proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme and mutant E181Q


enzyme_display_name: sphingosine kinase

organism: Mus musculus

substrate_name: ATP

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03 and applied mutation signature E181Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: sphingosine kinase

substrate: ATP

source: brenda


substrate_name: sphingosine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03 and applied mutation signature D177N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: sphingosine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8CI15 direct lookup on 2026-06-03 and applied mutation signature E179Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

substrate_name: Unknown

km_display: Not reported

mutation_signature: Unknown

ki_unit: mM

sequence_source: UniProtKB:Q1HGK5 direct REST lookup; PMID 18028875 cross-check

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

substrate: Unknown


substrate_name: Sphingosine; ATP

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

sequence_source: UniProtKB:Q91V26 direct REST lookup; PMID 9575218 PubMed cross-check

assay_conditions_summary: cofactor ATP

substrate: Sphingosine; ATP


organism: Saccharomyces cerevisiae

substrate_name: Sphinganine; ATP

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

sequence_source: UniProtKB:Q12246 direct REST lookup; PMID 9677363 PubMed/UniProt cross-check

substrate: Sphinganine; ATP


sequence_source: UniProtKB:Q06147 direct REST lookup; PMID 9677363 PubMed/UniProt cross-check


enzyme_display_name: (d)CMP kinase

organism: Escherichia coli

substrate_name: dCMP

sequence_variant_note: Resolved canonical sequence from RCSB PDB 1KDO/1KDP/1KDR/1KDT SIFTS mapping to UniProtKB:P0A6I0; variant reconstructed from checked P0A6I0 sequence and applied mutation signature R181M to reconstruct the assayed variant sequence.

enzyme: (d)CMP kinase

substrate: dCMP


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1KDO/1KDP/1KDR/1KDT SIFTS mapping to UniProtKB:P0A6I0; variant reconstructed from checked P0A6I0 sequence and applied mutation signature S101A to reconstruct the assayed variant sequence.


sequence_source: RCSB PDB 1KDO/1KDP/1KDR/1KDT SIFTS mapping to UniProtKB:P0A6I0; canonical sequence from P0A6I0


substrate_name: CMP

sequence_variant_note: Resolved canonical sequence from RCSB PDB 1KDO/1KDP/1KDR/1KDT SIFTS mapping to UniProtKB:P0A6I0; variant reconstructed from checked P0A6I0 sequence and applied mutation signature D185A to reconstruct the assayed variant sequence.

substrate: CMP


substrate_name: UMP

source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132S substitution and applied mutation signature D132S to reconstruct the assayed variant sequence.

data_origin: experimental

substrate: UMP

source: oed


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132A substitution and applied mutation signature D132A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132A substitution


substrate_name: ATP; CMP

sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132H substitution and applied mutation signature D132H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant D132H

substrate: ATP; CMP


sequence_source: UniProt REST accession P0A6I0 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied R110M substitution and applied mutation signature R110M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132N substitution and applied mutation signature D132N to reconstruct the assayed variant sequence.


sequence_source: UniProt REST accession P0A6I0 canonical sequence with reviewer-applied D132S substitution


organism: Escherichia coli K-12

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature R110M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH

column_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373). The table carries one enzyme column, one nucleotide column and three numeric columns headed Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1). The cited cell set is the enzyme row R110M, nucleotide dCMP: column Km (mM) = 7.3; column kcat (s^-1) = 0.05; column kcat/Km (s^-1 mM^-1) = 0.0068.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.05 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 0.05 s^(-1). Km: printed Table 2 cell 7.3 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 7.3 mM. kcat/Km: printed Table 2 cell 0.0068 under the column head kcat/Km (s^-1 mM^-1); the printed unit is the canonical unit, so no unit conversion applies and the printed efficiency is 0.0068 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row R110M, nucleotide dCMP: Km = 7.3 mM; kcat = 0.05 s^-1; printed kcat/Km = 0.0068 s^-1 mM^-1.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature D132H to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373). The table carries one enzyme column, one nucleotide column and three numeric columns headed Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1). The cited cell set is the enzyme row D132H, nucleotide dCMP: column Km (mM) = 0.055; column kcat (s^-1) = 0.06; column kcat/Km (s^-1 mM^-1) = 1.1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.06 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 0.06 s^(-1). Km: printed Table 2 cell 0.055 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.055 mM. kcat/Km: printed Table 2 cell 1.1 under the column head kcat/Km (s^-1 mM^-1); the printed unit is the canonical unit, so no unit conversion applies and the printed efficiency is 1.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row D132H, nucleotide dCMP: Km = 0.055 mM; kcat = 0.06 s^-1; printed kcat/Km = 1.1 s^-1 mM^-1.


