column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row 3M; column KM (uM) = 3.12 ± 0.12; column kcat (s^-1) = 253.9 ± 3.61; column Vmax (nM/min) = 25.39; column kcat/Km (s^-1 uM^-1) = 81.37 ± 3.34.

normalized_value_unit_evidence: kcat: printed Table 2 cell 253.9 s^-1; already in s^-1, so no conversion is applied; the exported value is 253.9 s^(-1). Km: printed Table 2 cell 3.12 uM; 3.12 / 1000 = 0.00312 mM; the exported value is 0.00312 mM. kcat/Km: printed Table 2 cell 81.37 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 81.37 * 1000 = 81370.0 s^-1 mM^-1; the exported value is 81378.20512820513.

raw_value_unit_evidence: Table 2, MTA block, enzyme row 3M: KM = 3.12 ± 0.12 uM; kcat = 253.9 ± 3.61 s^-1; printed kcat/Km = 81.37 ± 3.34 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row 3M


enzyme_display_name: S-methyl-5'-thioadenosine phosphorylase

organism: Schistosoma mansoni

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I0B503 and applied mutation signature S12T/N87T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), 2'deoxy adenosine block, enzyme row 2M; column KM (uM) = 3.89 ± 0.16; column kcat (s^-1) = 372.8 ± 6.31; column Vmax (nM/min) = 37.28; column kcat/Km (s^-1 uM^-1) = 95.83 ± 4.26.

normalized_value_unit_evidence: kcat: printed Table 2 cell 372.8 s^-1; already in s^-1, so no conversion is applied; the exported value is 372.8 s^(-1). Km: printed Table 2 cell 3.89 uM; 3.89 / 1000 = 0.00389 mM; the exported value is 0.00389 mM. kcat/Km: printed Table 2 cell 95.83 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 95.83 * 1000 = 95830.0 s^-1 mM^-1; the exported value is 95835.47557840617.

raw_value_unit_evidence: Table 2, 2'deoxy adenosine block, enzyme row 2M: KM = 3.89 ± 0.16 uM; kcat = 372.8 ± 6.31 s^-1; printed kcat/Km = 95.83 ± 4.26 s^-1 uM^-1.

table_label: Table 2: Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis (PLoS Negl Trop Dis 2016, 10(12): e0005178)

data_origin: experimental

enzyme: S-methyl-5'-thioadenosine phosphorylase

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I0B503 and applied mutation signature Q289L to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row Q289L; column KM (uM) = 2.49 ± 0.1; column kcat (s^-1) = 241.6 ± 3.91; column Vmax (nM/min) = 72.48; column kcat/Km (s^-1 uM^-1) = 97.02 ± 4.20.

normalized_value_unit_evidence: kcat: printed Table 2 cell 241.6 s^-1; already in s^-1, so no conversion is applied; the exported value is 241.6 s^(-1). Km: printed Table 2 cell 2.49 uM; 2.49 / 1000 = 0.00249 mM; the exported value is 0.00249 mM. kcat/Km: printed Table 2 cell 97.02 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 97.02 * 1000 = 97020.0 s^-1 mM^-1; the exported value is 97028.1124497992.

raw_value_unit_evidence: Table 2, MTA block, enzyme row Q289L: KM = 2.49 ± 0.1 uM; kcat = 241.6 ± 3.91 s^-1; printed kcat/Km = 97.02 ± 4.20 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row Q289L


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row 2M; column KM (uM) = 2.12 ± 0.08; column kcat (s^-1) = 416.2 ± 7.20; column Vmax (nM/min) = 41.62; column kcat/Km (s^-1 uM^-1) = 196.32 ± 8.15.

normalized_value_unit_evidence: kcat: printed Table 2 cell 416.2 s^-1; already in s^-1, so no conversion is applied; the exported value is 416.2 s^(-1). Km: printed Table 2 cell 2.12 uM; 2.12 / 1000 = 0.00212 mM; the exported value is 0.002124 mM. kcat/Km: printed Table 2 cell 196.32 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 196.32 * 1000 = 196320.0 s^-1 mM^-1; the exported value is 195951.03578154425.

raw_value_unit_evidence: Table 2, MTA block, enzyme row 2M: KM = 2.12 ± 0.08 uM; kcat = 416.2 ± 7.20 s^-1; printed kcat/Km = 196.32 ± 8.15 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row 2M


substrate_name: adenosine

source_db: brenda

kcat_over_km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB:I0B503 canonical sequence with reconstructed N87T variant; substrate tuple unresolved and applied mutation signature N87T to reconstruct the assayed variant sequence.

substrate: adenosine

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I0B503 and applied mutation signature S12T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row S12T; column KM (uM) = 1.22 ± 0.09; column kcat (s^-1) = 145.1 ± 4.53; column Vmax (nM/min) = 54.4; column kcat/Km (s^-1 uM^-1) = 118.93 ± 9.53.

normalized_value_unit_evidence: kcat: printed Table 2 cell 145.1 s^-1; already in s^-1, so no conversion is applied; the exported value is 145.1 s^(-1). Km: printed Table 2 cell 1.22 uM; 1.22 / 1000 = 0.00122 mM; the exported value is 0.00122 mM. kcat/Km: printed Table 2 cell 118.93 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 118.93 * 1000 = 118930.0 s^-1 mM^-1; the exported value is 118934.4262295082.

raw_value_unit_evidence: Table 2, MTA block, enzyme row S12T: KM = 1.22 ± 0.09 uM; kcat = 145.1 ± 4.53 s^-1; printed kcat/Km = 118.93 ± 9.53 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row S12T


verification_status: unverified

mutation_signature: Unknown

kcat_over_km_origin: calculated

sequence_source: UniProtKB:I0B503 canonical wild-type sequence; selected OED source accession exact match

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

status: unverified


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), 2'deoxy adenosine block, enzyme row S12T; column KM (uM) = 0.99 ± 0.09; column kcat (s^-1) = 48.44 ± 1.40; column Vmax (nM/min) = 18.18; column kcat/Km (s^-1 uM^-1) = 48.92 ±4.67.

normalized_value_unit_evidence: kcat: printed Table 2 cell 48.44 s^-1; already in s^-1, so no conversion is applied; the exported value is 48.44 s^(-1). Km: printed Table 2 cell 0.99 uM; 0.99 / 1000 = 0.00099 mM; the exported value is 0.00099 mM. kcat/Km: printed Table 2 cell 48.92 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 48.92 * 1000 = 48920.0 s^-1 mM^-1; the exported value is 48929.292929292926.

raw_value_unit_evidence: Table 2, 2'deoxy adenosine block, enzyme row S12T: KM = 0.99 ± 0.09 uM; kcat = 48.44 ± 1.40 s^-1; printed kcat/Km = 48.92 ±4.67 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I0B503 and applied mutation signature N87T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row N87T; column KM (uM) = 0.71 ± 0.04; column kcat (s^-1) = 84.62 ± 2.24; column Vmax (nM/min) = 31.73; column kcat/Km (s^-1 uM^-1) = 119.18 ± 7.42.

normalized_value_unit_evidence: kcat: printed Table 2 cell 84.62 s^-1; already in s^-1, so no conversion is applied; the exported value is 84.62 s^(-1). Km: printed Table 2 cell 0.71 uM; 0.71 / 1000 = 0.00071 mM; the exported value is 0.00071 mM. kcat/Km: printed Table 2 cell 119.18 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 119.18 * 1000 = 119180.0 s^-1 mM^-1; the exported value is 119183.0985915493.

raw_value_unit_evidence: Table 2, MTA block, enzyme row N87T: KM = 0.71 ± 0.04 uM; kcat = 84.62 ± 2.24 s^-1; printed kcat/Km = 119.18 ± 7.42 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row N87T


sequence_variant_note: Resolved canonical sequence from UniProtKB:I0B503 direct JSON/FASTA lookup; variant reconstructed from canonical residue checks and PMID 27935959 mutation label. and applied mutation signature S12T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:I0B503 direct JSON/FASTA lookup; variant reconstructed from canonical residue checks and PMID 27935959 mutation label. and applied mutation signature S12T/N87T/Q289L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S12T/N87T/Q289L, at pH 7.4 and 25°C


sequence_source: UniProtKB:I0B503 direct JSON/FASTA lookup.


sequence_variant_note: Resolved canonical sequence from UniProtKB:I0B503 direct JSON/FASTA lookup; variant reconstructed from canonical residue checks and PMID 27935959 mutation label. and applied mutation signature Q289L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:I0B503 direct JSON/FASTA lookup; variant reconstructed from canonical residue checks and PMID 27935959 mutation label.


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), adenosine block, enzyme row N87T; column KM (uM) = 3.3 ± 0.21; column kcat (s^-1) = 62.63 ± 1.51; column Vmax (nM/min) = 23.49; column kcat/Km (s^-1 uM^-1) = 18.97 + 1.29.

normalized_value_unit_evidence: kcat: printed Table 2 cell 62.63 s^-1; already in s^-1, so no conversion is applied; the exported value is 62.63 s^(-1). Km: printed Table 2 cell 3.3 uM; 3.3 / 1000 = 0.0033 mM; the exported value is 0.0033 mM. kcat/Km: printed Table 2 cell 18.97 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 18.97 * 1000 = 18970.0 s^-1 mM^-1; the exported value is 18978.78787878788.

raw_value_unit_evidence: Table 2, adenosine block, enzyme row N87T: KM = 3.3 ± 0.21 uM; kcat = 62.63 ± 1.51 s^-1; printed kcat/Km = 18.97 + 1.29 s^-1 uM^-1.


