substrate_name: L-Phe

sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature H285Q to reconstruct the assayed variant sequence.

substrate: L-Phe


enzyme_display_name: phenylalanine 4-monooxygenase

organism: Rattus norvegicus

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature H290Q to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: phenylalanine 4-monooxygenase

source: brenda


substrate_name: L-phenylalanine

sequence_source: UniProtKB:P04176 reviewed canonical sequence retained as context only

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

substrate: L-phenylalanine


substrate_name: phenylalanine

mutation_signature: Unknown

sequence_source: UniProtKB:P04176 reviewed canonical sequence; BRENDA EC 1.14.16.1 Rattus norvegicus accession context

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

substrate: phenylalanine


substrate_name: tetrahydrobiopterin

sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16A to reconstruct the assayed variant sequence.

substrate: tetrahydrobiopterin


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04176 reviewed canonical sequence plus cited paper mutation and applied mutation signature S16N to reconstruct the assayed variant sequence.


organism: Homo sapiens

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


substrate_name: Abz-VAA

proof_lines:
mutant Y325F, 25°C, pH 7.0
mutant enzyme Y325F, 25°C, pH 7.0

substrate: Abz-VAA


proof_lines:
mutant Y325L, 25°C, pH 7.0
mutant enzyme Y325L, 25°C, pH 7.0


mutation_signature: Asp112-Lys452 deletion mutant

mutation_type: deletion

proof_lines: Asp112-Lys452 deletion mutant, tetrameric form

proof_lines: Asp112-Lys452 deletion mutant, L-phenylalanine activated, tetrameric form

proof_lines: Asp112-Lys452 deletion mutant, lysophosphatidylcholine and phenylalanine activated, tetrameric form


mutation_signature: Gly103-Gln428 deletion mutant

proof_lines: Gly103-Gln428 deletion mutant, tetrameric form

proof_lines: Gly103-Gln428 deletion mutant, L-phenylalanine activated, dimeric form

proof_lines: Gly103-Gln428 deletion mutant, lysophosphatidylcholine activated, dimeric form


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

proof_lines: recombinant enzyme, L-phenylalanine activated, tetrameric form

proof_lines: recombinant enzyme, lysophosphatidylcholine and phenylalanine activated, tetrameric form


mutation_signature: Ser2-Gln428 deletion mutant

proof_lines: Ser2-Gln428 deletion mutant, tetrameric form

proof_lines: Ser2-Gln428 deletion mutant, lysophosphatidylcholine and phenylalanine activated, dimeric form

proof_lines: Ser2-Gln428 deletion mutant, L-phenylalanine activated, dimeric form


mutation_signature: truncated enzyme containing C-terminal 334 amino acids truncated enzyme containing C-terminal 334 amino acids

mutation_type: truncation


proof_lines: allelic combination wild-type/mutant I65T, Vmax: 1 micromol/min/mg, pH 6.8, 37°C

proof_lines: allelic combination wild-type/mutant R68S, Vmax: 1 micromol/min/mg, pH 6.8, 37°C


substrate_name: tryptophan

assay_conditions_summary: pH 7

proof_lines: truncated enzyme containing C-terminal 334 amino acids, pH 7.0

proof_lines: truncated enzyme containing C-terminal 334 amino acids, pH 8.0

substrate: tryptophan


organism: Legionella pneumophila


organism: Mus musculus

proof_lines: using 6-methyltetrahydropterin as cofactor

proof_lines: using 5,6,7,8-tetrahydrobiopterin as cofactor


organism: Caenorhabditis elegans

substrate_name: L-phenylalanine (at 25 degrees Celsius)

source_db: uniprot

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

substrate: L-phenylalanine (at 25 degrees Celsius)

source: uniprot


organism: Pseudomonas sp.

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


proof_lines: phosphorylated recombinant wild-type enzyme


proof_lines: pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH V379D

proof_lines: pH 7.0, 25°C, recombinant mutant DELTA 117PheH V379D


proof_lines: pH 7.0, 25°C, recombinant mutant DELTA 117PheH

proof_lines: pH 7.0, 25°C, with cofactor 6-methyl-tetrahydrobiopterin, recombinant mutant DELTA 117PheH


enzyme_display_name: leucyl aminopeptidase

organism: Unknown

enzyme: leucyl aminopeptidase


organism: Arabidopsis thaliana

substrate_name: L-leucine-p-nitroanilide

substrate: L-leucine-p-nitroanilide


organism: Solanum lycopersicum


organism: Bos taurus

substrate_name: L-Leucylglycine

source_db: oed

kcat_over_km_origin: calculated

data_origin: experimental

substrate: L-Leucylglycine

source: oed


substrate_name: Cys-Gly

source_db: brenda,skid

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

source_databases_merged: brenda skid

substrate: Cys-Gly

source: brenda,skid


substrate_name: Ser-Gly

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

substrate: Ser-Gly


substrate_name: H2O; L-Cysteinylglycine

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

substrate: H2O; L-Cysteinylglycine


substrate_name: Met-Gly

substrate: Met-Gly


organism: Clonorchis sinensis


proof_lines:
pH 8, 20°C
pH 7.5, 37°, Vmax: 10.7 microM/min


organism: Cryptosporidium parvum


organism: Sus scrofa

substrate_name: H2O; Leu-p-nitroanilide

substrate: H2O; Leu-p-nitroanilide


substrate_name: H2O; Arg-7-amino-4-methylcoumarin

substrate: H2O; Arg-7-amino-4-methylcoumarin


substrate_name: Leu-p-nitroanilide

substrate: Leu-p-nitroanilide


organism: Thermotoga maritima


organism: Trypanosoma cruzi


proof_lines:
pH 9.0, 50°C
native enzyme, pH 7.5, 37°C
recombinant enzyme, pH 7.5, 37°C


organism: Desulfurococcus amylolyticus

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

proof_lines: pH 7.5, 50°C, enzyme activated by heating at 70°C


organism: Geobacillus kaustophilus

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q7X2C8 and applied mutation signature N345L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 20 mM Tris-HCl

proof_lines: mutant enzyme N345L, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2


proof_lines: wild type enzyme, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q7X2C8 and applied mutation signature N345Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N345Q, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2


organism: Haemaphysalis longicornis


organism: Leishmania amazonensis

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme


organism: Leishmania donovani


organism: Leishmania major


organism: Plasmodium berghei


organism: Acinetobacter calcoaceticus

substrate_name: leucinamide

substrate: leucinamide


organism: Aspergillus oryzae


proof_lines:
Zn2+-Zn2+-enzyme form
similar value
lens enzyme


organism: Cannabis sativa


organism: Eisenia fetida


organism: Gadus morhua


organism: Gallus gallus


organism: Hippoglossus hippoglossus


organism: Homo sapiens


organism: Hordeum vulgare

substrate_name: H2O; Leu-Tyr

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

substrate: H2O; Leu-Tyr


organism: Lactobacillus acidophilus

substrate_name: L-Leu-Gly

substrate: L-Leu-Gly


organism: Bos taurus

substrate_name: Cys-Gly (at pH 6.9 and 25 degrees Celsius)

proof_lines: kcat is 3400 min(-1) for Cys-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 11500 min(-1) for Leu-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 8150 min(-1) for Met-Gly hydrolysis activity (at pH 6


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: H-Leu-NHMec (in the presence of Zn(2+), but only metal binding site 2 occupied)

assay_conditions_summary: pH 8

proof_lines: kcat is 2200 sec(-1) with for H-Leu-NHMec as substrate (in the presence of Zn(2+), but only metal binding site 2 occupied) (PubMed:19408962). kcat is 3800 sec(-1) with for H-Leu-NHMec as substrate (in the presence of Zn(2+), both metal bind


organism: Plasmodium vivax (strain Salvador I)

substrate_name: H-Leu-NHMec

proof_lines: kcat is 0.04 sec(-1) with for H-Leu-NHMec as substrate (at pH 8, at 37 degrees Celsius and in the presence of Co(2+)) (PubMed:34133730). kcat is 0.98 sec(-1) with for H-Leu-NHMec as substrate (at pH 8, at 37 degrees Celsius and in the prese

substrate: H-Leu-NHMec


organism: Solanum lycopersicum

substrate_name: Leu-Gly

proof_lines: kcat is 120 sec(-1) with Leu-Gly as substrate.

substrate: Leu-Gly


organism: Lingulaulax polyedra


organism: Morimus funereus


organism: Pagrus major

assay_conditions_summary: pH 7; 310.15 K; buffer 25 mM sodium phosphate

proof_lines: in 25 mM sodium phosphate buffer (pH 7.0) containing 1 mM dithiothreitol and 0.02% NaN3, at 37°C


organism: Phaseolus vulgaris

substrate_name: Ala-Ala-Ala-Ala

substrate: Ala-Ala-Ala-Ala


organism: Plasmodium falciparum

proof_lines: pH 8.0, 37°C, recombinant enzyme in presence of Zn2+ and Mg2+, best ion combination at metal binding sites 1 and 2


organism: Plasmodium vivax


organism: Schistosoma mansoni


organism: Setaria cervi


substrate_name: Gly-Gly

proof_lines:
His-tagged recombinant enzyme, 37°C
free recombinant enzyme, 37°C

substrate: Gly-Gly


organism: Acanthamoeba castellanii

verification_status: unverified

status: unverified


organism: Arabidopsis thaliana

substrate_name: H2O; L-Leucinyl-p-nitroanilide

substrate: H2O; L-Leucinyl-p-nitroanilide


substrate_name: L-Cysteinylglycine

substrate: L-Cysteinylglycine


substrate_name: Cys-Leu

substrate: Cys-Leu


substrate_name: H2O; L-Cysteinylglycine


substrate_name: Leu-Cys

substrate: Leu-Cys


organism: Babesia gibsoni


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


organism: Bacillus subtilis


proof_lines: inhibitory activity against recombinant enzyme


substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Pseudoalteromonas agarivorans

