column_label: Table 2 (Kinetic constants for the diphenolase activity of mushroom tyrosinase) prints one substrate column, o-Diphenol, followed by four numeric columns whose heads are Vmax^D (uM min^-1), kcat^D (s^-1), Km^D (mM) and kcat^D/Km^D (s^-1 mM^-1) in that printed order. The cited cell set is Table 2, o-diphenol row DHPAA: kcat^D (s^-1) = 631.6; Km^D (mM) = 5.1; kcat^D/Km^D (s^-1 mM^-1) = 123.8. The printed uncertainties of that row are Vmax 144.0 +/- 10.1, kcat 631.6 +/- 30.5, Km 5.1 +/- 0.2 and kcat/Km 123.8 +/- 11.

normalized_value_unit_evidence: kcat: printed Table 2 cell 631.6 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 631.6 s^(-1). Km: printed Table 2 cell 5.1 under the millimolar column head, so no unit conversion applies and the paper value is 5.1 mM. kcat/Km: printed Table 2 cell 123.8 under the s^-1 mM^-1 column head, so no unit conversion applies and the paper value is 123.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, o-diphenol row DHPAA: kcat = 631.6 s-1; Km = 5.1 mM; printed kcat/Km = 123.8 s-1 mM-1.

row_label: Table 2, o-diphenol row DHPAA


enzyme_display_name: tyrosinase

organism: Agaricus bisporus

substrate_name: L-alpha-Methyltyrosine

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 4 (Kinetic constants for the monophenolase activity of mushroom tyrosinase) prints one substrate column, Monophenol, followed by four numeric columns whose heads are Vmax^D (uM min^-1), Kcat^M (s^-1), Km^M (mM) and kcat^M/Km^M (s^-1 mM^-1) in that printed order. The cited cell set is Table 4, monophenol row L-alpha-Methyl tyrosine: Kcat^M (s^-1) = 0.6; Km^M (mM) = 1.20; kcat^M/Km^M (s^-1 mM^-1) = 0.5. The printed uncertainties of that row are Vmax 0.13 +/- 0.005, kcat 0.6 +/- 0.03, Km 1.20 +/- 0.08 and kcat/Km 0.5 +/- 0.06.

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.6 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 0.6 s^(-1). Km: printed Table 4 cell 1.20 under the millimolar column head, so no unit conversion applies and the paper value is 1.2 mM. kcat/Km: printed Table 4 cell 0.5 under the s^-1 mM^-1 column head, so no unit conversion applies and the paper value is 0.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, monophenol row L-alpha-Methyl tyrosine: kcat = 0.6 s-1; Km = 1.20 mM; printed kcat/Km = 0.5 s-1 mM-1.

table_label: Table 4: Kinetic constants for the monophenolase activity of mushroom tyrosinase (Eur J Biochem 2000, 267(5):1270-1279)

data_origin: experimental

enzyme: tyrosinase

substrate: L-alpha-Methyltyrosine

status: verified

source: oed


substrate_name: Dopa methyl ester

column_label: Table 2 (Kinetic constants for the diphenolase activity of mushroom tyrosinase) prints one substrate column, o-Diphenol, followed by four numeric columns whose heads are Vmax^D (uM min^-1), kcat^D (s^-1), Km^D (mM) and kcat^D/Km^D (s^-1 mM^-1) in that printed order. The cited cell set is Table 2, o-diphenol row Dopa methyl ester: kcat^D (s^-1) = 35.5; Km^D (mM) = 1.0; kcat^D/Km^D (s^-1 mM^-1) = 35.5. The printed uncertainties of that row are Vmax 8.1 +/- 0.4, kcat 35.5 +/- 1.4, Km 1.0 +/- 0.05 and kcat/Km 35.5 +/- 3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 35.5 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 35.5 s^(-1). Km: printed Table 2 cell 1.0 under the millimolar column head, so no unit conversion applies and the paper value is 1.0 mM. kcat/Km: printed Table 2 cell 35.5 under the s^-1 mM^-1 column head, so no unit conversion applies and the paper value is 35.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, o-diphenol row Dopa methyl ester: kcat = 35.5 s-1; Km = 1.0 mM; printed kcat/Km = 35.5 s-1 mM-1.

table_label: Table 2: Kinetic constants for the diphenolase activity of mushroom tyrosinase (Eur J Biochem 2000, 267(5):1270-1279)

substrate: Dopa methyl ester


kcat_over_km_origin: calculated

column_label: Table 4 (Kinetic constants for the monophenolase activity of mushroom tyrosinase) prints one substrate column, Monophenol, followed by four numeric columns whose heads are Vmax^D (uM min^-1), Kcat^M (s^-1), Km^M (mM) and kcat^M/Km^M (s^-1 mM^-1) in that printed order. The cited cell set is Table 4, monophenol row PHPAA: Kcat^M (s^-1) = 44.3; Km^M (mM) = 1.91; kcat^M/Km^M (s^-1 mM^-1) = 23. The printed uncertainties of that row are Vmax 10.1 +/- 0.7, kcat 44.3 +/- 1.5, Km 1.91 +/- 0.08 and kcat/Km 23 +/- 2.

normalized_value_unit_evidence: kcat: printed Table 4 cell 44.3 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 44.3 s^(-1). Km: printed Table 4 cell 1.91 under the millimolar column head, so no unit conversion applies and the paper value is 1.91 mM. kcat/Km: printed Table 4 cell 23 under the s^-1 mM^-1 column head, so no unit conversion applies and the paper value is 23.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, monophenol row PHPAA: kcat = 44.3 s-1; Km = 1.91 mM; printed kcat/Km = 23 s-1 mM-1.

row_label: Table 4, monophenol row PHPAA


substrate_name: L-Tyrosine

column_label: Table 4 (Kinetic constants for the monophenolase activity of mushroom tyrosinase) prints one substrate column, Monophenol, followed by four numeric columns whose heads are Vmax^D (uM min^-1), Kcat^M (s^-1), Km^M (mM) and kcat^M/Km^M (s^-1 mM^-1) in that printed order. The cited cell set is Table 4, monophenol row L-Tyrosine: Kcat^M (s^-1) = 7.9; Km^M (mM) = 0.21; kcat^M/Km^M (s^-1 mM^-1) = 38. The printed uncertainties of that row are Vmax 1.8 +/- 0.06, kcat 7.9 +/- 0.3, Km 0.21 +/- 0.01 and kcat/Km 38 +/- 3.

normalized_value_unit_evidence: kcat: printed Table 4 cell 7.9 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 7.9 s^(-1). Km: printed Table 4 cell 0.21 under the millimolar column head, so no unit conversion applies and the paper value is 0.21 mM. kcat/Km: printed Table 4 cell 38 under the s^-1 mM^-1 column head, so no unit conversion applies and the paper value is 38.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, monophenol row L-Tyrosine: kcat = 7.9 s-1; Km = 0.21 mM; printed kcat/Km = 38 s-1 mM-1.

row_label: Table 4, monophenol row L-Tyrosine

substrate: L-Tyrosine


verification_status: unverified

status: unverified


substrate_name: 4-Hydroxyphenyl propionic acid

column_label: Table 4 (Kinetic constants for the monophenolase activity of mushroom tyrosinase) prints one substrate column, Monophenol, followed by four numeric columns whose heads are Vmax^D (uM min^-1), Kcat^M (s^-1), Km^M (mM) and kcat^M/Km^M (s^-1 mM^-1) in that printed order. The cited cell set is Table 4, monophenol row PHPPA: Kcat^M (s^-1) = 66.7; Km^M (mM) = 0.44; kcat^M/Km^M (s^-1 mM^-1) = 152. The printed uncertainties of that row are Vmax 15.2 +/- 1.1, kcat 66.7 +/- 2.7, Km 0.44 +/- 0.01 and kcat/Km 152 +/- 10.

normalized_value_unit_evidence: kcat: printed Table 4 cell 66.7 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 66.7 s^(-1). Km: printed Table 4 cell 0.44 under the millimolar column head, so no unit conversion applies and the paper value is 0.44 mM. kcat/Km: printed Table 4 cell 152 under the s^-1 mM^-1 column head, so no unit conversion applies and the paper value is 152.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, monophenol row PHPPA: kcat = 66.7 s-1; Km = 0.44 mM; printed kcat/Km = 152 s-1 mM-1.

row_label: Table 4, monophenol row PHPPA

substrate: 4-Hydroxyphenyl propionic acid


organism: Priestia megaterium

substrate_name: L-tyrosine

sequence_source: UniProtKB B2ZB02 canonical sequence fetched by REST on 2026-05-31; V218G reconstructed after confirming canonical residue 218 is V.

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

mutation_type: substitution

substrate: L-tyrosine


substrate_name: L-Dopa

source_db: skid

kcat_over_km_display: Not reported

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB B2ZB02 canonical sequence fetched by REST on 2026-05-31.

substrate: L-Dopa

source: skid


organism: Ralstonia solanacearum

substrate_name: D-Tyrosine

sequence_source: UniProtKB Q8Y2J8 canonical sequence fetched by REST on 2026-05-31; N322S reconstructed after confirming canonical residue 322 is N.

substrate: D-Tyrosine


sequence_source: UniProtKB Q8Y2J8 canonical sequence fetched by REST on 2026-05-31 and matched to NCBI Protein NP_518458.


sequence_source: UniProtKB Q8Y2J8 canonical sequence fetched by REST on 2026-05-31; V153A reconstructed after confirming canonical residue 153 is V.


sequence_source: UniProtKB Q8Y2J8 canonical sequence fetched by REST on 2026-05-31; T359M reconstructed after confirming canonical residue 359 is T.

sequence_variant_note: Mutation signature T359M matches the mutant residue at offset +0 and the reference residue at offset +15; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB Q8Y2J8 canonical sequence cross-checked against NCBI NP_518458.1/WP_011000301.1.


sequence_source: UniProtKB Q8Y2J8 canonical sequence cross-checked against NCBI NP_518458.1/WP_011000301.1; residue 317 is D and was changed to Y during review.

sequence_variant_note: Mutation signature D317Y matches the mutant residue at offset +0 and the reference residue at offset -6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB Q8Y2J8 canonical sequence cross-checked against NCBI NP_518458.1/WP_011000301.1; residue 183 is T and was changed to I during review.

sequence_variant_note: Mutation signature T183I matches the mutant residue at offset +0 and the reference residue at offset +7; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB Q8Y2J8 canonical sequence cross-checked against NCBI NP_518458.1/WP_011000301.1; residue 185 is F and was changed to Y during review.

