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

proof_lines:
pH 7.8, 30°C, cosubstrate adipyl-CoA
pH 7.8, 30°C, cosubstrate glutaryl-CoA
pH 7.8, 30°C, cosubstrate succinyl-CoA


organism: Rattus norvegicus

substrate_name: malonate

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7.8; cofactor CoA

proof_lines: pH 7.8, 30°C, cosubstrate 3-hydroxy-3-methylglutaryl-CoA , reverse reaction

proof_lines: pH 7.8, 30°C, cosubstrate succinyl-CoA or methylmalonyl-CoA

data_origin: experimental

substrate: malonate

status: unverified

source: brenda


substrate_name: methylmalonate

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

proof_lines: pH 7.8, 30°C, cosubstrate 3-hydroxy-3-methylglutaryl-CoA, reverse reaction

substrate: methylmalonate


enzyme_display_name: L-cysteine S-thiosulfotransferase subunit SoxA

organism: Ancylobacter novellus (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIMB 10456)

substrate_name: glutathione (at pH 6.0)

source_db: uniprot

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

assay_conditions_summary: pH 6

proof_lines: kcat is 8.72 sec(-1) and 5.7 sec(-1) for glutathione at pH 6.0 and pH 7.0, respectively.

substrate: glutathione (at pH 6.0)

source: uniprot


substrate_name: succinylCoA

proof_lines:
pH 7.8, 30°C, cosubstrate malonate
pH 8.5, 30°C

substrate: succinylCoA


enzyme_display_name: formyl-CoA transferase

organism: Oxalobacter formigenes

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

assay_conditions_summary: pH 6.7; cofactor CoA

proof_lines: chloride is a weak competitive inhibitor to oxalate

proof_lines: kcat is 5.3 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius). kcat is 149 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with succinate as acce

source_databases_merged: brenda uniprot

enzyme: formyl-CoA transferase

substrate: Unknown


enzyme_display_name: L-cysteine S-thiosulfotransferase

substrate_name: oxalate

sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.

proof_lines: W48Q FRC, the W48F FRC is not inhibited by oxalate at concentrations of up to 154 mM

enzyme: L-cysteine S-thiosulfotransferase

substrate: oxalate


enzyme: L-cysteine S-thiosulfotransferase subunit SoxA


enzyme_display_name: tRNA 2-selenouridine synthase

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

substrate_name: selenophosphate

verification_status: verified

column_label: Abstract states reaction velocity dependence on selenophosphate concentration obeys Michaelis-Menten kinetics indicating an apparent Km value of 17.1 microM.

raw_value_unit_evidence: Km raw_value=17.1 raw_unit=microM

row_label: Salmonella typhimurium tRNA 2-selenouridine synthase with selenophosphate

table_label: PubMed/PMC abstract PMID 7520175

enzyme: tRNA 2-selenouridine synthase

substrate: selenophosphate

status: verified


organism: Acetobacter aceti

substrate_name: formyl-CoA

source_db: oed

kcat_over_km_origin: calculated

assay_conditions_summary: pH 6.7; 298.15 K; cofactor CoA

column_label: Table I Formyl-CoA row: kcat 4.5 s^-1 and Km 3.4 uM; the exact same-row cells yield 1323.5294117647059 s^-1 mM^-1. Footnote c says determined at 50 mM oxalate.

raw_value_unit_evidence: Formyl-CoA row reports kcat/Km (1.3 +/- 0.2) x 10^6 M^-1 s^-1 with kcat 4.5 s^-1 and Km 3.4 uM in the same row.

row_label: Formyl-CoA row for H6UctB

table_label: Table I. Kinetic Constants

substrate: formyl-CoA

source: oed


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

column_label: Table I Oxalate row: kcat 5.00 s^-1 and Km 1.11 mM; the exact same-row cells yield 4.504504504504504 s^-1 mM^-1. Footnote b says determined at 0.1 mM formyl-CoA.

raw_value_unit_evidence: Oxalate row reports kcat/Km (4.5 +/- 0.4) x 10^3 M^-1 s^-1 with kcat 5.00 s^-1 and Km 1.11 mM in the same row.

row_label: Oxalate row for H6UctB


enzyme_display_name: Molybdopterin biosynthesis protein CNX1

organism: Arabidopsis thaliana

substrate_name: ATP for domain G

assay_conditions_summary: cofactor ATP

enzyme: Molybdopterin biosynthesis protein CNX1

substrate: ATP for domain G


substrate_name: Zn(2+) for domain E

substrate: Zn(2+) for domain E


substrate_name: Mg(2+) for domain E

substrate: Mg(2+) for domain E


organism: Escherichia coli

substrate_name: Selenophosphate; tRNA containing 5-methylaminomethyl-2-(S-geranyl)thiouridine; H2O

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

proof_lines: kcat is 0.00014 min(-1) for the geranylation reaction. kcat is 0.53 min(-1) for the selenation reaction.


sequence_source: multiple


enzyme_display_name: citrate CoA-transferase

organism: Klebsiella aerogenes

substrate_name: acetyl-CoA

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

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

proof_lines: pH 8.0, 25°C, integrated into deacetyl citrate lyase

enzyme: citrate CoA-transferase

substrate: acetyl-CoA


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: acetyl-dephospho-CoA

substrate: acetyl-dephospho-CoA


enzyme_display_name: molybdopterin molybdotransferase

substrate_name: molybdate

proof_lines: in presence of Mg2+, pH 7.2, temperature not specified in the publication

proof_lines: in presence of Zn2+, pH 7.2, temperature not specified in the publication

enzyme: molybdopterin molybdotransferase

substrate: molybdate


enzyme_display_name: L-seryl-tRNASec selenium transferase

substrate_name: thiophosphate

enzyme: L-seryl-tRNASec selenium transferase

substrate: thiophosphate


substrate_name: Selenophosphate

substrate: Selenophosphate


assay_conditions_summary: cofactor CoA


enzyme_display_name: hexokinase

organism: Mus musculus

substrate_name: ATP; D-Glucose

enzyme: hexokinase

substrate: ATP; D-Glucose


organism: Clostridium sporogenes

substrate_name: (E)-cinnamoyl-CoA (at pH 7 and 25 degrees Celsius)

assay_conditions_summary: cofactor NADH


substrate_name: 3-phenylpropanoate (at pH 7 and 25 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: Clostridium sporogenes phenyllactate dehydratase


enzyme_display_name: Succinyl-CoA:(R)-benzylsuccinate CoA-transferase subunit BbsF

organism: Thauera aromatica

column_label: Results prose reports K_m = 40 +/- 8 uM for 2- plus 3-(R)-benzylsuccinyl-CoA, calculated from the best-fitting ternary-complex equation.

row_label: 2- plus 3-(R)-benzylsuccinyl-CoA

table_label: Results prose kinetic parameters; Figure 4 supporting double-reciprocal plot


substrate_name: succinate

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

column_label: Results prose reports K_m = 160 +/- 30 uM for succinate, calculated from the best-fitting ternary-complex equation.

row_label: succinate

enzyme: Succinyl-CoA:(R)-benzylsuccinate CoA-transferase subunit BbsF

substrate: succinate


enzyme_display_name: Succinyl-CoA:(R)-benzylsuccinate CoA-transferase subunit BbsE


enzyme: Succinyl-CoA:(R)-benzylsuccinate CoA-transferase subunit BbsE


substrate_name: ATP

substrate: ATP


organism: Mycobacterium tuberculosis

substrate_name: Unknown

proof_lines: bound to the pyridoxamine 5'-phosphate form, 100 mM EPPS buffer, pH 8.6

proof_lines: binding to the the pyridoxamine 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication

substrate: Unknown


enzyme_display_name: selenide, water dikinase

proof_lines: SPS2-CYS protein expressed in Escherichia coli

enzyme: selenide, water dikinase


substrate_name: D-glucose

proof_lines: pH and temperature not specified in the publication

substrate: D-glucose


organism: Oncorhynchus mykiss

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


assay_conditions_summary: pH 7.2; 295.15 K; cofactor ATP


organism: Oryctolagus cuniculus

substrate_name: ATP; D-Fructose 6-phosphate

assay_conditions_summary: pH 7.1; cofactor ATP

substrate: ATP; D-Fructose 6-phosphate


smiles: CC(C(=O)CCCCCC(=O)[O-])N


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: MgATP2-, bound mitochondrial HK I, at pH 7.5

proof_lines: MgATP2-, solubilized mitochondrial HK I, at pH 7.5


substrate_name: N-acetyl-D-glucosamine

proof_lines: erythrocyte enzyme, competitive to glucose

substrate: N-acetyl-D-glucosamine


enzyme_display_name: fructokinase

organism: Oryza sativa

substrate_name: D-fructose

enzyme: fructokinase

substrate: D-fructose


organism: Plasmodium falciparum


enzyme_display_name: salicylate 1-monooxygenase

organism: Pseudomonas fluorescens

substrate_name: salicylate

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

enzyme: salicylate 1-monooxygenase

substrate: salicylate


organism: Pseudomonas putida


enzyme_display_name: N-acetylmuramate 1-kinase

enzyme: N-acetylmuramate 1-kinase


organism: Pseudomonas sp.

substrate_name: NADH

proof_lines:
cosubstrate salicylate
cosubstrate p-aminosalicylate
enzyme form NahU

substrate: NADH


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


enzyme_display_name: gluconokinase

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

enzyme: gluconokinase


organism: Rattus norvegicus

smiles: C(C(C(C(C(C=O)F)O)O)O)O

proof_lines:
HK I, at 25°C, pH 7.4
HK II, at 25°C, pH 7.4


enzyme_display_name: ethanolaminephosphotransferase

substrate_name: CDP-ethanolamine

proof_lines:
cosubstrate 1,2-dioleoyl-sn-glycerol
30°C, pH 8.0

enzyme: ethanolaminephosphotransferase

substrate: CDP-ethanolamine


substrate_name: ATP; Glucose

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: catalytically active 51 kDa C fragment of hexokinase

substrate: ATP; Glucose


substrate_name: Adenylyl-molybdopterin; Molybdate

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

substrate: Adenylyl-molybdopterin; Molybdate


substrate_name: Cinnamoyl-CoA; Phenylpropanoate

substrate: Cinnamoyl-CoA; Phenylpropanoate


enzyme_display_name: L-cysteine S-thiosulfotransferase subunit SoxA

organism: Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)

substrate_name: thiosulfate using purified SoxAX-CT1020, SoxYZ and SoxB in the assay system (at pH 6.0)


organism: Paracoccus pantotrophus

substrate_name: thiosulfate using purified SoxAX complex (at pH 7.5)