substrate_name: L-Leu 7-amido-4-methylcoumarin

substrate: L-Leu 7-amido-4-methylcoumarin


organism: Salmonella enterica

substrate_name: Asp-Phe

substrate: Asp-Phe


organism: Schizosaccharomyces pombe


substrate_name: Leu-p-nitroanilide


substrate_name: Arg-Leu

substrate: Arg-Leu


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


substrate_name: Leu-Leu

substrate: Leu-Leu


substrate_name: Glycyl-leucine

substrate: Glycyl-leucine


substrate_name: Arg-Gly

substrate: Arg-Gly


substrate_name: Leu-Gly-Gly

substrate: Leu-Gly-Gly


substrate_name: Arg-Gly-Asp

substrate: Arg-Gly-Asp


substrate_name: Arg-Gly-Phe

substrate: Arg-Gly-Phe


substrate_name: H2O; Leu-Gly

substrate: H2O; Leu-Gly


substrate_name: L-Leucylglycine

substrate: L-Leucylglycine


organism: Solanum tuberosum


organism: Staphylococcus aureus


organism: Sus scrofa

substrate_name: Gly-Phe

proof_lines:
Zn2+-Zn2+-enzyme form
Mg2+-Zn2+-enzyme form
native enzyme, pH 8.0, 25°C

substrate: Gly-Phe


organism: Telchin licus licus

proof_lines: pH 7.0, temperature not specified in the publication


organism: Thermomyces lanuginosus


organism: Toxoplasma gondii


organism: Vibrio proteolyticus


enzyme_display_name: beta-glucosidase

organism: Oryza sativa subsp. japonica

substrate_name: p-nitrophenyl beta-D-glucoside (at pH 5.0)

enzyme: beta-glucosidase


substrate: p-nitrophenyl beta-D-glucoside (at pH 5.0)


organism: Phanerodontia chrysosporium

substrate_name: cellobiose

substrate: cellobiose


organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)


organism: Zea mays

substrate_name: p-nitrophenyl beta-D-glucopyranoside (PNPG) (with recombinant enzyme)


organism: Halothermothrix orenii

verification_status: verified

sequence_source: UniProtKB:B8CYA8 direct REST lookup; active primary accession B8CYA8

assay_conditions_summary: pH 7; 343.15 K; buffer the coupled glucose oxidase/peroxidase method in 20 mM HEPES

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'WT', D-cellobiose block: k_cat,app = 387 ± 15; K_m = 10.0 ± 1.0; k_cat,app/K_m = 38.7.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 387 ± 15 in column 'k_cat,app (s^-1)' of the D-cellobiose block; the value is already s^-1, so no conversion is applied and the paper value is 387.0 s^(-1). K_m: printed Table 2 cell 10.0 ± 1.0 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 10.0 mM. k_cat/K_m: printed Table 2 cell 38.7 in column 'k_cat,app/K_m (mM^-1 s^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 38.7 s^(-1)*mM^(-1). Closure check: 387.0 / 10.0 = 38.7 s^-1 mM^-1, which rounds to the printed efficiency cell 38.7 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'WT', D-cellobiose block: column 'k_cat,app (s^-1)' prints 387 ± 15; column 'K_m (mM)' prints 10.0 ± 1.0; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 38.7.

row_label: Table 2, body row 'WT' (wild type (the unmarked 70 °C row)), D-cellobiose block

status: verified


substrate_name: lactose

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature F417Y to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'F417Y', D-lactose block: k_cat,app = 41.5 ± 1.2; K_m = 10.3 ± 0.9; k_cat,app/K_m = 4.0.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 41.5 ± 1.2 in column 'k_cat,app (s^-1)' of the D-lactose block; the value is already s^-1, so no conversion is applied and the paper value is 41.5 s^(-1). K_m: printed Table 2 cell 10.3 ± 0.9 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 10.3 mM. k_cat/K_m: printed Table 2 cell 4.0 in column 'k_cat,app/K_m (s^-1 mM^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 4.0 s^(-1)*mM^(-1). Closure check: 41.5 / 10.3 = 4.02913 s^-1 mM^-1, which rounds to the printed efficiency cell 4.0 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'F417Y', D-lactose block: column 'k_cat,app (s^-1)' prints 41.5 ± 1.2; column 'K_m (mM)' prints 10.3 ± 0.9; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 4.0.

row_label: Table 2, body row 'F417Y' (variant F417Y), D-lactose block

substrate: lactose

status: corrected


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Homo sapiens

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

sequence_source: UniProtKB:Q9H227 direct REST lookup; active primary accession Q9H227


organism: Hordeum vulgare

substrate_name: H2O; Sophorose

sequence_source: UniProtKB:Q40025 direct REST lookup; active primary accession Q40025

substrate: H2O; Sophorose


organism: Lamium galeobdolon


substrate_name: oleuropein

substrate: oleuropein


substrate_name: Dhurrin

substrate: Dhurrin


organism: Listeria innocua Clip11262

sequence_source: UniProtKB:Q92AS9 direct REST lookup; active primary accession Q92AS9


substrate_name: sophorotetraose

assay_conditions_summary: pH 6; 293.15 K; buffer 50 mM Mes

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Sop4: kcat (s^-1) = 3.5 ± 0.9; Km (mM) = 10 ± 4; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 0.34 ± 0.04.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.5 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 3.5 s^(-1). Km: printed Table 1 cell 10 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 10.0 mM. kcat/Km: printed Table 1 cell 0.34 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 0.34 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Sop4: kcat = 3.5 ± 0.9 s^-1; Km = 10 ± 4 mM; printed kcat/Km = 0.34 ± 0.04 s^-1 mM^-1.

table_label: Table 1: Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc (PLoS ONE 2016, 11(2))

substrate: sophorotetraose


substrate_name: laminaribiose

sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB:Q92AS9 canonical sequence by applying R572K and applied mutation signature R572K to reconstruct the assayed variant sequence.

substrate: laminaribiose


substrate_name: Laminaripentaose

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Lam5: kcat (s^-1) = 12 ± 5; Km (mM) = 5.5 ± 2.8; Kis (mM) = 2.7 ± 1.6; kcat/Km (s^-1 mM^-1) = 2.1 ± 0.2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 12 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 12.0 s^(-1). Km: printed Table 1 cell 5.5 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 5.5 mM. kcat/Km: printed Table 1 cell 2.1 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 2.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Lam5: kcat = 12 ± 5 s^-1; Km = 5.5 ± 2.8 mM; printed kcat/Km = 2.1 ± 0.2 s^-1 mM^-1.

substrate: Laminaripentaose


substrate_name: laminaritriose

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Lam3: kcat (s^-1) = 11 ± 1; Km (mM) = 3.7 ± 0.3; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 2.9 ± 0.1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 11 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 11.0 s^(-1). Km: printed Table 1 cell 3.7 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 3.7 mM. kcat/Km: printed Table 1 cell 2.9 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 2.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Lam3: kcat = 11 ± 1 s^-1; Km = 3.7 ± 0.3 mM; printed kcat/Km = 2.9 ± 0.1 s^-1 mM^-1.

substrate: laminaritriose


substrate_name: sophorose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q92AS9 and applied mutation signature R572K to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the R572K enzyme block, substrate row Sop2: kcat (s^-1) = 15 ± 1; Km (mM) = 21 ± 2; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 0.69 ± 0.03.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 15.0 s^(-1). Km: printed Table 1 cell 21 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 21.0 mM. kcat/Km: printed Table 1 cell 0.69 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 0.69 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, R572K enzyme block, substrate row Sop2: kcat = 15 ± 1 s^-1; Km = 21 ± 2 mM; printed kcat/Km = 0.69 ± 0.03 s^-1 mM^-1.

substrate: sophorose


substrate_name: sophoropentaose

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Sop5: kcat (s^-1) = 1.0 ± 0.4; Km (mM) = 11 ± 6; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 0.098 ± 0.020.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.0 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 1.0 s^(-1). Km: printed Table 1 cell 11 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 11.0 mM. kcat/Km: printed Table 1 cell 0.098 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 0.098 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Sop5: kcat = 1.0 ± 0.4 s^-1; Km = 11 ± 6 mM; printed kcat/Km = 0.098 ± 0.020 s^-1 mM^-1.

substrate: sophoropentaose


organism: Thermotoga neapolitana

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

sequence_source: UniProtKB:Q0GC07 direct REST lookup

substrate: 4-nitrophenyl beta-D-glucopyranoside


substrate_name: quercetin 3-O-beta-D-glucopyranoside

sequence_source: UniProtKB:B9K7M5 direct REST lookup

substrate: quercetin 3-O-beta-D-glucopyranoside


organism: Triticum aestivum

substrate_name: H2O; Luteolin 7-O-beta-D-glucoside

substrate: H2O; Luteolin 7-O-beta-D-glucoside


substrate_name: HBOA glucoside; H2O

substrate: HBOA glucoside; H2O


substrate_name: H2O; Apigenin 7-O-beta-D-glucoside

substrate: H2O; Apigenin 7-O-beta-D-glucoside


substrate_name: H2O; p-Nitrophenyl-beta-D-fucoside

substrate: H2O; p-Nitrophenyl-beta-D-fucoside


substrate_name: H2O; p-Nitrophenyl-beta-D-glucoside

sequence_source: UniProtKB:Q1XIR9 direct REST lookup

substrate: H2O; p-Nitrophenyl-beta-D-glucoside


sequence_source: UniProtKB:Q1XH04 direct REST lookup

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1c', pNP-Glc block; column 'Km (mM)' = 1.75; column 'kcat (s^-1)' = 235.9; column 'kcat/Km (s^-1/mM)' = 135.

normalized_value_unit_evidence: kcat: printed Table II cell 235.9 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 235.9 s^(-1). Km: printed cell 1.75 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 1.75 mM. kcat/Km: printed cell 135 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 135.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1c, pNP-Glc block: Km cell 1.75 mM; kcat cell 235.9 s^-1; printed kcat/Km cell 135 s^-1/mM.

row_label: Table II, row TaGlu1c, pNP-Glc block


sequence_source: UniProtKB:Q1XH05 direct REST lookup

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1b', pNP-Glc block; column 'Km (mM)' = 2.16; column 'kcat (s^-1)' = 128.2; column 'kcat/Km (s^-1/mM)' = 59.3.

normalized_value_unit_evidence: kcat: printed Table II cell 128.2 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 128.2 s^(-1). Km: printed cell 2.16 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 2.16 mM. kcat/Km: printed cell 59.3 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 59.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1b, pNP-Glc block: Km cell 2.16 mM; kcat cell 128.2 s^-1; printed kcat/Km cell 59.3 s^-1/mM.