sequence_variant_note: Mutation signature F185Y matches the mutant residue at offset +0 and the reference residue at offset +3; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: Saccharomyces cerevisiae

substrate_name: O2; L-Adrenaline

kcat_display: Not reported

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

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

substrate: O2; L-Adrenaline


sequence_source: Reconstructed from the direct UniProtKB Q8Y2J8 / NCBI Protein NP_518458.1 canonical FASTA match after confirming residue 330 is L and applying L330V.


sequence_source: Reconstructed from the direct UniProtKB Q8Y2J8 / NCBI Protein NP_518458.1 canonical FASTA match after confirming residue 119 is Y and applying Y119F.


substrate_name: O2; L-Dopa

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

assay_conditions_summary: pH 7; 298.15 K; buffer phosphate

proof_lines: pH and temperature not specified in the publication

source_db: brenda

substrate: O2; L-Dopa


organism: Hahella sp. (strain CCB-MM4)

source_db: uniprot

proof_lines: kcat is 6.12 sec(-1) with L-tyrosine as substrate. kcat is 9.94 sec(-1) with L-dopa as substrate.

source: uniprot


substrate_name: L-tyrosine (for latent-HcTyr1)

proof_lines: kcat is 0.71 sec(-1) with L-tyrosine as substrate (for latent-HcTyr1). kcat is 21.8 sec(-1) with L-tyrosine as substrate (for cleaved-HcTyr1). kcat is 1.00 sec(-1) with L-dopa as substrate (for latent-HcTyr1). kcat is 51.3 sec(-1) with L-do

substrate: L-tyrosine (for latent-HcTyr1)


organism: Sarcophaga argyrostoma

substrate_name: L-dopa

substrate: L-dopa


substrate_name: D-Dopa

sequence_source: UniProtKB B2ZB02, linked to PMID 19672047

assay_conditions_summary: pH 7; buffer phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.0), with 30% (v/v) DMSO

substrate: D-Dopa

source: brenda


assay_conditions_summary: pH 7; 301.15 K; buffer Tris-HCl

proof_lines: wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C


organism: Prunus persica

substrate_name: O2; (+)-Catechin

ki_unit: mM

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: O2; (+)-Catechin


enzyme_display_name: glucuronosyltransferase

organism: Homo sapiens

substrate_name: Scopoletin; UDPglucuronate

sequence_source: UniProtKB P19224 FASTA checked directly; canonical residue H371 matched and was replaced with A for H371A.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant isoenzyme UGT1A6 H371A

enzyme: glucuronosyltransferase

substrate: Scopoletin; UDPglucuronate


sequence_source: UniProtKB O60656 FASTA checked directly; canonical residue H369 matched and was replaced with A for H369A.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant isoenzyme UGT1A9 H369A


substrate_name: UDPglucuronate; 4-Methylumbelliferone

sequence_source: UniProtKB P22309 FASTA checked directly; canonical residue P229 matched and was replaced with Q for P229Q.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant UGT1A1*27 (P229Q)

substrate: UDPglucuronate; 4-Methylumbelliferone


substrate_name: 4-Methylumbelliferone; UDPglucuronate

sequence_source: UniProtKB P35503 FASTA checked directly; requested Y486D did not match canonical residue Q486.

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

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant UGT1A3 (Y486D)

substrate: 4-Methylumbelliferone; UDPglucuronate


km_display: Not reported

sequence_source: UniProtKB P22309 FASTA checked directly; canonical residue Y486 matched and was replaced with D for Y486D.

sequence_variant_note: Mutation signature Y486D matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant UGT1A1*7 (Y486D)


sequence_source: UniProtKB P19224 FASTA checked directly; requested Y486D did not match canonical residue H486.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant UGT1A6 (Y486D)


sequence_source: UniProtKB P22309 FASTA checked directly; canonical residue G71 matched and was replaced with R for G71R.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant UGT1A1*6 (G71R)


sequence_source: UniProtKB REST lookup for P19224; canonical accession sequence.

proof_lines: pH 7.4, 37°C, recombinant UGT1A6, substrate inhibition model


sequence_source: UniProtKB REST lookup for P19224; canonical sequence with E379A applied after residue check.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant isoenzyme UGT1A6 E379A


substrate_name: UDPglucuronate; Scopoletin

proof_lines:
isozyme UGT1A10, pH 6.4, 37°C
isozyme UGT1A9, pH 7.4, 37°C
UGT1A9/UGT2B7 heterodimer, pH 7.4, 37°C

substrate: UDPglucuronate; Scopoletin


substrate_name: Androstanediol; UDPglucuronate

proof_lines: isozyme UGT2B7 in COS-1 cell microsomes, pH 7.8, 37°C, in presence with CYP2C9

substrate: Androstanediol; UDPglucuronate


sequence_source: UniProt REST Q9HAW8 canonical sequence fetched 2026-05-31; M59I substitution applied after confirming residue 59 is M.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant UGT1A10 M59I


sequence_source: UniProt REST Q9HAW8 canonical sequence fetched 2026-05-31; T202I substitution applied after confirming residue 202 is T.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant UGT1A10 T202I


substrate_name: UDPglucuronate; Aldosterone

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) wildtype allelic variant UGT2B7H268

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) wildtype allelic variant UGT2B7Y268

substrate: UDPglucuronate; Aldosterone


substrate_name: UDPglucuronate; Zidovudine

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) wildtype UGT2B7*2 (polymorphism H268Y)

proof_lines: UGT1A9/UGT2B7(mutant H268Y)-CFP heterodimer, pH 7.4, 37°C

proof_lines: pH 7.4, 37°C, recombinant HA-tagged mutant H268Y dimer

substrate: UDPglucuronate; Zidovudine


substrate_name: Entacapone; UDPglucuronate

sequence_source: UniProtKB:P35503 direct REST lookup

proof_lines:
isozyme UGT1A3, pH 7.4, 37°C
pH 7.4, 37°C, isozyme UGT1A3
pH 7.4, 37°C

substrate: Entacapone; UDPglucuronate


substrate_name: 8-Hydroxyquinoline; UDPglucuronate

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:P54855 direct REST lookup

proof_lines:
pH 7.4, 37°C, isozyme UGT2B15
37°C, pH 7.4
isoform UGT2B15, at pH 7.4 and 37°C

source_databases_merged: sabio_rk brenda skid

substrate: 8-Hydroxyquinoline; UDPglucuronate


substrate_name: Testosterone; UDPglucuronate

sequence_source: UniProtKB:O75795 direct REST lookup

proof_lines:
pH 7.4, 37°C, isozyme UGT2B17
37°C, pH 7.5
37°C, pH 7.4

substrate: Testosterone; UDPglucuronate


sequence_source: UniProtKB:P22310 direct REST lookup

proof_lines: imipramine N-glucuronide formation, 1A4 co-expressed with isoform 1A4

proof_lines: imipramine N-glucuronide formation, 1A4 co-expressed with isoform 1A6


sequence_variant_note: Resolved canonical sequence from UniProtKB P16662 direct accession; current canonical residue 268 is Y and UniProt natural variant feature records Y268H for allele UGT2B7*1, matching the source note for wildtype UGT2B7*1/H268H. and applied mutation signature H268H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) wildtype UGT2B7*1 (polymorphism H268H)


substrate_name: UDPglucuronate; Eugenol

sequence_source: UniProtKB Q9HAW8 direct accession sequence; reviewed human UGT1A10 with EC 2.4.1.17.

proof_lines: isozyme UGT1A10, Michaelis-Menten kinetic, pH 7.4, 37°C

substrate: UDPglucuronate; Eugenol


sequence_source: UniProtKB Q9HAW7 direct accession sequence; reviewed human UGT1A7 with EC 2.4.1.17.

proof_lines: isozyme UGT1A7, Michaelis-Menten kinetic, pH 7.4, 37°C


sequence_source: UniProtKB P22309 direct accession sequence; reviewed human UGT1A1 with EC 2.4.1.17.

proof_lines: recombinant isozyme UGT1A1, pH 7.4, 37°C


substrate_name: UDPglucuronate; Phloretin

sequence_source: UniProtKB Q9HAW9 direct accession sequence; reviewed human UGT1A8 with EC 2.4.1.17.

proof_lines: pH 7.4, temperature not specified in the publication, isozyme UGT1A8

substrate: UDPglucuronate; Phloretin


sequence_source: UniProtKB Q0VAJ1 direct accession sequence; active TrEMBL human UDP-glucuronosyltransferase entry annotated with gene UGT1A4 and EC 2.4.1.17.


sequence_source: UniProtKB Q5DT03 direct accession sequence; active TrEMBL human UDP-glucuronosyltransferase entry annotated with gene UGT1A1 and EC 2.4.1.17.


substrate_name: UDPglucuronate; Clozapine

sequence_source: UniProtKB P22310 direct accession; reviewed human UGT1A4 with EC 2.4.1.17. Direct residue check found canonical L at residue 48 and UniProt records L48V as a natural variant, so the row-specific sequence was reconstructed by substituting V at residue 48.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant isoform UGT1A4 L48V

proof_lines: recombinant mutant isozyme UGT1A4 L48V, pH 8.4, 37°C

substrate: UDPglucuronate; Clozapine


organism: Bellis perennis

sequence_source: UniProtKB Q5NTH0 REST FASTA direct check; accession supplied by OED source snapshot.


sequence_source: UniProtKB Q5NTH0 REST FASTA direct check; accession supplied by SABIO-RK source snapshot.


substrate_name: UDPglucuronate

substrate: UDPglucuronate


organism: Canis familiaris

sequence_source: UniProtKB Q6K1J1 REST FASTA direct check; accession supplied by SABIO-RK source snapshot.


sequence_source: Canonical UniProtKB P19224 checked as context only; not accepted as row sequence because H361A coordinates are unresolved against the current canonical sequence.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant isoenzyme UGT1A6 H361A


sequence_source: Canonical UniProtKB P19224 checked as context only; not accepted as row sequence because H370Q coordinates are unresolved against the current canonical sequence.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant isoenzyme UGT1A6 H370Q


sequence_source: Canonical UniProtKB P19224 checked as context only; not accepted as row sequence because H370A coordinates are unresolved against the current canonical sequence.