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature D132N to reconstruct the assayed variant sequence.

status: unverified


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature S36A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature R188M to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373). The table carries one enzyme column, one nucleotide column and three numeric columns headed Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1). The cited cell set is the enzyme row R188M, nucleotide dCMP: column Km (mM) = 0.77; column kcat (s^-1) = 0.04; column kcat/Km (s^-1 mM^-1) = 0.052.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.04 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 0.04 s^(-1). Km: printed Table 2 cell 0.77 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.77 mM. kcat/Km: printed Table 2 cell 0.052 under the column head kcat/Km (s^-1 mM^-1); the printed unit is the canonical unit, so no unit conversion applies and the printed efficiency is 0.052 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row R188M, nucleotide dCMP: Km = 0.77 mM; kcat = 0.04 s^-1; printed kcat/Km = 0.052 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature D132S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature D132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 direct REST lookup plus row-specific single-substitution reconstruction and applied mutation signature R110M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature S36A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant S36A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature R110M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature D132N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature R188M to reconstruct the assayed variant sequence.


substrate_name: CMP; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature R110M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant R110M

substrate: CMP; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature D132A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant D132A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature D132A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373). The table carries one enzyme column, one nucleotide column and three numeric columns headed Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1). The cited cell set is the enzyme row D132A, nucleotide dCMP: column Km (mM) = 1.8; column kcat (s^-1) = 0.73; column kcat/Km (s^-1 mM^-1) = 0.40.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.73 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 0.73 s^(-1). Km: printed Table 2 cell 1.8 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 1.8 mM. kcat/Km: printed Table 2 cell 0.40 under the column head kcat/Km (s^-1 mM^-1); the printed unit is the canonical unit, so no unit conversion applies and the printed efficiency is 0.40 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row D132A, nucleotide dCMP: Km = 1.8 mM; kcat = 0.73 s^-1; printed kcat/Km = 0.40 s^-1 mM^-1.


sequence_source: UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03

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 reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature S36A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature R188M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature D132S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A6I0 direct REST/FASTA check on 2026-06-03 and applied mutation signature D132N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant D132N


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature D132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature D132S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature S36A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature R188M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 FASTA/REST lookup performed on 2026-06-03; reviewed KCY_ECOLI cytidylate kinase, Escherichia coli strain K12, EC 2.7.4.25. and applied mutation signature D132N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03 and applied mutation signature R188M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03

proof_lines: wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03 and applied mutation signature D132A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03 and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A6I0 REST/FASTA direct check on 2026-06-03 and applied mutation signature S36A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


enzyme_display_name: Cytidylate kinase / CMP kinase

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; D132N reconstructed by direct residue substitution. and applied mutation signature D132N to reconstruct the assayed variant sequence.

enzyme: Cytidylate kinase / CMP kinase


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; D132H reconstructed by direct residue substitution. and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; R110M reconstructed by direct residue substitution. and applied mutation signature R110M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; D132S reconstructed by direct residue substitution. and applied mutation signature D132S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C


sequence_source: UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; R110M reconstructed by direct residue substitution.


sequence_source: UniProtKB:P0A6I0 canonical sequence checked 2026-06-03; D132N reconstructed by direct residue substitution.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6I0 and applied mutation signature D132A to reconstruct the assayed variant sequence.

row_label: Table 2, enzyme row D132A, nucleotide dCMP

table_label: Table 2: Kinetic parameters of E. coli CMP kinase variants with three NMP substrates at a single fixed concentration of ATP (1 mM) (FEBS Journal 274 (2007) 3363-3373)


source_db: brenda, skid

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

sequence_source: UniProtKB:P0A6I0 canonical sequence checked 2026-06-03.