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), adenosine block, enzyme row Q289L; column KM (uM) = 1.81 ± 0.08; column kcat (s^-1) = 95.79 ± 1.69; column Vmax (nM/min) = 35.92; column kcat/Km (s^-1 uM^-1) = 54.58 ± 2.59.

normalized_value_unit_evidence: kcat: printed Table 2 cell 95.79 s^-1; already in s^-1, so no conversion is applied; the exported value is 95.79 s^(-1). Km: printed Table 2 cell 1.81 uM; 1.81 / 1000 = 0.00181 mM; the exported value is 0.00181 mM. kcat/Km: printed Table 2 cell 54.58 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 54.58 * 1000 = 54580.0 s^-1 mM^-1; the exported value is 52922.65193370166.

raw_value_unit_evidence: Table 2, adenosine block, enzyme row Q289L: KM = 1.81 ± 0.08 uM; kcat = 95.79 ± 1.69 s^-1; printed kcat/Km = 54.58 ± 2.59 s^-1 uM^-1.


enzyme_display_name: adenosylhomocysteine nucleosidase

organism: Arabidopsis thaliana

substrate_name: S-adenosyl-L-homocysteine

kcat_display: Not reported

sequence_source: UniProtKB:Q7XA67 direct lookup on 2026-06-05

assay_conditions_summary: pH 8; 310.15 K; buffer 100 mM sodium phosphate

proof_lines: in 100 mM sodium phosphate buffer, at pH 8.0 and 37°C

enzyme: adenosylhomocysteine nucleosidase

substrate: S-adenosyl-L-homocysteine


organism: Borreliella burgdorferi

sequence_source: UniProtKB:O50860 direct lookup on 2026-06-05

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


sequence_source: UniProtKB:O50162 direct lookup on 2026-06-05

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication


sequence_source: UniProtKB:O51534 direct lookup on 2026-06-05


organism: Campylobacter jejuni

sequence_source: UniProtKB:Q0PC20 direct lookup on 2026-06-05

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer, pH 7.0, at 25°C


organism: Escherichia coli

substrate_name: H2O; 5'-Deoxy-5'-(methylthio)adenosine

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

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature S76A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 2, enzyme row Ser76Ala, substrate row MTA; column Km (uM) cell = 2.7; column kcat (s-1) cell = 1.3; column kcat/Km (s-1 uM-1) cell = 0.5; column catalytic efficiency (%) cell = 13.4; column apparent Tma (C) cell = 70. captured primary segment: MTA | S76A MTAN | Table 2 | pH 7.0 | Km 2.7 uM | kcat 1.3 s^-1 | kcat/Km 0.5 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 2.7 uM; 1 uM is 1/1000 mM, so 2.7 / 1000 = 0.0027 mM. kcat: printed Table 2 kcat cell 1.3 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 1.3 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 0.5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.5 x 1000 = 500.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.3 / 0.0027 = 481.48148148148147 s^-1 mM^-1, beside the printed efficiency cell 500.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 2, enzyme row Ser76Ala, substrate row MTA: Km = 2.7 uM; kcat = 1.3 s^-1; kcat/Km = 0.5 s^-1 uM^-1.

substrate: H2O; 5'-Deoxy-5'-(methylthio)adenosine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature F105A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Phe105Ala, substrate row MTA; column Km (uM) cell = 3.3; column kcat (s-1) cell = 10.2; column kcat/Km (s-1 uM-1) cell = 3.1; column catalytic efficiency (%) cell = 87.4; column apparent Tma (C) cell = 66. captured primary segment: MTA | F105A MTAN | Table 3 | pH 7.0 | Km 3.3 uM | kcat 10.2 s^-1 | kcat/Km 3.1 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 3.3 uM; 1 uM is 1/1000 mM, so 3.3 / 1000 = 0.0033 mM. kcat: printed Table 3 kcat cell 10.2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 10.2 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 3.1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.1 x 1000 = 3100.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 10.2 / 0.0033 = 3090.9090909090905 s^-1 mM^-1, beside the printed efficiency cell 3100.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Phe105Ala, substrate row MTA: Km = 3.3 uM; kcat = 10.2 s^-1; kcat/Km = 3.1 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF12 direct lookup on 2026-06-05 plus direct F151A substitution from selected mutation_signature and applied mutation signature F151A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylhomocysteine nucleosidase(Enzyme) mutant F151A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature S196A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters for Purine Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11052 (PDF page 4). Table 1, enzyme row Ser196Ala, substrate row MTA; column Km (uM) cell = 2.9; column kcat (s-1) cell = 0.23; column kcat/Km (s-1 uM-1) cell = 0.081; column catalytic efficiency (%) cell = 2.3; column apparent Tma (C) cell = 66. captured primary segment: MTA | S196A MTAN | Table 1 | pH 7.0 | Km 2.9 uM | kcat 0.23 s^-1 | kcat/Km 0.081 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 2.9 uM; 1 uM is 1/1000 mM, so 2.9 / 1000 = 0.0029 mM. kcat: printed Table 1 kcat cell 0.23 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.23 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.081 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.081 x 1000 = 81.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.23 / 0.0029 = 79.31034482758622 s^-1 mM^-1, beside the printed efficiency cell 81.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11052, Table 1, enzyme row Ser196Ala, substrate row MTA: Km = 2.9 uM; kcat = 0.23 s^-1; kcat/Km = 0.081 s^-1 uM^-1.


row_label: Table 2, enzyme row Ser76Ala, substrate row MTA

table_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C)


substrate_name: S-Adenosyl-L-homocysteine

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Phe105Ala, substrate row AdoHcy; column Km (uM) cell = 2.8; column kcat (s-1) cell = 7.5; column kcat/Km (s-1 uM-1) cell = 2.7; column catalytic efficiency (%) cell = 128; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | F105A MTAN | Table 3 | pH 7.0 | Km 2.8 uM | kcat 7.5 s^-1 | kcat/Km 2.7 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 2.8 uM; 1 uM is 1/1000 mM, so 2.8 / 1000 = 0.0028 mM. kcat: printed Table 3 kcat cell 7.5 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 7.5 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 2.7 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.7 x 1000 = 2700.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.5 / 0.0028 = 2678.5714285714284 s^-1 mM^-1, beside the printed efficiency cell 2700.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Phe105Ala, substrate row AdoHcy: Km = 2.8 uM; kcat = 7.5 s^-1; kcat/Km = 2.7 s^-1 uM^-1.

substrate: S-Adenosyl-L-homocysteine


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AF12 canonical sequence with selected mutation_signature applied and applied mutation signature M9A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature I50A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Ile50Ala, substrate row MTA; column Km (uM) cell = 7.1; column kcat (s-1) cell = 3.0; column kcat/Km (s-1 uM-1) cell = 0.42; column catalytic efficiency (%) cell = 11.8; column apparent Tma (C) cell = 75. captured primary segment: MTA | I50A MTAN | Table 3 | pH 7.0 | Km 7.1 uM | kcat 3.0 s^-1 | kcat/Km 0.42 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 7.1 uM; 1 uM is 1/1000 mM, so 7.1 / 1000 = 0.0071 mM. kcat: printed Table 3 kcat cell 3.0 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 3.0 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.42 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.42 x 1000 = 420.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.0 / 0.0071 = 422.53521126760563 s^-1 mM^-1, beside the printed efficiency cell 420.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Ile50Ala, substrate row MTA: Km = 7.1 uM; kcat = 3.0 s^-1; kcat/Km = 0.42 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature M173A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 2, enzyme row Met173Ala, substrate row AdoHcy; column Km (uM) cell = 490; column kcat (s-1) cell = 0.8; column kcat/Km (s-1 uM-1) cell = 0.0017; column catalytic efficiency (%) cell = 0.1; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | M173A MTAN | Table 2 | pH 7.0 | Km 490 uM | kcat 0.8 s^-1 | kcat/Km 0.0017 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 490 uM; 1 uM is 1/1000 mM, so 490 / 1000 = 0.49 mM. kcat: printed Table 2 kcat cell 0.8 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.8 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 0.0017 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.0017 x 1000 = 1.7 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.8 / 0.49 = 1.6326530612244898 s^-1 mM^-1, beside the printed efficiency cell 1.7 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 2, enzyme row Met173Ala, substrate row AdoHcy: Km = 490 uM; kcat = 0.8 s^-1; kcat/Km = 0.0017 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AF12 canonical sequence with selected mutation_signature applied and applied mutation signature R193A to reconstruct the assayed variant sequence.


substrate_name: 5'-Deoxy-5'-(methylthio)adenosine; H2O

row_label: Table 1, enzyme row Ser196Ala, substrate row MTA

table_label: Table 1: Kinetic Parameters for Purine Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C)

substrate: 5'-Deoxy-5'-(methylthio)adenosine; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature M9A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Met9Ala, substrate row MTA; column Km (uM) cell = 1.4; column kcat (s-1) cell = 0.63; column kcat/Km (s-1 uM-1) cell = 0.5; column catalytic efficiency (%) cell = 12.6; column apparent Tma (C) cell = 71. captured primary segment: MTA | M9A MTAN | Table 3 | pH 7.0 | Km 1.4 uM | kcat 0.63 s^-1 | kcat/Km 0.5 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 1.4 uM; 1 uM is 1/1000 mM, so 1.4 / 1000 = 0.0014 mM. kcat: printed Table 3 kcat cell 0.63 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.63 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.5 x 1000 = 500.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.63 / 0.0014 = 450.0 s^-1 mM^-1, beside the printed efficiency cell 500.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Met9Ala, substrate row MTA: Km = 1.4 uM; kcat = 0.63 s^-1; kcat/Km = 0.5 s^-1 uM^-1.


row_label: Table 3, enzyme row Ile50Ala, substrate row MTA

table_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C)


column_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 2, enzyme row Met173Ala, substrate row MTA; column Km (uM) cell = 34; column kcat (s-1) cell = 0.72; column kcat/Km (s-1 uM-1) cell = 0.021; column catalytic efficiency (%) cell = 0.6; column apparent Tma (C) cell = 71. captured primary segment: MTA | M173A MTAN | Table 2 | pH 7.0 | Km 34 uM | kcat 0.72 s^-1 | kcat/Km 0.021 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 34 uM; 1 uM is 1/1000 mM, so 34 / 1000 = 0.034 mM. kcat: printed Table 2 kcat cell 0.72 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.72 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 0.021 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.021 x 1000 = 21.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.72 / 0.034 = 21.176470588235293 s^-1 mM^-1, beside the printed efficiency cell 21.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 2, enzyme row Met173Ala, substrate row MTA: Km = 34 uM; kcat = 0.72 s^-1; kcat/Km = 0.021 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature V102A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Val102Ala, substrate row MTA; column Km (uM) cell = 3.0; column kcat (s-1) cell = 10.2; column kcat/Km (s-1 uM-1) cell = 3.4; column catalytic efficiency (%) cell = 95.0; column apparent Tma (C) cell = 67. captured primary segment: MTA | V102A MTAN | Table 3 | pH 7.0 | Km 3.0 uM | kcat 10.2 s^-1 | kcat/Km 3.4 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 3.0 uM; 1 uM is 1/1000 mM, so 3.0 / 1000 = 0.003 mM. kcat: printed Table 3 kcat cell 10.2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 10.2 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 3.4 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.4 x 1000 = 3400.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 10.2 / 0.003 = 3399.9999999999995 s^-1 mM^-1, beside the printed efficiency cell 3400.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Val102Ala, substrate row MTA: Km = 3.0 uM; kcat = 10.2 s^-1; kcat/Km = 3.4 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb:P0AF12:F151A and applied mutation signature F151A to reconstruct the assayed variant sequence.