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

proof_lines:
rat brain enzyme, hexokinase I
bovine heart enzyme, hexokinase II
HKI, at 25°C, pH 7.4


enzyme_display_name: glutamine-phenylpyruvate transaminase

substrate_name: L-glutamine

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

proof_lines:
pH 9.0, 37.5°C
pH 7.0, 30°C
pH 8.5, 37°C, phenylpyruvate

enzyme: glutamine-phenylpyruvate transaminase

substrate: L-glutamine


substrate_name: ATP

assay_conditions_summary: pH 8.4; cofactor ATP

proof_lines: 12 h after isoproterenol administration, PFK-1


substrate_name: CMP

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

substrate: CMP


substrate_name: Unknown


substrate_name: diacylglycerol

substrate: diacylglycerol


organism: Rhizobium leguminosarum


organism: Saccharomyces cerevisiae

proof_lines:
hexokinases PI and PII
S-nitrosoglutathione treated enzyme


substrate_name: ATP; 6-Aminoglucose

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines: pH 7.5, 22°C, versus ATP, dependennt on Mg2+ concentration

substrate: ATP; 6-Aminoglucose


organism: Solanum tuberosum

substrate: Unknown


organism: Sparus aurata

proof_lines: Ki(slope) Ki(intercept)


assay_conditions_summary: pH 7; cofactor ATP

proof_lines: purified enzyme, at pH 7.0, in the absence of D-fructose 2,6-bisphosphate

proof_lines: purified enzyme, at pH 7.0, in the presence of 0.005 mM D-fructose 2,6-bisphosphate

substrate: ATP


organism: Salmonella enterica

substrate_name: D-glucose[side 1]

substrate: D-glucose[side 1]


enzyme_display_name: 4,4'-diapophytoene synthase

organism: Staphylococcus aureus

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

enzyme: 4,4'-diapophytoene synthase


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


organism: Streptococcus mutans

substrate_name: sucrose[side 1]

substrate: sucrose[side 1]


organism: Sus scrofa


organism: Spinacia oleracea

assay_conditions_summary: pH 7.7; 298.15 K; cofactor ATP


substrate_name: (R,S)-4-amino-3-fluorobutanoic acid

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

substrate: (R,S)-4-amino-3-fluorobutanoic acid


organism: Triticum aestivum


organism: Zea mays

proof_lines:
non-cytosolic hexokinase from root
root, non-cytosolic enzyme
non-cytoslic hexokinase from root


enzyme_display_name: thiamine diphosphokinase

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

enzyme: thiamine diphosphokinase


organism: Trypanosoma cruzi

substrate_name: D-glucose

proof_lines: natural hexokinase from epimastigotes, at pH 7.5

proof_lines: recombinant hexokinase expressed in Escherichia coli XL-1 Blue, at pH 7.5

substrate: D-glucose


substrate_name: UTP

substrate: UTP


substrate_name: D-fructose

substrate: D-fructose


organism: Trypanosoma brucei

assay_conditions_summary: pH 6.5; cofactor ATP

proof_lines: pH 6.5, temperature not specified in the publication

proof_lines: pH 7.4, temperature not specified in the publication


organism: Mus musculus

substrate_name: ATP; D-Fructose 6-phosphate

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: pH 7.2, 25°C, mammary gland and ascites tumor PFK

substrate: ATP; D-Fructose 6-phosphate


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

organism: Escherichia coli

substrate_name: NADPH

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

enzyme: NAD(P)H dehydrogenase (quinone)

substrate: NADPH


substrate_name: NADH

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: carboxylesterase

organism: Bos taurus

substrate_name: 4-nitrophenyl palmitate

proof_lines:
at 70°C
at 150°C

enzyme: carboxylesterase

substrate: 4-nitrophenyl palmitate


organism: Sulfurisphaera tokodaii

substrate_name: 4-nitrophenyl hexadecanoate

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl tetradecanoate

substrate: 4-nitrophenyl tetradecanoate


substrate_name: 4-nitrophenyl dodecanoate

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl decanoate

substrate: 4-nitrophenyl decanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: phenyl acetate

substrate: phenyl acetate


organism: Rhizobium viscosum


substrate_name: Glucose pentaacetate

substrate: Glucose pentaacetate


enzyme_display_name: UniProt F0QXN6

organism: Vulcanisaeta moutnovskia

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt F0QXN6

source: skid


enzyme_display_name: UniProt O28511

organism: Archaeoglobus fulgidus

enzyme: UniProt O28511


enzyme_display_name: UniProt O28558

substrate_name: 4-nitrophenyl propionate

enzyme: UniProt O28558

substrate: 4-nitrophenyl propionate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl pentanoate

substrate: 4-nitrophenyl pentanoate


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


enzyme_display_name: UniProt P13001

substrate_name: 4-nitrophenyl laurate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P13001

substrate: 4-nitrophenyl laurate


substrate_name: 4-nitrophenyl caproate

substrate: 4-nitrophenyl caproate


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


enzyme_display_name: UniProt Q0ZPV7

organism: Actinidia eriantha

substrate_name: 4-methylumbelliferyl laurate

enzyme: UniProt Q0ZPV7

substrate: 4-methylumbelliferyl laurate


enzyme_display_name: UniProt Q8TZJ1

organism: Pyrococcus furiosus

substrate_name: 4-methylumbelliferyl heptanoate

enzyme: UniProt Q8TZJ1

substrate: 4-methylumbelliferyl heptanoate


substrate_name: 4-Methylumbelliferyl butyrate

substrate: 4-Methylumbelliferyl butyrate


enzyme_display_name: UniProt Q97VU1

organism: Saccharolobus solfataricus

substrate_name: 4-nitrophenyl caprylate

enzyme: UniProt Q97VU1

substrate: 4-nitrophenyl caprylate


enzyme_display_name: UniProt Q9YBQ2

organism: Aeropyrum pernix

substrate_name: 4-nitrophenyl dodecanoate

enzyme: UniProt Q9YBQ2

substrate: 4-nitrophenyl dodecanoate


enzyme_display_name: UniProt F0NDQ1

organism: Sulfolobus islandicus

substrate_name: 4-nitrophenyl palmitate

assay_conditions_summary: pH 8

enzyme: UniProt F0NDQ1

substrate: 4-nitrophenyl palmitate


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 4-nitrophenyl decanoate

substrate: 4-nitrophenyl decanoate


enzyme_display_name: UniProt P12337

organism: Oryctolagus cuniculus

substrate_name: irinotecan

enzyme: UniProt P12337

substrate: irinotecan


enzyme_display_name: UniProt P23141

organism: Homo sapiens

substrate_name: oxybutynin

enzyme: UniProt P23141

substrate: oxybutynin


substrate_name: imidapril

substrate: imidapril


substrate_name: derapril

substrate: derapril


enzyme_display_name: UniProt P37967

organism: Bacillus subtilis

substrate_name: p-nitrophenyl acetate

enzyme: UniProt P37967

substrate: p-nitrophenyl acetate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl hexadecanoate

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl tetradecanoate

substrate: 4-nitrophenyl tetradecanoate


enzyme_display_name: Carboxylesterase

organism: Thermobifida fusca

substrate_name: p-nitrophenol acetate

enzyme: Carboxylesterase

substrate: p-nitrophenol acetate


substrate_name: p-nitrophenol butyrate

substrate: p-nitrophenol butyrate


enzyme_display_name: acetylesterase

organism: Streptomyces sp.

enzyme: acetylesterase


substrate_name: Alpha-naphthyl acetate

substrate: Alpha-naphthyl acetate


enzyme_display_name: acetylcholinesterase

substrate_name: acetylthiocholine iodide

enzyme: acetylcholinesterase

substrate: acetylthiocholine iodide


enzyme_display_name: UniProt P21836

organism: Mus musculus

substrate_name: Acetylcholine

smiles: CC(=O)OCC[N+](C)(C)C

enzyme: UniProt P21836

substrate: Acetylcholine


enzyme_display_name: UniProt P22303

substrate_name: heroin

enzyme: UniProt P22303

substrate: heroin


substrate_name: acetylthiocholine

smiles: CC(=O)SCC[N+](C)(C)C

proof_lines:
Raw SKiD Env: Temp=22°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

substrate: acetylthiocholine


substrate_name: propionylthiocholine

smiles: CCC(=O)SCC[N+](C)(C)C

substrate: propionylthiocholine


substrate_name: butyrylthiocholine

smiles: CCCC(=O)SCC[N+](C)(C)C

substrate: butyrylthiocholine


enzyme_display_name: UniProt P06276

enzyme: UniProt P06276


substrate_name: (-)-cocaine

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.4

substrate: (-)-cocaine


organism: Cupriavidus necator


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


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


enzyme_display_name: ribonucleoside-diphosphate reductase

organism: Streptococcus pyogenes

substrate_name: 1,4-Dithiothreitol; CDP

enzyme: ribonucleoside-diphosphate reductase

substrate: 1,4-Dithiothreitol; CDP


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

organism: Sus scrofa

substrate_name: NADPH; H+; Menadione

assay_conditions_summary: cofactor NADPH

enzyme: NAD(P)H dehydrogenase (quinone)

substrate: NADPH; H+; Menadione


organism: Salmonella typhimurium

substrate_name: Lipopolysaccharide; UDPgalactose

substrate: Lipopolysaccharide; UDPgalactose


enzyme_display_name: hexokinase

organism: Drosophila melanogaster

substrate_name: D-Glucose; ATP

assay_conditions_summary: cofactor ATP

enzyme: hexokinase

substrate: D-Glucose; ATP


enzyme_display_name: chlorophyllase

organism: Capsicum annuum

substrate_name: pheophytin a

enzyme: chlorophyllase

substrate: pheophytin a


substrate_name: chlorophyll b

substrate: chlorophyll b


substrate_name: pheophytin b

substrate: pheophytin b


substrate_name: chlorophyll a

substrate: chlorophyll a


enzyme_display_name: Chlorophyllase-1, chloroplastic

organism: Citrus sinensis

substrate_name: chlorophyll

enzyme: Chlorophyllase-1, chloroplastic

substrate: chlorophyll


enzyme_display_name: Chlorophyllase type 2

organism: Chenopodium album

sequence: SEKITVFQKNFQVTENSSHFV

wild_type_sequence: SEKITVFQKNFQVTENSSHFV

enzyme: Chlorophyllase type 2


enzyme_display_name: Chlorophyllase type 1

sequence: SEKITVFQKGNFQVTEXSSHFV

enzyme: Chlorophyllase type 1


organism: Canis familiaris

substrate_name: Glucose; ATP

substrate: Glucose; ATP


organism: Nicotiana tabacum

substrate_name: ATP; D-Glucose

substrate: ATP; D-Glucose


organism: Bos taurus

substrate_name: D-Fructose 6-phosphate; ATP

substrate: D-Fructose 6-phosphate; ATP


enzyme_display_name: ferroxidase

organism: Saccharomyces cerevisiae

enzyme: ferroxidase


organism: Lactococcus lactis subsp. lactis

substrate_name: ATP; D-Fructose 6-phosphate

substrate: ATP; D-Fructose 6-phosphate


enzyme_display_name: UniProt B3Y018

organism: Lactiplantibacillus plantarum

substrate_name: methyl gallate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=37°C, pH=7
Raw SKiD Env: Temp=-----, pH=8

enzyme: UniProt B3Y018

substrate: methyl gallate


substrate_name: epigallocatechin gallate

substrate: epigallocatechin gallate


substrate_name: catechin gallate

substrate: catechin gallate


substrate_name: Tannic acid

substrate: Tannic acid


enzyme_display_name: UniProt Q99685

organism: Homo sapiens

substrate_name: 4-Methylumbelliferyl butyrate

enzyme: UniProt Q99685

substrate: 4-Methylumbelliferyl butyrate


smiles: CCCCCCCCCC(=O)OCC(CO)O


organism: Escherichia coli


organism: Mustela vison


organism: Musa acuminata


organism: Plasmodium falciparum


organism: Oncorhynchus mykiss


organism: Ricinus communis


enzyme_display_name: Acylcarnitine hydrolase

organism: Mus musculus

substrate_name: p-nitrophenylacetate

enzyme: Acylcarnitine hydrolase

substrate: p-nitrophenylacetate


substrate_name: ATP; beta-D-Fructose 6-phosphate

substrate: ATP; beta-D-Fructose 6-phosphate


organism: Gallus gallus


organism: Thermus sp.