row_label: Table II, row TaGlu1b, pNP-Glc block


organism: uncultured microorganism

substrate_name: 4-nitrophenyl beta-D-fucopyranoside

sequence_source: UniProtKB:A0A1E1FFN6 direct REST lookup

proof_lines: pH 6.0, 60°C, additive: 25 mM cellobiose

proof_lines: pH 6.0, 60°C, additive: 250 mM D-galactose

substrate: 4-nitrophenyl beta-D-fucopyranoside


sequence_source: UniProtKB:Q41761 direct REST lookup


substrate_name: Dhurrin; H2O

sequence_source: UniProtKB:P49235 direct REST lookup

substrate: Dhurrin; H2O


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=5.8


substrate_name: DIBOA-beta-D-glucoside (with native hexamer)

proof_lines: kcat is 48.8 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 338 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 99.2 sec(-1) with p-nitrophenyl beta-D-glucopyranoside


proof_lines: kcat is 137 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 773 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 235.9 sec(-1) with p-nitrophenyl beta-D-glucopyranoside

substrate: DIBOA-beta-D-glucoside (with native hexamer)


proof_lines: kcat is 214 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 1201 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 128.2 sec(-1) with p-nitrophenyl beta-D-glucopyranosid


proof_lines: kcat is 5728 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 330 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme).


organism: Prunus dulcis

substrate_name: beta-Methyl-D-glucopyranoside; H2O

proof_lines: enzyme immobilized on polysulphone capillary membranes, at pH 6.5 and 25°C

proof_lines: increased Km if enzyme immobilized on cellulose

substrate: beta-Methyl-D-glucopyranoside; H2O


organism: Raphanus sativus


organism: Rattus norvegicus


organism: Sinapis alba


organism: Sulfolobus solfataricus


organism: Thermosphaera aggregans


sequence_source: UniProtKB exact accession Q92AS9

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Lam2: kcat (s^-1) = 23 ± 1; Km (mM) = 2.7 ± 0.2; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 8.8 ± 0.4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 23 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 23.0 s^(-1). Km: printed Table 1 cell 2.7 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 2.7 mM. kcat/Km: printed Table 1 cell 8.8 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 8.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Lam2: kcat = 23 ± 1 s^-1; Km = 2.7 ± 0.2 mM; printed kcat/Km = 8.8 ± 0.4 s^-1 mM^-1.


substrate_name: laminaritetraose

substrate: laminaritetraose


substrate_name: sophorotriose

column_label: Table 1 (Kinetic parameters of Lin1840r for beta-linked gluco-oligosaccharides and pNP-beta-Glc) carries an enzyme-block column, a substrate column, a linkage column, and the kinetic column heads kcat (s^-1), Km (mM), Kis (mM) and kcat/Km (s^-1 mM^-1). The cited cell set is the WT enzyme block, substrate row Sop3: kcat (s^-1) = 56 ± 11; Km (mM) = 15 ± 4; Kis (mM) is blank for this row; kcat/Km (s^-1 mM^-1) = 3.8 ± 0.3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 56 under the column head kcat (s^-1); the column is already per second, so no conversion applies and the paper value is 56.0 s^(-1). Km: printed Table 1 cell 15 under the column head Km (mM); the column is already in mM, so no conversion applies and the paper value is 15.0 mM. kcat/Km: printed Table 1 cell 3.8 under the column head kcat/Km (s^-1 mM^-1); the column is already in s^-1 mM^-1, so no conversion applies and the paper value is 3.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, WT enzyme block, substrate row Sop3: kcat = 56 ± 11 s^-1; Km = 15 ± 4 mM; printed kcat/Km = 3.8 ± 0.3 s^-1 mM^-1.

substrate: sophorotriose


substrate_name: sophorotetraose

substrate: sophorotetraose


organism: Oryza sativa

sequence_source: UniProtKB exact accession Q75I93


substrate_name: H2O; N-Heptyl-beta-D-glucoside

substrate: H2O; N-Heptyl-beta-D-glucoside


sequence_source: UniProtKB exact accession Q8L7J2


sequence_source: UniProtKB exact accession A3BMZ5


sequence_source: UniProtKB exact accession Q75I94


organism: Phanerochaete chrysosporium

substrate_name: H2O; Cellobiose

sequence_source: UniProtKB exact accession Q25BW4

assay_conditions_summary: pH 4

substrate: H2O; Cellobiose


sequence_source: UniProtKB exact accession Q25BW5


organism: Pyrococcus furiosus

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

sequence_source: UniProtKB exact accession Q51723

source_databases_merged: sabio_rk brenda skid


organism: Secale cereale

sequence_source: UniProtKB exact accession Q9FYS3


organism: Sorghum bicolor

sequence_source: UniProtKB exact accession Q41290


organism: Spodoptera frugiperda

substrate_name: 4-nitrophenyl beta-D-glucoside

sequence_source: UniProtKB exact accession O61594

substrate: 4-nitrophenyl beta-D-glucoside


substrate_name: 2-nitrophenyl beta-D-glucopyranoside

sequence_source: UniProtKB exact accession Q9YGA8

substrate: 2-nitrophenyl beta-D-glucopyranoside


organism: Acetivibrio thermocellus


enzyme_display_name: Beta-glucosidase 45

organism: Arabidopsis thaliana

substrate_name: H2O; Coniferin

enzyme: Beta-glucosidase 45

substrate: H2O; Coniferin


enzyme_display_name: Beta-glucosidase 46

enzyme: Beta-glucosidase 46


enzyme_display_name: Myrosinase 5

enzyme: Myrosinase 5


enzyme_display_name: Myrosinase 4

enzyme: Myrosinase 4


enzyme_display_name: Myrosinase 1

enzyme: Myrosinase 1


enzyme_display_name: Beta-glucosidase BoGH3A

organism: Bacteroides ovatus

substrate_name: H2O; Cellotetraose

enzyme: Beta-glucosidase BoGH3A

substrate: H2O; Cellotetraose


enzyme_display_name: Beta-glucosidase BoGH3B

enzyme: Beta-glucosidase BoGH3B


organism: Bifidobacterium breve


organism: Cellulomonas fimi

substrate_name: p-Nitrophenyl-beta-D-glucoside; H2O

substrate: p-Nitrophenyl-beta-D-glucoside; H2O


enzyme_display_name: Beta-glucosidase

organism: Halothermothrix orenii

substrate_name: lactose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature Y296F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'Y296F', D-lactose block: k_cat,app = 6.9 ± 0.2; K_m = 29.1 ± 2.3; k_cat,app/K_m = 0.24.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 6.9 ± 0.2 in column 'k_cat,app (s^-1)' of the D-lactose block; the value is already s^-1, so no conversion is applied and the paper value is 6.9 s^(-1). K_m: printed Table 2 cell 29.1 ± 2.3 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 29.1 mM. k_cat/K_m: printed Table 2 cell 0.24 in column 'k_cat,app/K_m (s^-1 mM^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 0.24 s^(-1)*mM^(-1). Closure check: 6.9 / 29.1 = 0.237113 s^-1 mM^-1, which rounds to the printed efficiency cell 0.24 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'Y296F', D-lactose block: column 'k_cat,app (s^-1)' prints 6.9 ± 0.2; column 'K_m (mM)' prints 29.1 ± 2.3; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 0.24.

row_label: Table 2, body row 'Y296F' (variant Y296F), D-lactose block

enzyme: Beta-glucosidase

substrate: lactose


column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'WT', D-lactose block: k_cat,app = 366 ± 17; K_m = 26.3 ± 2.8; k_cat,app/K_m = 13.9.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 366 ± 17 in column 'k_cat,app (s^-1)' of the D-lactose block; the value is already s^-1, so no conversion is applied and the paper value is 366.0 s^(-1). K_m: printed Table 2 cell 26.3 ± 2.8 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 26.3 mM. k_cat/K_m: printed Table 2 cell 13.9 in column 'k_cat,app/K_m (s^-1 mM^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 13.9 s^(-1)*mM^(-1). Closure check: 366.0 / 26.3 = 13.9163 s^-1 mM^-1, which rounds to the printed efficiency cell 13.9 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'WT', D-lactose block: column 'k_cat,app (s^-1)' prints 366 ± 17; column 'K_m (mM)' prints 26.3 ± 2.8; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 13.9.

row_label: Table 2, body row 'WT' (wild type (the unmarked 70 °C row)), D-lactose block


substrate_name: cellobiose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature N222F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'N222F', D-cellobiose block: k_cat,app = 16.9 ± 1.3; K_m = 93.2 ± 12.6; k_cat,app/K_m = 0.18.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 16.9 ± 1.3 in column 'k_cat,app (s^-1)' of the D-cellobiose block; the value is already s^-1, so no conversion is applied and the paper value is 16.9 s^(-1). K_m: printed Table 2 cell 93.2 ± 12.6 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 93.2 mM. k_cat/K_m: printed Table 2 cell 0.18 in column 'k_cat,app/K_m (mM^-1 s^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 0.18 s^(-1)*mM^(-1). Closure check: 16.9 / 93.2 = 0.18133 s^-1 mM^-1, which rounds to the printed efficiency cell 0.18 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'N222F', D-cellobiose block: column 'k_cat,app (s^-1)' prints 16.9 ± 1.3; column 'K_m (mM)' prints 93.2 ± 12.6; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 0.18.

row_label: Table 2, body row 'N222F' (variant N222F), D-cellobiose block

substrate: cellobiose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature N294T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'N294T', D-lactose block: k_cat,app = 7.4 ± 0.2; K_m = 30.8 ± 2.0; k_cat,app/K_m = 0.24.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 7.4 ± 0.2 in column 'k_cat,app (s^-1)' of the D-lactose block; the value is already s^-1, so no conversion is applied and the paper value is 7.4 s^(-1). K_m: printed Table 2 cell 30.8 ± 2.0 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 30.8 mM. k_cat/K_m: printed Table 2 cell 0.24 in column 'k_cat,app/K_m (s^-1 mM^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 0.24 s^(-1)*mM^(-1). Closure check: 7.4 / 30.8 = 0.24026 s^-1 mM^-1, which rounds to the printed efficiency cell 0.24 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'N294T', D-lactose block: column 'k_cat,app (s^-1)' prints 7.4 ± 0.2; column 'K_m (mM)' prints 30.8 ± 2.0; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 0.24.