column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Ile50Ala, substrate row AdoHcy; column Km (uM) cell = 3.7; column kcat (s-1) cell = 1.8; column kcat/Km (s-1 uM-1) cell = 0.5; column catalytic efficiency (%) cell = 23.3; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | I50A MTAN | Table 3 | pH 7.0 | Km 3.7 uM | kcat 1.8 s^-1 | kcat/Km 0.5 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 3.7 uM; 1 uM is 1/1000 mM, so 3.7 / 1000 = 0.0037 mM. kcat: printed Table 3 kcat cell 1.8 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 1.8 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.5 x 1000 = 500.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.8 / 0.0037 = 486.48648648648646 s^-1 mM^-1, beside the printed efficiency cell 500.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Ile50Ala, substrate row AdoHcy: Km = 3.7 uM; kcat = 1.8 s^-1; kcat/Km = 0.5 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature F207A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Phe207Ala, substrate row AdoHcy; column Km (uM) cell = 5.5; column kcat (s-1) cell = 0.31; column kcat/Km (s-1 uM-1) cell = 0.056; column catalytic efficiency (%) cell = 2.7; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | F207A MTAN | Table 3 | pH 7.0 | Km 5.5 uM | kcat 0.31 s^-1 | kcat/Km 0.056 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 5.5 uM; 1 uM is 1/1000 mM, so 5.5 / 1000 = 0.0055 mM. kcat: printed Table 3 kcat cell 0.31 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.31 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.056 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.056 x 1000 = 56.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.31 / 0.0055 = 56.36363636363637 s^-1 mM^-1, beside the printed efficiency cell 56.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Phe207Ala, substrate row AdoHcy: Km = 5.5 uM; kcat = 0.31 s^-1; kcat/Km = 0.056 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature Y107F to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Tyr107Phe, substrate row MTA; column Km (uM) cell = 2.2; column kcat (s-1) cell = 2.5; column kcat/Km (s-1 uM-1) cell = 1.2; column catalytic efficiency (%) cell = 32.2; column apparent Tma (C) cell = 67. captured primary segment: MTA | Y107F MTAN | Table 3 | pH 7.0 | Km 2.2 uM | kcat 2.5 s^-1 | kcat/Km 1.2 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 2.2 uM; 1 uM is 1/1000 mM, so 2.2 / 1000 = 0.0022 mM. kcat: printed Table 3 kcat cell 2.5 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 2.5 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 1.2 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.2 x 1000 = 1200.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.5 / 0.0022 = 1136.3636363636363 s^-1 mM^-1, beside the printed efficiency cell 1200.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Tyr107Phe, substrate row MTA: Km = 2.2 uM; kcat = 2.5 s^-1; kcat/Km = 1.2 s^-1 uM^-1.


column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Phe207Ala, substrate row MTA; column Km (uM) cell = 1.7; column kcat (s-1) cell = 0.13; column kcat/Km (s-1 uM-1) cell = 0.080; column catalytic efficiency (%) cell = 2.2; column apparent Tma (C) cell = 72. captured primary segment: MTA | F207A MTAN | Table 3 | pH 7.0 | Km 1.7 uM | kcat 0.13 s^-1 | kcat/Km 0.080 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 1.7 uM; 1 uM is 1/1000 mM, so 1.7 / 1000 = 0.0017 mM. kcat: printed Table 3 kcat cell 0.13 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.13 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.080 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.080 x 1000 = 80.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.13 / 0.0017 = 76.47058823529413 s^-1 mM^-1, beside the printed efficiency cell 80.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Phe207Ala, substrate row MTA: Km = 1.7 uM; kcat = 0.13 s^-1; kcat/Km = 0.080 s^-1 uM^-1.


row_label: Table 3, enzyme row Tyr107Phe, substrate row MTA


verification_status: verified

sequence_source: UniProtKB REST FASTA P0AF12 direct lookup on 2026-06-05.

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

column_label: Table 1: Kinetic Parameters for Purine Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11052 (PDF page 4). Table 1, enzyme row WT, substrate row MTA; column Km (uM) cell = 0.8; column kcat (s-1) cell = 3.0; column kcat/Km (s-1 uM-1) cell = 3.6; column catalytic efficiency (%) cell = 100; column apparent Tma (C) cell = 68. captured primary segment: MTA | WT MTAN | Table 1 | pH 7.0 | Km 0.8 uM | kcat 3.0 s^-1 | kcat/Km 3.6 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.8 uM; 1 uM is 1/1000 mM, so 0.8 / 1000 = 0.0008 mM. kcat: printed Table 1 kcat cell 3.0 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 3.0 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 3.6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.6 x 1000 = 3600.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.0 / 0.0008 = 3750.0 s^-1 mM^-1, beside the printed efficiency cell 3600.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11052, Table 1, enzyme row WT, substrate row MTA: Km = 0.8 uM; kcat = 3.0 s^-1; kcat/Km = 3.6 s^-1 uM^-1.

status: verified


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA P0AF12 direct lookup on 2026-06-05; selected F151A mutation applied once after confirming canonical residue F151. and applied mutation signature F151A to reconstruct the assayed variant sequence.


column_label: Table 1: Kinetic Parameters for Purine Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11052 (PDF page 4). Table 1, enzyme row Ser196Ala, substrate row AdoHcy; column Km (uM) cell = 1.7; column kcat (s-1) cell = 0.14; column kcat/Km (s-1 uM-1) cell = 0.084; column catalytic efficiency (%) cell = 4.0; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | S196A MTAN | Table 1 | pH 7.0 | Km 1.7 uM | kcat 0.14 s^-1 | kcat/Km 0.084 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 1.7 uM; 1 uM is 1/1000 mM, so 1.7 / 1000 = 0.0017 mM. kcat: printed Table 1 kcat cell 0.14 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.14 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.084 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.084 x 1000 = 84.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.14 / 0.0017 = 82.3529411764706 s^-1 mM^-1, beside the printed efficiency cell 84.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11052, Table 1, enzyme row Ser196Ala, substrate row AdoHcy: Km = 1.7 uM; kcat = 0.14 s^-1; kcat/Km = 0.084 s^-1 uM^-1.


row_label: Table 3, enzyme row Phe207Ala, substrate row MTA


row_label: Table 3, enzyme row Met9Ala, substrate row MTA


column_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 2, enzyme row Ser76Ala, substrate row AdoHcy; column Km (uM) cell = 1.9; column kcat (s-1) cell = 0.93; column kcat/Km (s-1 uM-1) cell = 0.5; column catalytic efficiency (%) cell = 22.9; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | S76A MTAN | Table 2 | pH 7.0 | Km 1.9 uM | kcat 0.93 s^-1 | kcat/Km 0.5 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 1.9 uM; 1 uM is 1/1000 mM, so 1.9 / 1000 = 0.0019 mM. kcat: printed Table 2 kcat cell 0.93 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.93 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 0.5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.5 x 1000 = 500.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.93 / 0.0019 = 489.47368421052636 s^-1 mM^-1, beside the printed efficiency cell 500.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 2, enzyme row Ser76Ala, substrate row AdoHcy: Km = 1.9 uM; kcat = 0.93 s^-1; kcat/Km = 0.5 s^-1 uM^-1.


organism: Klebsiella pneumoniae

substrate_name: 5'-methylthioadenosine (at pH 7 and 37 degrees Celsius)

source_db: uniprot

sequence: MKIGIIGAMEEEVTLLRDKIENRQTITIGGSEIYT

wild_type_sequence: MKIGIIGAMEEEVTLLRDKIENRQTITIGGSEIYT

sequence_source: source_record; UniProt Q9R4A1 direct check

source: uniprot


organism: Helicobacter pylori

source_db: skid

km_display: Not reported

source_license: CC BY-NC-ND 4.0

source: skid


organism: Mycobacterium tuberculosis

proof_lines: pH and temperature not specified in the publication


organism: Staphylococcus aureus

proof_lines: recombinant enzyme, in 50 mM potassium phosphate, pH 7.0


organism: Vibrio cholerae

sequence_variant_note: Resolved canonical sequence from UniProtKB:A5F5R2 canonical sequence plus selected-batch mutation_signature V153I and applied mutation signature V153I to reconstruct the assayed variant sequence.

proof_lines: mutant V153I, pH 7.7, temperature not specified in the publication


proof_lines: wild-type, pH 7.7, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5F5R2 canonical sequence plus selected-batch mutation_signature A113P and applied mutation signature A113P to reconstruct the assayed variant sequence.

proof_lines: mutant A113P, pH 7.7, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5F5R2 canonical sequence plus selected-batch mutation_signature A113P/V153I and applied mutation signature A113P/V153I to reconstruct the assayed variant sequence.

proof_lines: mutant A113P/V153I, pH 7.7, temperature not specified in the publication


sequence_source: UniProtKB reviewed entry P0AF12 fetched by direct REST lookup on 2026-06-05.

row_label: Table 1, enzyme row WT, substrate row MTA


sequence_source: UniProtKB reviewed entry P0AF14 fetched by direct REST lookup on 2026-06-05.


proof_lines: pH 7.5, 25°C, wild-type enzyme, the assay uses the adenine deaminase enzyme from Pseudomonas aeruginosa


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry P0AF12 fetched by direct REST lookup on 2026-06-05, with S76V reconstructed from the selected mutation signature. and applied mutation signature S76V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant enzyme S76V, the assay uses the adenine deaminase enzyme from Pseudomonas aeruginosa


sequence_source: UniProtKB reviewed entry Q9ZMY2 fetched by direct REST lookup on 2026-06-05.

proof_lines: at 37°C in 100 mM HEPES, 50 mM KCl, pH 7.5


sequence_source: UniProtKB reviewed entry Q9ZMY2 fetched by direct REST lookup on 2026-06-05; variant sequence not reconstructed.