enzyme_display_name: gluconokinase

organism: Sus scrofa

substrate_name: D-Gluconate; ATP

enzyme: gluconokinase

substrate: D-Gluconate; ATP


organism: Salmonella typhimurium

substrate_name: D-Mannose; Protein N-phosphohistidine

substrate: D-Mannose; Protein N-phosphohistidine


enzyme_display_name: glucokinase

organism: Rattus norvegicus

substrate_name: ATP; Glucose

enzyme: glucokinase

substrate: ATP; Glucose


enzyme_display_name: UniProt Q9WXT2

organism: Thermotoga maritima

substrate_name: 4-methylumbelliferyl acetate

enzyme: UniProt Q9WXT2

substrate: 4-methylumbelliferyl acetate


substrate_name: Glucose pentaacetate

substrate: Glucose pentaacetate


substrate_name: xylose tetraacetate

substrate: xylose tetraacetate


enzyme_display_name: chlorogenate hydrolase

organism: Aspergillus niger

substrate_name: chlorogenate

enzyme: chlorogenate hydrolase

substrate: chlorogenate


enzyme_display_name: Chlorogenic acid esterase

organism: Mycosarcoma maydis

substrate_name: chlorogenic acid

enzyme: Chlorogenic acid esterase

substrate: chlorogenic acid


enzyme_display_name: alpha-amino-acid esterase

organism: Xanthomonas citri

substrate_name: 7-amino-3-deacetoxycephalosporanic acid

enzyme: alpha-amino-acid esterase

substrate: 7-amino-3-deacetoxycephalosporanic acid


enzyme_display_name: fructokinase

organism: Pisum sativum

substrate_name: ATP; Fructose

enzyme: fructokinase

substrate: ATP; Fructose


organism: Lactococcus lactis subsp. lactis

substrate_name: Protein N-phosphohistidine; Lactose

substrate: Protein N-phosphohistidine; Lactose


organism: Zea mays

substrate_name: D-Fructose; ATP

substrate: D-Fructose; ATP


organism: Streptococcus pyogenes

substrate_name: ATP; D-Glucose

substrate: ATP; D-Glucose


organism: Salmo salar


enzyme_display_name: UniProt Q9GPG0

organism: Manduca sexta

substrate_name: Alpha-naphthyl acetate

enzyme: UniProt Q9GPG0

substrate: Alpha-naphthyl acetate


enzyme_display_name: taurine dioxygenase

organism: Bacteria

smiles: O=O

enzyme: taurine dioxygenase


enzyme_display_name: salicylate 1-monooxygenase

organism: Sphingomonas sp.

assay_conditions_summary: pH 7

enzyme: salicylate 1-monooxygenase


organism: Pseudomonas sp.

substrate_name: 5-pyridoxic acid

substrate: 5-pyridoxic acid


enzyme_display_name: macrocin O-methyltransferase

organism: Streptomyces fradiae

substrate_name: demethylmacrocin

enzyme: macrocin O-methyltransferase

substrate: demethylmacrocin


enzyme_display_name: shikimate O-hydroxycinnamoyltransferase

organism: Arabidopsis thaliana

enzyme: shikimate O-hydroxycinnamoyltransferase


enzyme_display_name: rhamnulokinase

organism: Escherichia coli

substrate_name: L-Rhamnulose; ATP

enzyme: rhamnulokinase

substrate: L-Rhamnulose; ATP


enzyme_display_name: L-demethylnoviosyl transferase

organism: Streptomyces niveus

enzyme: L-demethylnoviosyl transferase


organism: Naegleria fowleri

substrate_name: D-glucosamine

substrate: D-glucosamine


enzyme_display_name: fatty-acyl-ethyl-ester synthase

organism: Oryctolagus cuniculus

substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

enzyme: fatty-acyl-ethyl-ester synthase

substrate: palmitate


substrate_name: arachidonate

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

substrate: arachidonate


substrate_name: linoleate

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

substrate: linoleate


substrate_name: stearate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: stearate


smiles: CCCCO


smiles: CCCO


substrate_name: methanol

smiles: CO

proof_lines: pH 7.2, 37°C, cosubstrate oleate, value above

substrate: methanol


enzyme_display_name: acetylxylan esterase

organism: uncultured microorganism

substrate_name: 2-naphthyl acetate

enzyme: acetylxylan esterase

substrate: 2-naphthyl acetate


substrate_name: 4-methylumbelliferyl acetate

substrate: 4-methylumbelliferyl acetate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Homo sapiens


enzyme_display_name: UniProt A0A1D3S5H0

organism: Fusarium oxysporum

substrate_name: methyl sinapate

enzyme: UniProt A0A1D3S5H0

substrate: methyl sinapate


substrate_name: methyl ferulate

substrate: methyl ferulate


substrate_name: methyl p-coumarate

substrate: methyl p-coumarate


substrate_name: methyl caffeate

substrate: methyl caffeate


enzyme_display_name: UniProt O42807

organism: Aspergillus niger

substrate_name: coniferyl p-coumarate

enzyme: UniProt O42807

substrate: coniferyl p-coumarate


substrate_name: methyl sinapinate

substrate: methyl sinapinate


substrate_name: ferulate

substrate: ferulate


substrate_name: n-propyl ferulate

substrate: n-propyl ferulate


substrate_name: ethyl ferulate

substrate: ethyl ferulate


enzyme_display_name: feruloyl esterase

organism: Thermochaetoides dissita

substrate_name: 1-naphthyl acetate

enzyme: feruloyl esterase

substrate: 1-naphthyl acetate


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 4-nitrophenyl ferulate

substrate: 4-nitrophenyl ferulate


organism: Aspergillus oryzae

substrate_name: alpha-naphthyl propionate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W142F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: alpha-naphthyl propionate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W144Y with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt E9LVH9

organism: Thermobifida cellulosilytica

substrate_name: 4-nitrophenyl butyrate

enzyme: UniProt E9LVH9

substrate: 4-nitrophenyl butyrate


enzyme_display_name: UniProt A0A075B5G4

organism: Humicola insolens

enzyme: UniProt A0A075B5G4


enzyme_display_name: cutinase

substrate_name: p-Nitrophenyl acetate

enzyme: cutinase

substrate: p-Nitrophenyl acetate


organism: Fusarium vanettenii

substrate_name: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


organism: Arcticibacterium luteifluviistationis

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:A0A2Z4G9P0 and applied mutation signature N98A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9

column_label: Requested kcat/KM quotient is 0.0033333333333333335, but the exact table cell reports 0.01 mM^-1 s^-1.

table_label: Table 4 Kinetic parameters of AlAXEase and its mutants

status: corrected


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:A0A2Z4G9P0 and applied mutation signature D200A to reconstruct the assayed variant sequence.

column_label: Requested row expects KM 6.7 mM and quotient 0.0029850746268656717, but the exact D200A table row reports KM 5.0 mM and kcat/KM 0.01.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E190A to reconstruct the assayed variant sequence.

proof_lines:
pH 9.0, 40°C, recombinant mutant E190A
pH 9.0, 30°C, recombinant mutant E190A
pH 9.0, 10°C, recombinant mutant E190A


proof_lines: pH 9.0, 50°C, recombinant wild-type enzyme

proof_lines: pH 9.0, 40°C, recombinant wild-type enzyme

proof_lines: pH 9.0, 10°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:A0A2Z4G9P0 and applied mutation signature G69A to reconstruct the assayed variant sequence.

column_label: Requested row expects KM 5.6 mM and quotient 0.2142857142857143, but the exact G69A table row reports KM 5.3 mM and kcat/KM 0.23.


organism: Bacteroides thetaiotaomicron


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: 4-methylumbelliferyl acetate

substrate: 4-methylumbelliferyl acetate


substrate_name: oleate

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

proof_lines: enzyme with FAEES/carboxylesterase activity from heart

substrate: oleate


substrate_name: ethanol

smiles: CCO

substrate: ethanol


organism: Actinomyces sp. oral taxon 448

substrate_name: methyl caffeate

substrate: methyl caffeate


organism: Bacillus amyloliquefaciens


substrate_name: methyl ferulate

substrate: methyl ferulate


substrate_name: chlorogenate

substrate: chlorogenate


substrate_name: methyl p-coumarate

substrate: methyl p-coumarate


organism: Schizophyllum commune


substrate_name: chlorogenic acid

substrate: chlorogenic acid


substrate_name: methyl 4-hydroxybenzoate

substrate: methyl 4-hydroxybenzoate


organism: Talaromyces stipitatus

substrate_name: methyl sinapate

column_label: Table 4, row MSA, columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 4 row MSA: kcat 9.26 s^-1; Km 0.37 mM; kcat/Km 25 mM^-1 s^-1.

row_label: MSA (methyl sinapate)

table_label: Table 4

substrate: methyl sinapate


column_label: Table 4, row MpCA, columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 4 row MpCA: kcat 9.55 s^-1; Km 0.01 mM; kcat/Km 746 mM^-1 s^-1.

row_label: MpCA (methyl p-coumarate)


column_label: Table 4, row MFA, columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 4 row MFA: kcat 9.65 s^-1; Km 0.04 mM; kcat/Km 323 mM^-1 s^-1.

row_label: MFA (methyl ferulate)


substrate_name: H2O; Methyl p-coumarate

assay_conditions_summary: pH 6

normalized_value_unit_evidence: kcat/Km 746 s^-1 mM^-1, equivalent to 746000 M^-1 s^-1; actual kcat is 9.55 s^-1.

substrate: H2O; Methyl p-coumarate


substrate_name: Methyl caffeate; H2O

substrate: Methyl caffeate; H2O


organism: uncultured bacterium

substrate_name: methyl 4-coumarate

column_label: Table 1 row Methyl p-coumarate (MpCA), columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1). Table footnote: ND = Not determined; ND does not apply to this row.

raw_value_unit_evidence: Table 1 row Methyl p-coumarate (MpCA): Km 1.25 +/- 0.04 mM; kcat 7.5 +/- 1.0 s^-1; kcat/Km 6 +/- 1.5 s^-1 mM^-1.

row_label: Methyl p-coumarate (MpCA)

table_label: Table 1, substrate specificity and selected kinetic parameters of recombinant EstF27

substrate: methyl 4-coumarate


enzyme_display_name: UniProt E7DJY5

enzyme: UniProt E7DJY5


substrate_name: 4-nitrophenyl ferulate

proof_lines:
Raw SKiD Env: Temp=40°C, pH=6.8
Raw SKiD Env: Temp=65°C, pH=7
Raw SKiD Env: Temp=40°C, pH=7

substrate: 4-nitrophenyl ferulate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R187K to reconstruct the assayed variant sequence.

column_label: Table II row Thc_Cut2_Arg187Lys, PNPA columns: KM (mM)=0.8 +/- 0.1; kcat (s^-1)=35; kcat/KM (s^-1 mM^-1)=44.

normalized_value_unit_evidence: kcat 35 s^-1; Km 0.8 mM; kcat/Km 44 s^-1 mM^-1 as displayed in Table II.

row_label: Thc_Cut2_Arg187Lys with PNPA (4-nitrophenyl acetate/p-nitrophenyl acetate)

table_label: PMID 23592055 Wiley Table II, Kinetic parameters with soluble substrates, PNPA columns


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R19S/R29N/A30V to reconstruct the assayed variant sequence.

column_label: Table II row Thc_Cut2_Arg19Ser_Arg29Asn_Ala30Val, PNPA columns: KM (mM)=1.2 +/- 0.1; kcat (s^-1)=76; kcat/KM (s^-1 mM^-1)=65.

