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


enzyme_display_name: beta-glucosidase

organism: Bacteroides ovatus

substrate_name: Cellotetraose

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7.6; 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

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

data_origin: experimental

enzyme: beta-glucosidase

substrate: Cellotetraose

status: corrected

source: oed


substrate_name: cellohexaose

verification_status: verified

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

status: verified


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


verification_status: unverified

status: unverified


organism: Homo sapiens

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

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.

mutation_type: substitution


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

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

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

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


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

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


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

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


substrate_name: p-Nitrophenyl-beta-D-galactoside

substrate: p-Nitrophenyl-beta-D-galactoside


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.


kcat_over_km_display: Not reported

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


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


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.


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

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


sequence_source: UniProtKB Q97UH8 canonical FASTA, fetched 2026-05-31


substrate_name: N,N'-diacetyl-beta-chitobiose

substrate: N,N'-diacetyl-beta-chitobiose


substrate_name: 4-nitrophenyl beta-D-glucoside

substrate: 4-nitrophenyl beta-D-glucoside


organism: Secale cereale

substrate_name: p-Nitrophenyl-beta-D-glucoside

sequence_source: UniProtKB Q9FYS3 canonical FASTA with PMID 16751439 mutation signature reconstructed on full precursor coordinates, fetched 2026-05-31

sequence_variant_note: Mutation signature S465L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: p-Nitrophenyl-beta-D-glucoside


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature G464S/S465L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y378F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y378A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:Q9FYS3 exact accession lookup via UniProt REST

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


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 exact accession lookup via UniProt REST and applied mutation signature G464S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 exact accession lookup via UniProt REST and applied mutation signature G464F to reconstruct the assayed variant sequence.


organism: Sorghum bicolor

substrate_name: Dhurrin

sequence_source: UniProtKB:Q41290 exact accession lookup via UniProt REST

substrate: Dhurrin


enzyme_display_name: Beta-glucosidase 8

enzyme_name_source: UniProtKB exact accession follow-up

sequence_source: UniProtKB reviewed accession Q75I94 exact lookup; fetched 2026-05-31

enzyme: Beta-glucosidase 8


enzyme_display_name: Beta-glucosidase 26

sequence_source: UniProtKB reviewed accession A3BMZ5 exact lookup; fetched 2026-05-31

enzyme: Beta-glucosidase 26


substrate_name: cellohexaose

substrate: cellohexaose


substrate_name: Cellopentaose

substrate: Cellopentaose


enzyme_display_name: Beta-glucosidase 1A

substrate_name: Cellobiose

sequence_source: UniProtKB reviewed accession Q25BW5 exact lookup; fetched 2026-05-31

enzyme: Beta-glucosidase 1A

substrate: Cellobiose


enzyme_display_name: Beta-glucosidase 1B

sequence_source: UniProtKB reviewed accession Q25BW4 exact lookup; fetched 2026-05-31

enzyme: Beta-glucosidase 1B


organism: Thermofilum pendens

sequence_source: UniProtKB REST accession A1S0B1 checked 2026-05-31


organism: Thermoplasma acidophilum

sequence_source: UniProtKB REST accession Q9HIL6 checked 2026-05-31


organism: Halothermothrix orenii

substrate_name: lactose

sequence_variant_note: Resolved canonical sequence from UniProtKB:B8CYA8 direct accession check on 2026-05-31 and applied mutation signature Y296F to reconstruct the assayed variant sequence.

substrate: lactose


sequence_source: UniProtKB:B8CYA8 direct accession check on 2026-05-31


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8CYA8 direct accession check on 2026-05-31 and applied mutation signature N222F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8CYA8 direct accession check on 2026-05-31 and applied mutation signature N294T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8CYA8 direct accession check on 2026-05-31 and applied mutation signature F417S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8CYA8 direct accession check on 2026-05-31 and applied mutation signature F417Y to reconstruct the assayed variant sequence.


enzyme_display_name: Probable beta-galactosidase

sequence_source: UniProtKB TrEMBL accession Q9HIL6 exact lookup; fetched 2026-05-31

enzyme: Probable beta-galactosidase


enzyme_display_name: Beta-glycosidase

organism: Thermosphaera aggregans

substrate_name: 2-nitrophenyl beta-D-glucopyranoside

sequence_variant_note: Resolved canonical sequence from UniProtKB TrEMBL accession Q9YGA8 exact lookup; fetched 2026-05-31 plus direct residue substitution validation for N62Y/Q63K/L231F/V303A/E386G/A412V and applied mutation signature N62Y/Q63K/L231F/V303A/E386G/A412V to reconstruct the assayed variant sequence.

enzyme: Beta-glycosidase

substrate: 2-nitrophenyl beta-D-glucopyranoside


sequence_source: UniProtKB TrEMBL accession Q9YGA8 exact lookup; fetched 2026-05-31


enzyme_display_name: Beta-glucosidase

organism: Thermotoga neapolitana

sequence_variant_note: Resolved canonical sequence from UniProtKB TrEMBL accession Q0GC07 exact lookup; fetched 2026-05-31 plus direct residue substitution validation for D242G and applied mutation signature D242G to reconstruct the assayed variant sequence.

enzyme: Beta-glucosidase


sequence_source: UniProtKB TrEMBL accession Q0GC07 exact lookup; fetched 2026-05-31


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0GC07; direct REST lookup 2026-05-31 and applied mutation signature W243F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0GC07; direct REST lookup 2026-05-31 and applied mutation signature D58A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0GC07; direct REST lookup 2026-05-31 and applied mutation signature E458G to reconstruct the assayed variant sequence.