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

proof_lines: pH 7.5, 25°C, mutant enzyme V79S, the assay uses the adenine deaminase enzyme from Pseudomonas aeruginosa


proof_lines: pH 7.5, 25°C, mutant enzyme P17A, the assay uses the adenine deaminase enzyme from Pseudomonas aeruginosa


column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Tyr107Phe, substrate row AdoHcy; column Km (uM) cell = 1.7; column kcat (s-1) cell = 2.0; column kcat/Km (s-1 uM-1) cell = 1.2; column catalytic efficiency (%) cell = 58.1; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | Y107F MTAN | Table 3 | pH 7.0 | Km 1.7 uM | kcat 2.0 s^-1 | kcat/Km 1.2 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 1.7 uM; 1 uM is 1/1000 mM, so 1.7 / 1000 = 0.0017 mM. kcat: printed Table 3 kcat cell 2.0 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 2.0 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 1.2 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.2 x 1000 = 1200.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.0 / 0.0017 = 1176.4705882352941 s^-1 mM^-1, beside the printed efficiency cell 1200.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Tyr107Phe, substrate row AdoHcy: Km = 1.7 uM; kcat = 2.0 s^-1; kcat/Km = 1.2 s^-1 uM^-1.


column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Val102Ala, substrate row AdoHcy; column Km (uM) cell = 1.9; column kcat (s-1) cell = 9.1; column kcat/Km (s-1 uM-1) cell = 4.9; column catalytic efficiency (%) cell = 233; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | V102A MTAN | Table 3 | pH 7.0 | Km 1.9 uM | kcat 9.1 s^-1 | kcat/Km 4.9 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 1.9 uM; 1 uM is 1/1000 mM, so 1.9 / 1000 = 0.0019 mM. kcat: printed Table 3 kcat cell 9.1 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 9.1 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 4.9 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 4.9 x 1000 = 4900.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 9.1 / 0.0019 = 4789.473684210526 s^-1 mM^-1, beside the printed efficiency cell 4900.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Val102Ala, substrate row AdoHcy: Km = 1.9 uM; kcat = 9.1 s^-1; kcat/Km = 4.9 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature F105A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Phe105Ala, substrate row MTA; column Km (uM) cell = 3.3; column kcat (s-1) cell = 10.2; column kcat/Km (s-1 uM-1) cell = 3.1; column catalytic efficiency (%) cell = 87.4; column apparent Tma (C) cell = 66. captured primary segment: MTA | F105A MTAN | Table 3 | pH 7.0 | Km 3.3 uM | kcat 10.2 s^-1 | kcat/Km 3.1 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 3.3 uM; 1 uM is 1/1000 mM, so 3.3 / 1000 = 0.0033 mM. kcat: printed Table 3 kcat cell 10.2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 10.2 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 3.1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.1 x 1000 = 3100.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 10.2 / 0.0033 = 3090.9090909090905 s^-1 mM^-1, beside the printed efficiency cell 3100.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Phe105Ala, substrate row MTA: Km = 3.3 uM; kcat = 10.2 s^-1; kcat/Km = 3.1 s^-1 uM^-1.


sequence_source: UniProtKB:P0AF12 direct FASTA/JSON lookup.

column_label: Table 1: Kinetic Parameters for Purine Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11052 (PDF page 4). Table 1, enzyme row WT, substrate row AdoHcy; column Km (uM) cell = 1.3; column kcat (s-1) cell = 2.6; column kcat/Km (s-1 uM-1) cell = 2.1; column catalytic efficiency (%) cell = 100; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | WT MTAN | Table 1 | pH 7.0 | Km 1.3 uM | kcat 2.6 s^-1 | kcat/Km 2.1 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 1.3 uM; 1 uM is 1/1000 mM, so 1.3 / 1000 = 0.0013 mM. kcat: printed Table 1 kcat cell 2.6 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 2.6 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 2.1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.1 x 1000 = 2100.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.6 / 0.0013 = 2000.0000000000002 s^-1 mM^-1, beside the printed efficiency cell 2100.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11052, Table 1, enzyme row WT, substrate row AdoHcy: Km = 1.3 uM; kcat = 2.6 s^-1; kcat/Km = 2.1 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF12 direct FASTA/JSON lookup; variant reconstructed from canonical sequence. and applied mutation signature V102A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature R193A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 2, enzyme row Arg193Ala, substrate row MTA; column Km (uM) cell = 3.2; column kcat (s-1) cell = 1.5; column kcat/Km (s-1 uM-1) cell = 0.5; column catalytic efficiency (%) cell = 12.9; column apparent Tma (C) cell = 72. captured primary segment: MTA | R193A MTAN | Table 2 | pH 7.0 | Km 3.2 uM | kcat 1.5 s^-1 | kcat/Km 0.5 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 3.2 uM; 1 uM is 1/1000 mM, so 3.2 / 1000 = 0.0032 mM. kcat: printed Table 2 kcat cell 1.5 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 1.5 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 0.5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.5 x 1000 = 500.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.5 / 0.0032 = 468.75 s^-1 mM^-1, beside the printed efficiency cell 500.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 2, enzyme row Arg193Ala, substrate row MTA: Km = 3.2 uM; kcat = 1.5 s^-1; kcat/Km = 0.5 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF12 direct FASTA/JSON lookup; variant reconstructed from canonical sequence. and applied mutation signature M173A to reconstruct the assayed variant sequence.


row_label: Table 2, enzyme row Arg193Ala, substrate row MTA


substrate_name: 5'-methylthioadenosine (MTA)

proof_lines: kcat is 2.0 sec(-1) with MTA as substrate.

substrate: 5'-methylthioadenosine (MTA)


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: aminodeoxyfutalosine

proof_lines: kcat is 0.53 sec(-1) with aminodeoxyfutalosine as substrate. kcat is 2.7 sec(-1) with 5'-methylthioadenosine as substrate.

substrate: aminodeoxyfutalosine


organism: Escherichia coli (strain K12)

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

proof_lines: kcat is 3.0 sec(-1) and 2.6 sec(-1) with 5'-methylthioadenosine and S-adenosylhomocysteine as substrate, respectively.

proof_lines: kcat is 84 sec(-1) with S-adenosyl-L-homocysteine as substrate. kcat is 150 sec(-1) with S-methyl-5'-thioadenosine as substrate. kcat is 57 sec(-1) with 5'-deoxyadenosine as substrate. kcat is 0.24 sec(-1) with adenine as substrate.

substrate: 5'-methylthioadenosine (at pH 7 and 37 degrees Celsius)


organism: Helicobacter pylori (strain J99 / ATCC 700824)

proof_lines: kcat is 12.1 sec(-1) with 5'-methylthioadenosine as substrate, and 4.3 sec(-1) with aminodeoxyfutalosine as substrate (PubMed:22891633). kcat is 4.92 sec(-1) with 5'-methylthioadenosine as substrate (at pH 7.5 and 37 degrees Celsius) (PubMe


enzyme_display_name: urease

organism: Unknown

substrate_name: Urea

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

enzyme: urease

substrate: Urea


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: urea

substrate: urea


organism: Oryza sativa subsp. indica


organism: Prochlorococcus marinus subsp. pastoris (strain PCC 9511)


organism: Canavalia ensiformis

substrate_name: urea (at 37 degrees Celsius and pH 6.5)

substrate: urea (at 37 degrees Celsius and pH 6.5)


organism: Helicobacter pylori (strain ATCC 700392 / 26695)


organism: Klebsiella aerogenes


organism: Brucella suis bv. 1

sequence_source: UniProtKB:Q8FZW3 direct lookup

smiles: N=C(N)O

proof_lines: by hyperbolic regression, Lineweaver-Burk: 5.24 mM


substrate_name: Urea; H2O

sequence_source: UniProtKB:P07374 direct lookup and accession reuse cache

proof_lines: pH 7.0, 25°C, urease encapsulated in chitosan-coated alginate-magnetite

proof_lines: pH 7.0, 25°C, urease encapsulated in chitosan-magnetite beads

substrate: Urea; H2O


organism: Enterobacter aerogenes

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

sequence_variant_note: Resolved canonical sequence from UniProtKB:P18314 direct lookup plus PMID 10913264 mutagenesis reconstruction (H320N) and applied mutation signature H320N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant H320N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18314 direct lookup plus PMID 10913264 mutagenesis reconstruction (D221A) and applied mutation signature D221A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant D221A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18314 direct lookup plus PMID 10913264 mutagenesis reconstruction (H219Q) and applied mutation signature H219Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant H219Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18314 direct lookup plus PMID 10913264 mutagenesis reconstruction (H320Q) and applied mutation signature H320Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant H320Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18314 direct lookup plus PMID 10913264 mutagenesis reconstruction (H320A) and applied mutation signature H320A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant H320A


substrate_name: H2O; Urea

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

substrate: H2O; Urea


proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant D221N


proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant H219N


proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant H219A


proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant R336Q


proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant C319D


proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant C319S


proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant C319A


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

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


organism: Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)


organism: Synechococcus sp. (strain WH7805)


proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant betaH39A

proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant betaH41A


proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant gammaH96A

proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant alphaH219A

proof_lines: SABIO-RK modifier species: urease(Enzyme) mutant alphaH312A


organism: Helicobacter pylori


organism: Oryza sativa


organism: Sporosarcina pasteurii

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Streptococcus salivarius


sequence_source: source_record; UniProt O87400 direct check


organism: Streptococcus salivarius (strain 57.I)

substrate_name: urea (at pH 7.0 and 37 degrees Celsius)

smiles: NC(N)=O

proof_lines: Urea concentrations in the oral cavity of humans normally range from 3 mM to 10 mM.

substrate: urea (at pH 7.0 and 37 degrees Celsius)


enzyme_display_name: adenosine kinase

organism: Toxoplasma gondii

enzyme: adenosine kinase


organism: Triticum aestivum


organism: Trypanosoma brucei

substrate_name: Inosine

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

substrate: Inosine


enzyme_display_name: tannase

organism: Aspergillus oryzae

substrate_name: ethyl gallate

proof_lines:
recombinant enzyme, at pH 5.0 and 30°C
native enzyme, at pH 5.0 and 30°C
tannase I

enzyme: tannase

substrate: ethyl gallate


organism: Aspergillus sp.