normalized_value_unit_evidence: kcat 76 s^-1; Km 1.2 mM; kcat/Km 65 s^-1 mM^-1 as displayed in Table II.

row_label: Thc_Cut2_Arg19Ser_Arg29Asn_Ala30Val with PNPA (4-nitrophenyl acetate/p-nitrophenyl acetate)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R29N to reconstruct the assayed variant sequence.

column_label: Table II row Thc_Cut2_Arg29Asn, PNPA columns: KM (mM)=1.3 +/- 0.4; kcat (s^-1)=207; kcat/KM (s^-1 mM^-1)=159.

normalized_value_unit_evidence: kcat 207 s^-1; Km 1.3 mM; kcat/Km 159 s^-1 mM^-1 as displayed in Table II.

row_label: Thc_Cut2_Arg29Asn with PNPA (4-nitrophenyl acetate/p-nitrophenyl acetate)


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


column_label: Table 1 row Methyl ferulate (MFA), columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1). Table footnote: ND = Not determined; ND does not apply to this row.

row_label: Methyl ferulate (MFA)


column_label: Table 1 row p-Nitrophenyl ferulate (pNPF), columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1). Table footnote: ND = Not determined; ND does not apply to this row.

raw_value_unit_evidence: Table 1 row p-Nitrophenyl ferulate (pNPF): Km 0.5 +/- 0.04 mM; kcat 19.7 +/- 3 s^-1; kcat/Km 39.4 +/- 5 s^-1 mM^-1.

row_label: p-Nitrophenyl ferulate (pNPF)


column_label: Table 1 row p-Nitrophenyl butyrate (C4), columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1). Table footnote: ND = Not determined; ND does not apply to this row.

row_label: p-Nitrophenyl butyrate (C4)


column_label: Table 1 row p-Nitrophenyl acetate (C2), columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1). Table footnote: ND = Not determined; ND does not apply to this row.

row_label: p-Nitrophenyl acetate (C2)


column_label: Table 1 row Methyl sinapate (MSA), columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1). Table footnote: ND = Not determined; ND does not apply to this row.

row_label: Methyl sinapate (MSA)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T27I/S84L/V161I/H195L/G243C/A259V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R29N/A30V to reconstruct the assayed variant sequence.

column_label: Table II row Thc_Cut2_Arg29Asn_Ala30Val, PNPA columns: KM (mM)=1.3 +/- 0.3; kcat (s^-1)=100; kcat/KM (s^-1 mM^-1)=76.

normalized_value_unit_evidence: kcat 100 s^-1; Km 1.3 mM; kcat/Km 76 s^-1 mM^-1 as displayed in Table II.

row_label: Thc_Cut2_Arg29Asn_Ala30Val with PNPA (4-nitrophenyl acetate/p-nitrophenyl acetate)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q65E to reconstruct the assayed variant sequence.

column_label: Table II row Thc_Cut2_Gln65Glu, PNPA columns: KM (mM)=1.5 +/- 0.2; kcat (s^-1)=7; kcat/KM (s^-1 mM^-1)=5.

normalized_value_unit_evidence: kcat 7 s^-1; Km 1.5 mM; kcat/Km 5 s^-1 mM^-1 as displayed in Table II.

row_label: Thc_Cut2_Gln65Glu with PNPA (4-nitrophenyl acetate/p-nitrophenyl acetate)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30V to reconstruct the assayed variant sequence.

column_label: Table II row Thc_Cut2_Ala30Val, PNPA columns: KM (mM)=1.7 +/- 0.2; kcat (s^-1)=260; kcat/KM (s^-1 mM^-1)=153.

normalized_value_unit_evidence: kcat 260 s^-1; Km 1.7 mM; kcat/Km 153 s^-1 mM^-1 as displayed in Table II.

row_label: Thc_Cut2_Ala30Val with PNPA (4-nitrophenyl acetate/p-nitrophenyl acetate)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R19S to reconstruct the assayed variant sequence.


organism: Thermobifida fusca

substrate_name: p-Nitrophenyl butyrate

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

substrate: p-Nitrophenyl butyrate


substrate_name: p-Nitrophenyl acetate; H2O

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

substrate: p-Nitrophenyl acetate; H2O


substrate_name: p-Nitrophenyl acetate

substrate: p-Nitrophenyl acetate


enzyme_display_name: UniProt H6BDX1

substrate_name: 4-nitrophenyl acetate

enzyme: UniProt H6BDX1

substrate: 4-nitrophenyl acetate


enzyme_display_name: UniProt Q0GMU2

substrate_name: p-nitrophenyl butyrate

enzyme: UniProt Q0GMU2

substrate: p-nitrophenyl butyrate


enzyme_display_name: hormone-sensitive lipase

organism: Mycobacterium marinum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H342A to reconstruct the assayed variant sequence.

column_label: SI Table S3 (S5), text lines 164-166; row block=H342A; substrate row=7; metric column=kcat; cell=0.000053 +/- 0.000017 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 342 is H; kinetic table variant block is H342A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 0.000053 s^-1; SI central kcat 0.000053 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: H342A / substrate 7 (substrate 7, four-atom chain alkyl ether ester / MOAME / fluorescein bis((2-methoxy)acetoxymethyl ether))

table_label: SI Table S3

enzyme: hormone-sensitive lipase


column_label: SI Table S3 (S5), text lines 164-167; row block=H342A; substrate row=20; metric column=Km; cell=0.31 +/- 0.63 uM (0.00031 mM). Sequence/mutation support: SI Table S6 M. marinum position 342 is H; kinetic table variant block is H342A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.00031 mM; SI central Km 0.31 uM = 0.00031 mM.

row_label: H342A / substrate 20 (substrate 20, oxazole ester / fluorescein bis((5-oxazolyl)carboxymethyl ether))


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


substrate_name: fluorescein diacetoxymethyl ether

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S216G to reconstruct the assayed variant sequence.

column_label: SI Table S4 (S7), text lines 191-192; row block=S216G; substrate row=1; metric column=kcat; cell=0.00070 +/- 0.00027 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 216 is S; kinetic table variant block is S216G. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 0.0007 s^-1; SI central kcat 0.00070 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: S216G / substrate 1 (substrate 1, acetyl ester / fluorescein diacetoxymethyl ether)

table_label: SI Table S4

substrate: fluorescein diacetoxymethyl ether


column_label: SI Table S4 (S7), text lines 191-194; row block=S216G; substrate row=20; metric column=Km; cell=3.6 +/- 1.8 uM (0.0036 mM). Sequence/mutation support: SI Table S6 M. marinum position 216 is S; kinetic table variant block is S216G. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.0036 mM; SI central Km 3.6 uM = 0.0036 mM.

row_label: S216G / substrate 20 (substrate 20, oxazole ester / fluorescein bis((5-oxazolyl)carboxymethyl ether))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S216C to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme S216C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W146C to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme W146C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S216N to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme S216N


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W146A to reconstruct the assayed variant sequence.

column_label: SI Table S5 (S8), text lines 228-229; row block=W146A; substrate row=1; metric column=kcat; cell=0.075 +/- 0.006 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 146 is W; kinetic table variant block is W146A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 0.075 s^-1; SI central kcat 0.075 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: W146A / substrate 1 (substrate 1, acetyl ester / fluorescein diacetoxymethyl ether)

table_label: SI Table S5


column_label: SI Table S5 (S8), text lines 228-231; row block=W146A; substrate row=20; metric column=Km; cell=0.71 +/- 0.11 uM (0.00071 mM). Sequence/mutation support: SI Table S6 M. marinum position 146 is W; kinetic table variant block is W146A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.00071 mM; SI central Km 0.71 uM = 0.00071 mM.

row_label: W146A / substrate 20 (substrate 20, oxazole ester / fluorescein bis((5-oxazolyl)carboxymethyl ether))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W146S to reconstruct the assayed variant sequence.

column_label: SI Table S5 (S8), text lines 240-242; row block=W146S; substrate row=7; metric column=kcat; cell=0.17 +/- 0.01 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 146 is W; kinetic table variant block is W146S. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 0.17 s^-1; SI central kcat 0.17 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: W146S / substrate 7 (substrate 7, four-atom chain alkyl ether ester / MOAME / fluorescein bis((2-methoxy)acetoxymethyl ether))


column_label: SI Table S5 (S8), text lines 240-243; row block=W146S; substrate row=20; metric column=Km; cell=3.5 +/- 0.4 uM (0.0035 mM). Sequence/mutation support: SI Table S6 M. marinum position 146 is W; kinetic table variant block is W146S. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.0035 mM; SI central Km 3.5 uM = 0.0035 mM.

row_label: W146S / substrate 20 (substrate 20, oxazole ester / fluorescein bis((5-oxazolyl)carboxymethyl ether))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G145A to reconstruct the assayed variant sequence.

column_label: SI Table S3 (S5), text lines 136-138; row block=G145A; substrate row=7; metric column=kcat; cell=0.18 +/- 0.11 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 145 is G; kinetic table variant block is G145A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 0.18 s^-1; SI central kcat 0.18 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: G145A / substrate 7 (substrate 7, four-atom chain alkyl ether ester / MOAME / fluorescein bis((2-methoxy)acetoxymethyl ether))


column_label: SI Table S3 (S5), text lines 136-139; row block=G145A; substrate row=20; metric column=Km; cell=0.30 +/- 0.16 uM (0.0003 mM). Sequence/mutation support: SI Table S6 M. marinum position 145 is G; kinetic table variant block is G145A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.00037 mM; SI central Km 0.30 uM = 0.0003 mM. The exported value is not the SI central table-cell value, even though it may fall inside the reported SD interval.

row_label: G145A / substrate 20 (substrate 20, oxazole ester / fluorescein bis((5-oxazolyl)carboxymethyl ether))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W146Q to reconstruct the assayed variant sequence.

column_label: SI Table S5 (S8), text lines 236-238; row block=W146Q; substrate row=7; metric column=kcat; cell=0.075 +/- 0.0023 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 146 is W; kinetic table variant block is W146Q. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

row_label: W146Q / substrate 7 (substrate 7, four-atom chain alkyl ether ester / MOAME / fluorescein bis((2-methoxy)acetoxymethyl ether))


column_label: SI Table S5 (S8), text lines 236-237; row block=W146Q; substrate row=1; metric column=Km; cell=1.4 +/- 0.4 uM (0.0014 mM). Sequence/mutation support: SI Table S6 M. marinum position 146 is W; kinetic table variant block is W146Q. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.0014 mM; SI central Km 1.4 uM = 0.0014 mM.

row_label: W146Q / substrate 1 (substrate 1, acetyl ester / fluorescein diacetoxymethyl ether)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D215A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme D215A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H154A to reconstruct the assayed variant sequence.

column_label: SI Table S3 (S5), text lines 140-142; row block=H154A; substrate row=7; metric column=kcat; cell=0.28 +/- 0.15 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 154 is H; kinetic table variant block is H154A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 0.28 s^-1; SI central kcat 0.28 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: H154A / substrate 7 (substrate 7, four-atom chain alkyl ether ester / MOAME / fluorescein bis((2-methoxy)acetoxymethyl ether))


column_label: SI Table S3 (S5), text lines 140-143; row block=H154A; substrate row=20; metric column=Km; cell=3.4 +/- 0.4 uM (0.0034 mM). Sequence/mutation support: SI Table S6 M. marinum position 154 is H; kinetic table variant block is H154A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.0034 mM; SI central Km 3.4 uM = 0.0034 mM.