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

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C

source_databases_merged: brenda skid

source: brenda, skid


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WPA9

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


enzyme_display_name: estrone sulfotransferase

organism: Cavia porcellus

substrate_name: Estrone; 3'-Phosphoadenylyl sulfate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature S262A/D264A/N267A and applied mutation signature S262A/D264A/N267A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant S262A D264A N267A

enzyme: estrone sulfotransferase

substrate: Estrone; 3'-Phosphoadenylyl sulfate


sequence_source: UniProtKB reviewed accession P49887


substrate_name: 3'-Phosphoadenylyl sulfate; Estrone

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature G263A and applied mutation signature G263A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G263A

substrate: 3'-Phosphoadenylyl sulfate; Estrone


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature S262A/D264A and applied mutation signature S262A/D264A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant S262A D264A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature G260A/K266A and applied mutation signature G260A/K266A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G260A K266A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature G260A and applied mutation signature G260A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G260A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P49887 plus reconstructed mutation signature G263A/K266A and applied mutation signature G263A/K266A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G263A K266A


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

sequence_source: UniProtKB:P0A6I0 REST lookup

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.4


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature D132H and applied mutation signature D132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature S36A and applied mutation signature S36A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature R188M and applied mutation signature R188M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant R188M


sequence_source: reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature D132H


proof_lines:
wild-type enzyme
wild type


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P0A6I0 canonical sequence plus selected-row mutation_signature D132S and applied mutation signature D132S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (d)CMP kinase(Enzyme) mutant D132S


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature T51V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant T51V


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature K106R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K106R


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature K106A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K106A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature K48R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K48R


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

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant H108K GST-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature K106S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K106S


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature Y240F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant Y240F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 canonical sequence; direct reconstruction from selected mutation_signature and applied mutation signature T52V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant T52V


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49887/ST1E1_CAVPO; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature K266A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K266A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49887/ST1E1_CAVPO; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature G260A/G263A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant G260A G263A


organism: Homo sapiens

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

sequence_source: UniProtKB reviewed P49888/ST1E1_HUMAN; direct UniProtKB REST/FASTA check 2026-06-03

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

assay_conditions_summary: pH 6.5; 310.15 K; buffer 50 mM Tris/HCl

proof_lines: SULT1E1, pH and temperature not specified in the publication

proof_lines: isoform SULT1E1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C

source_databases_merged: sabio_rk brenda skid


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888/ST1E1_HUMAN; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature V145E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant V145E His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888/ST1E1_HUMAN; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature K85A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant K85A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888/ST1E1_HUMAN; direct UniProtKB REST/FASTA check 2026-06-03 and applied mutation signature S137A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant hEST S137A


substrate_name: 3'-Phosphoadenylyl sulfate

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

substrate: 3'-Phosphoadenylyl sulfate


substrate_name: nitrobenzoxadiazole-labeled sphingosine

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

proof_lines: pH 7.4, 35°C, presence of 25 microM 3-O-sulfogalactosylceramide

proof_lines: pH 7.4, 35°C, presence of 10 microM 3-O-sulfogalactosylceramide

substrate: nitrobenzoxadiazole-labeled sphingosine


organism: Unknown

substrate_name: estradiol

substrate: estradiol


enzyme_display_name: mevalonate kinase

enzyme: mevalonate kinase


enzyme_display_name: steroid 21-monooxygenase

organism: Bos taurus

substrate_name: progesterone

source_db: uniprot

enzyme: steroid 21-monooxygenase

substrate: progesterone

source: uniprot


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: (RS)-mevalonate (at 70 degrees Celsius)

smiles: CC(CCO)(CC(=O)[O-])O

substrate: (RS)-mevalonate (at 70 degrees Celsius)


substrate_name: (R,S)-mevalonate

substrate: (R,S)-mevalonate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: mevalonate

substrate: mevalonate


substrate_name: sphingosine

proof_lines: kcat is 124 sec(-1) for sphingosine and increases to 304 sec(-1) upon interaction with EEF1A1.