organism: Aspergillus tubingensis

substrate_name: propyl gallate

proof_lines:
free enzyme, pH 5.0, 30°C
immobilized enzyme, pH 5.0, 30°C

substrate: propyl gallate


organism: Cryptosporidium parvum

substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


organism: Homo sapiens

substrate_name: adenosine

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
at pH 7.5 and 37°C
pH 7.4, 37ºC
pH 7.5, 30ºC

substrate: adenosine


organism: Leishmania donovani

proof_lines: pH 7.5, 30°C, recombinant mutants R131A and R69K/R131A


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH 7.5, 30°C, recombinant mutant R69K/R131A


organism: Mus musculus

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines:
pH 6.8, 37ºC, 12 mM ATP and 3 mM MgCl2
pH 6.0, 37ºC
pH 5.8, 25ºC


organism: Oryctolagus cuniculus

proof_lines:
pH 5.8, 25ºC
pH 5.8, 25ºC, natural
pH 5.8, 25ºC, synthetic


organism: Pelophylax ridibundus


organism: Prunus persica

assay_conditions_summary: pH 9; cofactor ATP


organism: Rattus norvegicus

assay_conditions_summary: pH 5.6; cofactor ATP


organism: Saccharomyces cerevisiae

substrate_name: guanosine

assay_conditions_summary: pH 8; cofactor ATP

proof_lines:
51fold reduction
25fold reduction
15fold reduction

substrate: guanosine


proof_lines:
pH 7.5, 30°C, recombinant mutant R131A
mutant enzyme R131A


assay_conditions_summary: cofactor ATP


proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme


assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: pH 7.5, 30ºC, with adenosine and ATP saturating concentrations


organism: Lupinus luteus

assay_conditions_summary: pH 7.35; cofactor ATP


organism: Bacillus pumilus

substrate_name: rosmarinic acid

substrate: rosmarinic acid


organism: Bacillus subtilis

substrate_name: Tannic acid

proof_lines: pH and temperature not specified in the publication

substrate: Tannic acid


organism: Clostridium butyricum

proof_lines: isoform Tan3, 37°C, pH not specified in the publication

proof_lines: isoform Tan2, 37°C, pH not specified in the publication

proof_lines: isoform Tan1, 37°C, pH not specified in the publication


organism: Enterobacter cloacae


organism: Enterobacter sp.

substrate_name: methyl gallate

substrate: methyl gallate


organism: Fusarium subglutinans


organism: Geotrichum cucujoidarum


organism: Herbaspirillum camelliae

sequence_source: PMID 34641872 / PMCID PMC8507159; TanHcw coding region KV880769.1:4574529-4575635 translated during review

proof_lines:
pH 6, 30°C
pH 7, 40°C


organism: Kluyveromyces marxianus


organism: Lachnospiraceae

substrate_name: lauryl gallate

sequence_source: PMID 34976993 / PMCID PMC8715002; NCBI protein MBQ6323131.1

substrate: lauryl gallate


organism: Lactiplantibacillus paraplantarum

substrate_name: catechin gallate

sequence_source: PMID 24708557 / UniProt M5B2V9 / GenBank BAN10246.1

substrate: catechin gallate


organism: Lactiplantibacillus pentosus

sequence_source: PMID 24708557 / UniProt M5AP49 / GenBank BAN10247.1


organism: Paecilomyces variotii


organism: Penicillium chrysogenum

proof_lines:
purified enzyme, at pH 5.0 and 37°C
crude enzyme, at pH 5.0 and 37°C


organism: Quercus robur


organism: Rhizopus arrhizus


organism: Rhodotorula diobovata

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


organism: Selenomonas ruminantium


enzyme_display_name: triacylglycerol lipase

organism: Micrococcus sp.

substrate_name: alpha-naphthyl caprylate

enzyme: triacylglycerol lipase

substrate: alpha-naphthyl caprylate


organism: Oncorhynchus tshawytscha

substrate_name: 4-nitrophenyl caprate

substrate: 4-nitrophenyl caprate


organism: Oryctolagus cuniculus

substrate_name: 4-methylumbelliferyl oleate

substrate: 4-methylumbelliferyl oleate


organism: Oryza sativa

substrate_name: Triacetin

proof_lines:
native enzyme, at pH 7.4 and 25°C
recombinant enzyme, at pH 7.4 and 25°C
pH 7.5, 37°C

substrate: Triacetin


organism: Penaeus vannamei

substrate_name: 4-Methylumbelliferyl butyrate

proof_lines: apparent value, in 2.5 mM Tris-HCl, at pH 8.0 at 30°C

substrate: 4-Methylumbelliferyl butyrate


organism: Pleurotus ostreatus

substrate_name: 4-methylumbelliferyl palmitate

substrate: 4-methylumbelliferyl palmitate


organism: Bacillus pumilus

substrate_name: 4-nitrophenyl caprylate

substrate: 4-nitrophenyl caprylate


organism: Bacillus sp. (in: firmicutes)

substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


organism: Bacillus subtilis

substrate_name: 4-nitrophenyl laurate

substrate: 4-nitrophenyl laurate


organism: Bos taurus

substrate_name: trioleoylglycerol

substrate: trioleoylglycerol


organism: Burkholderia cepacia

substrate_name: 4-nitrophenyl palmitate

proof_lines:
native enzyme, at pH 7 and 37°C
recombinant enzyme, at pH 7 and 37°C

substrate: 4-nitrophenyl palmitate


organism: Burkholderia sp.


organism: Streptomyces sp.


organism: Talaromyces variabilis

substrate_name: propyl gallate; Tannic acid; methyl gallate

assay_conditions_summary: pH 5; 323.15 K; buffer citrate phosphate

proof_lines: in 0.5 M citrate phosphate buffer, pH 5.0, at 50°C


organism: Trametes elegans


organism: Aeromonas caviae

assay_conditions_summary: pH 9


organism: Alkalicoccobacillus gibsonii

assay_conditions_summary: pH 8

proof_lines:
at pH 8.0 and 30Â°C
at pH 8.0 and 10Â°C
at pH 8.0 and 60Â°C


organism: Amycolatopsis mediterranei

assay_conditions_summary: pH 8; 333.15 K; buffer 50 mM Tris-HCl

proof_lines: apparent value, in 50 mM Tris-HCl buffer, at pH 8.0, 60°C


organism: Aspergillus fumigatus

substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Aspergillus nidulans


organism: Aureobasidium pullulans


organism: Bacillus cereus

substrate_name: cotton seed oil

substrate: cotton seed oil


organism: Bacillus gibsonii

substrate_name: H2O; p-Nitrophenyl palmitate

substrate: H2O; p-Nitrophenyl palmitate


organism: Bacillus licheniformis

substrate_name: tristearin

substrate: tristearin


organism: Geobacillus thermoleovorans

proof_lines:
pH 7.5,60°C
BTID-A, pH 7.5, 60°C
BTID-B, pH 7.5, 60°C


organism: Geotrichum marinum

substrate_name: triolein

substrate: triolein


organism: Heyndrickxia coagulans


organism: Hyalomma dromedarii

substrate_name: Unknown

substrate: Unknown


organism: Lymantria dispar

assay_conditions_summary: pH 8.2; 310.15 K; buffer Tris-HCl

proof_lines: in Tris-HCl buffer (50 mM, pH 8.2), at 37°C


organism: Macruronus novaezelandiae

substrate_name: 4-nitrophenyl caprate


enzyme_display_name: RNA-directed DNA polymerase

organism: Human immunodeficiency virus

substrate_name: dTTP

enzyme: RNA-directed DNA polymerase

substrate: dTTP


substrate_name: dGTP

substrate: dGTP


sequence_source: UniProtKB:P03366 canonical sequence retrieved 2026-06-05


substrate_name: dCTP

substrate: dCTP


organism: Homo sapiens


organism: Xenotropic MuLV-related virus (isolate VP62)

substrate_name: RNA/DNA duplex

substrate: RNA/DNA duplex


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 direct lookup; variant reconstructed from RT-chain coordinate offset +599 and applied mutation signature K65R/Q151M with inferred residue-numbering offset +599 to reconstruct the assayed variant sequence.


substrate_name: dCTP; DNA

sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 direct lookup; variant reconstructed from RT-chain coordinate offset +599 and applied mutation signature D67N/K70R/T215Y/K219Q with inferred residue-numbering offset +599 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant D67N/K70R/T215Y/K219Q

substrate: dCTP; DNA


substrate_name: DNA; dCTP

sequence_source: UniProtKB P03366 direct lookup; variant reconstructed from RT-chain coordinate offset +599

proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant K65R/Q151M

substrate: DNA; dCTP


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 direct lookup; variant reconstructed from RT-chain coordinate offset +599 and applied mutation signature K65R/K103N with inferred residue-numbering offset +599 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 direct lookup; variant reconstructed from RT-chain coordinate offset +599 and applied mutation signature K65R/K103N/Q151M with inferred residue-numbering offset +599 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant K65R/K103N/Q151M


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 direct lookup; variant reconstructed from RT-chain coordinate offset +599 and applied mutation signature L74V/K103N with inferred residue-numbering offset +599 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 direct lookup; variant reconstructed from RT-chain coordinate offset +599 and applied mutation signature K65R with inferred residue-numbering offset +599 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant L74V/K103N


proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant K103N/Q151M


proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant Q151M


proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant L74V


sequence_variant_note: Resolved canonical sequence from UniProt:P03366 Reverse transcriptase/ribonuclease H chain 600-1159 and applied mutation signature K65R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P03366 Reverse transcriptase/ribonuclease H chain 600-1159 and applied mutation signature D67N/K70R/T215Y/K219Q to reconstruct the assayed variant sequence.


substrate_name: dCTP; DNA; dCTP; DNA; Diphosphate; DNA; dGTP; dGTP; dTTP; DNA; dTTP; DNA; dCTP

sequence_variant_note: Resolved canonical sequence from UniProt:P03366 Reverse transcriptase/ribonuclease H chain 600-1159 and applied mutation signature M184V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant M184V


sequence_variant_note: Resolved canonical sequence from UniProt:P03366 Reverse transcriptase/ribonuclease H chain 600-1159 and applied mutation signature L74V to reconstruct the assayed variant sequence.