row_label: H154A / substrate 20 (substrate 20, oxazole ester / fluorescein bis((5-oxazolyl)carboxymethyl ether))


substrate_name: methyl caffeate

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

substrate: methyl caffeate


substrate_name: ethyl ferulate

substrate: ethyl ferulate


substrate_name: methyl p-coumarate

substrate: methyl p-coumarate


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 1-naphthyl acetate

substrate: 1-naphthyl acetate


organism: Salinisphaera sp. P7-4

proof_lines: pH 8.0, temperature not specified in the publication, wild-type enzyme


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

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme L208A


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme E201A


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D227A


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme R207A


organism: Thermothelomyces heterothallicus


substrate_name: methyl sinapinate

substrate: methyl sinapinate


substrate_name: n-propyl ferulate

substrate: n-propyl ferulate


substrate_name: n-butyl ferulate

substrate: n-butyl ferulate


substrate_name: L-arabinose

proof_lines: transesterification in a n-hexane/t-butanol/water solvent system, 35°C

substrate: L-arabinose


organism: Streptomyces coelicolor

substrate_name: p-nitrophenyl acetate

substrate: p-nitrophenyl acetate


substrate_name: Alpha-naphtyl acetate

substrate: Alpha-naphtyl acetate


proof_lines: double mutant V158A/W87F, Vmax: 0.032 mM/min


substrate_name: 2-naphthyl acetate

substrate: 2-naphthyl acetate


sequence_variant_note: Resolved canonical sequence from official_uniprot_accession_sequence_asset:B2HIK1 and applied mutation signature G144A to reconstruct the assayed variant sequence.

column_label: SI Table S3 (S5), text lines 132-134; row block=G144A; substrate row=7; metric column=kcat; cell=0.066 +/- 0.024 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 144 is G; kinetic table variant block is G144A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 0.066 s^-1; SI central kcat 0.066 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: G144A / substrate 7 (substrate 7, four-atom chain alkyl ether ester / MOAME / fluorescein bis((2-methoxy)acetoxymethyl ether))


column_label: SI Table S3 (S5), text lines 132-135; row block=G144A; substrate row=20; metric column=Km; cell=1.5 +/- 0.4 uM (0.0015 mM). Sequence/mutation support: SI Table S6 M. marinum position 144 is G; kinetic table variant block is G144A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.0015 mM; SI central Km 1.5 uM = 0.0015 mM.

row_label: G144A / substrate 20 (substrate 20, oxazole ester / fluorescein bis((5-oxazolyl)carboxymethyl ether))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D312A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: SI Table S3 (S5), text lines 160-162; row block=D312A; substrate row=7; metric column=kcat; cell=0.31 +/- 0.29 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 312 is D; kinetic table variant block is D312A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 0.31 s^-1; SI central kcat 0.31 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: D312A / substrate 7 (substrate 7, four-atom chain alkyl ether ester / MOAME / fluorescein bis((2-methoxy)acetoxymethyl ether))


column_label: SI Table S3 (S5), text lines 160-163; row block=D312A; substrate row=20; metric column=Km; cell=5.7 +/- 1.9 uM (0.0057 mM). Sequence/mutation support: SI Table S6 M. marinum position 312 is D; kinetic table variant block is D312A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.0057 mM; SI central Km 5.7 uM = 0.0057 mM.

row_label: D312A / substrate 20 (substrate 20, oxazole ester / fluorescein bis((5-oxazolyl)carboxymethyl ether))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D269A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme D269A


sequence_variant_note: Resolved canonical sequence from official_uniprot_accession_sequence_asset:B2HIK1 and applied mutation signature S226A to reconstruct the assayed variant sequence.

column_label: SI Table S4 (S7), text lines 203-204; row block=S226A; substrate row=1; metric column=kcat; cell=3.6 +/- 0.1 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 226 is S; kinetic table variant block is S226A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 3.6 s^-1; SI central kcat 3.6 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: S226A / substrate 1 (substrate 1, acetyl ester / fluorescein diacetoxymethyl ether)


column_label: SI Table S4 (S7), text lines 203-206; row block=S226A; substrate row=20; metric column=Km; cell=1.1 +/- 0.1 uM (0.0011 mM). Sequence/mutation support: SI Table S6 M. marinum position 226 is S; kinetic table variant block is S226A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.0011 mM; SI central Km 1.1 uM = 0.0011 mM.

row_label: S226A / substrate 20 (substrate 20, oxazole ester / fluorescein bis((5-oxazolyl)carboxymethyl ether))


sequence_variant_note: Resolved canonical sequence from official_uniprot_accession_sequence_asset:B2HIK1 and applied mutation signature S177A to reconstruct the assayed variant sequence.

column_label: SI Table S4 (S7), text lines 199-201; row block=S177A; substrate row=7; metric column=kcat; cell=1.8 +/- 0.1 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 177 is S; kinetic table variant block is S177A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 1.8 s^-1; SI central kcat 1.8 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: S177A / substrate 7 (substrate 7, four-atom chain alkyl ether ester / MOAME / fluorescein bis((2-methoxy)acetoxymethyl ether))


column_label: SI Table S4 (S7), text lines 199-200; row block=S177A; substrate row=1; metric column=Km; cell=1.1 +/- 0.1 uM (0.0011 mM). Sequence/mutation support: SI Table S6 M. marinum position 177 is S; kinetic table variant block is S177A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

row_label: S177A / substrate 1 (substrate 1, acetyl ester / fluorescein diacetoxymethyl ether)


sequence_variant_note: Resolved canonical sequence from official_uniprot_accession_sequence_asset:B2HIK1 and applied mutation signature R246A to reconstruct the assayed variant sequence.

column_label: SI Table S3 (S5), text lines 152-154; row block=R246A; substrate row=7; metric column=kcat; cell=0.10 +/- 0.02 s^-1. Sequence/mutation support: SI Table S6 M. marinum position 246 is R; kinetic table variant block is R246A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export kcat 0.1 s^-1; SI central kcat 0.10 s^-1. Table S1 and the reported kcat/Km values support interpreting the S3-S5 kcat cells as s^-1 despite the extracted header artifact.

row_label: R246A / substrate 7 (substrate 7, four-atom chain alkyl ether ester / MOAME / fluorescein bis((2-methoxy)acetoxymethyl ether))


column_label: SI Table S3 (S5), text lines 152-153; row block=R246A; substrate row=1; metric column=Km; cell=21 +/- 4 uM (0.021 mM). Sequence/mutation support: SI Table S6 M. marinum position 246 is R; kinetic table variant block is R246A. Main article Methods states proper mutations in the MmLipN DNA sequence were confirmed by DNA sequencing.

normalized_value_unit_evidence: Expected export Km 0.021 mM; SI central Km 21 uM = 0.021 mM.

row_label: R246A / substrate 1 (substrate 1, acetyl ester / fluorescein diacetoxymethyl ether)


substrate_name: 4-nitrophenyl myristate

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

column_label: Table S2; row label C14; p-nitrophenyl myristate; columns kcat, Km, and/or kcat/Km as printed in supporting information.

raw_value_unit_evidence: Table S2 row C14; p-nitrophenyl myristate: kcat 0.28 s^-1; km 0.12 mM; kcat_over_km 2300 M^-1 s^-1

row_label: C14; p-nitrophenyl myristate

table_label: Table S2

substrate: 4-nitrophenyl myristate


substrate_name: 4-nitrophenyl octanoate

column_label: Table S2; row label C8; p-nitrophenyl octanoate; columns kcat, Km, and/or kcat/Km as printed in supporting information.

raw_value_unit_evidence: Table S2 row C8; p-nitrophenyl octanoate: kcat 1.1 s^-1; km 0.41 mM; kcat_over_km 2700 M^-1 s^-1

row_label: C8; p-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl valerate

column_label: Table S2; row label C6; p-nitrophenyl valerate; columns kcat, Km, and/or kcat/Km as printed in supporting information.

normalized_value_unit_evidence: kcat 15 s^-1; km 0.25 mM; kcat_over_km 59 s^-1 mM^-1

raw_value_unit_evidence: Table S2 row C6; p-nitrophenyl valerate: kcat 15 s^-1; km 0.25 mM; kcat_over_km 59000 M^-1 s^-1

row_label: C6; p-nitrophenyl valerate

substrate: 4-nitrophenyl valerate


substrate_name: 4-nitrophenyl acetate

column_label: Table S2; row label C2; p-nitrophenyl acetate; columns kcat, Km, and/or kcat/Km as printed in supporting information.

normalized_value_unit_evidence: kcat 94 s^-1; km 2.4 mM; kcat_over_km 39 s^-1 mM^-1

raw_value_unit_evidence: Table S2 row C2; p-nitrophenyl acetate: kcat 94 s^-1; km 2.4 mM; kcat_over_km 39000 M^-1 s^-1

row_label: C2; p-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl butyrate

column_label: Table S2; row label C4; p-nitrophenyl butyrate; columns kcat, Km, and/or kcat/Km as printed in supporting information.

raw_value_unit_evidence: Table S2 row C4; p-nitrophenyl butyrate: kcat 190 s^-1; km 0.02 mM; kcat_over_km 9300000 M^-1 s^-1