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

sequence_source: UniProtKB:B9K7M5; direct REST lookup 2026-05-31

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9K7M5; direct REST lookup 2026-05-31 and applied mutation signature F224I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9K7M5; direct REST lookup 2026-05-31 and applied mutation signature N220S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9K7M5; direct REST lookup 2026-05-31 and applied mutation signature N221F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:B9K7M5 direct REST check; UniProtKB B9K7M5 canonical residue N221 matched; variant reconstructed as N221S

sequence_variant_note: Mutation signature N221S matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:B9K7M5 direct REST check; UniProtKB B9K7M5 canonical residue N220 matched; variant reconstructed as N220F

sequence_variant_note: Mutation signature N220F matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:B9K7M5 direct REST check; wild-type canonical sequence from UniProtKB B9K7M5

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


sequence_source: UniProtKB:B9K7M5 direct REST check; UniProtKB B9K7M5 canonical residue F310 matched; variant reconstructed as F310E

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


sequence_source: UniProtKB:B9K7M5 direct REST check; UniProtKB B9K7M5 canonical residue F310 matched; variant reconstructed as F310L


sequence_source: UniProtKB:B9K7M5 direct REST check; UniProtKB B9K7M5 canonical residue W322 matched; variant reconstructed as W322A

sequence_variant_note: Mutation signature W322A matches the mutant residue at offset +0 and the reference residue at offset +9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:B9K7M5 direct REST check; UniProtKB B9K7M5 canonical residue N220 matched; variant reconstructed as N220S

sequence_variant_note: Mutation signature N220S matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: Thermotoga petrophila

substrate_name: 4-nitrophenyl beta-D-xylopyranoside

sequence_source: UniProtKB:A5IL97 direct lookup on 2026-05-31; live TrEMBL entry A5IL97_THEP1, beta-glucosidase EC 3.2.1.21, Thermotoga petrophila strain RKU-1, CRC64 97D590DA3C511738.

substrate: 4-nitrophenyl beta-D-xylopyranoside


substrate_name: 4-nitrophenyl beta-D-cellobioside

substrate: 4-nitrophenyl beta-D-cellobioside


substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


sequence_source: Candidate UniProtKB:D2C716 direct lookup on 2026-05-31 found a live TrEMBL GH3-domain protein from Thermotoga petrophila strain RKU-10, CRC64 CE85ED8A486BC09D, but it was not accepted as the EC 3.2.1.21 sequence.

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


substrate_name: 4-nitrophenyl beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


substrate_name: cellobiose

substrate: cellobiose


organism: Triticum aestivum

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


sequence_source: UniProtKB:Q1XH05 canonical sequence from direct REST lookup


organism: uncultured microorganism

substrate_name: 4-nitrophenyl beta-D-fucopyranoside

substrate: 4-nitrophenyl beta-D-fucopyranoside


sequence_source: UniProtKB:A0A1E1FFN6 canonical sequence from direct REST lookup


sequence_source: UniProtKB REST direct accession check:A5IL43


substrate_name: 4-nitrophenyl alpha-D-fucopyranoside

sequence_source: UniProtKB REST direct accession check:D2C716

substrate: 4-nitrophenyl alpha-D-fucopyranoside


organism: Thermus thermophilus

sequence_source: UniProtKB REST direct accession check:Q0GA07


sequence_source: UniProtKB REST direct accession check:Q1XH04


sequence_source: UniProtKB REST direct accession check:Q1XIR9


organism: Zea mays


substrate_name: o-Nitrophenyl-beta-D-glucopyranoside

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F193Y with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

substrate: o-Nitrophenyl-beta-D-glucopyranoside


organism: Oryza sativa

substrate_name: Laminaritriose

sequence_source: UniProtKB reviewed Q75I94/BGL08_ORYSJ direct REST lookup on 2026-05-31; sequence version 1; EC 3.2.1.21 and kinetics cite PMID 19766588.

substrate: Laminaritriose


sequence_source: UniProtKB reviewed A3BMZ5/BGL26_ORYSJ direct REST lookup on 2026-05-31; sequence version 1; EC 3.2.1.21 and kinetics cite PMID 19766588.