row_label: Table 2, body row 'N294T' (variant N294T), D-lactose block


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B8CYA8 and applied mutation signature F417S to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'F417S', D-cellobiose block: k_cat,app = 0.38 ± 0.01; K_m = 11.9 ± 0.9; k_cat,app/K_m = 0.032.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 0.38 ± 0.01 in column 'k_cat,app (s^-1)' of the D-cellobiose block; the value is already s^-1, so no conversion is applied and the paper value is 0.38 s^(-1). K_m: printed Table 2 cell 11.9 ± 0.9 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 11.9 mM. k_cat/K_m: printed Table 2 cell 0.032 in column 'k_cat,app/K_m (mM^-1 s^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 0.032 s^(-1)*mM^(-1). Closure check: 0.38 / 11.9 = 0.0319328 s^-1 mM^-1, which rounds to the printed efficiency cell 0.032 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'F417S', D-cellobiose block: column 'k_cat,app (s^-1)' prints 0.38 ± 0.01; column 'K_m (mM)' prints 11.9 ± 0.9; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 0.032.

row_label: Table 2, body row 'F417S' (variant F417S), D-cellobiose block


column_label: Table 2 (Kinetic parameters for beta-glucosidase and beta-galactosidase activities). Column 1 is the enzyme form; columns 2-4 are the D-cellobiose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (mM^-1 s^-1)'; columns 5-7 are the D-lactose block with heads 'k_cat,app (s^-1)', 'K_m (mM)', 'k_cat,app/K_m (s^-1 mM^-1)'; column 8 is the selectivity ratio. Body row 'N294T', D-cellobiose block: k_cat,app = 16.5 ± 0.4; K_m = 9.0 ± 0.8; k_cat,app/K_m = 1.8.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 16.5 ± 0.4 in column 'k_cat,app (s^-1)' of the D-cellobiose block; the value is already s^-1, so no conversion is applied and the paper value is 16.5 s^(-1). K_m: printed Table 2 cell 9.0 ± 0.8 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 9.0 mM. k_cat/K_m: printed Table 2 cell 1.8 in column 'k_cat,app/K_m (mM^-1 s^-1)'; mM^-1 s^-1 and s^-1 mM^-1 are the same unit, already the export unit, so no conversion and the paper value is 1.8 s^(-1)*mM^(-1). Closure check: 16.5 / 9.0 = 1.83333 s^-1 mM^-1, which rounds to the printed efficiency cell 1.8 at the precision the table prints, so the printed ratio and the quotient of the printed components agree.

raw_value_unit_evidence: Table 2: Kinetic parameters for β-glucosidase and β-galactosidase activities (Applied microbiology and biotechnology 2016, 100(8):3533-3543), body row 'N294T', D-cellobiose block: column 'k_cat,app (s^-1)' prints 16.5 ± 0.4; column 'K_m (mM)' prints 9.0 ± 0.8; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 1.8.

row_label: Table 2, body row 'N294T' (variant N294T), D-cellobiose block


substrate_name: p-nitrophenyl-beta-D-mannopyranoside

substrate: p-nitrophenyl-beta-D-mannopyranoside


substrate_name: syringin (at pH 5.5)

substrate: syringin (at pH 5.5)


substrate_name: p-coumaryl alcohol glucoside (at pH 5.5)


substrate_name: sinigrin (at pH 4.5)

substrate: sinigrin (at pH 4.5)


substrate_name: scopolin (with recombinant enzyme)

substrate: scopolin (with recombinant enzyme)


substrate_name: pNP-beta-D-glucoside

substrate: pNP-beta-D-glucoside


organism: Fulvia fulva

substrate_name: pNPG

substrate: pNPG


sequence: GVDVLLGQGLLAPRTPFTGEGPSQKSYGTELLSKPNDGK

wild_type_sequence: GVDVLLGQGLLAPRTPFTGEGPSQKSYGTELLSKPNDGK


organism: Oryza sativa subsp. japonica

substrate_name: p-nitrophenyl beta-D-glucoside (at pH 5.0)

assay_conditions_summary: pH 5


proof_lines: kcat is 1.30 sec(-1) with kaempferol 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate. kcat is 1.10 sec(-1) with quercetin 3-O-beta-glucoside-7-O-alpha-rhamnoside as substrate. kcat is 0.92 sec(-1) with kaempferol 3-O-beta-glucoside as


substrate_name: pNP beta-D-glucopyranoside

proof_lines: kcat is 10.2 sec(-1) with pNP beta-D-glucopyranoside as substrate (PubMed:34965581). kcat is 12.9 sec(-1) with pNP beta-D-fucopyranoside as substrate (PubMed:34965581). kcat is 13.6 sec(-1) with pNP beta-D-galactopyranoside as substrate (Pu

substrate: pNP beta-D-glucopyranoside


organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)

proof_lines: kcat is 1.57 sec(-1) for cellobiose. kcat is 3.99 sec(-1) for cellotetraose. kcat is 4.91 sec(-1) for cellohexaose.


substrate_name: cellotetraose

proof_lines: kcat is 65.0 sec(-1) for cellotetraose. kcat is 0.62 sec(-1) for cellohexaose.

substrate: cellotetraose


organism: Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL)

substrate_name: p-nitrophenyl beta-D-galactopyranoside (pNPGal) (at pH 5.5 and 75 degrees Celsius)

proof_lines: kcat is 4522 sec(-1) with pNPGal as substrate. kcat is 3750.6 sec(-1) with pNPGlu as substrate. kcat is 944.3 sec(-1) with pNPC as substrate. kcat is 652.6 sec(-1) with pNPX as substrate. kcat is 2149 sec(-1) with cellobiose as substrate.


proof_lines: The catalytic efficiencies against 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 4'-nitrophenyl beta-D-glucopyranoside are similar.


organism: Homo sapiens

substrate_name: glucosylceramide (at 37 degrees Celsius and pH 6.0)

assay_conditions_summary: pH 6

proof_lines: kcat is 0.43 min(-1) for the hydrolysis of glucosylceramide (PubMed:17595169). kcat<0.01 min(-1) for the hydrolysis of galactosylceramide (PubMed:17595169). kcat is 7.26 min(-1) for the hydrolysis of C6-NBD-glucosylceramide (PubMed:17595169


substrate_name: p-nitrophenyl beta-D-glucopyranoside

proof_lines: kcat is 18.5 sec(-1) with p-nitrophenyl beta-D-glucopyranoside as substrate. kcat is 0.27 sec(-1) with p-nitrophenyl beta-D-thioglucoside as substrate. kcat is 12.1 sec(-1) with n-heptyl-beta-D-glucoside as substrate. kcat is 9.8 sec(-1) wi

substrate: p-nitrophenyl beta-D-glucopyranoside


substrate_name: para-nitrophenyl beta-D-glucopyranoside

proof_lines: kcat is 3.82 sec(-1) with para-nitrophenyl beta-D-glucopyranoside as substrate. kcat is 23.8 sec(-1) with para-nitrophenyl beta-D-fucopyranoside as substrate. kcat is 0.381 sec(-1) with para-nitrophenyl beta-D-xylopyranoside as substrate. k

substrate: para-nitrophenyl beta-D-glucopyranoside


proof_lines: kcat is 3.05 sec(-1) with para-nitrophenyl beta-D-glucopyranoside as substrate. kcat is 6.92 sec(-1) with para-nitrophenyl beta-D-fucopyranoside as substrate. kcat is 0.788 sec(-1) with para-nitrophenyl beta-D-xylopyranoside as substrate. k


substrate_name: DIBOA-beta-D-glucoside

proof_lines: kcat is 172 sec(-1) with DIBOA-beta-D-glucoside as substrate. kcat is 118 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 119 sec(-1) with DIMBOA-beta-D-glucoside as substrate. kcat is 158 sec(-1) with DI

substrate: DIBOA-beta-D-glucoside


organism: Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E)

proof_lines: kcat is 285.0, 345.7 and 333.7 sec(-1) for the hydrolysis of cellobiose, cellotriose and cellotetraose, respectively.


enzyme_display_name: carboxylesterase

organism: Thermobifida fusca

substrate_name: p-nitrophenol acetate

enzyme: carboxylesterase

substrate: p-nitrophenol acetate


substrate_name: cis-Permethrin; H2O

assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.1 M potassium phosphate

proof_lines:
pH 7.5, 25°C
pH 7.0, 37°C, isoform CES2
pH 7.0, 37°C

substrate: cis-Permethrin; H2O


organism: Rattus norvegicus

substrate_name: trans-Permethrin; H2O

proof_lines:
hydrolase A, pH 7.4, 37°C
hydrolase B, pH 7.4, 37°C
pH 5.0, 37°C

substrate: trans-Permethrin; H2O


organism: Sus scrofa

substrate_name: H2O; 4-Nitrophenyl acetate

proof_lines:
pH 7.4, 37°C
at pH 7.4 and 37Â°C
isoenzyme V

substrate: H2O; 4-Nitrophenyl acetate


column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-2'; substrate row 'A6'; column 'Km(uM)' = 2.1; column 'kcat(min-1)' = 0.34; column 'kcat/Km(uM-1 min-1)' = 0.16.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-2', substrate row 'A6': Km = 2.1 uM; kcat = 0.34 min^-1; printed kcat/Km = 0.16 uM^-1 min^-1.

table_label: Table 5: Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates (Arch Biochem Biophys 2006;445(1):115-123)


substrate_name: H2O; Carboxylic ester

substrate: H2O; Carboxylic ester


organism: Lactobacillus casei


organism: Lactococcus lactis subsp. cremoris


organism: Oryctolagus cuniculus

substrate_name: 1-R,S-cis-Permethrin; H2O

proof_lines:
isoform CES1, at pH 6.5 and 37Â°C
ratio kcat/Km is 180 per min and mM
at pH 7.4 and 37Â°C

substrate: 1-R,S-cis-Permethrin; H2O


organism: Pseudomonas aeruginosa

substrate_name: H2O; p-Nitrophenyl butyrate

substrate: H2O; p-Nitrophenyl butyrate


organism: Pseudomonas putida


organism: Pyrobaculum sp.

substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl decanoate

substrate: 4-nitrophenyl decanoate


organism: Pyrococcus furiosus

substrate_name: 4-Methylumbelliferyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8TZJ1 and applied mutation signature W194A to reconstruct the assayed variant sequence.