row_label: C4; p-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


organism: Mycothermus thermophilus

substrate_name: 4-nitrophenyl palmitate

substrate: 4-nitrophenyl palmitate


substrate_name: triolein

substrate: triolein


substrate_name: tributyrin

smiles: CCCC(=O)OCC(COC(=O)CCC)OC(=O)CCC

substrate: tributyrin


substrate_name: tricaprylin

substrate: tricaprylin


organism: Cryptococcus sp. S-2

substrate_name: 4-nitrophenyl hexadecanoate

proof_lines: pH and temperature not specified in the publication

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl dodecanoate

substrate: 4-nitrophenyl dodecanoate


organism: Acetivibrio thermocellus

substrate_name: n-hexyl ferulate

substrate: n-hexyl ferulate


substrate_name: n-propyl ferulate

substrate: n-propyl ferulate


substrate_name: ethyl ferulate

substrate: ethyl ferulate


substrate_name: methyl ferulate

substrate: methyl ferulate


organism: Aspergillus ochraceus

substrate_name: methyl caffeate

substrate: methyl caffeate


substrate_name: methyl sinapinate

substrate: methyl sinapinate


substrate_name: methyl p-coumarate

substrate: methyl p-coumarate


organism: Aspergillus niger

substrate_name: coniferyl p-coumarate

substrate: coniferyl p-coumarate


substrate_name: 5-O-p-coumaroylquinic acid

substrate: 5-O-p-coumaroylquinic acid


substrate_name: chlorogenic acid

substrate: chlorogenic acid


substrate_name: chlorogenate

substrate: chlorogenate


organism: Pseudoalteromonas haloplanktis

substrate_name: methylumbelliferyl acetate

substrate: methylumbelliferyl acetate


substrate_name: beta-naphthyl acetate

substrate: beta-naphthyl acetate


substrate_name: p-nitrophenyl acetate

substrate: p-nitrophenyl acetate


substrate_name: Alpha-naphthyl acetate

substrate: Alpha-naphthyl acetate


organism: Parageobacillus thermoglucosidasius

substrate_name: 4-nitrophenyl laurate

substrate: 4-nitrophenyl laurate


substrate_name: 4-nitrophenyl caprate

substrate: 4-nitrophenyl caprate


substrate_name: 4-nitrophenyl caprylate

substrate: 4-nitrophenyl caprylate


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


organism: rumen bacterium

substrate_name: n-decyl ferulate

substrate: n-decyl ferulate


substrate_name: ethyl ferulate

substrate: ethyl ferulate


substrate_name: n-propyl ferulate

substrate: n-propyl ferulate


substrate_name: methyl ferulate

substrate: methyl ferulate


organism: Caldanaerobacter subterraneus subsp. tengcongensis

substrate_name: methyl p-coumarate

assay_conditions_summary: pH 8; 338.15 K; buffer 50 mM sodium phosphate

proof_lines: at 65°C, in 50 mM sodium phosphate buffer, pH 8.0

substrate: methyl p-coumarate


substrate_name: methyl sinapate

substrate: methyl sinapate


substrate_name: methyl cinnamate

substrate: methyl cinnamate


substrate_name: methyl 3-hydroxy-4-methoxy cinnamate

substrate: methyl 3-hydroxy-4-methoxy cinnamate


organism: Burkholderia pyrrocinia

substrate_name: methyl 4-coumarate

substrate: methyl 4-coumarate


substrate_name: methyl caffeate

substrate: methyl caffeate


organism: Escherichia coli

substrate_name: ferulic acid ethyl ester

substrate: ferulic acid ethyl ester


substrate_name: ferulic acid methyl ester

substrate: ferulic acid methyl ester


substrate_name: p-coumaric acid methyl ester

substrate: p-coumaric acid methyl ester


organism: Streptomyces cinnamoneus


proof_lines:
isozyme R43, pH 7.0, 50°C
isozyme R18, pH 7.0, 50°C


organism: Pseudomonas fluorescens


substrate_name: methyl sinapinate

proof_lines: pH not specified in the publication, 50°C

substrate: methyl sinapinate


organism: Thermobifida cellulosilytica

proof_lines: pH 7.0, 25°C, recombinant wild-type isozyme


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Pseudomonas putida

substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


substrate_name: p-nitrophenylbutanoate

substrate: p-nitrophenylbutanoate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


organism: Halalkalibacterium halodurans

substrate_name: tricaproyl glycerol

substrate: tricaproyl glycerol


substrate_name: tripalmitoyl glycerol

substrate: tripalmitoyl glycerol


substrate_name: 4-nitrophenyl palmitate

substrate: 4-nitrophenyl palmitate


organism: Falsihalocynthiibacter arcticus

column_label: Figure 5D columns are Substrate, Vmax (uM s^-1), Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); p-NH row cells are 0.78 +/- 0.13, 2.32 +/- 0.63, 0.20 +/- 0.03, and 0.085.

normalized_value_unit_evidence: Km 2.32 mM; kcat 0.20 s^-1; printed kcat/Km 0.085 s^-1 mM^-1. Export expected kcat/Km 0.08620689655172414 is within figure precision/rounding.

row_label: HaHSL / p-NH (4-nitrophenyl hexanoate)

table_label: Figure 5D, Kinetic parameters of HaHSL


substrate_name: 4-nitrophenyl butyrate

column_label: Figure 5D columns are Substrate, Vmax (uM s^-1), Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); p-NB row cells are 4.40 +/- 0.70, 1.97 +/- 0.53, 3.32 +/- 0.52, and 1.69.

normalized_value_unit_evidence: Km 1.97 mM; kcat 3.32 s^-1; printed kcat/Km 1.69 s^-1 mM^-1. Export expected kcat/Km 1.6852791878172588 is within figure precision/rounding.

row_label: HaHSL / p-NB (4-nitrophenyl butyrate)

substrate: 4-nitrophenyl butyrate


normalized_value_unit_evidence: Paper Km is 0.21 mM; export Km 0.2 mM is the rounded value. kcat is 23.02 s^-1; printed kcat/Km is 110.46 s^-1 mM^-1. Export expected kcat/Km 115.1 is a recomputation from rounded Km, so the primary figure metric is preserved.

row_label: HaHSL / p-NA (4-nitrophenyl acetate)


organism: Irpex lacteus

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

assay_conditions_summary: pH 6; buffer pH 6

column_label: Europe PMC public PDF Table 2 row p-Nitrophenyl acetate / pNPAc, columns Km=1.4 +/- 0.3 mM, kcat=29.1 +/- 4.3 s-1, kcat/Km=20.6 mM-1 s-1.

raw_value_unit_evidence: Table 2 row p-Nitrophenyl acetate / pNPAc cells: Km 1.4 +/- 0.3 mM; kcat 29.1 +/- 4.3 s-1; kcat/Km 20.6 mM-1 s-1.

row_label: p-Nitrophenyl acetate / pNPAc

table_label: Table 2. Kinetic parameters of IlAXE1.


substrate_name: 4-methylumbelliferyl acetate

column_label: Europe PMC public PDF Table 2 row 4-Metylumbelliferyl acetate / MUAc, columns Km=0.4 +/- 0.1 mM, kcat=33.8 +/- 5.7 s-1, kcat/Km=85.5 mM-1 s-1.

raw_value_unit_evidence: Table 2 row 4-Metylumbelliferyl acetate / MUAc cells: Km 0.4 +/- 0.1 mM; kcat 33.8 +/- 5.7 s-1; kcat/Km 85.5 mM-1 s-1.

row_label: 4-Metylumbelliferyl acetate / MUAc

substrate: 4-methylumbelliferyl acetate


organism: Actinomyces sp. oral taxon 448

substrate_name: ethyl ferulate

substrate: ethyl ferulate


substrate_name: methyl p-coumarate

substrate: methyl p-coumarate


substrate_name: methyl ferulate

proof_lines:
pH 6.0, 37°C, native enzyme
isoenzyme FAEB
isoenzyme FAEA

substrate: methyl ferulate


organism: Bacteroides intestinalis


proof_lines: recombinant wild-type enzyme, pH 6.0, 45°C


organism: Rasamsonia emersonii

substrate_name: 2-naphthyl acetate

assay_conditions_summary: pH 5

substrate: 2-naphthyl acetate


organism: Fusarium oxysporum

proof_lines:
pH 7.0, 45°C
45°C, pH 6.0, isoenzyme FAE-I
pH 7.0, 55°C


proof_lines:
pH 7.0, 45°C
45°C, pH 6.0, isoenzyme FAE-I
45°C, pH 6.0, isoenzyme FAE-II


substrate_name: methyl caffeate

substrate: methyl caffeate


substrate_name: methyl sinapate

proof_lines:
pH 7.0, 55°C
45°C, pH 6.0, isoenzyme FAE-I
pH 6.0, 45°C

substrate: methyl sinapate


organism: Limosilactobacillus fermentum

substrate_name: methyl 4-coumarate

substrate: methyl 4-coumarate


organism: Pleurotus sapidus


organism: Thermoclostridium stercorarium


organism: Ascochyta rabiei


organism: uncultured bacterium

proof_lines: pH 8.0, 70°C, recombinant mutant C275A/C292A, absence of 1% PEG

proof_lines: pH 8.0, 50°C, recombinant mutant C275A/C292A, absence of 1% PEG

proof_lines: pH 8.0, 30°C, recombinant mutant C275A/C292A, absence of 1% PEG


proof_lines: pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG

proof_lines: pH 8.0, 30°C, recombinant wild-type enzyme, absence of 1% PEG

proof_lines: pH 8.0, 30°C, recombinant wild-type enzyme, presence of 1% PEG


organism: Saccharolobus solfataricus

substrate_name: p-nitrophenyl hexanoate

substrate: p-nitrophenyl hexanoate


organism: Oryctolagus cuniculus

substrate_name: ethanol

proof_lines: pH 7.2, 37°C, minor cytosolic enzyme activity

proof_lines: pH 7.2, 37°C, major cytosolic enzyme activity

substrate: ethanol


substrate_name: oleate

proof_lines:
pH 7.2, 20°C, formation of ethyl oleate
pH 7.2, 30°C, formation of ethyl oleate
pH 7.2, 37°C, formation of ethyl oleate

substrate: oleate


enzyme_display_name: cetraxate benzylesterase

organism: Aspergillus niger

substrate_name: benzyl cetraxate

enzyme: cetraxate benzylesterase

substrate: benzyl cetraxate


organism: Anoxybacillus flavithermus

substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Arion ater


organism: Bacillus pumilus

substrate_name: 1-naphthyl acetate

substrate: 1-naphthyl acetate


organism: Orpinomyces sp.


organism: Penicillium chrysogenum


organism: Phanerodontia chrysosporium


organism: Streptomyces lividans


organism: Thermoanaerobacterium saccharolyticum

substrate_name: 4-yethylumbelliferyl acetate

proof_lines:
isoenzyme4 II
isoenzyme I
isoenzyme II

substrate: 4-yethylumbelliferyl acetate


organism: Termitomyces clypeatus


proof_lines:
isoenzyme FAEB
pH 6.0, 40°C
pH 3.2


organism: Thermobifida fusca

substrate_name: p-nitrophenyl acetate

substrate: p-nitrophenyl acetate


organism: Actinomyces sp.


organism: Eleusine coracana

substrate_name: p-nitrophenylferulate

substrate: p-nitrophenylferulate


organism: Auricularia auricula-judae


organism: Lactarius hatsudake


organism: Neocallimastix sp.

proof_lines:
FAE-II
40°C, pH 7.0, isoenzyme FAE-II
FAE-I


organism: Lactobacillus acidophilus


organism: Pleurotus giganteus


organism: rumen microorganism

proof_lines: transesterification, immobilized enzyme, pH not specified in the publication, 40°C

proof_lines: transesterification, free enzyme, pH not specified in the publication, 40°C

proof_lines: hydrolysis, immobilized enzyme, pH not specified in the publication, 40°C


organism: Bacillus sp. KY0701

substrate_name: 4-nitrophenyl butanoate

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

substrate: 4-nitrophenyl butanoate


organism: Blastobotrys adeninivorans

substrate_name: ethyl adipate

smiles: CCOC(=O)CCCCC(=O)OCC

proof_lines:
pH 4.9, 30°C, recombinant enzyme
pH 7.2, 30°C, recombinant enzyme

substrate: ethyl adipate


organism: Russula virescens


organism: Mycothermus thermophilus

substrate_name: 4-nitrophenyl butyrate

proof_lines:
pH 7.5, 25°C
pH 7.5, 30°C, recombinant enzyme

substrate: 4-nitrophenyl butyrate


organism: Thermobifida cellulosilytica

proof_lines: pH and temperature not specified in the publication


proof_lines:
pH 8.0, 60°C, isozyme Tfu 0882
pH 8.0, 60°C, isozyme Tfu 0883
pH 8.0, 50°C


organism: Zea mays

substrate_name: methyl ferulate

substrate: methyl ferulate


enzyme_display_name: poly(3-hydroxybutyrate) depolymerase

organism: Thermobifida sp. BCC23166

substrate_name: p-nitrophenyl butyrate

enzyme: poly(3-hydroxybutyrate) depolymerase

substrate: p-nitrophenyl butyrate


organism: Lihuaxuella thermophila


enzyme_display_name: poly(3-hydroxyoctanoate) depolymerase

organism: Pseudomonas aeruginosa

enzyme: poly(3-hydroxyoctanoate) depolymerase


organism: Streptomyces venezuelae

substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


organism: Mycobacterium tuberculosis

substrate_name: triolein

substrate: triolein


organism: Bjerkandera adusta

substrate_name: 2-naphthyl acetate

proof_lines: pH 7.0, temperature not specified in the publication

substrate: 2-naphthyl acetate


organism: uncultured bacterium


organism: Ralstonia pickettii

substrate_name: 4-nitrophenyl pentanoate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A66V/N251S/T290A with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant A66V/N251S/T290A, pH 7.0, 30°C

substrate: 4-nitrophenyl pentanoate


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G108G/Q125L/R230R/K260M/T284S/G310G with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant G108G/Q125L/R230R/K260M/T284S/G310G, pH 7.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S92S/G180D/I292F with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant S92S/G180D/I292F, pH 7.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T145S/S246T/T252T/S257T with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant T145S/S246T/T252T/S257T, pH 7.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A66V/T145S/N285D with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant A66V/T145S/N285D, pH 7.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A66V/N285D/G310G with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant A66V/N285D/G310G, pH 7.0, 30°C