sequence_source: UniProt:P03366 Reverse transcriptase/ribonuclease H chain 600-1159


sequence_variant_note: Resolved canonical sequence from UniProt:P03366 Reverse transcriptase/ribonuclease H chain 600-1159 and applied mutation signature L74V/K103N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P03366 Reverse transcriptase/ribonuclease H chain 600-1159 and applied mutation signature K103N/Q151M to reconstruct the assayed variant sequence.


substrate_name: DNA; dCTP; DNA; dCTP; Diphosphate; DNA; dGTP; dGTP; DNA; dTTP; dTTP; dCTP; DNA

sequence_variant_note: Resolved canonical sequence from UniProt:P03366 Reverse transcriptase/ribonuclease H chain 600-1159 and applied mutation signature K65R/K103N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant K65R/K103N


proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant K65R


proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant K103N


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 RT/RNase H chain residues 600-1159; K65R, K103N, and Q151M reconstructed on RT-chain numbering. and applied mutation signature K65R/K103N/Q151M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 RT/RNase H chain residues 600-1159; K65R and K103N reconstructed on RT-chain numbering. and applied mutation signature K65R/K103N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P03366 checked, but no row-specific wild-type or mutation state was present in the selected SABIO grouped source snapshots.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 RT/RNase H chain residues 600-1159; L74V and K103N reconstructed on RT-chain numbering. and applied mutation signature L74V/K103N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 RT/RNase H chain residues 600-1159; M184V reconstructed on RT-chain numbering. and applied mutation signature M184V to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P03366 RT/RNase H chain residues 600-1159.

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 P03366 RT/RNase H chain residues 600-1159; K103N and Q151M reconstructed on RT-chain numbering. and applied mutation signature K103N/Q151M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P03366 RT/RNase H chain residues 600-1159; K103N reconstructed on RT-chain numbering. and applied mutation signature K103N to reconstruct the assayed variant sequence.


organism: Human immunodeficiency virus 1


organism: Moloney murine leukemia virus

sequence_source: UniProtKB P03355 FASTA plus selected mutation note F155H; UniProt RT chain positions 660-1330 map RT F155 to full-polyprotein position 814.

sequence_variant_note: Mutation signature F155H could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P03355 FASTA checked as canonical context only; Q84A row-specific variant sequence not emitted because the PMID abstract frames Q84A in an RT-F155V background.

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 P03355 FASTA; live MoMLV Gag-Pol accession with RT/RNase H EC 2.7.7.49.


enzyme_display_name: catechol oxidase

organism: Streptomyces lavendulae

substrate_name: hydroquinone

sequence_source: UniProtKB Q8GB87 direct lookup; Q8GB87_STRLA, Streptomyces lavendulae laccase, sequence version 1, reference PMID 14586105 / DOI 10.1271/bbb.67.2167.

enzyme: catechol oxidase

substrate: hydroquinone


substrate_name: catechol

substrate: catechol


substrate_name: Guaiacol

substrate: Guaiacol


organism: Pouteria sapota

substrate_name: pyrogallol

assay_conditions_summary: pH 7; 298.15 K; buffer 0.2 M sodium phosphate

proof_lines: isozyme PPO 1, in 0.2 M sodium phosphate buffer pH 7.0, 25°C

substrate: pyrogallol


substrate_name: DNA; dTTP

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

substrate: DNA; dTTP


substrate_name: dTTP; DNA

proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant A114V

substrate: dTTP; DNA


proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant A114T


proof_lines:
mutant enzyme Y115aminomethyl-Phe
mutant enzyme Y1152-naphthyl-Tyr


substrate_name: dATP

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

substrate: dATP


proof_lines: pH 8.3, 25°C, recombinant enzyme, HIV-1 O RT

proof_lines: pH 8.0, 37°C, reaction with poly(rA)*oligo(dT)20, enzyme from group M


organism: feline immunodeficiency virus


organism: feline leukemia virus


proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant A114S


proof_lines: SABIO-RK modifier species: RNA-directed DNA polymerase(Enzyme) mutant A114G


proof_lines: pH 8.2, 37°C, recombinant enzyme, substrate is poly(rA)-p(dT)45


organism: mouse mammary tumor virus


organism: prototype foamy virus

proof_lines: determined for TTP on the homopolymeric substrate poly(rA)/oligo(dT), pH and temperature not specified in the publication, recombinant His-tagged protease domain

proof_lines: determined for dNTPs on a heteropolymeric single stranded M13 substrate, pH and temperature not specified in the publication, recombinant His-tagged protease domain


organism: Rauscher murine leukemia virus

proof_lines:
pH 8.5, 37°C
reaction with poly(dA-dT)


organism: Simian foamy virus

substrate_name: deoxynucleoside triphosphate

substrate: deoxynucleoside triphosphate


organism: Simian immunodeficiency virus


organism: Streptococcus agalactiae

substrate_name: 2'-deoxyguanosine 5'-triphosphate

substrate: 2'-deoxyguanosine 5'-triphosphate


organism: Thermus aquaticus


organism: Camelus dromedarius

substrate_name: tributyrin

substrate: tributyrin


organism: Candida albicans

substrate_name: 4-nitrophenyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9P8W0 FASTA plus selected BRENDA mutation note and PMID 21747717 literature anchor and applied mutation signature S154L/S293L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S154L/S293L, at pH 6.0 and 25°C

substrate: 4-nitrophenyl butyrate


organism: Diutina rugosa

proof_lines: pH 7.0, 37°C, enzyme immobilized with glutaraldehyde


organism: Enterobacter cloacae

substrate_name: 4-nitrophenyl laurate

substrate: 4-nitrophenyl laurate


organism: Fervidobacterium changbaicum

substrate_name: 4-nitrophenyl caproate

substrate: 4-nitrophenyl caproate


organism: Geobacillus stearothermophilus

substrate_name: 4-nitrophenyl palmitate

substrate: 4-nitrophenyl palmitate


organism: Pseudomonas aeruginosa

substrate_name: triolein

assay_conditions_summary: pH 8; 303.15 K; buffer 0.1 M Tris-HCl

proof_lines: in 0.1 M Tris-HCl buffer (pH 8.0), at 40°C

substrate: triolein


organism: Pseudomonas reinekei


organism: Rattus norvegicus

proof_lines:
enzyme from microsomes
enzyme from plasma membrane
enzyme from cytosol


organism: Rhizomucor miehei

substrate_name: eugenol

proof_lines: chitosan-chitin nanowhiskers supported lipase, pH not specified in the publication, 50°C

substrate: eugenol


organism: Rhodotorula glutinis


organism: Saccharolobus solfataricus

substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


organism: Saccharomyces cerevisiae

substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Scorpio maurus


organism: Serratia marcescens


organism: Serratia sp. W3

proof_lines:
recombinant enzyme, at pH 8.5 and 45°C
native enzyme, at pH 8.5 and 45°C


organism: Sphingobacterium sp. Ab3

substrate_name: olive oil

substrate: olive oil


organism: Staphylococcus caprae


organism: Staphylococcus xylosus

proof_lines: pH 8.5, 37°C, recombinant His-tagged wild-type enzyme


proof_lines: pH 8.5, 37°C, recombinant His-tagged mutant D290A


organism: Streptomyces sp.


organism: Sus scrofa

proof_lines: apparent value, in the presence of inhibitor lupeol acetate, pH and temperature not specified in the publication

proof_lines: apparent value, in the presence of inhibitor orlistat, pH and temperature not specified in the publication

proof_lines: in the absence of inhibitor, pH and temperature not specified in the publication


organism: Tausonia pullulans


enzyme_display_name: trehalose-phosphatase

organism: Ancylostoma ceylanicum

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

enzyme: trehalose-phosphatase

substrate: Unknown


organism: Caenorhabditis elegans

substrate_name: trehalose 6-phosphate

sequence_source: UniProtKB reviewed accession Q9XTQ5; direct UniProt REST lookup on 2026-06-05; entry cites PMID 16197937.

substrate: trehalose 6-phosphate


organism: Cyberlindnera jadinii

sequence_source: UniProtKB unreviewed accession A0A060GZD2; direct UniProt REST lookup on 2026-06-05; entry cites PMID 24446217.

proof_lines:
recombinant enzyme, at pH 8.5 and 30°C
native enzyme, at pH 8.5 and 30°C


organism: Escherichia coli

proof_lines:
pH 7.5, 30°C
pH 7.5, 30°C, chimeric enzyme


organism: Haemonchus contortus


organism: Mycolicibacterium smegmatis


organism: Phormia regina

substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Propionibacterium freudenreichii subsp. shermanii

assay_conditions_summary: pH 6.5; 310.15 K; buffer MES

proof_lines: in MES buffer (50 mM, pH 6.5), 10 mM MgCl2, and 5 mM trehalose 6-phosphate, at 37°C


organism: Pseudomonas aeruginosa


organism: Rubrobacter xylanophilus


organism: Saccharomyces cerevisiae

substrate_name: H2O; Trehalose 6-phosphate

substrate: H2O; Trehalose 6-phosphate


enzyme_display_name: alpha-L-fucosidase

organism: Biomphalaria glabrata

substrate_name: 4-nitrophenyl alpha-L-fucopyranoside

proof_lines: 30°C, pH not specified in the publication

enzyme: alpha-L-fucosidase

substrate: 4-nitrophenyl alpha-L-fucopyranoside


organism: Bos taurus

substrate_name: p-nitrophenyl alpha-L-fucoside

proof_lines:
pH 6.8, 25°C, epididymis
pH 6.8, 25°C, kidney
competitive inhibition

substrate: p-nitrophenyl alpha-L-fucoside


organism: Canis lupus lupus


organism: Cavia porcellus


organism: Chamelea gallina


organism: Cricetulus griseus

assay_conditions_summary: pH 5

proof_lines:
at pH 5.0
at pH 7.0
competitive inhibition


enzyme_display_name: lacto-N-biosidase

organism: Bifidobacterium longum subsp. Longum

enzyme: lacto-N-biosidase


organism: [Clostridium] nexile


organism: [Ruminococcus] lactaris


organism: Streptomyces sp.