substrate: 4-Methylumbelliferyl butyrate


substrate_name: 4-Methylumbelliferyl heptanoate

substrate: 4-Methylumbelliferyl heptanoate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8TZJ1 and applied mutation signature F198A to reconstruct the assayed variant sequence.


substrate_name: H2O; All-trans-Retinyl palmitate

substrate: H2O; All-trans-Retinyl palmitate


organism: Saccharolobus solfataricus

substrate_name: 4-nitrophenyl caproate

proof_lines: pH and temperature not specified in the publication

substrate: 4-nitrophenyl caproate


substrate_name: 4-nitrophenyl caprylate

column_label: Table 1 on journal page 1154, p-Nitrophenyl caprylate block, enzyme row Wild-type; column kcat/Km (s^-1 mM^-1) = 63; column Km (uM) = 28; column kcat (s^-1) = 1.7.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.7 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 1.7 s^(-1). Km: printed Table 1 cell 28 uM; 1 uM is 1/1000 mM, so 28 / 1000 = 0.028 mM. kcat/Km: printed Table 1 cell 63 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 63.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Wild-type, p-Nitrophenyl caprylate block: kcat/Km = 63 s^-1 mM^-1; Km = 28 uM; kcat = 1.7 s^-1.

table_label: Table 1: Kinetic parameters of wild-type SsoPEst and R210A (Biotechnology Letters 2010, volume 32, pages 1151-1157)

substrate: 4-nitrophenyl caprylate


column_label: Table 1 on journal page 1154, p-Nitrophenyl butyrate block, enzyme row Wild-type; column kcat/Km (s^-1 mM^-1) = 5.1; column Km (mM) = 0.93; column kcat (s^-1) = 4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 4.0 s^(-1). Km: printed Table 1 cell 0.93 mM; the printed column is already in mM, so no unit conversion applies and the value carries over as 0.93 mM. kcat/Km: printed Table 1 cell 5.1 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 5.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Wild-type, p-Nitrophenyl butyrate block: kcat/Km = 5.1 s^-1 mM^-1; Km = 0.93 mM; kcat = 4 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q97VU1 and applied mutation signature R210A to reconstruct the assayed variant sequence.

column_label: Table 1 on journal page 1154, p-Nitrophenyl caprylate block, enzyme row R210A; column kcat/Km (s^-1 mM^-1) = 192; column Km (uM) = 43; column kcat (s^-1) = 7.8.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.8 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 7.8 s^(-1). Km: printed Table 1 cell 43 uM; 1 uM is 1/1000 mM, so 43 / 1000 = 0.043 mM. kcat/Km: printed Table 1 cell 192 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 192.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R210A, p-Nitrophenyl caprylate block: kcat/Km = 192 s^-1 mM^-1; Km = 43 uM; kcat = 7.8 s^-1.


substrate_name: 5'-L-Phenylalanyl-floxuridine; H2O

substrate: 5'-L-Phenylalanyl-floxuridine; H2O


organism: Vibrio vulnificus

substrate_name: H2O; p-Nitrophenyl acetate

substrate: H2O; p-Nitrophenyl acetate


organism: Vulcanisaeta moutnovskia


organism: Actinidia eriantha

substrate_name: 4-methylumbelliferyl acetate

substrate: 4-methylumbelliferyl acetate


organism: Arabidopsis thaliana

substrate_name: the synthetic substrate p-nitrophenyl acetate (pNPA)


organism: Felis catus

substrate_name: p-NPA

substrate: p-NPA


organism: Geobacillus stearothermophilus

substrate_name: p-nitrophenyl caproate (at 60 degrees Celsius)


organism: Homo sapiens


substrate_name: p-nitrophenyl valerate

substrate: p-nitrophenyl valerate


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

substrate_name: p-nitrophenyl butyrate

substrate: p-nitrophenyl butyrate


organism: Rattus norvegicus


substrate_name: retinyl palmitate

substrate: retinyl palmitate


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: 4-methylumbelliferyl (4-MU) butyrate (at 37 degrees Celsius)


organism: Sus scrofa


organism: Vibrio vulnificus (strain CMCP6)

substrate_name: pNPA

proof_lines: kcat is 0.67 sec(-1) with pNPA as substrate.

substrate: pNPA


substrate_name: H2O; 4-Methylumbelliferyl acetate

sequence_source: UniProtKB direct accession lookup: Q0ZPV7

proof_lines:
pH 8.0, 25°C
Raw SKiD Env: Temp=25°C, pH=8

substrate: H2O; 4-Methylumbelliferyl acetate


organism: Alicyclobacillus acidocaldarius

substrate_name: p-Nitrophenyl dodecanoate; H2O

substrate: p-Nitrophenyl dodecanoate; H2O


substrate_name: Methyl indole-3-acetate; H2O

sequence_source: UniProtKB direct accession lookup: Q9SG92

substrate: Methyl indole-3-acetate; H2O


organism: Archaeoglobus fulgidus

substrate_name: Triacetin; H2O

sequence_source: UniProtKB direct accession lookup: O28558

proof_lines:
70°C, pH 7.1
pH 7.1, 50°C
Raw SKiD Env: Temp=70°C, pH=7.1

substrate: Triacetin; H2O


organism: Bacillus sp.

sequence_source: UniProtKB direct accession lookup: Q6DV85


sequence_source: UniProtKB direct accession lookup: Q6DV84


organism: Escherichia coli


organism: Felis silvestris catus

sequence_source: UniProtKB direct accession lookup: Q8I034


organism: Ferroplasma acidiphilum

substrate_name: 4-nitrophenyl butyrate

sequence_source: UniProtKB direct accession lookup: Q2PCE5

proof_lines:
pH 2.0, 50°C
Raw SKiD Env: Temp=50°C, pH=2
Raw SKiD Env: Temp=35°C, pH=6

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl hexanoate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q2PCE5 and applied mutation signature N248A/P256Q/E257G/S283F to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of EstFa_R and its AQGF mutant), AQGF block, row 'pNP caproate'; column 'kcat (s^-1)' = 159 ± 4; column 'Km (mM)' = 0.13 ± 0.02; column 'kcat/Km (s^-1 mM^-1)' = 1275.

normalized_value_unit_evidence: kcat: printed Table 1 cell 159 ± 4 s^-1; the cell is already in s^-1, so no unit conversion applies, and the paper value is 159.0 s^(-1), which is the value the catalog already carries. Km: printed Table 1 cell 0.13 ± 0.02 mM; the cell is already in mM, so no unit conversion applies, and the paper value is 0.13 mM, which is the value the catalog already carries. kcat/Km: printed Table 1 cell 1275 s^-1 mM^-1; the cell is already in s^-1 mM^-1, so no unit conversion applies, and the paper value is 1275.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, AQGF block, row 'pNP caproate': kcat = 159 ± 4 s^-1; Km = 0.13 ± 0.02 mM; printed kcat/Km = 1275 s^-1 mM^-1.

row_label: Table 1, AQGF (N248A/P256Q/E257G/S283F) block, row 'pNP caproate'

table_label: Table 1: Kinetic parameters of EstFa_R and its AQGF mutant (J. Biol. Chem. 2014, 289(35):24499-24510)

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl propionate

column_label: Table 1 (Kinetic parameters of EstFa_R and its AQGF mutant), AQGF block, row 'pNP propionate'; column 'kcat (s^-1)' = 59 ± 4; column 'Km (mM)' = 0.70 ± 0.14; column 'kcat/Km (s^-1 mM^-1)' = 84.6.

normalized_value_unit_evidence: kcat: printed Table 1 cell 59 ± 4 s^-1; the cell is already in s^-1, so no unit conversion applies, and the paper value is 59.0 s^(-1), which is the value the catalog already carries. Km: printed Table 1 cell 0.70 ± 0.14 mM; the cell is already in mM, so no unit conversion applies, and the paper value is 0.7 mM, which is the value the catalog already carries. kcat/Km: printed Table 1 cell 84.6 s^-1 mM^-1; the cell is already in s^-1 mM^-1, so no unit conversion applies, and the paper value is 84.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, AQGF block, row 'pNP propionate': kcat = 59 ± 4 s^-1; Km = 0.70 ± 0.14 mM; printed kcat/Km = 84.6 s^-1 mM^-1.

row_label: Table 1, AQGF (N248A/P256Q/E257G/S283F) block, row 'pNP propionate'

substrate: 4-nitrophenyl propionate


column_label: Table 1 (Kinetic parameters of EstFa_R and its AQGF mutant), AQGF block, row 'pNP butyrate'; column 'kcat (s^-1)' = 101 ± 7; column 'Km (mM)' = 0.48 ± 0.11; column 'kcat/Km (s^-1 mM^-1)' = 211.

normalized_value_unit_evidence: kcat: printed Table 1 cell 101 ± 7 s^-1; the cell is already in s^-1, so no unit conversion applies, and the paper value is 101.0 s^(-1), which is the value the catalog already carries. Km: printed Table 1 cell 0.48 ± 0.11 mM; the cell is already in mM, so no unit conversion applies, and the paper value is 0.48 mM, which is the value the catalog already carries. kcat/Km: printed Table 1 cell 211 s^-1 mM^-1; the cell is already in s^-1 mM^-1, so no unit conversion applies, and the paper value is 211.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, AQGF block, row 'pNP butyrate': kcat = 101 ± 7 s^-1; Km = 0.48 ± 0.11 mM; printed kcat/Km = 211 s^-1 mM^-1.

row_label: Table 1, AQGF (N248A/P256Q/E257G/S283F) block, row 'pNP butyrate'


substrate_name: 4-nitrophenyl acetate

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q2PCE5 canonical sequence plus N248A/P256Q/E257G/S283F and applied mutation signature N248A/P256Q/E257G/S283F to reconstruct the assayed variant sequence.

substrate: 4-nitrophenyl acetate


substrate_name: p-Nitrophenyl caproate

sequence_source: UniProtKB direct accession lookup: Q8GCC7

substrate: p-Nitrophenyl caproate


sequence_source: UniProtKB direct accession lookup: Q06174


substrate_name: H2O; p-Nitrophenyl caproate

substrate: H2O; p-Nitrophenyl caproate


organism: Amycolatopsis mediterranei (strain S699)

substrate_name: p-nitrophenyl palmitate (p-NPP) (at pH 8.0 and 60 degrees Celsius)

proof_lines: kcat is 1468 sec(-1) with p-nitrophenyl palmitate (p-NPP) as substrate (at pH 8.0 and 60 degrees Celsius).