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A66V with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


substrate_name: 4-nitrophenyl propionate

substrate: 4-nitrophenyl propionate


organism: Rhodospirillum rubrum

substrate_name: Unknown

substrate: Unknown


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

proof_lines: recombinant mutant T37A/N285Y, pH 7.0, 30°C


proof_lines: recombinant mutant S92S/T145S/N285Y, pH 7.0, 30°C


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


proof_lines: recombinant mutant T252T/S257T/N285D, pH 7.0, 30°C


proof_lines: recombinant mutant T37A/N285D, pH 7.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T37A/N285D with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T37A/N285Y with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N285D with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T252T/S257T/N285D with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N285Y with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S92S/T145S/N285Y with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


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


enzyme_display_name: UniProt A3FJ64

organism: Bacillus thuringiensis

substrate_name: N-octanoyl-L-homoserine lactone

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

enzyme: UniProt A3FJ64

substrate: N-octanoyl-L-homoserine lactone


substrate_name: N-heptanoyl-L-homoserine lactone

substrate: N-heptanoyl-L-homoserine lactone


substrate_name: N-pentanoyl-L-homoserine lactone

substrate: N-pentanoyl-L-homoserine lactone


enzyme_display_name: UniProt I7HB71

organism: Chryseobacterium sp. StRB126

substrate_name: N-dodecanoyl-L-homoserine lactone

enzyme: UniProt I7HB71

substrate: N-dodecanoyl-L-homoserine lactone


substrate_name: N-butyryl-L-homoserine lactone

substrate: N-butyryl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

substrate: N-hexanoyl-L-homoserine lactone


enzyme_display_name: UniProt P0CJ63

organism: Bacillus thuringiensis serovar kurstaki

enzyme: UniProt P0CJ63


substrate_name: N-decanoyl-L-homoserine lactone

substrate: N-decanoyl-L-homoserine lactone


organism: Geobacillus kaustophilus

substrate_name: paraoxon

assay_conditions_summary: pH 8.3; 310.15 K; buffer 2.5 mM Bicine

proof_lines: wild type enzyme, in 2.5 mM Bicine buffer, pH 8.3, at 37°C

substrate: paraoxon


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

proof_lines: pH 8.3, 37°C, recombinant mutant E101G/R230C

proof_lines: kcat below 0.009 s-1, mutant enzyme E101G/R230C, in 2.5 mM Bicine buffer, pH 8.3, at 37°C


proof_lines: kcat below 0.011 s-1, mutant enzyme E101N/R230I, in 2.5 mM Bicine buffer, pH 8.3, at 37°C


proof_lines: pH 8.3, 37°C, recombinant wild-type enzyme


proof_lines: mutant enzyme E101G/R230C, in 2.5 mM Bicine buffer, pH 8.3, at 37°C


proof_lines: pH 8.3, 37°C, recombinant mutant E101N/R230I

proof_lines: mutant enzyme E101N/R230I, in 2.5 mM Bicine buffer, pH 8.3, at 37°C


substrate_name: N-3-oxo-octanoyl-L-homoserine lactone

substrate: N-3-oxo-octanoyl-L-homoserine lactone


substrate_name: N-3-oxo-hexanoyl-L-homoserine lactone

substrate: N-3-oxo-hexanoyl-L-homoserine lactone


substrate_name: N-(3-oxooctanoyl)-L-homoserine lactone

proof_lines: mutant enzyme E101N/R230, in 2.5 mM Bicine buffer, pH 8.3, at 37°C

substrate: N-(3-oxooctanoyl)-L-homoserine lactone


substrate_name: N-(3-oxohexanoyl)-L-homoserine lactone

substrate: N-(3-oxohexanoyl)-L-homoserine lactone


organism: Aspergillus niger

substrate_name: methyl caffeate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y80S with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

substrate: methyl caffeate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y80V with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


substrate_name: methyl sinapinate

substrate: methyl sinapinate


substrate_name: methyl p-coumarate

substrate: methyl p-coumarate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W260V with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W260S with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


substrate_name: methyl ferulate

substrate: methyl ferulate


substrate_name: delta-nonalactone

substrate: delta-nonalactone


substrate_name: N-3-oxo-dodecanoyl-L-homoserine lactone

substrate: N-3-oxo-dodecanoyl-L-homoserine lactone


substrate_name: gamma-nonalactone

substrate: gamma-nonalactone


proof_lines: mutant enzyme E101V/R230T, in 2.5 mM Bicine buffer, pH 8.3, at 37°C


proof_lines: mutant enzyme E101K/R230P, in 2.5 mM Bicine buffer, pH 8.3, at 37°C


organism: Saccharococcus caldoxylosilyticus

substrate_name: whiskey lactone

substrate: whiskey lactone


substrate_name: epsilon-decalactone

substrate: epsilon-decalactone


substrate_name: delta-valerolactone

substrate: delta-valerolactone


substrate_name: N-octanoyl-L-homoserine lactone

substrate: N-octanoyl-L-homoserine lactone


substrate_name: gamma-heptalactone

substrate: gamma-heptalactone


substrate_name: gamma-butyrolactone

substrate: gamma-butyrolactone


substrate_name: gamma-decanolactone

substrate: gamma-decanolactone


substrate_name: delta-decalactone

substrate: delta-decalactone


substrate_name: N-(3-oxooctanoyl)-L-homoserine lactone

substrate: N-(3-oxooctanoyl)-L-homoserine lactone


substrate_name: epsilon-caprolactone

substrate: epsilon-caprolactone


substrate_name: delta-octanolactone

substrate: delta-octanolactone


organism: Saccharolobus solfataricus

proof_lines: mutant enzyme W263F, at pH 8.3, temperature not specified in the publication


substrate_name: N-(3-oxodecanoyl)-L-homoserine lactone

proof_lines: mutant enzyme V82I, at pH 8.3, temperature not specified in the publication

substrate: N-(3-oxodecanoyl)-L-homoserine lactone


proof_lines: mutant enzyme W263I, at pH 8.3, temperature not specified in the publication

proof_lines: mutant enzyme W263I, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme V82I/A275G, at pH 8.3, temperature not specified in the publication


proof_lines: mutant enzyme W263F, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme W263T, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme W263V, at 25°C, pH not specified in the publication


proof_lines: wild type enzyme, at 25°C, pH not specified in the publication


enzyme_display_name: pyrethroid hydrolase

organism: Escherichia coli

substrate_name: 4-nitrophenyl laurate

enzyme: pyrethroid hydrolase

substrate: 4-nitrophenyl laurate


substrate_name: 4-nitrophenyl decanoate

substrate: 4-nitrophenyl decanoate


substrate_name: 4-nitrophenyl caproate

substrate: 4-nitrophenyl caproate


substrate_name: 4-nitrophenyl caprylate

substrate: 4-nitrophenyl caprylate


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: N-3-oxododecanoyl-L-homoserine lactone

proof_lines: mutant enzyme C258L/I261F/W263A, at pH 8.0 and 25°C

substrate: N-3-oxododecanoyl-L-homoserine lactone


proof_lines: mutant enzyme L72I/Y99F/I122L/L228M/F229S/W263L, at pH 8.0 and 25°C


substrate_name: undecanoic-gamma-lactone

proof_lines: mutant enzyme V27A/I76T/Y97W/Y99F/L130P/L226V, at pH 8.0 and 25°C

substrate: undecanoic-gamma-lactone


proof_lines: mutant enzyme F46L/C258A/W263M/I280T, at pH 8.0 and 25°C


substrate_name: undecanoic-delta-lactone

proof_lines: mutant enzyme V27A/Y97W/L228M/W263M, at pH 8.0 and 25°C

substrate: undecanoic-delta-lactone


organism: Flagellimonas olearia

substrate_name: N-butyryl-L-homoserine lactone

substrate: N-butyryl-L-homoserine lactone


substrate_name: N-octanoyl-L-homoserine lactone

substrate: N-octanoyl-L-homoserine lactone


substrate_name: N-3-oxooctanoyl-L-homoserine lactone

substrate: N-3-oxooctanoyl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

substrate: N-hexanoyl-L-homoserine lactone


enzyme_display_name: cocaine esterase

organism: Stenotrophomonas maltophilia

substrate_name: cocaine

enzyme: cocaine esterase

substrate: cocaine


substrate_name: ethyl 2-hydroxybenzoate

substrate: ethyl 2-hydroxybenzoate


substrate_name: ethyl benzoate

substrate: ethyl benzoate


organism: Kurthia huakuii

substrate_name: N-tetradecanoyl-L-homoserine lactone

substrate: N-tetradecanoyl-L-homoserine lactone


substrate_name: N-3-oxohexanoyl-L-homoserine lactone

substrate: N-3-oxohexanoyl-L-homoserine lactone


substrate_name: N-decanoyl-L-homoserine lactone

substrate: N-decanoyl-L-homoserine lactone


organism: Brevundimonas diminuta

substrate_name: N-(3-oxododecyl)-L-homoserine lactone

substrate: N-(3-oxododecyl)-L-homoserine lactone


substrate_name: N-butyryl-DL-homoserine lactone

substrate: N-butyryl-DL-homoserine lactone


substrate_name: L-homoserine lactone

substrate: L-homoserine lactone


organism: Vulcanisaeta moutnovskia

substrate_name: dodecanoic-gamma-lactone

substrate: dodecanoic-gamma-lactone


substrate_name: N-octanoyl-DL-homoserine lactone

substrate: N-octanoyl-DL-homoserine lactone


substrate_name: (S)-gamma-caprolactone

substrate: (S)-gamma-caprolactone


enzyme_display_name: pheophorbidase

organism: Chenopodium album

substrate_name: pheophorbide a

enzyme: pheophorbidase

substrate: pheophorbide a


substrate_name: Unknown

substrate: Unknown


substrate_name: N-butanoyl-DL-homoserine lactone

substrate: N-butanoyl-DL-homoserine lactone


enzyme_display_name: rhamnogalacturonan acetylesterase

organism: Paenibacillus polymyxa

substrate_name: 4-nitrophenyl acetate

enzyme: rhamnogalacturonan acetylesterase

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: N-butyryl-L-homoserine lactone

proof_lines: pH and temperature not specified in the publication

substrate: N-butyryl-L-homoserine lactone


organism: Acetivibrio thermocellus

substrate_name: beta-D-gluco pentaacetate

substrate: beta-D-gluco pentaacetate


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature W263I with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


organism: Chlamydomonas reinhardtii


organism: Glycomyces salinus


organism: Plutella xylostella

substrate_name: Alpha-naphthyl acetate

substrate: Alpha-naphthyl acetate


substrate_name: N-(3-oxohexanoyl)-L-homoserine lactone

column_label: Table 1 row 3-oxo-C6-L-HSL has matching Km and kcat cells; package kcat/Km equals 0.52 / 5.6 = 0.09285714285714286 s^-1 mM^-1.