substrate: sphingosine


substrate_name: Acetyl-CoA (in presence of 10 uM of sphingosine)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 0.0185 min(-1) for Acetyl-CoA as substrate.


proof_lines: kcat is 55 min(-1) with (24S)-hydroxycholesterol.


substrate_name: PAPS

proof_lines: kcat is 23.5 sec(-1) with estradiol as substrate.

substrate: PAPS


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


assay_conditions_summary: pH 7.4; 310.15 K; buffer 50 mM potassium phosphate

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific S137C reconstruction and applied mutation signature S137C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific S137C reconstruction

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant hEST S137C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific E12G/N29D/D65N/C83R/N87D/M98V/F138Y/G182S/L195M/H224K reconstruction and applied mutation signature E12G/N29D/D65N/C83R/N87D/M98V/F138Y/G182S/L195M/H224K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E12G/N29D/D65N/C83R/N87D/M98V/F138Y/G182S/L195M/H224K, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication


sequence_source: UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup

proof_lines: wild type enzyme, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific K85E/A135T/F138Y/G182S/L251V reconstruction and applied mutation signature K85E/A135T/F138Y/G182S/L251V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K85E/A135T/F138Y/G182S/L251V, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49888 / ST1E1_HUMAN direct REST lookup with row-specific D65N/K85E/E86K/F138Y reconstruction and applied mutation signature D65N/K85E/E86K/F138Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D65N/K85E/E86K/F138Y, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication


sequence_source: UniProtKB reviewed P49891 / ST1E1_MOUSE direct REST lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P49891 / ST1E1_MOUSE direct REST lookup with row-specific T45V reconstruction and applied mutation signature T45V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: estrone sulfotransferase(Enzyme) mutant T45V


organism: Arabidopsis thaliana

substrate_name: phytosphingosine

substrate: phytosphingosine


substrate_name: dihydrosphingosine

substrate: dihydrosphingosine


substrate_name: sphinganine

substrate: sphinganine


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: CMP

substrate: CMP


proof_lines: mutant enzyme D322G, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C


proof_lines: mutant enzyme A265V, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C


organism: Oncorhynchus mykiss

proof_lines:
liver microsomes
head kidney microsomes


organism: Aedes aegypti

substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

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

substrate: ATP


organism: Agave americana


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH 7.5, 30°C, recombinant S201A mevalonate kinase


proof_lines: pH 7.5, 30°C, recombinant S145A mutant mevalonate kinase

proof_lines: pH 7.5, 30°C, recombinant S145A mevalonate kinase


proof_lines: pH 7.5, 30°C, recombinant T243A mevalonate kinase


assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup with row-specific E19D reconstruction and applied mutation signature E19D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup with row-specific D204N reconstruction and applied mutation signature D204N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup with row-specific E296Q reconstruction and applied mutation signature E296Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup with row-specific E193Q reconstruction and applied mutation signature E193Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q03426 / KIME_HUMAN direct REST lookup

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: pH 7.0, 25°C, recombinant mevalonate kinase


organism: Methanocaldococcus jannaschii

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q58487 / MVK_METJA direct REST lookup with row-specific K272R reconstruction and applied mutation signature K272R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 307.15 K; cofactor ATP

proof_lines: pH 7.5, 34°C, K272R mutant mevalonate kinase


sequence_source: UniProtKB Q58487 direct lookup resolved the Methanocaldococcus jannaschii mevalonate kinase canonical sequence; no row-specific R196L variant sequence was accepted because the paper names Arg196Lys instead.