substrate_name: cellotriose

substrate: cellotriose


substrate_name: Cellotetraose

substrate: Cellotetraose


substrate_name: cellohexaose

substrate: cellohexaose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical FASTA; mutation reconstructed using RCSB/UniProt mature-chain offset +54 and applied mutation signature F198V with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.


substrate_name: Dhurrin

sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical FASTA; mutation reconstructed using RCSB/UniProt mature-chain offset +54 and applied mutation signature M263F with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.

substrate: Dhurrin


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical FASTA; mutation reconstructed using RCSB/UniProt mature-chain offset +54 and applied mutation signature F205L with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical FASTA; mutation reconstructed using RCSB/UniProt mature-chain offset +54 and applied mutation signature Y473F with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical FASTA; mutation reconstructed using RCSB/UniProt mature-chain offset +54 and applied mutation signature P377A with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical FASTA; mutation reconstructed using RCSB/UniProt mature-chain offset +54 and applied mutation signature D261N with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical FASTA; mutation reconstructed using RCSB/UniProt mature-chain offset +54 and applied mutation signature F198V/F205L/P377A with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P49235 canonical FASTA; mutation reconstructed using RCSB/UniProt mature-chain offset +54


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical sequence with F198V/F205L applied at mature-chain offset +54 and applied mutation signature F198V/F205L with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical sequence with M263F applied at mature-chain offset +54 and applied mutation signature M263F with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical sequence with F466S/A467S applied at mature-chain offset +54 and applied mutation signature F466S/A467S with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.


substrate_name: p-Nitrophenyl-beta-D-glucoside

sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical sequence with F466S applied at mature-chain offset +54 and applied mutation signature F466S with inferred residue-numbering offset +54 to reconstruct the assayed variant sequence.

substrate: p-Nitrophenyl-beta-D-glucoside


sequence_source: UniProtKB:P49235 canonical sequence with F466S applied at mature-chain offset +54


sequence_source: UniProtKB:P49235 canonical sequence with F198V/F205L applied at mature-chain offset +54


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 canonical precursor sequence; F193I reconstructed by mapping PMID 11706179 Zm-p60.1 mature residue F193 to precursor residue 252 after the paper's stated Zm-p60.1/ZmGlu1 five-residue mature N-terminus offset. and applied mutation signature F193I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P49235 canonical precursor sequence from direct REST/FASTA lookup.

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


sequence_source: UniProtKB:P49235 canonical precursor sequence; E186Q reconstructed by mapping PMID 11706179 Zm-p60.1 mature residue E186 to precursor residue 245 after the paper's stated Zm-p60.1/ZmGlu1 five-residue mature N-terminus offset.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.


sequence_source: UniProtKB:P49235 canonical precursor sequence; F198V/F205L reconstructed by mapping PMID 12684498 ZmGlu1 mature residues F198 and F205 to precursor residues 252 and 259 using the UniProt transit peptide ending at residue 54.

sequence_variant_note: Mutation signature F198V/F205L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P49235 canonical precursor sequence; Y473F reconstructed by mapping PMID 12684498 ZmGlu1 mature residue Y473 to precursor residue 527 using the UniProt transit peptide ending at residue 54.

sequence_variant_note: Mutation signature Y473F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P49235 canonical precursor sequence; F466S reconstructed by mapping PMID 12684498 ZmGlu1 mature residue F466 to precursor residue 520 using the UniProt transit peptide ending at residue 54.

sequence_variant_note: Mutation signature F466S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P49235 canonical precursor sequence; F205L reconstructed by mapping PMID 12684498 ZmGlu1 mature residue F205 to precursor residue 259 using the UniProt transit peptide ending at residue 54.

sequence_variant_note: Mutation signature F205L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Humicola insolens

sequence_source: UniProtKB:O93784 canonical sequence; A0A076JRL8 is a secondary accession; direct REST lookup 2026-05-31


organism: Lamium galeobdolon

sequence_source: UniProtKB:A0A3G1VCB1 canonical sequence; selected from source bundle by LgGLU1/Bglu1 paper-table identity; direct REST lookup 2026-05-31


substrate_name: oleuropein

substrate: oleuropein


organism: Listeria innocua Clip11262

sequence_source: UniProtKB:Q92AS9 canonical sequence; direct REST lookup 2026-05-31


substrate_name: sophorotetraose

substrate: sophorotetraose


substrate_name: laminaribiose

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q92AS9 canonical sequence with R572K reconstructed after confirming residue 572 is R; direct REST lookup 2026-05-31 and applied mutation signature R572K to reconstruct the assayed variant sequence.