normalized_value_unit_evidence: Km 5.6 mM; kcat 0.52 s^-1; kcat/Km 0.092 s^-1 mM^-1 table-rounded; expected ratio 0.09285714285714286 s^-1 mM^-1 from table means

table_label: Table 1

substrate: N-(3-oxohexanoyl)-L-homoserine lactone


column_label: Primary Table 1 C12 row supports 0.17 mM / 0.95 s^-1, not the BRENDA tuple 0.0178 mM / 1.8 s^-1.


substrate_name: N-(3-oxooctanoyl)-L-homoserine lactone

column_label: Table 1 row 3-oxo-C8-L-HSL has matching Km and kcat cells; package kcat/Km equals 1.0 / 0.16 = 6.25 s^-1 mM^-1.

normalized_value_unit_evidence: Km 0.16 mM; kcat 1.0 s^-1; kcat/Km 6.6 s^-1 mM^-1 table-rounded; expected ratio 6.25 s^-1 mM^-1 from table means

substrate: N-(3-oxooctanoyl)-L-homoserine lactone


substrate_name: N-(3-oxodecanoyl)-L-homoserine lactone

column_label: Table 1 row 3-oxo-C10-L-HSL has the exact kcat and Km cells matching this tuple; package kcat/Km equals 1.5 / 0.050 = 30.0 s^-1 mM^-1.

normalized_value_unit_evidence: Km 0.050 mM; kcat 1.5 s^-1; kcat/Km 30.0 s^-1 mM^-1 from table mean kcat/Km; explicit table kcat/Km column reports 290 s^-1 mM^-1 and is internally inconsistent with the kcat and Km cells

substrate: N-(3-oxodecanoyl)-L-homoserine lactone


substrate_name: N-decanoyl-L-homoserine lactone

normalized_value_unit_evidence: Km 1.45 uM = 0.00145 mM; kcat 5.48 s^-1; printed kcat/Km 3.77 x 10^6 M^-1 s^-1 = 3770 s^-1 mM^-1; expected computed ratio 3779.310344827587 s^-1 mM^-1 is within table precision/rounding.

table_label: Table 1, Kinetic parameters of GcL at 25 C

substrate: N-decanoyl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

normalized_value_unit_evidence: Km 7.97 uM = 0.00797 mM; kcat 8.95 s^-1; printed kcat/Km 1.12 x 10^6 M^-1 s^-1 = 1120 s^-1 mM^-1; expected computed ratio 1122.961104140527 s^-1 mM^-1 is within table precision/rounding.

substrate: N-hexanoyl-L-homoserine lactone


substrate_name: N-3-oxododecanoyl-L-homoserine lactone

substrate: N-3-oxododecanoyl-L-homoserine lactone


organism: Homo sapiens

substrate_name: norcocaine

substrate: norcocaine


substrate_name: cocaethylene

substrate: cocaethylene


substrate_name: norcocaethylene

substrate: norcocaethylene


sequence_variant_note: Mutation signature A199S/S287G/A328W/Y332G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme A199S/S287G/A328W/Y332G, at pH 7.4 and 25°C


sequence_variant_note: Mutation signature A199S/F227A/S287G/A328W/Y332G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme A199S/F227A/S287G/A328W/Y332G, at pH 7.4 and 25°C


substrate_name: (-)-cocaine

proof_lines: mutant enzyme A199S/F227A/S287G/A328W/Y332G, pH not specified in the publication, at 25°C

substrate: (-)-cocaine


organism: Sphingobium sp.

substrate_name: bifenthrin

proof_lines: kcat is 3.03 sec(-1) with trans-Permethrin acetate as substrate. kcat is 3.00 sec(-1) with cis-Permethrin acetate as substrate. kcat is 2.61 sec(-1) with Fenpropathrin acetate as substrate. kcat is 2.53 sec(-1) with trans-Cypermethrin aceta

substrate: bifenthrin


substrate_name: deltamethrin

substrate: deltamethrin


substrate_name: cyhalothrin

substrate: cyhalothrin


substrate_name: trans-cypermethrin

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM sodium phosphate

column_label: TABLE 1: Kinetic constants determined for the purified recombinant PytH (Appl. Environ. Microbiol. 2009, 75(17):5496-5500). Column heads, in printed order: 'Substrate'; 'Sp act (umol/min/mg)'; 'kcat (s^-1)'; 'Km (uM)'; 'kcat/Km (uM^-1 . s^-1)', all under the banner head 'Mean +/- SD'. The line read here is the one whose substrate label is 'trans-Cypermethrin': its Sp act cell, its kcat cell 2.53, its Km cell 0.110 and its kcat/Km cell 23.01 sit at the four fixed character columns of the rendering, so each number belongs to the head above it.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.53 s^-1; the printed unit is already the canonical one, so no unit conversion applies; normalized 2.53 s^(-1). Km: printed Table 1 cell 0.110 uM; 0.110 / 1000 = 0.00011 mM. kcat/Km: printed Table 1 cell 23.01 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 23.01 x 1000 = 23010.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, line 'trans-Cypermethrin': kcat column (s^-1) = 2.53; Km column (uM) = 0.110; printed kcat/Km column (uM^-1 s^-1) = 23.01.

row_label: Table 1 line 'trans-Cypermethrin'

substrate: trans-cypermethrin


substrate_name: (alphaR)-fenpropathrin

substrate: (alphaR)-fenpropathrin


substrate_name: cis-permethrin

column_label: TABLE 1: Kinetic constants determined for the purified recombinant PytH (Appl. Environ. Microbiol. 2009, 75(17):5496-5500). Column heads, in printed order: 'Substrate'; 'Sp act (umol/min/mg)'; 'kcat (s^-1)'; 'Km (uM)'; 'kcat/Km (uM^-1 . s^-1)', all under the banner head 'Mean +/- SD'. The line read here is the one whose substrate label is 'cis-Permethrin': its Sp act cell, its kcat cell 3.00, its Km cell 0.065 and its kcat/Km cell 46.15 sit at the four fixed character columns of the rendering, so each number belongs to the head above it.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.00 s^-1; the printed unit is already the canonical one, so no unit conversion applies; normalized 3.0 s^(-1). Km: printed Table 1 cell 0.065 uM; 0.065 / 1000 = 0.00006500000000000001 mM. kcat/Km: printed Table 1 cell 46.15 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 46.15 x 1000 = 46150.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, line 'cis-Permethrin': kcat column (s^-1) = 3.00; Km column (uM) = 0.065; printed kcat/Km column (uM^-1 s^-1) = 46.15.

row_label: Table 1 line 'cis-Permethrin'

substrate: cis-permethrin


substrate_name: 4-nitrophenyl hexanoate

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

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Chryseobacterium sp. StRB126

substrate_name: N-dodecanoyl-L-homoserine lactone

proof_lines: pH 7.5, temperature not specified in the publication

substrate: N-dodecanoyl-L-homoserine lactone


substrate_name: N-decanoyl-L-homoserine lactone

substrate: N-decanoyl-L-homoserine lactone


substrate_name: N-butyryl-L-homoserine lactone

substrate: N-butyryl-L-homoserine lactone


substrate_name: N-octanoyl-L-homoserine lactone

substrate: N-octanoyl-L-homoserine lactone


substrate_name: N-pentanoyl-L-homoserine lactone

substrate: N-pentanoyl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

substrate: N-hexanoyl-L-homoserine lactone


substrate_name: N-heptanoyl-L-homoserine lactone

substrate: N-heptanoyl-L-homoserine lactone


organism: Marinactinospora thermotolerans

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C2 / MtCut, column MtCut; Km mM, raw cell 0.55 +/- 0.04, normalized 0.55 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C2 / MtCut, column MtCut; kcat s^-1, raw cell 4.47 +/- 0.28, normalized 4.47 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C2 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (8.19 +/- 0.34) x 10^3, normalized 8.19 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.55 normalized_unit=mM; kcat normalized_value=4.47 normalized_unit=s^-1; kcat/Km normalized_value=8.19 normalized_unit=s^-1*mM^-1

row_label: pNP-C2 / MtCut


substrate_name: 4-nitrophenyl palmitate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C16 / MtCut, column MtCut; Km mM, raw cell 0.15 +/- 0.01, normalized 0.15 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C16 / MtCut, column MtCut; kcat s^-1, raw cell 4.79 +/- 0.12, normalized 4.79 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C16 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (3.25 +/- 0.10) x 10^4, normalized 32.5 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.15 normalized_unit=mM; kcat normalized_value=4.79 normalized_unit=s^-1; kcat/Km normalized_value=32.5 normalized_unit=s^-1*mM^-1

row_label: pNP-C16 / MtCut

substrate: 4-nitrophenyl palmitate


substrate_name: 4-nitrophenyl myristate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C14 / MtCut, column MtCut; Km mM, raw cell 0.19 +/- 0.04, normalized 0.19 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C14 / MtCut, column MtCut; kcat s^-1, raw cell 9.87 +/- 1.52, normalized 9.87 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C14 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (5.14 +/- 0.29) x 10^4, normalized 51.4 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.19 normalized_unit=mM; kcat normalized_value=9.87 normalized_unit=s^-1; kcat/Km normalized_value=51.4 normalized_unit=s^-1*mM^-1

row_label: pNP-C14 / MtCut

substrate: 4-nitrophenyl myristate


substrate_name: 4-nitrophenyl butyrate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C4 / MtCut, column MtCut; Km mM, raw cell 1.33 +/- 0.15, normalized 1.33 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C4 / MtCut, column MtCut; kcat s^-1, raw cell 14.10 +/- 1.51, normalized 14.1 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C4 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (1.06 +/- 0.01) x 10^4, normalized 10.6 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=1.33 normalized_unit=mM; kcat normalized_value=14.1 normalized_unit=s^-1; kcat/Km normalized_value=10.6 normalized_unit=s^-1*mM^-1

row_label: pNP-C4 / MtCut

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl octadecanoate

column_label: TABLE 1 | MtCut kinetic parameters toward pNP esters; row pNP-C18; columns Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); normalized kcat/Km to s^-1 mM^-1.

normalized_value_unit_evidence: kcat paper=14.31 s^-1; km paper=0.45 mM; kcat_over_km paper=31.8 s^-1 mM^-1

raw_value_unit_evidence: TABLE 1 | MtCut kinetic parameters toward pNP esters, row pNP-C18: Km 0.45 mM; kcat 14.31 s^-1; kcat/Km 31.8 s^-1 mM^-1 after converting the printed M^-1 s^-1 value by dividing by 1000.

substrate: 4-nitrophenyl octadecanoate


substrate_name: 4-nitrophenyl dodecanoate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C12 / MtCut, column MtCut; Km mM, raw cell 1.68 +/- 0.12, normalized 1.68 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C12 / MtCut, column MtCut; kcat s^-1, raw cell 30.52 +/- 3.63, normalized 30.52 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C12 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (1.81 +/- 0.12) x 10^4, normalized 18.1 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=1.68 normalized_unit=mM; kcat normalized_value=30.52 normalized_unit=s^-1; kcat/Km normalized_value=18.1 normalized_unit=s^-1*mM^-1

row_label: pNP-C12 / MtCut

substrate: 4-nitrophenyl dodecanoate


column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C6 / MtCut, column MtCut; Km mM, raw cell 4.61 +/- 1.04, normalized 4.61 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C6 / MtCut, column MtCut; kcat s^-1, raw cell 41.72 +/- 6.35, normalized 41.72 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C6 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (9.23 +/- 0.90) x 10^3, normalized 9.23 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=4.61 normalized_unit=mM; kcat normalized_value=41.72 normalized_unit=s^-1; kcat/Km normalized_value=9.23 normalized_unit=s^-1*mM^-1

row_label: pNP-C6 / MtCut