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant isoenzyme UGT1A6 H370A


proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant UGT1A10 (Y486D)


proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant UGT1A1*62 (F83L)


substrate_name: Diclofenac; UDPglucuronate

proof_lines: membrane-bound recombinant isoform UGT1A10 from CHO cells, at pH 7.4 and 37°C

proof_lines: membrane-bound recombinant isoform UGT1A10 from HEK-293 cells, at pH 7.4 and 37°C

proof_lines: without phospholipid purified recombinant isoform UGT1A10 from CHO cells, at pH 7.4 and 37°C

substrate: Diclofenac; UDPglucuronate


organism: Macaca mulatta

sequence_source: UniProtKB REST accession lookup for Q95KM4, checked 2026-05-31


organism: Rattus norvegicus

substrate_name: UDPglucuronate; Diclofenac

sequence_source: UniProtKB REST accession lookup for P09875, checked 2026-05-31

substrate: UDPglucuronate; Diclofenac


substrate_name: UDP-alpha-D-glucuronate (when assaying glucuronidation with (1S,2R,4S)-borneol and 4-nitrophenol as substrates)


substrate_name: UDPglucuronate; Bilirubin

sequence_variant_note: Resolved canonical sequence from UniProtKB:P22309 direct sequence; F170del reconstructed from PMID:8226884 and SABIO-RK delta170 note and applied mutation signature Δ170 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: SABIO-RK modifier species: glucuronosyltransferase(Enzyme) mutant delta170

substrate: UDPglucuronate; Bilirubin


organism: Macaca fascicularis

sequence_source: UniProtKB:Q8WN97 direct accession lookup


sequence_source: UniProtKB:Q9XT55 direct accession lookup


sequence_source: UniProtKB:O97951 direct accession lookup


substrate_name: 17alpha-estradiol/epiestradiol (when assaying glucuronidation at position 3)

proof_lines: Some kinetic parameters were assessed using commercial enzymes, which may represent a mix of both active and inactive protein forms, and therefore modify the kinetic values.


substrate_name: 17beta-estradiol/estradiol (when assaying glucuronidation at position 17)


substrate_name: 17alpha-estradiol/epiestradiol (when assaying glucuronidation at position 17)


substrate_name: calcidiol (when assaying glucuronidation at position 25)


substrate_name: estrone (when assaying glucuronidation at position 3)


substrate_name: 17beta-estradiol/estradiol (when assaying glucuronidation at position 3)


substrate: 17alpha-estradiol/epiestradiol (when assaying glucuronidation at position 3)


substrate_name: (E)-ferulate (when assaying glucuronidation at the phenolic group)


substrate_name: androsterone

substrate: androsterone


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

substrate: 17beta-estradiol/estradiol (when assaying glucuronidation at position 17)


substrate: 17alpha-estradiol/epiestradiol (when assaying glucuronidation at position 17)


substrate_name: UDPglucuronate; Denopamine

substrate: UDPglucuronate; Denopamine


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

substrate: 17beta-estradiol/estradiol (when assaying glucuronidation at position 3)


substrate: estrone (when assaying glucuronidation at position 3)


substrate_name: bilirubin

substrate: bilirubin


proof_lines: isoform UGT2B9, at pH 7.4, temperature not specified in the publication


organism: Oryctolagus cuniculus

proof_lines: liver microsomes, substrate denopamine, pH 7.5, 37°C

proof_lines: 1.5 mM morphine added, ethanol-induced enzyme


proof_lines: 17beta-hydroxysteroid UDP-glucuronosyltransferase activity, Wistar strain


substrate_name: lamotrigine

substrate: lamotrigine


substrate_name: propofol

substrate: propofol


substrate_name: Mycophenolic acid

substrate: Mycophenolic acid


substrate_name: sulfinpyrazone

substrate: sulfinpyrazone


substrate_name: retigabine

substrate: retigabine


enzyme_display_name: beta-glucosidase

substrate_name: daidzin

sequence_source: UniProtKB Q9H227 canonical sequence, direct REST/FASTA check 2026-05-31.

enzyme: beta-glucosidase

substrate: daidzin


substrate_name: p-Nitrophenyl-beta-D-glucoside

substrate: p-Nitrophenyl-beta-D-glucoside


substrate_name: p-Nitrophenyl-beta-D-galactoside

substrate: p-Nitrophenyl-beta-D-galactoside


substrate_name: Naringenin 7-O-beta-D-glucoside

substrate: Naringenin 7-O-beta-D-glucoside


substrate_name: Eriodictyol 7-O-beta-D-glucoside

substrate: Eriodictyol 7-O-beta-D-glucoside


substrate_name: Genistein 7-O-beta-D-glucoside

substrate: Genistein 7-O-beta-D-glucoside


sequence_source: UniProtKB Q9H227 canonical sequence, direct REST/FASTA check 2026-05-31; Y308F reconstructed by 1-based coordinate substitution after confirming residue 308 is Y.


sequence_source: UniProtKB REST Q9H227 canonical sequence; local residue check confirmed V168; row-specific V168Y sequence reconstructed by substituting Y at position 168.


substrate_name: p-Nitrophenyl-beta-D-fucopyranoside

substrate: p-Nitrophenyl-beta-D-fucopyranoside


sequence_source: UniProtKB REST Q9H227 canonical sequence; local residue check confirmed Y308; row-specific Y308F sequence reconstructed by substituting F at position 308.


substrate_name: Quercetin 7-O-beta-D-glucoside

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9H227 and applied mutation signature V168Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 310.15 K; buffer the substrate at 10-500 uM in 50 mM sodium phosphate

column_label: Table 3 prints one Substrate column and then one column block per enzyme, each block headed K m (uM), k cat (s-1 ) and k cat /K m (mM-1 s-1 ). The cited cell set is the Val168 to Tyr block (V168Y), substrate row Quercetin-7-Glc, where the printed cells are K m = 158, k cat = 0.12 and k cat /K m = 0.75. The printed K m number of this flavonoid glucoside row is micromolar on the paper's own arithmetic, because 158 uM is 0.158 mM and the quotient of the two printed component cells is then 0.76 mM^-1 s^-1, alongside the printed efficiency cell 0.75 mM^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 158 under the head K m (uM) in the Val168 to Tyr block (V168Y), and 158 / 1000 = 0.158 mM. kcat: printed Table 3 cell 0.12 under the head k cat (s-1 ), already per second, so no unit conversion applies and the paper value is 0.12 s^(-1). kcat/Km: printed Table 3 cell 0.75 under the head k cat /K m (mM-1 s-1 ), and 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the paper value is 0.75 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.12 / 0.158 = 0.7594936708860759 s^-1 mM^-1, alongside the printed efficiency cell 0.75 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, Val168 to Tyr block (V168Y), substrate row Quercetin-7-Glc: K m = 158 uM, k cat = 0.12 s^-1, printed k cat /K m = 0.75 mM^-1 s^-1.

table_label: Table 3: Kinetic parameters of wild-type and mutant hCBGs on pNP-glycosides and flavonoid glucosides (Biochem. J. 2003, 373:41-48)

substrate: Quercetin 7-O-beta-D-glucoside

status: corrected


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

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


column_label: Table 3 prints one Substrate column and then one column block per enzyme, each block headed K m (uM), k cat (s-1 ) and k cat /K m (mM-1 s-1 ). The cited cell set is the Val168 to Tyr block (V168Y), substrate row Naringenin-7-Glc, where the printed cells are K m = 1240, k cat = 0.33 and k cat /K m = 0.26. The printed K m number of this flavonoid glucoside row is micromolar on the paper's own arithmetic, because 1240 uM is 1.24 mM and the quotient of the two printed component cells is then 0.27 mM^-1 s^-1, alongside the printed efficiency cell 0.26 mM^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 1240 under the head K m (uM) in the Val168 to Tyr block (V168Y), and 1240 / 1000 = 1.24 mM. kcat: printed Table 3 cell 0.33 under the head k cat (s-1 ), already per second, so no unit conversion applies and the paper value is 0.33 s^(-1). kcat/Km: printed Table 3 cell 0.26 under the head k cat /K m (mM-1 s-1 ), and 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the paper value is 0.26 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.33 / 1.24 = 0.26612903225806456 s^-1 mM^-1, alongside the printed efficiency cell 0.26 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, Val168 to Tyr block (V168Y), substrate row Naringenin-7-Glc: K m = 1240 uM, k cat = 0.33 s^-1, printed k cat /K m = 0.26 mM^-1 s^-1.


organism: Bacteroides ovatus

assay_conditions_summary: pH 6; 310.15 K; buffer and pH optimum

column_label: Extended Data Table ED1; row Bo GH3B / Glc-β-PNP; columns k cat (s -1 ), K m (mM), and same-row kcat/Km quotient; raw kcat 1.74 ± 0.21; raw Km 0.155 ± 0.039.

row_label: Bo GH3B / Glc-β-PNP

table_label: Extended Data Table ED1: Summary of kinetic analyses of XyGUL glycoside hydrolases


organism: Bifidobacterium breve


organism: Caldicellulosiruptor saccharolyticus


organism: Halothermothrix orenii

substrate_name: cellobiose

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

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 'F417Y', D-cellobiose block: k_cat,app = 38.7 ± 0.6; K_m = 3.5 ± 0.2; k_cat,app/K_m = 11.1.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 38.7 ± 0.6 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 38.7 s^(-1). K_m: printed Table 2 cell 3.5 ± 0.2 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 3.5 mM. k_cat/K_m: printed Table 2 cell 11.1 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 11.1 s^(-1)*mM^(-1). Closure check: 38.7 / 3.5 = 11.0571 s^-1 mM^-1, which rounds to the printed efficiency cell 11.1 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-cellobiose block: column 'k_cat,app (s^-1)' prints 38.7 ± 0.6; column 'K_m (mM)' prints 3.5 ± 0.2; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 11.1.

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

substrate: cellobiose


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-cellobiose block: k_cat,app = 8.5 ± 0.3; K_m = 20.2 ± 1.6; k_cat,app/K_m = 0.42.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 8.5 ± 0.3 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 8.5 s^(-1). K_m: printed Table 2 cell 20.2 ± 1.6 in column 'K_m (mM)' of the D-cellobiose block; already mM, no conversion, paper value 20.2 mM. k_cat/K_m: printed Table 2 cell 0.42 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 0.42 s^(-1)*mM^(-1). Closure check: 8.5 / 20.2 = 0.420792 s^-1 mM^-1, which rounds to the printed efficiency cell 0.42 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-cellobiose block: column 'k_cat,app (s^-1)' prints 8.5 ± 0.3; column 'K_m (mM)' prints 20.2 ± 1.6; column 'k_cat,app/K_m (mM^-1 s^-1)' prints 0.42.