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, 34°C, R196L mutant mevalonate kinase


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58487 direct lookup; variant sequence reconstructed by changing canonical residue R196 to V after confirming residue 196=R. and applied mutation signature R196V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 34°C, R196V mutant mevalonate kinase


sequence_source: UniProtKB Q58487 direct lookup resolved the canonical wild-type mevalonate kinase sequence.

proof_lines: pH 8.0, 70°C, recombinant mevalonate kinase


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58487 direct lookup; variant sequence reconstructed by changing canonical residue R196 to Q after confirming residue 196=R. and applied mutation signature R196Q to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 34°C, R196Q mutant mevalonate kinase


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58487 direct lookup; variant sequence reconstructed by changing canonical residue K272 to A after confirming residue 272=K. and applied mutation signature K272A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 34°C, K272A mutant mevalonate kinase


substrate_name: (R)-mevalonate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q58487 direct lookup; variant sequence reconstructed by changing canonical residue C281 to A after confirming residue 281=C. and applied mutation signature C281A to reconstruct the assayed variant sequence.

substrate: (R)-mevalonate


organism: Methanosarcina mazei

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

assay_conditions_summary: pH 7.6; 303.15 K; cofactor ATP

proof_lines: apparent value, in 50 mM Tris, 50 mM NaCl (pH 7.6), at 30°C


organism: Oryctolagus cuniculus

substrate_name: DL-mevalonate

substrate: DL-mevalonate


organism: Phaseolus vulgaris

proof_lines: pH 7.0, 30°C, enzyme from etiolated cotyledons


organism: Pinus pinaster

assay_conditions_summary: pH 7.9; 310.15 K; cofactor ATP


organism: Rattus norvegicus

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines:
H20Y mutant enzyme enzyme, pH 7.5, 25°C
H20Y mutant enzyme, pH 7.5, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C107S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C107A/C281A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03

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 reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C107A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C281S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q58487 (MVK_METJA); sequence fetched from UniProt REST on 2026-06-03 and applied mutation signature C107S/C281S to reconstruct the assayed variant sequence.


organism: Arachis hypogaea

substrate_name: (R)-Mevalonate; ATP

substrate: (R)-Mevalonate; ATP


organism: Catharanthus roseus


organism: Cucumis melo


organism: Enterococcus faecalis

substrate_name: GTP

sequence_source: NCBI Protein NP_814642.1; PMID 14767074 / PMC2286734 paper names NP_814642 as the E. faecalis mvaK1 open reading frame and reports the expressed mevalonate kinase.

assay_conditions_summary: pH 10; 310.15 K; cofactor ATP

substrate: GTP


organism: Hevea brasiliensis


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03426 canonical human MVK sequence; reconstructed S146A using PMID 11278915 and the selected BRENDA note. and applied mutation signature S146A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, recombinant S146A mevalonate kinase


organism: Sarcophaga bullata


organism: Staphylococcus aureus

substrate_name: R,S-mevalonate

proof_lines: PMID 14679225 full text reports R,S-mevalonate Km 41 ± 3 μM under pH 7.5, 30°C assay context.

substrate: R,S-mevalonate


organism: Sus scrofa

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
pH 8.0
liver mevalonate kinase
pH 6.5, 30°C, at 1 mM Mg2+


substrate_name: D-(+)-erythro-sphinganine

substrate: D-(+)-erythro-sphinganine


organism: Tetrahymena pyriformis


organism: Bacillus subtilis

proof_lines: at 30°C in 50mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1mM phosphoenolpyruvate, 0.2 mM NADH


organism: Escherichia coli

substrate_name: dGMP

proof_lines:
reaction with ATP
pH 7.4, 30°C
pH 7.4, reaction with CMP

substrate: dGMP


organism: Mycobacterium tuberculosis

substrate_name: dCMP

proof_lines: pH and temperature not specified in the publication

substrate: dCMP


organism: Bos taurus


organism: Cavia porcellus

proof_lines:
pH 7.4, 37°C
pH 7.4, 37°C, competitive inhibition


substrate_name: dehydroepiandrosterone

sequence_variant_note: Resolved canonical sequence from direct_uniprot_lookup:P49888_with_K85A_reconstruction and applied mutation signature K85A to reconstruct the assayed variant sequence.