organism: Glycine max

substrate_name: 2,7-dihydroxy-4'-methoxyisoflavanone (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 1.6 sec(-1) with 2,7-dihydroxy-4'-methoxyisoflavanone, 5.3 sec(-1) with 2,7,4'-trihydroxyisoflavanone and 18.1 sec(-1) with 2,5,7,4'-tetrahydroxyisoflavanone as substrates, respectively (at pH 7.5 and 30 degrees Celsius).


organism: Glycyrrhiza echinata

proof_lines: kcat is 9.8 sec(-1) with 2,7-dihydroxy-4'-methoxyisoflavanone, 0.12 sec(-1) with 2,7,4'-trihydroxyisoflavanone and 0.19 sec(-1) with 2,5,7,4'-tetrahydroxyisoflavanone as substrates, respectively (at pH 7.5 and 30 degrees Celsius).

substrate: 2,7-dihydroxy-4'-methoxyisoflavanone (at pH 7.5 and 30 degrees Celsius)


substrate_name: p-nitrophenyl acetate

proof_lines: kcat is 59 min(-1), 29 min(-1), 90 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.

substrate: p-nitrophenyl acetate


substrate_name: cocaine

proof_lines: kcat is 43 min(-1), 49 min(-1), 150 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.

substrate: cocaine


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: triacetin

proof_lines: kcat is 581.2 sec(-1) for triacetin. kcat is 223.7 sec(-1) for tributyrin. kcat is 122.9 sec(-1) for tricaproin. kcat is 15.6 sec(-1) for tricaprylin. kcat is 501.8 sec(-1) for p-nitrophenyl acetate. kcat is 119.7 sec(-1) for p-nitrophenyl

substrate: triacetin


substrate_name: pNP-myristate

proof_lines: kcat is 1312 sec(-1) with pNP-myristate as substrate.

substrate: pNP-myristate


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: p-nitrophenyl butyrate

proof_lines: The N-terminal esterase domain, when expressed alone, shows activities five to ten times higher than those of the complete enzyme EstP towards all tested substrates, whereas substrate affinity and the activity profiles are still the same.

substrate: p-nitrophenyl butyrate


substrate_name: retinyl palmitate

proof_lines: kcat is 0.19 min(-1) with retinyl palmitate as substrate.

substrate: retinyl palmitate


proof_lines: kcat is 0.45 min(-1) with retinyl palmitate as substrate.


substrate_name: oleic acid

proof_lines: kcat is 0.22 min(-1) with retinyl palmitate as substrate.

substrate: oleic acid


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: pNP-acetate (at pH 7 and 70 degrees Celsius)

proof_lines: kcat is 1.0 sec(-1) with pNP-acetate as substrate. kcat is 14.9 sec(-1) with pNP-butyrate as substrate. kcat is 10.2 sec(-1) with pNP-valerate as substrate. kcat is 1.6 sec(-1) with pNP-octanoate as substrate. kcat is 1.3 sec(-1) with pNP-d


organism: Geobacillus stearothermophilus

sequence_source: UniProtKB REST direct accession lookup (Q06174)


organism: Geobacillus thermoleovorans

substrate_name: H2O; p-Nitrophenyl laurate

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

unit: mol/min

substrate: H2O; p-Nitrophenyl laurate


organism: Homo sapiens

substrate_name: Irinotecan

sequence_source: UniProtKB REST direct accession lookup (P23141)

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

substrate: Irinotecan


sequence_source: UniProtKB REST direct accession lookup (O00748)


substrate_name: H2O; o-Nitrophenyl acetate

substrate: H2O; o-Nitrophenyl acetate


substrate_name: H2O; Irinotecan

sequence_source: UniProtKB REST direct accession lookup (Q6UWW8)

substrate: H2O; Irinotecan


sequence_source: UniProtKB REST direct accession lookup (Q4G0E9)


substrate_name: H2O; Capecitabine

substrate: H2O; Capecitabine


substrate_name: Tripropionin; H2O

substrate: Tripropionin; H2O


substrate_name: Cypermethrin

column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-1'; substrate row 'Cypermethrin (B3)'; column 'Km(uM)' = 20; column 'kcat(min-1)' = 1.3; column 'kcat/Km(uM-1 min1)' = 0.07.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-1', substrate row 'Cypermethrin (B3)': Km = 20 uM; kcat = 1.3 min^-1; printed kcat/Km = 0.07 uM^-1 min^-1.

substrate: Cypermethrin


column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-1'; substrate row 'A6'; column 'Km(uM)' = 1.8; column 'kcat(min-1)' = 0.25; column 'kcat/Km(uM-1 min1)' = 0.14.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-1', substrate row 'A6': Km = 1.8 uM; kcat = 0.25 min^-1; printed kcat/Km = 0.14 uM^-1 min^-1.


column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-2'; substrate row 'Cypermethrin (B3)'; column 'Km(uM)' = 9.1; column 'kcat(min-1)' = 4.0; column 'kcat/Km(uM-1 min-1)' = 0.44.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-2', substrate row 'Cypermethrin (B3)': Km = 9.1 uM; kcat = 4.0 min^-1; printed kcat/Km = 0.44 uM^-1 min^-1.


column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-1'; substrate row 'A8'; column 'Km(uM)' = 1.5; column 'kcat(min-1)' = 0.30; column 'kcat/Km(uM-1 min1)' = 0.20.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-1', substrate row 'A8': Km = 1.5 uM; kcat = 0.30 min^-1; printed kcat/Km = 0.20 uM^-1 min^-1.


substrate_name: H2O; 4-Nitrophenyl acetate

column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-2'; substrate row 'pNPA'; column 'Km(uM)' = 31; column 'kcat(min-1)' = 4200; column 'kcat/Km(uM-1 min-1)' = 140.

normalized_value_unit_evidence: Km: printed Table 5 cell 31 uM; 31 / 1000 = 0.031 mM; the exported value is 0.0009000000000000001 mM. kcat: printed Table 5 cell 4200 min^-1; 4200 / 60 = 70.0 s^(-1); the exported value is 70.0 s^(-1). kcat/Km: printed Table 5 cell 140 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 140 x 1000 / 60 = 2333.3333333333335 s^-1 mM^-1; the catalog carries no catalytic-efficiency value for this row, so the printed cell is kept as paper evidence only.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-2', substrate row 'pNPA': Km = 31 uM; kcat = 4200 min^-1; printed kcat/Km = 140 uM^-1 min^-1.

substrate: H2O; 4-Nitrophenyl acetate


proof_lines:
isoform hCE-2, pH 8.0, 37°C
isoform hCE-1, pH 8.0, 37°C
enzyme from liver cytosol


substrate_name: p-Nitrophenyl acetate

row_label: Table 5, enzyme block 'hCE-2', substrate row 'pNPA'

substrate: p-Nitrophenyl acetate


substrate_name: p-Nitrophenyl octanoate; H2O

sequence_source: RCSB 1EVQ polymer entity mapped to UniProtKB Q7SIG1

substrate: p-Nitrophenyl octanoate; H2O


organism: Bacillus subtilis

substrate_name: H2O; p-Nitrophenyl butyrate

substrate: H2O; p-Nitrophenyl butyrate


organism: Mus musculus

substrate_name: cis-Permethrin; H2O

substrate: cis-Permethrin; H2O


enzyme_display_name: tyrosinase

organism: Agaricus bisporus

substrate_name: O2; L-Dopa

assay_conditions_summary: pH 7; 298.15 K; buffer phosphate

proof_lines: pH and temperature not specified in the publication

enzyme: tyrosinase

substrate: O2; L-Dopa


organism: Prunus persica

substrate_name: (+)-Catechin; O2

proof_lines: membrane-bound (PPO-B) peach polyphenol oxidase without SDS

proof_lines: membrane-bound (PPO-B) peach polyphenol oxidase with 2 mM SDS

proof_lines: soluble (PPO-S) peach polyphenol oxidase without SDS

substrate: (+)-Catechin; O2


organism: Solanum tuberosum

substrate_name: L-Dopa

proof_lines: with catechol as a substrate, at pH 6.8 and 25°C

proof_lines: with 4-methylcatechol as a substrate, at pH 6.8 and 25°C

substrate: L-Dopa


sequence_source: UniProtKB exact accession O42713 REST lookup on 2026-07-01

proof_lines: Sigma mushroom tyrosinase (SMT, crude powder, lot 105k7026)

proof_lines: Worthington mushroom tyrosinase (WMT, crude powder, lot 33H6588Q)


organism: Bos taurus

substrate_name: O2; L-Noradrenaline

substrate: O2; L-Noradrenaline


organism: Concholepas concholepas


substrate_name: L-Tyrosine; O2

sequence_source: UniProtKB exact accession P14679 REST lookup on 2026-07-01

substrate: L-Tyrosine; O2


organism: Pholiota nameko

substrate_name: O2; 4-Cresol

sequence_source: UniProtKB exact accession A7BHQ9 REST lookup on 2026-07-01

substrate: O2; 4-Cresol


organism: Saccharomyces cerevisiae

substrate_name: O2; Epinephrine

substrate: O2; Epinephrine


enzyme_display_name: laccase

organism: Bacillus sp.

substrate_name: O2; 2,6-Dimethoxyphenol

sequence_source: UniProtKB:B9W2C5 direct lookup

enzyme: laccase

substrate: O2; 2,6-Dimethoxyphenol


substrate_name: O2; Syringaldazine

substrate: O2; Syringaldazine


organism: Bacillus sp. HR03


organism: Bacillus sp. LS03


organism: Bacillus sp. SL-1

sequence_source: UniProtKB:A0A165W3F6 direct lookup


sequence_source: UniProtKB:P07788 direct lookup


substrate_name: Syringaldazine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 direct lookup and applied mutation signature L431F to reconstruct the assayed variant sequence.

substrate: Syringaldazine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 direct lookup and applied mutation signature R146K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 direct lookup and applied mutation signature R476K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 direct lookup and applied mutation signature T480A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A386JCD3 direct lookup


organism: Ochrobactrum sp. 531


organism: Paenibacillus glucanolyticus

sequence_source: UniProtKB exact accession A0A165SC98 REST lookup, retrieved 2026-07-01


organism: Pleurotus ostreatus

sequence_source: UniProtKB exact accession O60199 REST lookup, retrieved 2026-07-01


organism: Pseudomonas fluorescens

sequence_source: UniProtKB exact accession Q4KCN4 REST lookup, retrieved 2026-07-01


organism: Pseudomonas sp.