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


substrate_name: lactose

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-lactose block: k_cat,app = 1.47 ± 0.05; K_m = 41.3 ± 3.1; k_cat,app/K_m = 0.036.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 1.47 ± 0.05 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 1.47 s^(-1). K_m: printed Table 2 cell 41.3 ± 3.1 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 41.3 mM. k_cat/K_m: printed Table 2 cell 0.036 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 0.036 s^(-1)*mM^(-1). Closure check: 1.47 / 41.3 = 0.0355932 s^-1 mM^-1, which rounds to the printed efficiency cell 0.036 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-lactose block: column 'k_cat,app (s^-1)' prints 1.47 ± 0.05; column 'K_m (mM)' prints 41.3 ± 3.1; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 0.036.

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

substrate: lactose


sequence_source: UniProtKB reviewed accession Q9H227 canonical sequence; worker confirmed canonical residue Y at position 308 and reconstructed Y308F on 2026-05-31.


sequence_source: UniProtKB reviewed accession Q9H227 canonical sequence; worker confirmed canonical residue V at position 168 and reconstructed V168Y on 2026-05-31.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9H227 and applied mutation signature Y308F to reconstruct the assayed variant sequence.

column_label: Table 3 prints one Substrate column and then one column block per enzyme, each block headed K m (uM), k cat (s-1 ) and k cat /K m (mM-1 s-1 ). The cited cell set is the Tyr308 to Phe block (Y308F), substrate row pNPFuc, where the printed cells are K m = 0.18, k cat = 1.18 and k cat /K m = 6.55. The printed K m number of this pNP-glycoside row is millimolar on the paper's own arithmetic, because reading 0.18 in mM puts the quotient of the two printed component cells at 6.56 mM^-1 s^-1, alongside the printed efficiency cell 6.55 mM^-1 s^-1, while reading it in uM would put that quotient at 6555556 mM^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.18 under the head K m (uM) in the Tyr308 to Phe block (Y308F), read in mM as the paper's own printed efficiency cell for this row requires, so no unit conversion applies and the paper value is 0.18 mM. kcat: printed Table 3 cell 1.18 under the head k cat (s-1 ), already per second, so no unit conversion applies and the paper value is 1.18 s^(-1). kcat/Km: printed Table 3 cell 6.55 under the head k cat /K m (mM-1 s-1 ), and 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the paper value is 6.55 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.18 / 0.18 = 6.555555555555555 s^-1 mM^-1, alongside the printed efficiency cell 6.55 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, Tyr308 to Phe block (Y308F), substrate row pNPFuc: K m = 0.18 mM, k cat = 1.18 s^-1, printed k cat /K m = 6.55 mM^-1 s^-1.


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


column_label: Table 3 prints one Substrate column and then one column block per enzyme, each block headed K m (uM), k cat (s-1 ) and k cat /K m (mM-1 s-1 ). The cited cell set is the Val168 to Tyr block (V168Y), substrate row Daidzein-7-Glc, where the printed cells are K m = 470, k cat = 0.69 and k cat /K m = 1.46. The printed K m number of this flavonoid glucoside row is micromolar on the paper's own arithmetic, because 470 uM is 0.47 mM and the quotient of the two printed component cells is then 1.47 mM^-1 s^-1, alongside the printed efficiency cell 1.46 mM^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 470 under the head K m (uM) in the Val168 to Tyr block (V168Y), and 470 / 1000 = 0.47 mM. kcat: printed Table 3 cell 0.69 under the head k cat (s-1 ), already per second, so no unit conversion applies and the paper value is 0.69 s^(-1). kcat/Km: printed Table 3 cell 1.46 under the head k cat /K m (mM-1 s-1 ), and 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the paper value is 1.46 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.69 / 0.47 = 1.4680851063829787 s^-1 mM^-1, alongside the printed efficiency cell 1.46 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, Val168 to Tyr block (V168Y), substrate row Daidzein-7-Glc: K m = 470 uM, k cat = 0.69 s^-1, printed k cat /K m = 1.46 mM^-1 s^-1.


substrate_name: p-Nitrophenyl-beta-L-arabinopyranoside

column_label: Table 3 prints one Substrate column and then one column block per enzyme, each block headed K m (uM), k cat (s-1 ) and k cat /K m (mM-1 s-1 ). The cited cell set is the Val168 to Tyr block (V168Y), substrate row pNPAra, where the printed cells are K m = 0.18, k cat = 0.52 and k cat /K m = 2.96. The printed K m number of this pNP-glycoside row is millimolar on the paper's own arithmetic, because reading 0.18 in mM puts the quotient of the two printed component cells at 2.89 mM^-1 s^-1, alongside the printed efficiency cell 2.96 mM^-1 s^-1, while reading it in uM would put that quotient at 2888889 mM^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.18 under the head K m (uM) in the Val168 to Tyr block (V168Y), read in mM as the paper's own printed efficiency cell for this row requires, so no unit conversion applies and the paper value is 0.18 mM. kcat: printed Table 3 cell 0.52 under the head k cat (s-1 ), already per second, so no unit conversion applies and the paper value is 0.52 s^(-1). kcat/Km: printed Table 3 cell 2.96 under the head k cat /K m (mM-1 s-1 ), and 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the paper value is 2.96 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.52 / 0.18 = 2.8888888888888893 s^-1 mM^-1, alongside the printed efficiency cell 2.96 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, Val168 to Tyr block (V168Y), substrate row pNPAra: K m = 0.18 mM, k cat = 0.52 s^-1, printed k cat /K m = 2.96 mM^-1 s^-1.

substrate: p-Nitrophenyl-beta-L-arabinopyranoside


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-lactose block: k_cat,app = 7.8 ± 0.4; K_m = 23.2 ± 2.7; k_cat,app/K_m = 0.34.

normalized_value_unit_evidence: k_cat: printed Table 2 cell 7.8 ± 0.4 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 7.8 s^(-1). K_m: printed Table 2 cell 23.2 ± 2.7 in column 'K_m (mM)' of the D-lactose block; already mM, no conversion, paper value 23.2 mM. k_cat/K_m: printed Table 2 cell 0.34 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 0.34 s^(-1)*mM^(-1). Closure check: 7.8 / 23.2 = 0.336207 s^-1 mM^-1, which rounds to the printed efficiency cell 0.34 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-lactose block: column 'k_cat,app (s^-1)' prints 7.8 ± 0.4; column 'K_m (mM)' prints 23.2 ± 2.7; column 'k_cat,app/K_m (s^-1 mM^-1)' prints 0.34.

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


sequence_source: UniProtKB Q9H227 live REST direct lookup; reviewed Swiss-Prot GBA3_HUMAN canonical sequence.

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


substrate_name: p-Nitrophenyl-beta-D-xylopyranoside

substrate: p-Nitrophenyl-beta-D-xylopyranoside


sequence_source: UniProt Q9H227 canonical sequence reconstructed with Q307N after validating residue Q307

sequence_variant_note: Mutation signature Q307N matches the mutant residue at offset +0 and the reference residue at offset +10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProt Q9H227 canonical sequence reconstructed with W345M after validating residue W345


sequence_source: UniProt Q9H227 canonical sequence reconstructed with W345A after validating residue W345


sequence_source: UniProt Q9H227 canonical sequence reconstructed with M172L after validating residue M172

sequence_variant_note: Mutation signature M172L matches the mutant residue at offset +0 and the reference residue at offset +6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_Q9H227_canonical_sequence and applied mutation signature W345A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_Q9H227_canonical_sequence and applied mutation signature M172L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_Q9H227_canonical_sequence and applied mutation signature Q307N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_Q9H227_canonical_sequence and applied mutation signature W345M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9H227 canonical FASTA checked directly; reconstructed Q307N from canonical Q307


sequence_source: UniProtKB Q9H227 canonical FASTA checked directly; reconstructed W345M from canonical W345


sequence_source: UniProtKB Q9H227 canonical FASTA checked directly; reconstructed W345A from canonical W345


organism: Arabidopsis thaliana

assay_conditions_summary: pH 4.5; 310.15 K; buffer 50 mM sodium citrate

column_label: Table label: Table 2 Kinetic parameters of recombinant TGG1, TGG4 and TGG5. Row: TGG1 | pNPG. Columns read: Km (mM) cell 34, Kcat (s^-1) cell 1.2, Kcat/Km (s^-1 mM^-1) cell 0.035. metric: kcat; raw value: 1.2; raw unit: s^-1; normalized value: 1.2 s^(-1); metric: Km; raw value: 34; raw unit: mM; normalized value: 34.0 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.03529411764705882 s^-1 mM^-1; assay condition: Recombinant Arabidopsis thaliana myrosinase expressed in Pichia pastoris with a 6xHis-tag; O-b-glucosidase activity assay (Methods 5.6): myrosinase was dissolved in 50 mM sodium citrate buffer, pH 4.5, and p-Nitrophenyl b-D-glucopyranoside (PNPG) was dissolved in 50 mM sodium citrate buffer, pH 4.5; the PNPG solution was incubated in an Eppendorf Thermomixer (37 °C, 350 rpm) for 5 min prior to the experiment; the reaction was terminated with 1 M sodium carbonate and the product read at 405 nm. Export row conditions: pH 4.5; 310.15 K.

normalized_value_unit_evidence: Table 2 row TGG1 | pNPG: kcat 1.2 s^-1 = 1.2 s^(-1) (no conversion needed); Km 34 mM = 34.0 mM (already in mM, no conversion needed); kcat/Km 0.03529411764705882 s^-1 mM^-1, the quotient of this row's own printed kcat and Km cells (1.2 / 34). In the PDF text extraction the micro sign of µmol renders as the letter l (`lmol`) and superscript minus-one exponents are flattened to a control character (U+0002) followed by 1, so the header cell `Kcat (s1)` is the paper's Kcat (s^-1) and the header cell `Kcat/Km (s1 mM1)` is the paper's Kcat/Km (s^-1 mM^-1). The printed Kcat/Km cell 0.035 is already in s^-1 mM^-1, the export's ratio unit.

raw_value_unit_evidence: Table 2 Kinetic parameters of recombinant TGG1, TGG4 and TGG5. | metric header row of Table 2 (as extracted): Enzyme Substrate Km (mM) Vmax (lmol min1 g1) Kcat (s1) Kcat/Km (s1 mM1) | row: TGG1 pNPG 34 ± 0 1.2 ± 0 1.2 ± 0 0.035 | cells read: Km = 34 mM; Vmax = 1.2 ± 0 lmol min1 mg1; Kcat = 1.2 s^-1; Kcat/Km = 0.035 s^-1 mM^-1. Table 2 footnote: The data represent the means and standard deviations of three (sinigrin) or two experiments (pNPG) with values calculated from Hanes plots. Sinigrin concentrations varied from 0.03 to 7.2 mM while p-nitrophenyl b-D-glucopyranoside (pNPG) concentrations varied from 1.5 to 99 mM depending on enzyme.