substrate: laminaribiose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 REST check on 2026-05-31; canonical precursor sequence from reviewed Swiss-Prot entry HGGL1_MAIZE; mutation reconstructed with paper-to-UniProt residue offset +59 and applied mutation signature M258F with inferred residue-numbering offset +59 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 REST check on 2026-05-31; canonical precursor sequence from reviewed Swiss-Prot entry HGGL1_MAIZE; mutation reconstructed with paper-to-UniProt residue offset +59 and applied mutation signature E186D with inferred residue-numbering offset +59 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P49235 REST check on 2026-05-31; canonical precursor sequence from reviewed Swiss-Prot entry HGGL1_MAIZE


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 REST check on 2026-05-31; canonical precursor sequence from reviewed Swiss-Prot entry HGGL1_MAIZE; mutation reconstructed with paper-to-UniProt residue offset +59 and applied mutation signature E401Q with inferred residue-numbering offset +59 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 REST check on 2026-05-31; canonical precursor sequence from reviewed Swiss-Prot entry HGGL1_MAIZE; mutation reconstructed with paper-to-UniProt residue offset +59 and applied mutation signature M258V with inferred residue-numbering offset +59 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 REST check on 2026-05-31; canonical precursor sequence from reviewed Swiss-Prot entry HGGL1_MAIZE; mutation reconstructed with paper-to-UniProt residue offset +59 and applied mutation signature F193W with inferred residue-numbering offset +59 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 REST check on 2026-05-31; canonical precursor sequence from reviewed Swiss-Prot entry HGGL1_MAIZE; mutation reconstructed with paper-to-UniProt residue offset +59 and applied mutation signature E401D with inferred residue-numbering offset +59 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49235 REST check on 2026-05-31; canonical precursor sequence from reviewed Swiss-Prot entry HGGL1_MAIZE; mutation reconstructed with paper-to-UniProt residue offset +59 and applied mutation signature M258I with inferred residue-numbering offset +59 to reconstruct the assayed variant sequence.


enzyme_display_name: beta-galactosidase

organism: Arabidopsis thaliana

substrate_name: o-Nitrophenyl-beta-D-galactoside

sequence_source: canonical UniProtKB sequence from Q9SCV8

enzyme: beta-galactosidase

substrate: o-Nitrophenyl-beta-D-galactoside


substrate_name: p-Nitrophenyl-beta-D-galactoside

substrate: p-Nitrophenyl-beta-D-galactoside


organism: Arthrobacter sp.

substrate_name: lactose

sequence_source: canonical UniProtKB sequence from Q7WTU5

substrate: lactose


organism: Aspergillus oryzae

substrate_name: 2-nitrophenyl beta-D-galactoside

sequence_source: canonical UniProtKB sequence from Q2UCU3

substrate: 2-nitrophenyl beta-D-galactoside


sequence_source: UniProtKB Q2UCU3 canonical sequence with W806F reconstructed after confirming W at residue 806

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


substrate_name: 4-nitrophenyl beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


organism: Escherichia coli

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


sequence_source: UniProt REST FASTA P00722; >sp|P00722|BGAL_ECOLI Beta-galactosidase OS=Escherichia coli (strain K12) OX=83333 GN=lacZ PE=1 SV=2


sequence_source: UniProt REST FASTA P06864; >sp|P06864|BGA2_ECOLI Evolved beta-galactosidase subunit alpha OS=Escherichia coli (strain K12) OX=83333 GN=ebgA PE=1 SV=4


sequence_source: UniProtKB P00722 checked directly; variant sequence not populated because H540 does not map directly to residue 540 in the current canonical sequence.


substrate_name: p-Nitrophenyl-beta-D-fucopyranoside

substrate: p-Nitrophenyl-beta-D-fucopyranoside


sequence_source: UniProtKB P00722 canonical sequence fetched from rest.uniprot.org on 2026-05-31; accession organism and EC matched the selected record.


substrate_name: Phenyl-beta-D-galactopyranoside

sequence_source: UniProtKB:P06864 direct REST/FASTA lookup on 2026-05-31

substrate: Phenyl-beta-D-galactopyranoside


sequence_source: UniProtKB:P00722 direct REST/FASTA lookup on 2026-05-31

assay_conditions_summary: pH 7; 298.15 K; buffer 30 mM TES

column_label: Table I (Kinetic and energetic values for the action of the wild type and the substituted enzymes on galactosyl substrates and on substrates that are similar to galactose but do not have C6 hydroxyl groups), PNPA substrate block, enzyme column 'WILD'; metric row 'kcat (s^-1)' = 211; metric row 'Km (mM)' = 11.6; metric row 'kcat/Km (s^-1 mM^-1)' = 18.2; metric row 'DDGS (kJ/mol)' prints no value in the WILD column.

normalized_value_unit_evidence: kcat: printed Table I cell 211 in the PNPA block, column 'WILD', under the metric row head kcat (s^-1); the row is already per second, so no conversion applies and the paper value is 211.0 s^(-1). Km: printed Table I cell 11.6 under the metric row head Km (mM); the row is already in mM, so no conversion applies and the paper value is 11.6 mM. kcat/Km: printed Table I cell 18.2 under the metric row head kcat/Km (s^-1 mM^-1); the row is already in s^-1 mM^-1, so no conversion applies and the paper value is 18.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, PNPA substrate block, enzyme column 'WILD': kcat = 211 s^-1; Km = 11.6 mM; printed kcat/Km = 18.2 s^-1 mM^-1.