organism: Rheinheimera sp.


organism: Rhodococcus erythropolis

substrate_name: 2,6-Dimethoxyphenol; O2

substrate: 2,6-Dimethoxyphenol; O2


organism: Stenotrophomonas maltophilia


organism: Streptomyces californicus


substrate_name: O2; Potassium ferrocyanide

substrate: O2; Potassium ferrocyanide


organism: Streptomyces coelicolor

substrate_name: O2; Osmium complex

sequence_source: UniProtKB:Q9XAL8 direct accession check (REST, 2026-07-01)

substrate: O2; Osmium complex


organism: Streptomyces cyaneus


organism: Streptomyces griseoflavus

sequence_source: UniProtKB:A0A0M4FJ81 direct accession check (REST, 2026-07-01)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature I170A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the SgfSL variants), ABTS block, protein row 'I170A'; column 'Km (mM)' = 0.63 ± 0.11; column 'kcat (s-1)' = 0.70 ± 0.20; column 'kcat/Km (mM-1 s-1)' = 1.11; column 'Activity nM O2 min-1 ug-1' = 0.11 ± 0.01.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.70 under the column head kcat (s-1); the cell is already in s^-1, so no unit conversion applies and the canonical value is 0.7 s^(-1). Km: printed Table 3 cell 0.63 under the column head Km (mM); the cell is already in mM, so no unit conversion applies and the canonical value is 0.63 mM. kcat/Km: printed Table 3 cell 1.11 under the column head kcat/Km (mM-1 s-1); the cell is already in mM^-1 s^-1, so no unit conversion applies and the printed cell carries over as 1.11 s^-1 mM^-1, while the full-precision quotient of the same line's two printed component cells is 0.70 / 0.63 = 1.111111111111111 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, ABTS block, protein row 'I170A': Km = 0.63 mM; kcat = 0.70 s-1; printed kcat/Km = 1.11 mM-1 s-1.

table_label: Table 3: Kinetic parameters of the SgfSL variants (Int. J. Mol. Sci. 2019, volume 20, article 3184, page 6); printed column heads Substrate | Protein | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1) | Activity nM O2 min-1 ug-1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature M199A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 303.15 K; buffer 50 mM Britton-Robinson

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'K4[Fe(CN)6]', protein row 'Met199Ala'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.35 ± 0.02; column 'kcat (s-1)' = 54 ± 1; column 'kcat/Km(s-1 mM-1)' = 155.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.35 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.35 mM. kcat: printed Table 2 cell 54 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 54.0 s^(-1). kcat/Km: printed Table 2 cell 155 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 155.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 54 / 0.35 = 154.2857142857143 s^-1 mM^-1, which is the value the export stores for kcat_over_km (154.2857142857143); the paper's own printed efficiency cell is 155.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'K4[Fe(CN)6]', protein row 'Met199Ala': Km = 0.35 ± 0.02 mM; kcat = 54 ± 1 s^-1; printed kcat/Km = 155 s^-1 mM^-1; printed pHopt = 4.0.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0M4FJ81 canonical sequence plus mutation_signature reconstruction (2026-07-01) and applied mutation signature M199G/R240H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature M199G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer 50 mM Britton-Robinson

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block '2.6-DMP', protein row 'Met199Gly'; column 'pHopt' = 8.0; column 'Km(mM)' = 0.67 ± 0.12; column 'kcat (s-1)' = 3.39 ± 0.17; column 'kcat/Km(s-1 mM-1)' = 5.07.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.67 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.67 mM. kcat: printed Table 2 cell 3.39 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 3.39 s^(-1). kcat/Km: printed Table 2 cell 5.07 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 5.07 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 3.39 / 0.67 = 5.059701492537314 s^-1 mM^-1, which is the value the export stores for kcat_over_km (5.059701492537314); the paper's own printed efficiency cell is 5.07 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block '2.6-DMP', protein row 'Met199Gly': Km = 0.67 ± 0.12 mM; kcat = 3.39 ± 0.17 s^-1; printed kcat/Km = 5.07 s^-1 mM^-1; printed pHopt = 8.0.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0M4FJ81 canonical sequence plus mutation_signature reconstruction (2026-07-01) and applied mutation signature H165A/R240H to reconstruct the assayed variant sequence.


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'ABTS', protein row 'Met199Ala'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.32 ± 0.05; column 'kcat (s-1)' = 33 ± 2; column 'kcat/Km(s-1 mM-1)' = 102.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.32 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.32 mM. kcat: printed Table 2 cell 33 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 33.0 s^(-1). kcat/Km: printed Table 2 cell 102 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 102.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 33 / 0.32 = 103.125 s^-1 mM^-1, which is the value the export stores for kcat_over_km (103.125); the paper's own printed efficiency cell is 102.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'ABTS', protein row 'Met199Ala': Km = 0.32 ± 0.05 mM; kcat = 33 ± 2 s^-1; printed kcat/Km = 102 s^-1 mM^-1; printed pHopt = 4.0.


sequence_source: UniProtKB:A0A0M4FJ81 canonical sequence plus mutation_signature reconstruction (2026-07-01)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature Y230A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 303.15 K; buffer 50 mM Britton-Robinson

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block '2.6-DMP', protein row 'Tyr230Ala'; column 'pHopt' = 8.5; column 'Km(mM)' = 0.76 ± 0.03; column 'kcat (s-1)' = 1.68 ± 0.07; column 'kcat/Km(s-1 mM-1)' = 2.22.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.76 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.76 mM. kcat: printed Table 2 cell 1.68 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 1.68 s^(-1). kcat/Km: printed Table 2 cell 2.22 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 2.22 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 1.68 / 0.76 = 2.2105263157894735 s^-1 mM^-1, which is the value the export stores for kcat_over_km (2.2105263157894735); the paper's own printed efficiency cell is 2.22 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block '2.6-DMP', protein row 'Tyr230Ala': Km = 0.76 ± 0.03 mM; kcat = 1.68 ± 0.07 s^-1; printed kcat/Km = 2.22 s^-1 mM^-1; printed pHopt = 8.5.


assay_conditions_summary: pH 3.5; 303.15 K; buffer 50 mM Britton-Robinson

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'ABTS', protein row 'Tyr230Ala'; column 'pHopt' = 3.5; column 'Km(mM)' = 0.17 ± 0.04; column 'kcat (s-1)' = 29 ± 3; column 'kcat/Km(s-1 mM-1)' = 169.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.17 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.17 mM. kcat: printed Table 2 cell 29 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 29.0 s^(-1). kcat/Km: printed Table 2 cell 169 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 169.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 29 / 0.17 = 170.58823529411762 s^-1 mM^-1, which is the value the export stores for kcat_over_km (170.58823529411762); the paper's own printed efficiency cell is 169.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'ABTS', protein row 'Tyr230Ala': Km = 0.17 ± 0.04 mM; kcat = 29 ± 3 s^-1; printed kcat/Km = 169 s^-1 mM^-1; printed pHopt = 3.5.


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'ABTS', protein row 'SgfSLwt'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.36 ± 0.07; column 'kcat (s-1)' = 15 ± 1; column 'kcat/Km(s-1 mM-1)' = 42.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.36 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.36 mM. kcat: printed Table 2 cell 15 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 15.0 s^(-1). kcat/Km: printed Table 2 cell 42 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 42.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 15 / 0.36 = 150.0 s^-1 mM^-1, which is the value the export stores for kcat_over_km (150.0); the paper's own printed efficiency cell is 42.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'ABTS', protein row 'SgfSLwt': Km = 0.36 ± 0.07 mM; kcat = 15 ± 1 s^-1; printed kcat/Km = 42 s^-1 mM^-1; printed pHopt = 4.0.


organism: Thermus sp.


organism: Thermus thermophilus


substrate_name: Guaiacol

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

substrate: Guaiacol


organism: Trametes versicolor

substrate_name: O2; Methyl syringate

substrate: O2; Methyl syringate


organism: unknown prokaryotic organism


organism: Acidobacteriaceae


organism: Acinetobacter baumannii

substrate_name: O2; Guaiacol

substrate: O2; Guaiacol


organism: Aeromonas hydrophila


organism: alpha proteobacterium Q-1


organism: Amycolatopsis sp.

sequence_source: UniProtKB:J9PBQ8 direct accession lookup on 2026-07-01


organism: Aquifex aeolicus


organism: Bacillus altitudinis


organism: Bacillus amyloliquefaciens


organism: Bacillus licheniformis

sequence_source: UniProtKB:Q65MU7 direct accession lookup on 2026-07-01


sequence_source: UniProtKB:H8WGE4 direct accession lookup on 2026-07-01


organism: Bacillus pumilus

sequence_source: UniProtKB:I3XLC2 direct accession lookup on 2026-07-01


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'K4[Fe(CN)6]', protein row 'Tyr230Ala'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.31 ± 0.01; column 'kcat (s-1)' = 86 ± 1; column 'kcat/Km(s-1 mM-1)' = 278.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.31 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.31 mM. kcat: printed Table 2 cell 86 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 86.0 s^(-1). kcat/Km: printed Table 2 cell 278 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 278.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 86 / 0.31 = 277.4193548387097 s^-1 mM^-1, which is the value the export stores for kcat_over_km (277.4193548387097); the paper's own printed efficiency cell is 278.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'K4[Fe(CN)6]', protein row 'Tyr230Ala': Km = 0.31 ± 0.01 mM; kcat = 86 ± 1 s^-1; printed kcat/Km = 278 s^-1 mM^-1; printed pHopt = 4.0.


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block '2.6-DMP', protein row 'Met199Ala'; column 'pHopt' = 8.0; column 'Km(mM)' = 0.83 ± 0.08; column 'kcat (s-1)' = 1.30 ± 0.05; column 'kcat/Km(s-1 mM-1)' = 1.55.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.83 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.83 mM. kcat: printed Table 2 cell 1.30 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 1.3 s^(-1). kcat/Km: printed Table 2 cell 1.55 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 1.55 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 1.30 / 0.83 = 1.566265060240964 s^-1 mM^-1, which is the value the export stores for kcat_over_km (1.566265060240964); the paper's own printed efficiency cell is 1.55 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block '2.6-DMP', protein row 'Met199Ala': Km = 0.83 ± 0.08 mM; kcat = 1.30 ± 0.05 s^-1; printed kcat/Km = 1.55 s^-1 mM^-1; printed pHopt = 8.0.


sequence_source: UniProtKB REST canonical sequence for A0A0M4FJ81


sequence_variant_note: Resolved canonical sequence from UniProtKB REST canonical sequence for A0A0M4FJ81 and applied mutation signature M199G/R240H to reconstruct the assayed variant sequence.