row_label: TGG1 | pNPG


column_label: Table label: Table 2 Kinetic parameters of recombinant TGG1, TGG4 and TGG5. Row: TGG4 | pNPG. Columns read: Km (mM) cell 28, Kcat (s^-1) cell 7.3, Kcat/Km (s^-1 mM^-1) cell 0.26. metric: kcat; raw value: 7.3; raw unit: s^-1; normalized value: 7.3 s^(-1); metric: Km; raw value: 28; raw unit: mM; normalized value: 28.0 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.26071428571428573 s^-1 mM^-1; assay condition: Recombinant Arabidopsis thaliana myrosinase expressed in Pichia pastoris with a 6xHis-tag; O-b-glucosidase activity assay (Methods 5.6): myrosinase was dissolved in 50 mM sodium citrate buffer, pH 4.5, and p-Nitrophenyl b-D-glucopyranoside (PNPG) was dissolved in 50 mM sodium citrate buffer, pH 4.5; the PNPG solution was incubated in an Eppendorf Thermomixer (37 °C, 350 rpm) for 5 min prior to the experiment; the reaction was terminated with 1 M sodium carbonate and the product read at 405 nm. Export row conditions: pH 4.5; 310.15 K.

normalized_value_unit_evidence: Table 2 row TGG4 | pNPG: kcat 7.3 s^-1 = 7.3 s^(-1) (no conversion needed); Km 28 mM = 28.0 mM (already in mM, no conversion needed); kcat/Km 0.26071428571428573 s^-1 mM^-1, the quotient of this row's own printed kcat and Km cells (7.3 / 28). In the PDF text extraction the micro sign of µmol renders as the letter l (`lmol`) and superscript minus-one exponents are flattened to a control character (U+0002) followed by 1, so the header cell `Kcat (s1)` is the paper's Kcat (s^-1) and the header cell `Kcat/Km (s1 mM1)` is the paper's Kcat/Km (s^-1 mM^-1). The printed Kcat/Km cell 0.26 is already in s^-1 mM^-1, the export's ratio unit.

raw_value_unit_evidence: Table 2 Kinetic parameters of recombinant TGG1, TGG4 and TGG5. | metric header row of Table 2 (as extracted): Enzyme Substrate Km (mM) Vmax (lmol min1 g1) Kcat (s1) Kcat/Km (s1 mM1) | row: TGG4 pNPG 28 ± 0 7.6 ± 0 7.3 ± 0 0.26 | cells read: Km = 28 mM; Vmax = 7.6 ± 0 lmol min1 mg1; Kcat = 7.3 s^-1; Kcat/Km = 0.26 s^-1 mM^-1. Table 2 footnote: The data represent the means and standard deviations of three (sinigrin) or two experiments (pNPG) with values calculated from Hanes plots. Sinigrin concentrations varied from 0.03 to 7.2 mM while p-nitrophenyl b-D-glucopyranoside (pNPG) concentrations varied from 1.5 to 99 mM depending on enzyme.

row_label: TGG4 | pNPG


column_label: Table label: Table 2 Kinetic parameters of recombinant TGG1, TGG4 and TGG5. Row: TGG5 | pNPG. Columns read: Km (mM) cell 80, Kcat (s^-1) cell 17, Kcat/Km (s^-1 mM^-1) cell 0.21. metric: kcat; raw value: 17; raw unit: s^-1; normalized value: 17.0 s^(-1); metric: Km; raw value: 80; raw unit: mM; normalized value: 80.0 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.2125 s^-1 mM^-1; assay condition: Recombinant Arabidopsis thaliana myrosinase expressed in Pichia pastoris with a 6xHis-tag; O-b-glucosidase activity assay (Methods 5.6): myrosinase was dissolved in 50 mM sodium citrate buffer, pH 4.5, and p-Nitrophenyl b-D-glucopyranoside (PNPG) was dissolved in 50 mM sodium citrate buffer, pH 4.5; the PNPG solution was incubated in an Eppendorf Thermomixer (37 °C, 350 rpm) for 5 min prior to the experiment; the reaction was terminated with 1 M sodium carbonate and the product read at 405 nm. Export row conditions: pH 4.5; 310.15 K.

normalized_value_unit_evidence: Table 2 row TGG5 | pNPG: kcat 17 s^-1 = 17.0 s^(-1) (no conversion needed); Km 80 mM = 80.0 mM (already in mM, no conversion needed); kcat/Km 0.2125 s^-1 mM^-1, the quotient of this row's own printed kcat and Km cells (17 / 80). In the PDF text extraction the micro sign of µmol renders as the letter l (`lmol`) and superscript minus-one exponents are flattened to a control character (U+0002) followed by 1, so the header cell `Kcat (s1)` is the paper's Kcat (s^-1) and the header cell `Kcat/Km (s1 mM1)` is the paper's Kcat/Km (s^-1 mM^-1). The printed Kcat/Km cell 0.21 is already in s^-1 mM^-1, the export's ratio unit.

raw_value_unit_evidence: Table 2 Kinetic parameters of recombinant TGG1, TGG4 and TGG5. | metric header row of Table 2 (as extracted): Enzyme Substrate Km (mM) Vmax (lmol min1 g1) Kcat (s1) Kcat/Km (s1 mM1) | row: TGG5 pNPG 80 ± 0 17.3 ± 0 17 ± 0 0.21 | cells read: Km = 80 mM; Vmax = 17.3 ± 0 lmol min1 mg1; Kcat = 17 s^-1; Kcat/Km = 0.21 s^-1 mM^-1. Table 2 footnote: The data represent the means and standard deviations of three (sinigrin) or two experiments (pNPG) with values calculated from Hanes plots. Sinigrin concentrations varied from 0.03 to 7.2 mM while p-nitrophenyl b-D-glucopyranoside (pNPG) concentrations varied from 1.5 to 99 mM depending on enzyme.

row_label: TGG5 | pNPG


substrate_name: Cellotetraose

assay_conditions_summary: pH 7.6; 310.15 K; buffer and pH optimum

column_label: Extended Data Table ED1; row Bo GH3B / cellotetraose; columns k cat (s -1 ), K m (mM), and same-row kcat/Km quotient; raw kcat 3.99 ± 0.31; raw Km 0.23 ± 0.060.

row_label: Bo GH3B / cellotetraose

substrate: Cellotetraose


substrate_name: cellohexaose

column_label: Extended Data Table ED1; row Bo GH3B / cellohexaose; columns k cat (s -1 ), K m (mM), and same-row kcat/Km quotient; raw kcat 4.91 ± 0.71; raw Km 0.47 ± 0.21.

raw_value_unit_evidence: kcat 4.91 ± 0.71 s^-1; Km 0.47 ± 0.21 mM; same-row kcat/Km derived as 4.91 / 0.47.

row_label: Bo GH3B / cellohexaose

substrate: cellohexaose


substrate_name: Cellobiose

column_label: Extended Data Table ED1; row Bo GH3B / cellobiose; columns k cat (s -1 ), K m (mM), and same-row kcat/Km quotient; raw kcat 1.57 ± 0.11; raw Km 0.68 ± 0.16.

raw_value_unit_evidence: kcat 1.57 ± 0.11 s^-1; Km 0.68 ± 0.16 mM; same-row kcat/Km derived as 1.57 / 0.68.

row_label: Bo GH3B / cellobiose

substrate: Cellobiose


sequence_source: UniProtKB reviewed accession Q9H227 FASTA; M172L reconstructed after direct residue check that canonical residue 172 is M.


sequence_source: UniProtKB reviewed accession Q9H227 FASTA; W345M reconstructed after direct residue check that canonical residue 345 is W.


substrate_name: Glucosylceramide

sequence_source: UniProtKB reviewed accession Q9H227 FASTA canonical sequence.

substrate: Glucosylceramide


sequence_source: UniProtKB:Q9H227 direct REST lookup on 2026-05-31; reviewed human GBA3 canonical sequence.


organism: Humicola insolens

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

sequence_source: Reconstructed from UniProtKB:A0A191KCR1 using PMID 27271847 Table 1/4: HiBgl3A Y509T; direct coordinate check maps mature Y509 to UniProt full position 529 after the 20-aa signal peptide.

sequence_variant_note: Mutation signature Y509T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: 4-nitrophenyl beta-D-glucopyranoside


sequence_source: Reconstructed from UniProtKB:A0A191KCR2 using PMID 27271847 Table 1/4: HiBgl3B I278F; direct residue matching maps article I278 to UniProt full position 311.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.


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


sequence_source: Reconstructed from UniProtKB:A0A191KCR2 using PMID 27271847 Table 1/4: HiBgl3B T484Y; direct residue matching maps article T484 to UniProt full position 517.

sequence_variant_note: Mutation signature T484Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: Reconstructed from UniProtKB:A0A191KCR2 using PMID 27271847 Table 1/4: HiBgl3B I48W/I278F/T484Y; direct residue matching maps article I48/I278/T484 to UniProt full positions 81/311/517.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +33, so it is treated as a source-provided variant sequence.


sequence_source: Reconstructed from UniProtKB:A0A191KCR2 using PMID 27271847 Table 1/4: HiBgl3B I48W; direct residue matching maps article I48 to UniProt full position 81.

sequence_variant_note: Mutation signature I48W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Oryza sativa

substrate_name: Dhurrin

sequence_source: UniProtKB reviewed accession Q75I93 canonical FASTA, direct lookup on 2026-05-31

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row Dhurrin: K m (mM) = 0.62; k cat (s-1) = 0.06; the efficiency column of the same row = 0.09.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.62 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.62 mM. kcat: printed Table 3 cell 0.06 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.06 s^(-1). kcat/Km: printed Table 3 cell 0.09 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.09 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row Dhurrin: Km = 0.62 mM; kcat = 0.06 s-1; printed kcat/Km = 0.09 s-1 . mM-1.

row_label: Table 3, substrate row Dhurrin

table_label: Table 3: Kinetic parameters of rice BGlu1 during the hydrolysis of pNP glycosides, alkyl glucosides and natural glucoside substrates (Biochem. J. 2004, 379:125-131)

substrate: Dhurrin


substrate_name: Gentiobiose

column_label: Table 1 prints the column heads Substrate | DP | K m (mM) | k cat (s-1) | k cat /K m (s-1 . mM-1). The cited cell set is Table 1, substrate row Gentiobiose: K m (mM) = 38.3; k cat (s-1) = 0.99; the efficiency column of the same row = 0.03.

normalized_value_unit_evidence: Km: printed Table 1 cell 38.3 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 38.3 mM. kcat: printed Table 1 cell 0.99 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.99 s^(-1). kcat/Km: printed Table 1 cell 0.03 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.03 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row Gentiobiose: Km = 38.3 mM; kcat = 0.99 s-1; printed kcat/Km = 0.03 s-1 . mM-1.