organism: Tyzzerella nexilis

substrate_name: p-Nitrophenyl lacto-N-bioside; H2O

mutation_type: truncation

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant TnXc C-terminal truncated (31-605)

substrate: p-Nitrophenyl lacto-N-bioside; H2O


organism: Bacillus fulminans


organism: Toxocara canis


enzyme_display_name: pyridoxal phosphatase

organism: Homo sapiens

substrate_name: H2O; Pyridoxal phosphate

enzyme: pyridoxal phosphatase

substrate: H2O; Pyridoxal phosphate


organism: Nicotiana tabacum

substrate_name: pyridoxal 5'-phosphate

substrate: pyridoxal 5'-phosphate


organism: Paenibacillus thiaminolyticus

proof_lines: 5 mM CoCl2, 1 mM dithiothreitol, 50 mM Tris/maleate pH 5.0, 37°C


organism: Sinorhizobium meliloti

assay_conditions_summary: pH 7


organism: Bifidobacterium bifidum JCM 1254

substrate_name: p-Nitrophenyl-lacto-N-bioside

substrate: p-Nitrophenyl-lacto-N-bioside


organism: Octopus vulgaris


organism: Pecten maximus

substrate_name: p-nitrophenyl alpha-L-fucopyranoside

substrate: p-nitrophenyl alpha-L-fucopyranoside


organism: Penaeus monodon


organism: Polititapes rhomboides


organism: Pomacea canaliculata

proof_lines:
isoform F1
isoform F2


organism: Prunus dulcis

substrate_name: lacto-N-fucopentaitol III

proof_lines:
alpha-fucosidase I
alpha-fucosidase II

substrate: lacto-N-fucopentaitol III


organism: Lacticaseibacillus rhamnosus


organism: Lamellidens corrianus


organism: Mercenaria mercenaria


organism: Mesocricetus auratus


organism: Mus musculus


organism: Niallia circulans

substrate_name: 2'-fucosyllactose; gastric mucin; 3'-fucosyllactose


organism: Dictyostelium discoideum


organism: Drosophila ananassae


organism: Emticicia oligotrophica


organism: Fusarium oxysporum


organism: Homo sapiens

proof_lines: pH 5.0, 37°C, undifferentiated HT-29 cells

proof_lines: pH 5.0, 37°C, differentiated HT-29 cells


organism: Lacticaseibacillus casei

substrate_name: 2-nitrophenyl alpha-L-fucopyranoside

substrate: 2-nitrophenyl alpha-L-fucopyranoside


organism: Saccharolobus solfataricus


proof_lines: mutant E292G at pH 6.3 in the presence of sodium phosphate or at pH 4.6 in the presence of sodium acetate


proof_lines:
mutant D242G
mutant enzyme D242G
pH 6.5, 65°C, D242G mutant


assay_conditions_summary: pH 4.6; buffer exact

proof_lines: mutant E58G, at pH 4.6, in the presence of sodium citrate

proof_lines: mutant E58G, at pH 6.3, in the presence of sodium phosphate and NaN3

proof_lines: mutant E58G, at pH 4.6, in the presence of sodium acetate


organism: Sus scrofa


organism: Thermotoga maritima

substrate_name: alpha-L-fucosyl fluoride

substrate: alpha-L-fucosyl fluoride


organism: Rattus sp.


proof_lines:
pH 6.5, 65°C, wild-type enzyme
pH5.0, 65°C, wild-type enzyme
wild-type, at pH 5.0


proof_lines:
pH 6.3, 65°C, mutant enzyme D124G
mutant D124G
mutant enzyme D124G


proof_lines:
pH 6.3, 65°C, mutant enzyme H46G
mutant enzyme H46G
mutant H46G


proof_lines:
pH 6.3, 65°C, mutant enzyme D146G
mutant D146G
mutant enzyme D146G


substrate_name: 4-nitrophenyl alpha-L-fucoside

sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 canonical sequence with mutation_signature substitutions applied during curation review and applied mutation signature G226S/T264A/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines:
mutant G226S/T264A/Y267F/L322P, at 70°C
mutant G226S/T264A/Y267F/L322P, at 40°C

substrate: 4-nitrophenyl alpha-L-fucoside


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 canonical sequence with mutation_signature substitutions applied during curation review and applied mutation signature T264A to reconstruct the assayed variant sequence.

proof_lines:
mutant T264A/L322P7, at 70°C
mutant T264A, at 70°C
mutant T264A, at 40°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 canonical sequence with mutation_signature substitutions applied during curation review and applied mutation signature P196L/Y237H/Y267F/G226S/T264A/L322P/M210V to reconstruct the assayed variant sequence.

proof_lines: mutant P196L/Y237H/Y267F and mutant G226S/Y237H/T264A/L322P, at 70°C. Mutant M210V/Y237H/T264A, at 40°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 canonical sequence with mutation_signature substitutions applied during curation review and applied mutation signature R147G/L322P/P196L/Y237H/Y267F/T264A to reconstruct the assayed variant sequence.

proof_lines: mutant R147G/L322P, mutant P196L/Y237H/Y267F and mutant T264A, at 40°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 canonical sequence with mutation_signature substitutions applied during curation review and applied mutation signature M210V/Y237H/T264A/Y267F to reconstruct the assayed variant sequence.

proof_lines:
mutant M210V/Y237H/T264A/Y267F, at 40°C
mutant M210V/Y237H/T264A/Y267F, at 70°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 canonical sequence with mutation_signature substitutions applied during curation review and applied mutation signature T264A/L322P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 plus RCSB/PDBe 1HL8 SIFTS mapping and applied mutation signature E66A to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 37°C, mutant E66A
pH 5.0, 25°C, mutant E66A


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 plus RCSB/PDBe 1HL8 SIFTS mapping and applied mutation signature P196L/Y237H/Y267F to reconstruct the assayed variant sequence.

proof_lines:
mutant P196L/Y237H/Y267F, at 70°C
mutant P196L/Y237H/Y267F, at 40°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 plus RCSB/PDBe 1HL8 SIFTS mapping and applied mutation signature M210V/Y237H/T264A to reconstruct the assayed variant sequence.

proof_lines:
mutant M210V/Y237H/T264A, at 70°C
mutant M210V/Y237H/T264A, at 40°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 plus RCSB/PDBe 1HL8 SIFTS mapping and applied mutation signature T264A/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines:
mutant T264A/Y267F/L322P, at 40°C
mutant T264A/Y267F/L322P, at 70°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9WYE2 plus RCSB/PDBe 1HL8 SIFTS mapping and applied mutation signature R147G/L322P to reconstruct the assayed variant sequence.

proof_lines:
mutant R147G/L322P, at 70°C
mutant R147G/L322P, at 40°C


sequence_source: UniProt Q9WYE2 plus RCSB/PDBe 1HL8 SIFTS mapping

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

proof_lines:
wild-type, at 70°C
wild-type, at 40°C
pH 5.0, 25°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 direct REST lookup plus row-specific reconstruction from the BRENDA mutation note and applied mutation signature M210V/Y237H/T264A/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines: mutant M210V/Y237H/T264A, at 70°C. Mutant T264A/Y267F/L322P, at 40°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 direct REST lookup plus row-specific reconstruction from the BRENDA mutation note and applied mutation signature G226S/Y237H/T264A/L322P to reconstruct the assayed variant sequence.

proof_lines:
mutant G226S/Y237H/T264A/L322P, at 40°C
mutant G226S/Y237H/T264A/L322P, at 70°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 direct REST lookup plus row-specific reconstruction from the BRENDA mutation note and applied mutation signature T264A/M210V/Y237H/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines: mutant T264A/L322P7 and mutant M210V/Y237H/T264A/Y267F/L322P, at 70°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 direct REST lookup plus row-specific reconstruction from the BRENDA mutation note and applied mutation signature Y237H/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines:
mutant Y237H/Y267F/L322P, at 70°C
mutant Y237H/Y267F/L322P, at 40°C


sequence_source: UniProtKB Q9WYE2 direct REST lookup

proof_lines:
pH 5.0, 60°C, immobilized enzyme
pH 5.0, 60°C, soluble enzyme


organism: Thermus sp.

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


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Coccidioides immitis

substrate_name: p-nitrophenyl-beta-D-glucopyranoside

enzyme: glucan 1,3-beta-glucosidase

substrate: p-nitrophenyl-beta-D-glucopyranoside


organism: Cyberlindnera jadinii

substrate_name: Laminarin

substrate: Laminarin


organism: Dichotomopilus indicus

substrate_name: Unknown

substrate: Unknown


organism: Euglena gracilis

substrate_name: Laminaripentaose

substrate: Laminaripentaose


organism: Fungi imperfecti


organism: Hordeum vulgare

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

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


organism: Kluyveromyces aestuarii

substrate_name: pustulan

proof_lines:
or 4.5 mg/ml
or 1.7 mg/ml

substrate: pustulan


organism: Phanerodontia chrysosporium

substrate_name: laminaritetraose

proof_lines:
30°C, pH 4.5, hydrolysis
30°C, pH 4.5, transglycosylation
30°C, pH 4.5, trynsglycosylation

substrate: laminaritetraose


organism: Rasamsonia emersonii

substrate_name: Laminaran

substrate: Laminaran


organism: Saccharomyces cerevisiae

substrate_name: gentiobiose

proof_lines:
pH 5.5, 30°C
under glycosylated form

substrate: gentiobiose


organism: Schizosaccharomyces japonicus


organism: Trichoderma harzianum

proof_lines:
or 2.08 mg/ml
molecular weight postulated to be 2448


organism: Trypanosoma congolense

proof_lines:
control semen
infected semen


organism: Unio elongatulus

proof_lines:
sperm-bound enzyme
gonad fluid enzyme


organism: Abracris flavolineata


organism: Aplysia kurodai


organism: Candida albicans

substrate_name: methylumbelliferyl-beta-glucoside

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

substrate: methylumbelliferyl-beta-glucoside


enzyme_display_name: chalcone synthase

organism: Medicago sativa

substrate_name: Malonyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 REST/FASTA direct check on 2026-06-05 and applied mutation signature C164S to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor CoA