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'K4[Fe(CN)6]', protein row 'Met199Gly'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.25 ± 0.02; column 'kcat (s-1)' = 66 ± 2; column 'kcat/Km(s-1 mM-1)' = 261.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.25 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.25 mM. kcat: printed Table 2 cell 66 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 66.0 s^(-1). kcat/Km: printed Table 2 cell 261 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 261.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 66 / 0.25 = 264.0 s^-1 mM^-1, which is the value the export stores for kcat_over_km (264.0); the paper's own printed efficiency cell is 261.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'K4[Fe(CN)6]', protein row 'Met199Gly': Km = 0.25 ± 0.02 mM; kcat = 66 ± 2 s^-1; printed kcat/Km = 261 s^-1 mM^-1; printed pHopt = 4.0.


organism: Streptomyces lividans


organism: Streptomyces sp. C1


organism: Streptomyces sviceus

sequence_source: UniProtKB REST canonical sequence for B5HSR1


organism: Streptomyces viridosporus

sequence_source: UniProtKB REST canonical sequence for J9PBR2


organism: Thermobifida fusca


organism: Unknown


organism: Achromobacter xylosoxidans


organism: Acremonium sp.


organism: Agaricus bisporus


organism: Alcaligenes faecalis


organism: Alkalihalobacillus ligniniphilus


organism: Bacillus coagulans


proof_lines: pH 7.0, 22°C, recombinant enzyme, with 25% v/v DMSO

proof_lines: pH 6.5, 22°C, recombinant enzyme, with 0.8% v/v DMSO


organism: Bacillus sp.


organism: Bacillus subtilis

proof_lines:
pH 7, holoCotA
pH 3, holoCotA
pH 7.5, 37°C


organism: Carica papaya


organism: Citrobacter freundii


organism: Corynebacterium efficiens


organism: Desulfovibrio sp. A2


organism: Enterobacter ludwigii


organism: Geobacillus thermopakistaniensis


organism: Klebsiella pneumoniae


organism: Kocuria sp.


organism: Kurthia huakuii


organism: Lactobacillus plantarum


organism: Thioalkalivibrio sp.


organism: Trametes hirsuta

proof_lines: pH 4.5, 50°C, enzyme conjugated with 1.1 kDa PEG


organism: Trametes polyzona

proof_lines: pH 5.0, temperature not specified in the publication


organism: Trametes sp.

proof_lines: pH 5.0, 30°C, surface display laccase (SDL) biocatalyst (where the enzyme laccase is displayed on the surface of biological cells through synthetic biology)


organism: Trametes versicolor

substrate_name: O2; Syringic acid

proof_lines: enzyme conjugated with chitosan of 214 kDa

proof_lines: enzyme conjugated with chitosan of 505 kDa

substrate: O2; Syringic acid


organism: Lepista nuda


organism: Lysobacter sp. T-15


organism: Myrothecium verrucaria


organism: Pleurotus nebrodensis


organism: Pseudomonas sp. LBC1

substrate_name: o-Tolidine; O2

substrate: o-Tolidine; O2


organism: Shewanella putrefaciens


organism: Shigella dysenteriae


organism: Sporothrix carnis


organism: Streptomyces coelicolor

substrate_name: Small laccase (SLAC)

substrate: Small laccase (SLAC)


organism: Streptomyces griseorubens


organism: Thielavia sp.


organism: basidiomycete PM1

proof_lines: pH 5.0, temperature not specified in the publication, engineered enzyme 7D5

proof_lines: pH 3.0, temperature not specified in the publication, engineered enzyme 7D5

proof_lines: pH 4.0, temperature not specified in the publication, engineered enzyme 7D5


organism: Escherichia coli

proof_lines:
pH 5, 30°C
presence of 0.25 mM Cu2+, pH 5, 30°C
presence of 0.1 mM Cu2+, pH 5, 30°C


organism: Ganoderma lucidum


organism: Geobacillus sp. JS12


organism: Geobacillus sp. WSUCF1


organism: Klebsiella pneumoniae


organism: Klebsiella sp. 601


organism: Marinomonas mediterranea

sequence_source: UniProtKB REST direct accession check on 2026-07-01: Q9KJB8

proof_lines: recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C


organism: uncultured bacterium

sequence_source: GenBank KP752045.1 CDS translation; protein_id AKN79754.1; PMID 30568647


enzyme_display_name: dUTP diphosphatase

organism: Mycobacterium tuberculosis

substrate_name: dUTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNS5 direct accession lookup (https://rest.uniprot.org/uniprotkb/P9WNS5.json) and applied mutation signature T138ter to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T138STOP, at pH 7.5 and 20°C

enzyme: dUTP diphosphatase

substrate: dUTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNS5 direct accession lookup (https://rest.uniprot.org/uniprotkb/P9WNS5.json) and applied mutation signature R140K/H145W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R140K/H145W, at pH 7.5 and 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNS5 direct accession lookup (https://rest.uniprot.org/uniprotkb/P9WNS5.json) and applied mutation signature G143ter to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G143STOP, at pH 7.5 and 20°C


sequence_source: UniProtKB:P9WNS5 direct accession lookup (https://rest.uniprot.org/uniprotkb/P9WNS5.json)


organism: Plasmodium falciparum

sequence_source: UniProtKB:Q8II92 direct accession lookup (https://rest.uniprot.org/uniprotkb/Q8II92.json)

proof_lines: Ki above 0.01 mM, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8II92 direct accession lookup (https://rest.uniprot.org/uniprotkb/Q8II92.json) and applied mutation signature F46A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8II92 direct accession lookup (https://rest.uniprot.org/uniprotkb/Q8II92.json) and applied mutation signature I117A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8II92 direct accession lookup (https://rest.uniprot.org/uniprotkb/Q8II92.json) and applied mutation signature K96A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme K96A, at pH 8.0 and 25°C
mutant enzyme K96A, at pH 8.0 and 25°


proof_lines:
mutant enzyme F46A, at pH 8.0 and 25°C
mutant enzyme F46A, at pH 8.0 and 25°


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


proof_lines:
mutant enzyme I117A, at pH 8.0 and 25°C
mutant enzyme I117A, at pH 8.0 and 25°


proof_lines:
wild type enzyme, at pH 8.0 and 25°C
wild type enzyme, at pH 8.0 and 25°


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from UniProtKB:P33317 direct accession lookup (https://rest.uniprot.org/uniprotkb/P33317.json) and applied mutation signature R111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P33317 direct accession lookup (https://rest.uniprot.org/uniprotkb/P33317.json) and applied mutation signature Y88A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P33317 direct accession lookup (https://rest.uniprot.org/uniprotkb/P33317.json) and applied mutation signature Q114A to reconstruct the assayed variant sequence.


enzyme_name_source: UniProtKB direct accession P33317

substrate_name: dITP

sequence_source: UniProtKB direct accession P33317 REST lookup (2026-07-01)

substrate: dITP


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession P33317 REST lookup (2026-07-01) and applied mutation signature Q114A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q114A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C


substrate_name: UTP; dUTP

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession P33317 REST lookup (2026-07-01) and applied mutation signature Y88A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C

substrate: UTP; dUTP


substrate_name: UTP

substrate: UTP


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession P33317 REST lookup (2026-07-01) and applied mutation signature R111A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R111A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C


substrate_name: dITP; dUTP

proof_lines: wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C

substrate: dITP; dUTP


substrate_name: dITP; dUTP; UTP

substrate: dITP; dUTP; UTP


enzyme_name_source: UniProtKB direct accession Q8SDV3

organism: Staphylococcus phage phi11

substrate_name: Unknown

sequence_source: UniProtKB direct accession Q8SDV3 REST lookup (2026-07-01)

substrate: Unknown


enzyme_display_name: dUTPase

enzyme_name_source: UniProtKB direct accession A0EWK2

organism: Staphylococcus phage phinm1

sequence_source: UniProtKB direct accession A0EWK2 REST lookup (2026-07-01)

enzyme: dUTPase


enzyme_name_source: UniProtKB direct accession A0A480PG39

organism: Sus scrofa

sequence_source: UniProtKB direct accession A0A480PG39 REST lookup (2026-07-01)

proof_lines: wild-type, 25°C, pH 7.5, presence of K+, Mg2+


enzyme_name_source: UniProtKB direct accession Q77J78

organism: white spot syndrome virus

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession Q77J78 REST lookup (2026-07-01) and applied mutation signature R24T/S115R/D170G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession Q77J78 REST lookup (2026-07-01) and applied mutation signature K150E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession Q77J78 REST lookup (2026-07-01) and applied mutation signature R24T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession Q77J78 REST lookup (2026-07-01) and applied mutation signature K150A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB direct accession Q77J78 REST lookup (2026-07-01)


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature K150E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature R158E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature D170L to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTD170L'; column 'kcat (s-1)' = 0.53; column 'Km (uM)' = 7.1; column 'kcat/Km (M-1 s-1)' = 7.5 x 10^4; column 'Relative efficiency (%)' = 1.7. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.53 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.53 s^(-1). Km: printed Table 1 cell 7.1 in a column headed Km (uM); 1 uM is 0.001 mM, so 7.1 / 1000 = 0.0071 mM. kcat/Km: printed Table 1 cell 7.5 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 75000 / 1000 = 75 s^-1 mM^-1. The exported values are kcat 0.53 s^(-1) and Km 0.0071 mM and kcat_over_km 74.64788732394366 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTD170L': kcat = 0.53 s-1; Km = 7.1 uM; printed kcat/Km = 7.5 x 10^4 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTD170L'

table_label: Table 1: Enzyme kinetics data (J. Biol. Chem. 2018, 293(3):1088-1099). Printed column heads: Enzyme; kcat (s-1); Km (uM); kcat/Km (M-1 s-1); Relative efficiency (%).