raw value (8.0 +/- 0.5) x 10^1

normalized_value_unit_evidence: kcat normalized_value=1 normalized_unit=s^-1; Km normalized_value=12.5 normalized_unit=mM; kcat/Km normalized_value=0.08 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1 raw_unit=s^-1; Km raw_value=12.5 raw_unit=mM; kcat/Km raw_value=(8.0 +/- 0.5) x 10^1 raw_unit=M^-1*s^-1

row_label: 1-aminobutyl phosphonic acid / PhnO Table 1 part B

table_label: Table 1. Kinetic parameters for PhnO with various acyl-CoAs and aminoalkylphosphonates

substrate: 1-aminobutyl phosphonic acid


substrate_name: 1-aminopropyl phosphonic acid

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

column_label: Table 1 part B; row 1-aminopropyl phosphonic acid; column Km (mM) raw value 4.1; column kcat (s^-1) raw value 7.4; column kcat/Km (M^-1 s^-1) raw value (1.8 +/- 0.1) x 10^3

normalized_value_unit_evidence: kcat normalized_value=7.4 normalized_unit=s^-1; Km normalized_value=4.1 normalized_unit=mM; kcat/Km normalized_value=1.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=7.4 raw_unit=s^-1; Km raw_value=4.1 raw_unit=mM; kcat/Km raw_value=(1.8 +/- 0.1) x 10^3 raw_unit=M^-1*s^-1

row_label: 1-aminopropyl phosphonic acid / PhnO Table 1 part B

substrate: 1-aminopropyl phosphonic acid


substrate_name: 2-aminoethanesulfinic acid

smiles: NCCS(=O)O

column_label: Table 1 part B; row 2-aminoethanesulfinic acid; column Km (mM) raw value 16.4; column kcat (s^-1) raw value 20; column kcat/Km (M^-1 s^-1) raw value (1.2 +/- 0.1) x 10^3

normalized_value_unit_evidence: kcat normalized_value=20 normalized_unit=s^-1; Km normalized_value=16.4 normalized_unit=mM; kcat/Km normalized_value=1.2 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=20 raw_unit=s^-1; Km raw_value=16.4 raw_unit=mM; kcat/Km raw_value=(1.2 +/- 0.1) x 10^3 raw_unit=M^-1*s^-1

row_label: 2-aminoethanesulfinic acid / PhnO Table 1 part B

substrate: 2-aminoethanesulfinic acid