row_label: Table 1, substrate row Gentiobiose

table_label: Table 1: Kinetic parameters of rice BGlu1 during the hydrolysis of oligosaccharides (Biochem. J. 2004, 379:125-131)

substrate: Gentiobiose


substrate_name: (R)-Amygdalin

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row Amygdalin: K m (mM) = 8.20; k cat (s-1) = 0.44; the efficiency column of the same row = 0.05.

normalized_value_unit_evidence: Km: printed Table 3 cell 8.20 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 8.2 mM. kcat: printed Table 3 cell 0.44 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.44 s^(-1). kcat/Km: printed Table 3 cell 0.05 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.05 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row Amygdalin: Km = 8.20 mM; kcat = 0.44 s-1; printed kcat/Km = 0.05 s-1 . mM-1.

row_label: Table 3, substrate row Amygdalin

substrate: (R)-Amygdalin


substrate_name: Laminaritriose

column_label: Table 1 prints the column heads Substrate | DP | K m (mM) | k cat (s-1) | k cat /K m (s-1 . mM-1). The cited cell set is Table 1, substrate row Laminari-oligosaccharides DP 3: K m (mM) = 1.92; k cat (s-1) = 21.2; the efficiency column of the same row = 11.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.92 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 1.92 mM. kcat: printed Table 1 cell 21.2 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 21.2 s^(-1). kcat/Km: printed Table 1 cell 11.0 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 11.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row Laminari-oligosaccharides DP 3: Km = 1.92 mM; kcat = 21.2 s-1; printed kcat/Km = 11.0 s-1 . mM-1.

substrate: Laminaritriose


substrate_name: p-Nitrophenyl-beta-D-galactoside

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row pNP beta-D-galactoside: K m (mM) = 3.16; k cat (s-1) = 3.40; the efficiency column of the same row = 1.08.

normalized_value_unit_evidence: Km: printed Table 3 cell 3.16 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 3.16 mM. kcat: printed Table 3 cell 3.40 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 3.4 s^(-1). kcat/Km: printed Table 3 cell 1.08 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 1.08 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row pNP beta-D-galactoside: Km = 3.16 mM; kcat = 3.40 s-1; printed kcat/Km = 1.08 s-1 . mM-1.

substrate: p-Nitrophenyl-beta-D-galactoside


column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row Methylumberiferyl beta-D-glucoside: K m (mM) = 0.28; k cat (s-1) = 5.01; the efficiency column of the same row = 17.98.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.28 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.28 mM. kcat: printed Table 3 cell 5.01 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 5.01 s^(-1). kcat/Km: printed Table 3 cell 17.98 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 17.98 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row Methylumberiferyl beta-D-glucoside: Km = 0.28 mM; kcat = 5.01 s-1; printed kcat/Km = 17.98 s-1 . mM-1.


column_label: Table 1 prints the column heads Substrate | DP | K m (mM) | k cat (s-1) | k cat /K m (s-1 . mM-1). The cited cell set is Table 1, substrate row Sophorose: K m (mM) = 13.89; k cat (s-1) = 5.87; the efficiency column of the same row = 0.42.

normalized_value_unit_evidence: Km: printed Table 1 cell 13.89 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 13.89 mM. kcat: printed Table 1 cell 5.87 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 5.87 s^(-1). kcat/Km: printed Table 1 cell 0.42 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.42 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row Sophorose: Km = 13.89 mM; kcat = 5.87 s-1; printed kcat/Km = 0.42 s-1 . mM-1.

row_label: Table 1, substrate row Sophorose


substrate_name: Torvoside A

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row Torvoside A: K m (mM) = 0.99; k cat (s-1) = 0.67; the efficiency column of the same row = 0.68.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.99 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.99 mM. kcat: printed Table 3 cell 0.67 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.67 s^(-1). kcat/Km: printed Table 3 cell 0.68 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.68 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row Torvoside A: Km = 0.99 mM; kcat = 0.67 s-1; printed kcat/Km = 0.68 s-1 . mM-1.

row_label: Table 3, substrate row Torvoside A

substrate: Torvoside A


substrate_name: cellotriose

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q75I93 canonical sequence retrieved 2026-05-31; reconstructed L442R as canonical L470R and applied mutation signature L442R to reconstruct the assayed variant sequence.

substrate: cellotriose


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q75I93 canonical sequence retrieved 2026-05-31; reconstructed I179V as canonical I207V and applied mutation signature I179V with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q75I93 canonical sequence retrieved 2026-05-31; reconstructed L442R as canonical L470R


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q75I93 canonical sequence retrieved 2026-05-31; reconstructed N245V as canonical N273V and applied mutation signature N245V with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q75I93 canonical sequence retrieved 2026-05-31; reconstructed N190H as canonical N218H and applied mutation signature N190H with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q75I93 canonical sequence retrieved 2026-05-31; reconstructed N190H as canonical N218H


sequence_source: UniProtKB reviewed Q75I93 canonical sequence retrieved 2026-05-31; reconstructed I179V as canonical I207V


sequence_source: UniProtKB reviewed Q75I93 canonical sequence retrieved 2026-05-31; reconstructed N245V as canonical N273V


sequence_source: UniProtKB reviewed accession Q8L7J2; fetched 2026-05-31

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

column_label: Table II: Hydrolysis of glycosides and oligosaccharides by Os3BGlu6 (Plant Physiology 2009, volume 151, issue 1, starting page 47); printed column heads Substrate | nmol Glc min-1 mg-1 Protein | Percent Relative Activity | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table II, substrate row Sophorose; column Km (mM) = 9.8; column kcat (s-1) = 9.8; column kcat/Km (mM-1 s-1) = 0.96. captured primary segment: Table II, substrate row Sophorose | construct Os3BGlu6 | substrate Sophorose | condition 100 mM sodium acetate, pH 5.0, at 30°C | Km 9.8 mM | kcat 9.8 s^-1 | kcat/Km 0.96 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table II Km cell 9.8 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 9.8 mM. kcat: printed Table II kcat cell 9.8 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 9.8 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.96 mM^-1 s^-1; that printed unit is already the canonical efficiency unit, so no unit conversion applies and the paper value is 0.96 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 9.8 / 9.8 = 1.0 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.96 s^-1 mM^-1, which the authors fitted directly.

raw_value_unit_evidence: Table II, substrate row Sophorose: Km = 9.8 mM; kcat = 9.8 s^-1; printed kcat/Km = 0.96 mM^-1 s^-1.

row_label: Table II, substrate row Sophorose


column_label: Table II: Hydrolysis of glycosides and oligosaccharides by Os3BGlu6 (Plant Physiology 2009, volume 151, issue 1, starting page 47); printed column heads Substrate | nmol Glc min-1 mg-1 Protein | Percent Relative Activity | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table II, substrate row Cellobiose; column Km (mM) = 15.3; column kcat (s-1) = 0.13; column kcat/Km (mM-1 s-1) = 0.0085. captured primary segment: Table II, substrate row Cellobiose | construct Os3BGlu6 | substrate Cellobiose | condition 100 mM sodium acetate, pH 5.0, at 30°C | Km 15.3 mM | kcat 0.13 s^-1 | kcat/Km 0.0085 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table II Km cell 15.3 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 15.3 mM. kcat: printed Table II kcat cell 0.13 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 0.13 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0085 mM^-1 s^-1; that printed unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 0.0085 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 0.13 / 15.3 = 0.00849673202614379 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.0085 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Cellobiose: Km = 15.3 mM; kcat = 0.13 s^-1; printed kcat/Km = 0.0085 mM^-1 s^-1.

row_label: Table II, substrate row Cellobiose


column_label: Table II: Hydrolysis of glycosides and oligosaccharides by Os3BGlu6 (Plant Physiology 2009, volume 151, issue 1, starting page 47); printed column heads Substrate | nmol Glc min-1 mg-1 Protein | Percent Relative Activity | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table II, substrate row Laminaritriose; column Km (mM) = 8.7; column kcat (s-1) = 1.64; column kcat/Km (mM-1 s-1) = 0.18. captured primary segment: Table II, substrate row Laminaritriose | construct Os3BGlu6 | substrate Laminaritriose | condition 100 mM sodium acetate, pH 5.0, at 30°C | Km 8.7 mM | kcat 1.64 s^-1 | kcat/Km 0.18 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table II Km cell 8.7 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 8.7 mM. kcat: printed Table II kcat cell 1.64 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 1.64 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.18 mM^-1 s^-1; that printed unit is already the canonical efficiency unit, so no unit conversion applies and the paper value is 0.18 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 1.64 / 8.7 = 0.18850574712643678 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.18 s^-1 mM^-1, which the authors fitted directly.

raw_value_unit_evidence: Table II, substrate row Laminaritriose: Km = 8.7 mM; kcat = 1.64 s^-1; printed kcat/Km = 0.18 mM^-1 s^-1.

row_label: Table II, substrate row Laminaritriose


column_label: Table II: Hydrolysis of glycosides and oligosaccharides by Os3BGlu6 (Plant Physiology 2009, volume 151, issue 1, starting page 47); printed column heads Substrate | nmol Glc min-1 mg-1 Protein | Percent Relative Activity | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table II, substrate row Gentiobiose; column Km (mM) = 14.9; column kcat (s-1) = 0.17; column kcat/Km (mM-1 s-1) = 0.011. captured primary segment: Table II, substrate row Gentiobiose | construct Os3BGlu6 | substrate Gentiobiose | condition 100 mM sodium acetate, pH 5.0, at 30°C | Km 14.9 mM | kcat 0.17 s^-1 | kcat/Km 0.011 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table II Km cell 14.9 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 14.9 mM. kcat: printed Table II kcat cell 0.17 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 0.17 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.011 mM^-1 s^-1; that printed unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 0.011 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 0.17 / 14.9 = 0.011409395973154364 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.011 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Gentiobiose: Km = 14.9 mM; kcat = 0.17 s^-1; printed kcat/Km = 0.011 mM^-1 s^-1.