proof_lines:
pH 7.0, 37°C, SULT1E1-K85A
pH 7.0, 37°C, mutant SULT1E1-K85A

substrate: dehydroepiandrosterone


proof_lines:
pH 7.0, 25°C
ATP in form of MgATP2-
native enzyme, pH 7.5, 25°C


proof_lines: pH 7.0, 30°C, K13M mutant mevalonate kinase


organism: Ricinus communis


organism: Saccharomyces cerevisiae


substrate_name: estrone

sequence_variant_note: Resolved canonical sequence from UniProtKB:P49888 reviewed human SULT1E1 canonical sequence; PubMed 11006110 describes human SULT1E1 V145E mutagenesis; direct residue check found P49888 residue 145 is V. and applied mutation signature V145E to reconstruct the assayed variant sequence.

proof_lines:
pH 7.0, 37°C, SULT1E1-V145E
pH 7.0, 37°C, mutant SULT1E1-V145E

substrate: estrone


sequence_source: UniProtKB:P49888 reviewed human SULT1E1 canonical sequence from direct EC 2.8.2.4 + Homo sapiens lookup.

proof_lines:
pH 6.1, 25°C
pH 6.3, 37°C forward reaction
pH 6.3, 37°C, reverse reaction


organism: Mus musculus

substrate_name: estradiol

sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 reviewed mouse SULT1E1 canonical sequence; selected BRENDA note and PubMed 10514486 identify Y81L estrogen sulfotransferase mutagenesis; direct residue check found P49891 residue 81 is Y. and applied mutation signature Y81L to reconstruct the assayed variant sequence.

substrate: estradiol


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 reviewed mouse SULT1E1 canonical sequence; selected BRENDA note and PubMed 10514486 identify Y81L/F142L estrogen sulfotransferase mutagenesis; direct residue check found P49891 residues 81=Y and 142=F. and applied mutation signature Y81L/F142L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49891 reviewed mouse SULT1E1 canonical sequence; selected BRENDA note and PubMed 10514486 identify Y81F estrogen sulfotransferase mutagenesis; direct residue check found P49891 residue 81 is Y. and applied mutation signature Y81F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P49891 reviewed mouse SULT1E1 canonical sequence from direct EC 2.8.2.4 + Mus musculus lookup.


substrate_name: androstenediol

sequence_variant_note: Resolved canonical sequence from Reconstructed F142L from UniProtKB reviewed P49891 (ST1E1_MOUSE) after direct residue check; RCSB 1AQU maps murine estrogen sulfotransferase to P49891 with full UniProt coverage. and applied mutation signature F142L to reconstruct the assayed variant sequence.

substrate: androstenediol


sequence_variant_note: Resolved canonical sequence from Reconstructed Y81A from UniProtKB reviewed P49891 (ST1E1_MOUSE); PubMed 10514486 studies Tyr-81 EST mutants and RCSB 1AQU maps murine estrogen sulfotransferase to P49891. and applied mutation signature Y81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed F142A from UniProtKB reviewed P49891 (ST1E1_MOUSE); PubMed 10514486 studies Phe-142 EST mutants and RCSB 1AQU maps murine estrogen sulfotransferase to P49891. and applied mutation signature F142A to reconstruct the assayed variant sequence.


organism: Rattus norvegicus


substrate_name: gamma-undecanoiclactone

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

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM Tris

proof_lines: isozyme 192Q, in 50 mM HEPES (pH 7.4), 37°C

substrate: gamma-undecanoiclactone


organism: Clonostachys rosea

substrate_name: zearalenone

sequence_variant_note: Resolved canonical sequence from Reconstructed V153H from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature V153H to reconstruct the assayed variant sequence.