row_label: Table I, PNPA block, WILD column

table_label: Table I: Kinetic and energetic values for the action of the wild type and the substituted enzymes on galactosyl substrates and on substrates that are similar to galactose but do not have C6 hydroxyl groups (J. Biol. Chem. 1996, 271(24):14296-14301)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00722 and applied mutation signature H540F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic and energetic values for the action of the wild type and the substituted enzymes on galactosyl substrates and on substrates that are similar to galactose but do not have C6 hydroxyl groups), PNPG substrate block, enzyme column 'H540F'; metric row 'kcat (s^-1)' = 0.1; metric row 'Km (mM)' = 0.45; metric row 'kcat/Km (s^-1 mM^-1)' = 0.22; metric row 'DDGS (kJ/mol)' = -22.8.

normalized_value_unit_evidence: kcat: printed Table I cell 0.1 in the PNPG block, column 'H540F', under the metric row head kcat (s^-1); the row is already per second, so no conversion applies and the paper value is 0.1 s^(-1). Km: printed Table I cell 0.45 under the metric row head Km (mM); the row is already in mM, so no conversion applies and the paper value is 0.45 mM. kcat/Km: printed Table I cell 0.22 under the metric row head kcat/Km (s^-1 mM^-1); the row is already in s^-1 mM^-1, so no conversion applies and the paper value is 0.22 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, PNPG substrate block, enzyme column 'H540F': kcat = 0.1 s^-1; Km = 0.45 mM; printed kcat/Km = 0.22 s^-1 mM^-1.

row_label: Table I, PNPG block, H540F column


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

column_label: Table I (Kinetic and energetic values for the action of the wild type and the substituted enzymes on galactosyl substrates and on substrates that are similar to galactose but do not have C6 hydroxyl groups), PNPF substrate block, enzyme column 'WILD'; metric row 'kcat (s^-1)' = 123.4; metric row 'Km (mM)' = 16.9; metric row 'kcat/Km (s^-1 mM^-1)' = 7.3; metric row 'DDGS (kJ/mol)' prints no value in the WILD column.

normalized_value_unit_evidence: kcat: printed Table I cell 123.4 in the PNPF block, column 'WILD', under the metric row head kcat (s^-1); the row is already per second, so no conversion applies and the paper value is 123.4 s^(-1). Km: printed Table I cell 16.9 under the metric row head Km (mM); the row is already in mM, so no conversion applies and the paper value is 16.9 mM. kcat/Km: printed Table I cell 7.3 under the metric row head kcat/Km (s^-1 mM^-1); the row is already in s^-1 mM^-1, so no conversion applies and the paper value is 7.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, PNPF substrate block, enzyme column 'WILD': kcat = 123.4 s^-1; Km = 16.9 mM; printed kcat/Km = 7.3 s^-1 mM^-1.

row_label: Table I, PNPF block, WILD column


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 direct REST/FASTA lookup on 2026-05-31 and applied mutation signature H540N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 direct REST/FASTA lookup on 2026-05-31 and applied mutation signature H540E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


column_label: Table I (Kinetic and energetic values for the action of the wild type and the substituted enzymes on galactosyl substrates and on substrates that are similar to galactose but do not have C6 hydroxyl groups), PNPG substrate block, enzyme column 'WILD'; metric row 'kcat (s^-1)' = 90; metric row 'Km (mM)' = 0.041; metric row 'kcat/Km (s^-1 mM^-1)' = 2200; metric row 'DDGS (kJ/mol)' prints no value in the WILD column.

normalized_value_unit_evidence: kcat: printed Table I cell 90 in the PNPG block, column 'WILD', under the metric row head kcat (s^-1); the row is already per second, so no conversion applies and the paper value is 90.0 s^(-1). Km: printed Table I cell 0.041 under the metric row head Km (mM); the row is already in mM, so no conversion applies and the paper value is 0.041 mM. kcat/Km: printed Table I cell 2200 under the metric row head kcat/Km (s^-1 mM^-1); the row is already in s^-1 mM^-1, so no conversion applies and the paper value is 2200.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, PNPG substrate block, enzyme column 'WILD': kcat = 90 s^-1; Km = 0.041 mM; printed kcat/Km = 2200 s^-1 mM^-1.

row_label: Table I, PNPG block, WILD column


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00722 and applied mutation signature H540N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic and energetic values for the action of the wild type and the substituted enzymes on galactosyl substrates and on substrates that are similar to galactose but do not have C6 hydroxyl groups), PNPG substrate block, enzyme column 'H540N'; metric row 'kcat (s^-1)' = 0.3; metric row 'Km (mM)' = 0.069; metric row 'kcat/Km (s^-1 mM^-1)' = 4.4; metric row 'DDGS (kJ/mol)' = -15.4.