row_label: Table II, substrate row Gentiobiose


column_label: Table I: Kinetic parameters of Os3BGlu6 for the hydrolysis of pNP glycosides, oligosaccharides, and alkyl and natural glucosides (Plant Physiology 2009, volume 151, issue 1, starting page 47); printed column heads Substrate | nmol pNP min-1 mg-1 Protein | Percent Relative Activity | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table I, substrate row pNP-b-D-glucoside; column Km (mM) = 6.3; column kcat (s-1) = 38.9; column kcat/Km (mM-1 s-1) = 6.2. captured primary segment: Table I, substrate row pNP-b-D-glucoside | construct Os3BGlu6 | substrate pNP-b-D-glucoside | condition 100 mM sodium acetate, pH 5.0, at 30°C | Km 6.3 mM | kcat 38.9 s^-1 | kcat/Km 6.2 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 6.3 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 6.3 mM. kcat: printed Table I kcat cell 38.9 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 38.9 s^(-1). kcat/Km: printed Table I kcat/Km cell 6.2 mM^-1 s^-1; that printed unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 6.2 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 38.9 / 6.3 = 6.174603174603175 s^-1 mM^-1, against the printed catalytic-efficiency cell 6.2 s^-1 mM^-1.

raw_value_unit_evidence: Table I, substrate row pNP-b-D-glucoside: Km = 6.3 mM; kcat = 38.9 s^-1; printed kcat/Km = 6.2 mM^-1 s^-1.


column_label: Table I. Kinetic parameters of Os3BGlu6 for the hydrolysis of pNP glycosides, oligosaccharides, and alkyl and natural glucosides. Substrate row 'pNP-beta-D-fucoside'; column 'Km (mM)' = 0.50; column 'kcat (s-1)' = 33.5; column 'kcat/Km (mM^-1 s^-1)' = 67.

normalized_value_unit_evidence: Km: printed Table I cell 0.50 in the column headed Km over the small-capital unit mm, which decodes to mM; already in mM, no conversion; the exported value is 0.5 mM. kcat: printed Table I cell 33.5 s-1; 1 s-1 is 1 s^(-1), so the printed cell is 33.5 s^(-1); the exported value is 33.5. kcat/Km: printed Table I cell 67 in the column headed kcat/Km over the small-capital unit mm^-1 s^-1, which decodes to mM^-1 s^-1, so the printed cell is 67 s^(-1)*mM^(-1); the exported value is 67.0.

raw_value_unit_evidence: Table I, substrate row 'pNP-beta-D-fucoside': Km = 0.50 mM; kcat = 33.5 s-1; printed kcat/Km = 67 mM^-1 s^-1.

row_label: Table I, decoded plain-numeral transcription (section 2), substrate row 'pNP-beta-D-fucoside'


column_label: Table I: Kinetic parameters of Os3BGlu6 for the hydrolysis of pNP glycosides, oligosaccharides, and alkyl and natural glucosides (Plant Physiology 2009, volume 151, issue 1, starting page 47); printed column heads Substrate | nmol pNP min-1 mg-1 Protein | Percent Relative Activity | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table I, substrate row pNP-b-D-galactoside; column Km (mM) = 6.06; column kcat (s-1) = 9.8; column kcat/Km (mM-1 s-1) = 1.6. captured primary segment: Table I, substrate row pNP-b-D-galactoside | construct Os3BGlu6 | substrate pNP-b-D-galactoside | condition 100 mM sodium acetate, pH 5.0, at 30°C | Km 6.06 mM | kcat 9.8 s^-1 | kcat/Km 1.6 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 6.06 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 6.06 mM. kcat: printed Table I kcat cell 9.8 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 9.8 s^(-1). kcat/Km: printed Table I kcat/Km cell 1.6 mM^-1 s^-1; that printed unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 1.6 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 9.8 / 6.06 = 1.6171617161716174 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.6 s^-1 mM^-1.

raw_value_unit_evidence: Table I, substrate row pNP-b-D-galactoside: Km = 6.06 mM; kcat = 9.8 s^-1; printed kcat/Km = 1.6 mM^-1 s^-1.


substrate_name: sophorose

table_label: Table II: Hydrolysis of glycosides and oligosaccharides by Os3BGlu6 (Plant Physiology 2009, volume 151, issue 1, starting page 47); printed column heads Substrate | nmol Glc min-1 mg-1 Protein | Percent Relative Activity | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1)

substrate: sophorose


substrate_name: N-Octyl-beta-D-glucoside

sequence_source: UniProtKB REST direct lookup for Q8L7J2 on 2026-05-31

column_label: Table II: Hydrolysis of glycosides and oligosaccharides by Os3BGlu6 (Plant Physiology 2009, volume 151, issue 1, starting page 47); printed column heads Substrate | nmol Glc min-1 mg-1 Protein | Percent Relative Activity | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table II, substrate row n-Octyl-b-D-glucoside; column Km (mM) = 4.5; column kcat (s-1) = 12.4; column kcat/Km (mM-1 s-1) = 2.7. captured primary segment: Table II, substrate row n-Octyl-b-D-glucoside | construct Os3BGlu6 | substrate n-Octyl-b-D-glucoside | condition 100 mM sodium acetate, pH 5.0, at 30°C | Km 4.5 mM | kcat 12.4 s^-1 | kcat/Km 2.7 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table II Km cell 4.5 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 4.5 mM. kcat: printed Table II kcat cell 12.4 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 12.4 s^(-1). kcat/Km: printed Table II kcat/Km cell 2.7 mM^-1 s^-1; that printed unit is already the canonical efficiency unit, so no unit conversion applies and the paper value is 2.7 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 12.4 / 4.5 = 2.7555555555555555 s^-1 mM^-1, against the printed catalytic-efficiency cell 2.7 s^-1 mM^-1, which the authors fitted directly.

raw_value_unit_evidence: Table II, substrate row n-Octyl-b-D-glucoside: Km = 4.5 mM; kcat = 12.4 s^-1; printed kcat/Km = 2.7 mM^-1 s^-1.

substrate: N-Octyl-beta-D-glucoside


substrate_name: laminaribiose

column_label: Table II: Hydrolysis of glycosides and oligosaccharides by Os3BGlu6 (Plant Physiology 2009, volume 151, issue 1, starting page 47); printed column heads Substrate | nmol Glc min-1 mg-1 Protein | Percent Relative Activity | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table II, substrate row Laminaribiose; column Km (mM) = 3.6; column kcat (s-1) = 6.17; column kcat/Km (mM-1 s-1) = 1.7. captured primary segment: Table II, substrate row Laminaribiose | construct Os3BGlu6 | substrate Laminaribiose | condition 100 mM sodium acetate, pH 5.0, at 30°C | Km 3.6 mM | kcat 6.17 s^-1 | kcat/Km 1.7 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table II Km cell 3.6 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 3.6 mM. kcat: printed Table II kcat cell 6.17 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 6.17 s^(-1). kcat/Km: printed Table II kcat/Km cell 1.7 mM^-1 s^-1; that printed unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 1.7 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 6.17 / 3.6 = 1.7138888888888888 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.7 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Laminaribiose: Km = 3.6 mM; kcat = 6.17 s^-1; printed kcat/Km = 1.7 mM^-1 s^-1.

row_label: Table II, substrate row Laminaribiose

substrate: laminaribiose


substrate_name: N-Heptyl-beta-D-glucoside

column_label: Table II. Hydrolysis of glycosides and oligosaccharides by Os3BGlu6. Substrate row 'n-Heptyl-beta-D-glucoside'; column 'Km (mM)' = 5.0; column 'kcat (s-1)' = 4.25; column 'kcat/Km (mM^-1 s^-1)' = 0.85.

normalized_value_unit_evidence: Km: printed Table II cell 5.0 in the column headed Km over the small-capital unit mm, which decodes to mM; already in mM, no conversion; the exported value is 5.0 mM. kcat: printed Table II cell 4.25 s-1; 1 s-1 is 1 s^(-1), so the printed cell is 4.25 s^(-1); the exported value is 4.25. kcat/Km: printed Table II cell 0.85 in the column headed kcat/Km over the small-capital unit mm^-1 s^-1, which decodes to mM^-1 s^-1, so the printed cell is 0.85 s^(-1)*mM^(-1); the exported value is 0.85.

raw_value_unit_evidence: Table II, substrate row 'n-Heptyl-beta-D-glucoside': Km = 5.0 mM; kcat = 4.25 s-1; printed kcat/Km = 0.85 mM^-1 s^-1.

row_label: Table II, decoded plain-numeral transcription (section 3), substrate row 'n-Heptyl-beta-D-glucoside'

substrate: N-Heptyl-beta-D-glucoside


substrate_name: p-Nitrophenyl-beta-D-mannopyranoside

sequence_source: UniProtKB REST direct lookup for A3BMZ5 on 2026-05-31

substrate: p-Nitrophenyl-beta-D-mannopyranoside


sequence_source: UniProtKB REST direct lookup for Q75I94 on 2026-05-31


substrate_name: Cellotetraose

substrate: Cellotetraose


substrate_name: Cellopentaose

substrate: Cellopentaose


sequence_source: UniProtKB reviewed Q75I93 direct REST/FASTA lookup on 2026-05-31

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row n-Octyl beta-D-glucoside: K m (mM) = 0.63; k cat (s-1) = 0.78; the efficiency column of the same row = 1.25.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.63 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.63 mM. kcat: printed Table 3 cell 0.78 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.78 s^(-1). kcat/Km: printed Table 3 cell 1.25 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 1.25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row n-Octyl beta-D-glucoside: Km = 0.63 mM; kcat = 0.78 s-1; printed kcat/Km = 1.25 s-1 . mM-1.


column_label: Table 1 prints the column heads Substrate | DP | K m (mM) | k cat (s-1) | k cat /K m (s-1 . mM-1). The cited cell set is Table 1, substrate row Cello-oligosaccharides DP 4: K m (mM) = 0.28; k cat (s-1) = 17.34; the efficiency column of the same row = 61.1.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.28 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.28 mM. kcat: printed Table 1 cell 17.34 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 17.34 s^(-1). kcat/Km: printed Table 1 cell 61.1 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 61.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row Cello-oligosaccharides DP 4: Km = 0.28 mM; kcat = 17.34 s-1; printed kcat/Km = 61.1 s-1 . mM-1.


column_label: Table 1 prints the column heads Substrate | DP | K m (mM) | k cat (s-1) | k cat /K m (s-1 . mM-1). The cited cell set is Table 1, substrate row Cello-oligosaccharides DP 5: K m (mM) = 0.24; k cat (s-1) = 16.90; the efficiency column of the same row = 71.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.24 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.24 mM. kcat: printed Table 1 cell 16.90 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 16.9 s^(-1). kcat/Km: printed Table 1 cell 71.5 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 71.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row Cello-oligosaccharides DP 5: Km = 0.24 mM; kcat = 16.90 s-1; printed kcat/Km = 71.5 s-1 . mM-1.