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant C164S

enzyme: chalcone synthase

substrate: Malonyl-CoA


substrate_name: Chalcone synthase; Coenzyme A

sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 REST/FASTA direct check on 2026-06-05 and applied mutation signature N336H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant N336H

substrate: Chalcone synthase; Coenzyme A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature C164S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM potassium phosphate; cofactor CoA

column_label: Table 4: Malonyl-CoA Decarboxylation Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1). Table 4, row C164S; column kcat (x10^-3 min^-1) = 403; column Km (uM) = 23.0; column kcat/Km (s^-1 M^-1) = 292. captured primary segment: Malonyl-CoA | C164S | Table 4, row C164S | kcat 403 x 10^-3 min^-1 | Km 23.0 uM | kcat/Km 292 s^-1 M^-1

raw_value_unit_evidence: Table 4, row C164S: kcat = 403 x 10^-3 min^-1 (printed cell 403 in the column headed kcat (x10^-3 min^-1)); Km = 23.0 uM; printed kcat/Km = 292 s^-1 M^-1.

row_label: Table 4, row C164S


sequence_source: UniProtKB P30074 REST/FASTA direct check on 2026-06-05

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 REST/FASTA direct check on 2026-06-05 and applied mutation signature C164D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant C164D


sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 REST/FASTA direct check on 2026-06-05 and applied mutation signature H303D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant H303D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature F215S to reconstruct the assayed variant sequence.

column_label: Table 3: CHS Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1), printed in a p-Coumaroyl-CoA section and a Malonyl-CoA section. Table 3, p-Coumaroyl-CoA section, row F215S; column kcat (x10^-3 min^-1) = 24.1; column Km (uM) = 3.8; column kcat/Km (s^-1 M^-1) = 106. captured primary segment: p-Coumaroyl-CoA | F215S | Table 3, p-Coumaroyl-CoA section, row F215S | kcat 24.1 x 10^-3 min^-1 | Km 3.8 uM | kcat/Km 106 s^-1 M^-1

raw_value_unit_evidence: Table 3, p-Coumaroyl-CoA section, row F215S: kcat = 24.1 x 10^-3 min^-1 (printed cell 24.1 in the column headed kcat (x10^-3 min^-1)); Km = 3.8 uM; printed kcat/Km = 106 s^-1 M^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature N336A to reconstruct the assayed variant sequence.

column_label: Table 4: Malonyl-CoA Decarboxylation Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1). Table 4, row N336A; column kcat (x10^-3 min^-1) = 28.9; column Km (uM) = 67.8; column kcat/Km (s^-1 M^-1) = 7.1. captured primary segment: Malonyl-CoA | N336A | Table 4, row N336A | kcat 28.9 x 10^-3 min^-1 | Km 67.8 uM | kcat/Km 7.1 s^-1 M^-1

raw_value_unit_evidence: Table 4, row N336A: kcat = 28.9 x 10^-3 min^-1 (printed cell 28.9 in the column headed kcat (x10^-3 min^-1)); Km = 67.8 uM; printed kcat/Km = 7.1 s^-1 M^-1.

row_label: Table 4, row N336A


substrate_name: Malonyl-CoA; 4-Coumaroyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P30074 canonical sequence reconstructed with N336K substitution; UniProt mutagenesis feature cites PMID 10653632 for Asn336 variants. and applied mutation signature N336K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant N336K

substrate: Malonyl-CoA; 4-Coumaroyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature N336K to reconstruct the assayed variant sequence.

column_label: Table 4: Malonyl-CoA Decarboxylation Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1). Table 4, row N336K; column kcat (x10^-3 min^-1) = 13.5; column Km (uM) = 339; column kcat/Km (s^-1 M^-1) = 0.7. captured primary segment: Malonyl-CoA | N336K | Table 4, row N336K | kcat 13.5 x 10^-3 min^-1 | Km 339 uM | kcat/Km 0.7 s^-1 M^-1

raw_value_unit_evidence: Table 4, row N336K: kcat = 13.5 x 10^-3 min^-1 (printed cell 13.5 in the column headed kcat (x10^-3 min^-1)); Km = 339 uM; printed kcat/Km = 0.7 s^-1 M^-1.

row_label: Table 4, row N336K


column_label: Table 3: CHS Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1), printed in a p-Coumaroyl-CoA section and a Malonyl-CoA section. Table 3, p-Coumaroyl-CoA section, row N336K; column kcat (x10^-3 min^-1) = 0.7; column Km (uM) = 28.1; column kcat/Km (s^-1 M^-1) = 0.4. captured primary segment: p-Coumaroyl-CoA | N336K | Table 3, p-Coumaroyl-CoA section, row N336K | kcat 0.7 x 10^-3 min^-1 | Km 28.1 uM | kcat/Km 0.4 s^-1 M^-1

raw_value_unit_evidence: Table 3, p-Coumaroyl-CoA section, row N336K: kcat = 0.7 x 10^-3 min^-1 (printed cell 0.7 in the column headed kcat (x10^-3 min^-1)); Km = 28.1 uM; printed kcat/Km = 0.4 s^-1 M^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature H303Q to reconstruct the assayed variant sequence.

column_label: Table 4: Malonyl-CoA Decarboxylation Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1). Table 4, row H303Q; column kcat (x10^-3 min^-1) = 658; column Km (uM) = 25.2; column kcat/Km (s^-1 M^-1) = 435. captured primary segment: Malonyl-CoA | H303Q | Table 4, row H303Q | kcat 658 x 10^-3 min^-1 | Km 25.2 uM | kcat/Km 435 s^-1 M^-1

raw_value_unit_evidence: Table 4, row H303Q: kcat = 658 x 10^-3 min^-1 (printed cell 658 in the column headed kcat (x10^-3 min^-1)); Km = 25.2 uM; printed kcat/Km = 435 s^-1 M^-1.

row_label: Table 4, row H303Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature C164A to reconstruct the assayed variant sequence.

column_label: Table 4: Malonyl-CoA Decarboxylation Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1). Table 4, row C164A; column kcat (x10^-3 min^-1) = 415; column Km (uM) = 18.5; column kcat/Km (s^-1 M^-1) = 374. captured primary segment: Malonyl-CoA | C164A | Table 4, row C164A | kcat 415 x 10^-3 min^-1 | Km 18.5 uM | kcat/Km 374 s^-1 M^-1

raw_value_unit_evidence: Table 4, row C164A: kcat = 415 x 10^-3 min^-1 (printed cell 415 in the column headed kcat (x10^-3 min^-1)); Km = 18.5 uM; printed kcat/Km = 374 s^-1 M^-1.

row_label: Table 4, row C164A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature F215W to reconstruct the assayed variant sequence.

column_label: Table 3: CHS Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1), printed in a p-Coumaroyl-CoA section and a Malonyl-CoA section. Table 3, p-Coumaroyl-CoA section, row F215W; column kcat (x10^-3 min^-1) = 20.4; column Km (uM) = 30.4; column kcat/Km (s^-1 M^-1) = 11.1. captured primary segment: p-Coumaroyl-CoA | F215W | Table 3, p-Coumaroyl-CoA section, row F215W | kcat 20.4 x 10^-3 min^-1 | Km 30.4 uM | kcat/Km 11.1 s^-1 M^-1

raw_value_unit_evidence: Table 3, p-Coumaroyl-CoA section, row F215W: kcat = 20.4 x 10^-3 min^-1 (printed cell 20.4 in the column headed kcat (x10^-3 min^-1)); Km = 30.4 uM; printed kcat/Km = 11.1 s^-1 M^-1.


substrate_name: 4-Coumaroyl-CoA; Malonyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P30074 canonical sequence reconstructed with H303Q substitution; RCSB 1D6I and PMID 10653632 support the H303Q mutant context. and applied mutation signature H303Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant H303Q

substrate: 4-Coumaroyl-CoA; Malonyl-CoA


organism: Glycine max

sequence_variant_note: Resolved canonical sequence from UniProtKB P24826 FASTA; R58A reconstructed after confirming P24826 residue 58 is R. and applied mutation signature R58A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R58A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P24826 FASTA; K55A reconstructed after confirming P24826 residue 55 is K. and applied mutation signature K55A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K55A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P24826 FASTA; K268A reconstructed after confirming P24826 residue 268 is K. and applied mutation signature K268A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K268A, pH and temperature not specified in the publication


sequence_source: UniProtKB P24826 reviewed Swiss-Prot FASTA.

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

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


organism: Humulus lupulus

sequence_source: UniProtKB Q9FEY5 reviewed Swiss-Prot FASTA.


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


organism: Malus domestica

sequence_source: UniProtKB K9MUA0 TrEMBL FASTA; submission name CHS2 chalcone synthase, EC 2.3.1.74 from EMBL AFX71920.1.

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA


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

proof_lines:
pH 7.0, 37°C
Raw SKiD Env: Temp=37°C, pH=7

source_databases_merged: brenda skid


sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 direct REST lookup plus selected source mutation signature and applied mutation signature F215Y to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P30074 direct REST lookup plus selected source mutation signature

sequence_variant_note: Mutation signature N336D matches the mutant residue at offset +0 and the reference residue at offset -11; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 direct REST lookup plus selected source mutation signature and applied mutation signature H303N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant H303N


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature F215Y to reconstruct the assayed variant sequence.

column_label: Table 3: CHS Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1), printed in a p-Coumaroyl-CoA section and a Malonyl-CoA section. Table 3, p-Coumaroyl-CoA section, row F215Y; column kcat (x10^-3 min^-1) = 38.8; column Km (uM) = 18.3; column kcat/Km (s^-1 M^-1) = 35.3. captured primary segment: p-Coumaroyl-CoA | F215Y | Table 3, p-Coumaroyl-CoA section, row F215Y | kcat 38.8 x 10^-3 min^-1 | Km 18.3 uM | kcat/Km 35.3 s^-1 M^-1

raw_value_unit_evidence: Table 3, p-Coumaroyl-CoA section, row F215Y: kcat = 38.8 x 10^-3 min^-1 (printed cell 38.8 in the column headed kcat (x10^-3 min^-1)); Km = 18.3 uM; printed kcat/Km = 35.3 s^-1 M^-1.


sequence_source: UniProtKB P30074 direct REST lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 direct REST lookup plus selected source mutation signature and applied mutation signature H303A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant H303A