normalized_value_unit_evidence: kcat: printed Table I cell 0.3 in the PNPG block, column 'H540N', under the metric row head kcat (s^-1); the row is already per second, so no conversion applies and the paper value is 0.3 s^(-1). Km: printed Table I cell 0.069 under the metric row head Km (mM); the row is already in mM, so no conversion applies and the paper value is 0.069 mM. kcat/Km: printed Table I cell 4.4 under the metric row head kcat/Km (s^-1 mM^-1); the row is already in s^-1 mM^-1, so no conversion applies and the paper value is 4.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, PNPG substrate block, enzyme column 'H540N': kcat = 0.3 s^-1; Km = 0.069 mM; printed kcat/Km = 4.4 s^-1 mM^-1.

row_label: Table I, PNPG block, H540N column


sequence_variant_note: Resolved canonical sequence from UniProt:P00722 FASTA; H391K reconstructed from PMID 11310566 using mature-chain offset +1 and applied mutation signature H391K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P00722 FASTA; W999L reconstructed from PMID 12578395 using mature-chain offset +1 and applied mutation signature W999L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProt:P00722 FASTA; W999L reconstructed from PMID 12578395 using mature-chain offset +1


sequence_variant_note: Resolved canonical sequence from UniProt:P00722 FASTA; W999G reconstructed from PMID 12578395 using mature-chain offset +1 and applied mutation signature W999G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P00722 FASTA; W999Y reconstructed from PMID 12578395 using mature-chain offset +1 and applied mutation signature W999Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProt:P00722 FASTA; W999Y reconstructed from PMID 12578395 using mature-chain offset +1


sequence_source: UniProt:P00722 FASTA; W999G reconstructed from PMID 12578395 using mature-chain offset +1


sequence_variant_note: Resolved canonical sequence from UniProt:P00722 FASTA; W999F reconstructed from PMID 12578395 using mature-chain offset +1 and applied mutation signature W999F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 REST canonical sequence; mutation applied with inferred residue-numbering offset +1 and applied mutation signature G794A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00722 REST canonical sequence; mutation applied with inferred residue-numbering offset +1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 REST canonical sequence; mutation applied with inferred residue-numbering offset +1 and applied mutation signature E461H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00722 and applied mutation signature E461D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer 30 mM

column_label: Table I: Kinetic constants and rate constants obtained for the beta-galactosidases with ONPG and PNPG as substrates (Journal of Biological Chemistry 1990, volume 265, number 10, pages 5512-5518); the PNPG substrate block; column head 'ASD' is the Asp substitution, the E461D-beta-galactosidase enzyme; the k_cat stub of that block, rendered 'k,, (s-l)', holds 0.007 in that column; the 'Km (mM)' stub holds 0.011 in that column; the block carries no kcat/Km stub

normalized_value_unit_evidence: kcat: printed Table I cell 0.007 s^-1; the cell is already in s^-1, so no unit conversion applies; the exported value is 0.007 s^(-1). Km: printed Table I cell 0.011 mM; the cell is already in mM, so no unit conversion applies; the exported value is 0.011 mM. kcat/Km: this paper prints no efficiency cell anywhere, so the catalog value is typed as the same-measurement quotient of the two printed cells of this one column, 0.007 / 0.011 = 0.6363636363636365 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Table I, PNPG block, column headed ASD (Asp), the E461D-beta-galactosidase enzyme: the k_cat stub prints 0.007 with the block unit s^-1, and the Km stub prints 0.011 with the block unit mM. Table I prints no catalytic-efficiency column.

row_label: Table I, PNPG substrate block, the k_cat and Km stubs read across to the column headed ASD, which is the Asp substitution, the E461D-beta-galactosidase enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00722 and applied mutation signature E461K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table I: Kinetic constants and rate constants obtained for the beta-galactosidases with ONPG and PNPG as substrates (Journal of Biological Chemistry 1990, volume 265, number 10, pages 5512-5518); the PNPG substrate block; column head 'LYS' is the Lys substitution, the E461K-beta-galactosidase enzyme; the k_cat stub of that block, rendered 'k,, (s-l)', holds 0.24 in that column; the 'Km (mM)' stub holds 0.008 in that column; the block carries no kcat/Km stub

normalized_value_unit_evidence: kcat: printed Table I cell 0.24 s^-1; the cell is already in s^-1, so no unit conversion applies; the exported value is 0.24 s^(-1). Km: printed Table I cell 0.008 mM; the cell is already in mM, so no unit conversion applies; the exported value is 0.008 mM. kcat/Km: this paper prints no efficiency cell anywhere, so the catalog value is typed as the same-measurement quotient of the two printed cells of this one column, 0.24 / 0.008 = 30.0 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Table I, PNPG block, column headed LYS (Lys), the E461K-beta-galactosidase enzyme: the k_cat stub prints 0.24 with the block unit s^-1, and the Km stub prints 0.008 with the block unit mM. Table I prints no catalytic-efficiency column.