column_label: Table 1 prints the column heads Substrate | DP | K m (mM) | k cat (s-1) | k cat /K m (s-1 . mM-1). The cited cell set is Table 1, substrate row Laminari-oligosaccharides DP 2: K m (mM) = 2.05; k cat (s-1) = 31.9; the efficiency column of the same row = 15.7.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.05 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 2.05 mM. kcat: printed Table 1 cell 31.9 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 31.9 s^(-1). kcat/Km: printed Table 1 cell 15.7 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 15.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row Laminari-oligosaccharides DP 2: Km = 2.05 mM; kcat = 31.9 s-1; printed kcat/Km = 15.7 s-1 . mM-1.


substrate_name: p-Nitrophenyl-beta-D-fucoside

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row pNP beta-D-fucoside: K m (mM) = 0.23; k cat (s-1) = 13.34; the efficiency column of the same row = 57.5.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.23 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.23 mM. kcat: printed Table 3 cell 13.34 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 13.34 s^(-1). kcat/Km: printed Table 3 cell 57.5 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 57.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row pNP beta-D-fucoside: Km = 0.23 mM; kcat = 13.34 s-1; printed kcat/Km = 57.5 s-1 . mM-1.

substrate: p-Nitrophenyl-beta-D-fucoside


substrate_name: p-Nitrophenyl-beta-D-mannoside

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row pNP beta-D-mannoside: K m (mM) = 1.27; k cat (s-1) = 1.32; the efficiency column of the same row = 1.01.

normalized_value_unit_evidence: Km: printed Table 3 cell 1.27 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 1.27 mM. kcat: printed Table 3 cell 1.32 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 1.32 s^(-1). kcat/Km: printed Table 3 cell 1.01 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 1.01 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row pNP beta-D-mannoside: Km = 1.27 mM; kcat = 1.32 s-1; printed kcat/Km = 1.01 s-1 . mM-1.

substrate: p-Nitrophenyl-beta-D-mannoside


substrate_name: o-Nitrophenyl-beta-D-glucopyranoside

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row o-Nitrophenyl beta-D-glucoside: K m (mM) = 0.43; k cat (s-1) = 15.95; the efficiency column of the same row = 37.6.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.43 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.43 mM. kcat: printed Table 3 cell 15.95 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 15.95 s^(-1). kcat/Km: printed Table 3 cell 37.6 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 37.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row o-Nitrophenyl beta-D-glucoside: Km = 0.43 mM; kcat = 15.95 s-1; printed kcat/Km = 37.6 s-1 . mM-1.

substrate: o-Nitrophenyl-beta-D-glucopyranoside


sequence_source: UniProtKB reviewed Q75I93, checked 2026-05-31 via UniProt REST; entry BGL07_ORYSJ / Beta-glucosidase 7, gene BGLU7 synonym BGLU1, organism Oryza sativa subsp. japonica, EC 3.2.1.21, sequence version 1.

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row n-Heptyl beta-D-glucoside: K m (mM) = 1.41; k cat (s-1) = 0.87; the efficiency column of the same row = 0.62.

normalized_value_unit_evidence: Km: printed Table 3 cell 1.41 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 1.41 mM. kcat: printed Table 3 cell 0.87 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.87 s^(-1). kcat/Km: printed Table 3 cell 0.62 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.62 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row n-Heptyl beta-D-glucoside: Km = 1.41 mM; kcat = 0.87 s-1; printed kcat/Km = 0.62 s-1 . mM-1.


substrate_name: cellohexaose

column_label: Table 1 prints the column heads Substrate | DP | K m (mM) | k cat (s-1) | k cat /K m (s-1 . mM-1). The cited cell set is Table 1, substrate row Cello-oligosaccharides DP 6: K m (mM) = 0.11; k cat (s-1) = 16.93; the efficiency column of the same row = 152.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.11 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.11 mM. kcat: printed Table 1 cell 16.93 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 16.93 s^(-1). kcat/Km: printed Table 1 cell 152.9 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 152.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row Cello-oligosaccharides DP 6: Km = 0.11 mM; kcat = 16.93 s-1; printed kcat/Km = 152.9 s-1 . mM-1.

substrate: cellohexaose


substrate_name: Cellobiose

assay_conditions_summary: pH 5; 303.15 K; buffer 50 mM sodium acetate

column_label: Table 1 (PDF page 2 of 7, journal page 126), substrate row `DP 2 (cellobiose)`: Km (mM) = 31.5; kcat (s^(-1)) = 1.52; kcat/Km (s^(-1)*mM^(-1)) = 0.05.

normalized_value_unit_evidence: kcat: printed cell 1.52 s^(-1) is already in the export unit -> 1.52 s^(-1); the exported value is 1.52 s^(-1). Km: printed cell 31.5 mM is already in the export unit -> 31.5 mM; the exported value is 22.0 mM. kcat/Km: the paper PRINTS the kcat/Km cell 0.05 s^(-1)*mM^(-1) for this substrate line, already in the export unit -> 0.05 s^(-1)*mM^(-1); the exported value is 0.06909090909090909 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `DP 2 (cellobiose)`

table_label: Table 1 (PDF page 2 of 7, journal page 126) 'Kinetic parameters of rice BGlu1 during the hydrolysis of oligosaccharides'

substrate: Cellobiose


substrate_name: p-Nitrophenyl-beta-D-glucoside

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row pNP beta-D-glucoside: K m (mM) = 0.23; k cat (s-1) = 7.93; the efficiency column of the same row = 34.7.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.23 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.23 mM. kcat: printed Table 3 cell 7.93 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 7.93 s^(-1). kcat/Km: printed Table 3 cell 34.7 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 34.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row pNP beta-D-glucoside: Km = 0.23 mM; kcat = 7.93 s-1; printed kcat/Km = 34.7 s-1 . mM-1.

substrate: p-Nitrophenyl-beta-D-glucoside


column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row Pyridoxine 5'-O-beta-D-glucoside: K m (mM) = 0.71; k cat (s-1) = 1.64; the efficiency column of the same row = 2.30.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.71 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 0.71 mM. kcat: printed Table 3 cell 1.64 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 1.64 s^(-1). kcat/Km: printed Table 3 cell 2.30 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 2.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row Pyridoxine 5'-O-beta-D-glucoside: Km = 0.71 mM; kcat = 1.64 s-1; printed kcat/Km = 2.30 s-1 . mM-1.


substrate_name: (R)-Prunasin

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row Prunasin: K m (mM) = 5.83; k cat (s-1) = 1.41; the efficiency column of the same row = 0.24.

normalized_value_unit_evidence: Km: printed Table 3 cell 5.83 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 5.83 mM. kcat: printed Table 3 cell 1.41 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 1.41 s^(-1). kcat/Km: printed Table 3 cell 0.24 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.24 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row Prunasin: Km = 5.83 mM; kcat = 1.41 s-1; printed kcat/Km = 0.24 s-1 . mM-1.

row_label: Table 3, substrate row Prunasin

substrate: (R)-Prunasin


substrate_name: p-Nitrophenyl-beta-D-xylopyranoside

column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row pNP beta-D-xyloside: K m (mM) = 1.29; k cat (s-1) = 1.14; the efficiency column of the same row = 0.88.

normalized_value_unit_evidence: Km: printed Table 3 cell 1.29 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 1.29 mM. kcat: printed Table 3 cell 1.14 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 1.14 s^(-1). kcat/Km: printed Table 3 cell 0.88 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.88 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row pNP beta-D-xyloside: Km = 1.29 mM; kcat = 1.14 s-1; printed kcat/Km = 0.88 s-1 . mM-1.

substrate: p-Nitrophenyl-beta-D-xylopyranoside


column_label: Table 3 prints the column heads Substrate | K m (mM) | k cat (s-1) | K cat /K m (s-1 . mM-1). The cited cell set is Table 3, substrate row pNP alpha-L-arabinoside: K m (mM) = 1.21; k cat (s-1) = 1.24; the efficiency column of the same row = 1.03.

normalized_value_unit_evidence: Km: printed Table 3 cell 1.21 in a column headed K m (mM); mM is already canonical, so no unit conversion applies and the paper value is 1.21 mM. kcat: printed Table 3 cell 1.24 in a column headed k cat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 1.24 s^(-1). kcat/Km: printed Table 3 cell 1.03 in a column headed with the unit s-1 . mM-1, which is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 1.03 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row pNP alpha-L-arabinoside: Km = 1.21 mM; kcat = 1.24 s-1; printed kcat/Km = 1.03 s-1 . mM-1.


organism: Listeria innocua Clip11262

substrate_name: Laminaripentaose

sequence_source: UniProtKB:Q92AS9 canonical sequence

substrate: Laminaripentaose


substrate_name: laminaritriose

substrate: laminaritriose


substrate_name: sophorose

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q92AS9 canonical sequence plus direct R572K reconstruction and applied mutation signature R572K to reconstruct the assayed variant sequence.

substrate: sophorose


substrate_name: sophoropentaose

substrate: sophoropentaose


substrate_name: laminaribiose

substrate: laminaribiose


substrate_name: laminaritetraose

substrate: laminaritetraose


substrate_name: sophorotriose

substrate: sophorotriose


organism: Phanerochaete chrysosporium

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


organism: Putranjiva roxburghii

substrate_name: 4-nitrophenyl beta-D-galactopyranoside

sequence_source: UniProtKB A0A023MIF8 direct accession lookup, retrieved 2026-05-31

substrate: 4-nitrophenyl beta-D-galactopyranoside


substrate_name: 4-nitrophenyl beta-D-fucopyranoside

substrate: 4-nitrophenyl beta-D-fucopyranoside


substrate_name: cellobiose

substrate: cellobiose


substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


organism: Rhizomucor miehei


substrate_name: Laminaran

substrate: Laminaran


substrate_name: cellotriose

substrate: cellotriose


substrate_name: cellotetraose

substrate: cellotetraose


organism: Saccharolobus solfataricus


organism: Pyrococcus furiosus

substrate_name: o-Nitrophenyl-beta-D-glucopyranoside

sequence_source: UniProtKB Q51723 canonical sequence fetched directly during review; E372A was reconstructed after confirming residue 372 is E.

sequence_variant_note: Mutation signature E372A matches the mutant residue at offset +0 and the reference residue at offset -7; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: o-Nitrophenyl-beta-D-glucopyranoside


sequence_source: UniProtKB Q51723 canonical sequence fetched directly during review.


sequence_source: UniProtKB E7FHY4 canonical sequence fetched directly during review.


organism: Rasamsonia emersonii

sequence_source: UniProtKB Q8TGI8 canonical sequence fetched directly during review.


substrate_name: gentobiose

sequence_source: UniProtKB A0A0B4RUW2 canonical sequence fetched directly during review.

substrate: gentobiose