row_label: Table I, PNPG substrate block, the k_cat and Km stubs read across to the column headed LYS, which is the Lys substitution, the E461K-beta-galactosidase enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 REST canonical sequence; mutation applied with inferred residue-numbering offset +1 and applied mutation signature E461G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00722 and applied mutation signature E461Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table I: Kinetic constants and rate constants obtained for the beta-galactosidases with ONPG and PNPG as substrates (Journal of Biological Chemistry 1990, volume 265, number 10, pages 5512-5518); the PNPG substrate block; column head 'Gin' is the Gln substitution, the E461Q-beta-galactosidase enzyme; the k_cat stub of that block, rendered 'k,, (s-l)', holds 0.34 in that column; the 'Km (mM)' stub holds 0.003 in that column; the block carries no kcat/Km stub

normalized_value_unit_evidence: kcat: printed Table I cell 0.34 s^-1; the cell is already in s^-1, so no unit conversion applies; the exported value is 0.34 s^(-1). Km: printed Table I cell 0.003 mM; the cell is already in mM, so no unit conversion applies; the exported value is 0.003 mM. kcat/Km: this paper prints no efficiency cell anywhere, so the catalog value is typed as the same-measurement quotient of the two printed cells of this one column, 0.34 / 0.003 = 113.33333333333334 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Table I, PNPG block, column headed Gin (Gln), the E461Q-beta-galactosidase enzyme: the k_cat stub prints 0.34 with the block unit s^-1, and the Km stub prints 0.003 with the block unit mM. Table I prints no catalytic-efficiency column.

row_label: Table I, PNPG substrate block, the k_cat and Km stubs read across to the column headed Gin, which is the Gln substitution, the E461Q-beta-galactosidase enzyme


sequence_source: UniProtKB:A0A1E1FFN6 direct REST/FASTA lookup on 2026-05-31


substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


substrate_name: 4-nitrophenyl beta-D-fucopyranoside

substrate: 4-nitrophenyl beta-D-fucopyranoside


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


organism: Lactobacillus delbrueckii

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


sequence_source: UniProtKB:Q1G9Z4 plus E491A reconstruction from checked residue 491

sequence_variant_note: Mutation signature E491A 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.


organism: Putranjiva roxburghii

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


substrate_name: cellobiose

substrate: cellobiose


sequence_source: UniProtKB:A0A023MIF8 direct FASTA lookup


organism: Saccharolobus solfataricus

sequence_source: UniProtKB:P22498 direct FASTA lookup


sequence_source: UniProtKB:P22498 canonical sequence with F441Y substitution reconstructed after direct residue check

sequence_variant_note: Mutation signature F441Y matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P22498 canonical sequence with F359Q substitution reconstructed after direct residue check

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


organism: Sulfolobus solfataricus

substrate_name: Methyl beta-D-galactoside

column_label: Table 3, row Methyl beta-D-galactopyranoside: Km cell 23 under mM; kcat cell 242 under min^-1; kcat/Km cell 10.5 under min^-1 mM^-1.

raw_value_unit_evidence: Literal retained Table 3 cells: Km 23 mM; kcat 242 min^-1; kcat/Km 10.5 min^-1 mM^-1.

row_label: Methyl beta-D-galactopyranoside

table_label: Table 3

substrate: Methyl beta-D-galactoside


column_label: Table 3, row P-NpGal: Km cell 0.225 under mM; kcat cell 5700 under min^-1; kcat/Km cell 25333 under min^-1 mM^-1.

raw_value_unit_evidence: Literal retained Table 3 cells: Km 0.225 mM; kcat 5700 min^-1; kcat/Km 25333 min^-1 mM^-1.

row_label: P-NpGal


substrate_name: alpha-Lactose

column_label: Table 3, row alpha-Lactose: Km cell 13 under mM; kcat cell 114 under min^-1; kcat/Km cell 8.7 under min^-1 mM^-1.

raw_value_unit_evidence: Literal retained Table 3 cells: Km 13 mM; kcat 114 min^-1; kcat/Km 8.7 min^-1 mM^-1.

row_label: alpha-Lactose

substrate: alpha-Lactose


column_label: Table 3, row Phenyl beta-D-galactopyranoside: Km cell 2.6 under mM; kcat cell 166 under min^-1; kcat/Km cell 63.8 under min^-1 mM^-1.

raw_value_unit_evidence: Literal retained Table 3 cells: Km 2.6 mM; kcat 166 min^-1; kcat/Km 63.8 min^-1 mM^-1.

row_label: Phenyl beta-D-galactopyranoside


sequence_variant_note: Resolved canonical sequence from UniProtKB P00722 REST canonical sequence; selected mutation reconstructed with residue-numbering offset +1 and applied mutation signature H540E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00722 REST canonical sequence; selected mutation reconstructed with residue-numbering offset +1 and applied mutation signature H357F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P00722 REST canonical sequence; selected mutation reconstructed with residue-numbering offset +1


sequence_variant_note: Resolved canonical sequence from UniProtKB P00722 REST canonical sequence; selected mutation reconstructed with residue-numbering offset +1 and applied mutation signature H357L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00722 REST canonical sequence; selected mutation reconstructed with residue-numbering offset +1 and applied mutation signature H357D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00722 REST canonical sequence; selected mutation reconstructed with residue-numbering offset +1 and applied mutation signature H357N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

sequence_source: UniProtKB O31529 canonical reviewed FASTA; direct REST TSV reports Beta-galactosidase YesZ, Bacillus subtilis strain 168, EC 3.2.1.23.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB O31529 canonical reviewed FASTA by applying E145A after direct residue check showed O31529 residue 145 is E; PMID 17485082 names the E145A YesZ mutant. and applied mutation signature E145A to reconstruct the assayed variant sequence.


organism: Bacteroides ovatus

sequence_source: UniProtKB A7LXS9 canonical reviewed FASTA; direct REST TSV reports Beta-galactosidase BoGH2A, Bacteroides ovatus strain ATCC 8483, EC 3.2.1.23.


sequence_source: UniProtKB P00722 was checked directly, but the row-specific variant sequence was not accepted because canonical P00722 residue 391 is S while residue 392 is H; the cited His-391 mutation needs explicit numbering/construct validation before reconstruction.


enzyme_display_name: laccase

organism: Bacillus pumilus

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB A0A0G2QNK1 canonical FASTA fetched 2026-05-31 plus selected mutation_signature and applied mutation signature L386W/G417L/G57L to reconstruct the assayed variant sequence.

enzyme: laccase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0G2QNK1 and applied mutation signature G417L to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters for the wild-type CotA and mutants using ABTS as substrate (Appl Microbiol Biotechnol 2017, 101:1935-1944); printed column heads Enzyme | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 1, body row 'G417L'; column kcat (s-1) = 51.67; column Km (mM) = 0.127; column kcat/Km (s-1 mM-1) = 406.82. captured primary segment: G417L | kcat 51.67 s-1 | Km 0.127 mM | kcat/Km 406.82 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 51.67 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 51.67 s^(-1). Km: printed Table 1 cell 0.127 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.127 mM. kcat/Km: printed Table 1 cell 406.82 in a column headed kcat/Km (s-1 mM-1); 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 406.82 s^(-1)*mM^(-1). The exported values are kcat 51.67 s^(-1) and Km 0.127 mM and kcat_over_km 406.85039370078744 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'G417L': kcat = 51.67 s-1; Km = 0.127 mM; printed kcat/Km = 406.82 s-1 mM-1.

row_label: Table 1, body row 'G417L'


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB A0A0G2QNK1 canonical FASTA fetched 2026-05-31 plus selected mutation_signature and applied mutation signature L386W/G417L/D152Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB A0A0G2QNK1 canonical FASTA fetched 2026-05-31 plus selected mutation_signature and applied mutation signature L386W/G417L/D152F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB A0A0G2QNK1 canonical FASTA fetched 2026-05-31 plus selected mutation_signature and applied mutation signature L386W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB A0A0G2QNK1 canonical FASTA fetched 2026-05-31 plus selected mutation_signature and applied mutation signature L386W/G417L/D195F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB A0A0G2QNK1 canonical FASTA fetched 2026-05-31 plus selected mutation_signature and applied mutation signature L386W/G417L/D195W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB A0A0G2QNK1 canonical FASTA fetched 2026-05-31 plus selected mutation_signature and applied mutation signature L386W/G417L/G57W to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A0G2QNK1; reconstructed_variant_sequence; direct lookup 2026-05-31


substrate_name: guaiacol

sequence_source: UniProtKB:K4PL78; reconstructed_variant_sequence; direct lookup 2026-05-31

substrate: guaiacol


sequence_source: UniProtKB:K4PL78; canonical_wild_type_sequence; direct lookup 2026-05-31

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


sequence_variant_note: Mutation signature L386Q/G417I matches the mutant residue at offset +0 and the reference residue at offset -35; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


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


organism: Bacillus licheniformis

substrate_name: Syringaldazine

sequence_source: UniProtKB REST A0A0A6ZHX8 FASTA fetched 2026-05-31

substrate: Syringaldazine


sequence_source: UniProtKB REST H8WGE4 FASTA fetched 2026-05-31; mutation_signature D500G applied after residue check


sequence_source: UniProtKB REST I3XLC2 FASTA fetched 2026-05-31


substrate_name: Guaiacol

sequence_source: UniProtKB REST I3RYX9 FASTA fetched 2026-05-31

substrate: Guaiacol