substrate: zearalenone


sequence_variant_note: Resolved canonical sequence from Reconstructed F222K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature F222K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed D157K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature D157K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed V158H from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature V158H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed D133K/D157K/E171K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature D133K/D157K/E171K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D133K/D157K/E171K, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from Reconstructed D133K/D157K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature D133K/D157K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D133K/D157K, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from Reconstructed N152K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature N152K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed D57K from UniProtKB reviewed Q8NKB0/ZHD_BIOOC canonical sequence after direct residue check; selected BRENDA source snapshots provide Q8NKB0, Clonostachys rosea, zearalenone, and the mutation note. and applied mutation signature D57K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature E145K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature E171K to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q8NKB0 REST lookup on 2026-06-03

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 Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature D133K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature L155K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature D133K/E171K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D133K/E171K, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature M154H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature D157K/E171K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D157K/E171K, at pH 8.0 and 37°C


organism: Saccharolobus islandicus

substrate_name: nonanoic-gamma-lactone

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:C4KKZ9 and applied mutation signature Y34Q to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH not specified in the publication, mutant enzyme Y34Q

substrate: nonanoic-gamma-lactone


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

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:C4KKZ9 and applied mutation signature E14K/Y34Q to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q

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


substrate_name: dodecanoic-gamma-lactone

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

substrate: dodecanoic-gamma-lactone


organism: Saccharolobus solfataricus

substrate_name: N-octanoylhomoserine lactone

substrate: N-octanoylhomoserine lactone


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

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q97VT7 and applied mutation signature W263T to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q97VT7 and applied mutation signature W263I to reconstruct the assayed variant sequence.


substrate_name: delta-undecanolactone

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q97VT7 and applied mutation signature W263L to reconstruct the assayed variant sequence.

substrate: delta-undecanolactone


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q97VT7 and applied mutation signature W263V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt direct accession lookup on 2026-06-03 and applied mutation signature E219K to reconstruct the assayed variant sequence.


organism: Fusarium proliferatum

substrate_name: DL-pantoyllactone

sequence_source: UniProt direct accession lookup on 2026-06-03

substrate: DL-pantoyllactone


organism: Homo sapiens

substrate_name: dihydrocoumarin

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

proof_lines:
25°C, enzyme variant R192
25°C, enzyme variant Q192

substrate: dihydrocoumarin


substrate_name: 5-Valerolactone; H2O

sequence_variant_note: Resolved canonical sequence from UniProt direct accession lookup on 2026-06-03 and applied mutation signature H134Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: SABIO-RK modifier species: 1,4-lactonase(Enzyme) mutant H134Q

substrate: 5-Valerolactone; H2O


substrate_name: delta-valerolactone

proof_lines:
pH 8.0, wild-type enzyme
wild-type, pH 8.3, 25°C

substrate: delta-valerolactone


substrate_name: H2O; 5-(Thiobutyl)butyrolactone

sequence_variant_note: Resolved canonical sequence from UniProt direct accession lookup on 2026-06-03 and applied mutation signature H115Q/H134Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 1,4-lactonase(Enzyme) mutant H115Q/H134Q

substrate: H2O; 5-(Thiobutyl)butyrolactone


substrate_name: H2O; 5-Valerolactone

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

assay_conditions_summary: pH 8; buffer notes

proof_lines: pH 8.3, activity buffer with 0.1% tergitol

proof_lines: isoform PON1, pH and temperature not specified in the publication

substrate: H2O; 5-Valerolactone


substrate_name: gamma-undecanolactone

sequence_variant_note: Resolved canonical sequence from UniProtKB Q97VT7 direct REST lookup; W263M reconstructed from canonical sequence and applied mutation signature W263M to reconstruct the assayed variant sequence.

substrate: gamma-undecanolactone


sequence_variant_note: Resolved canonical sequence from UniProtKB Q97VT7 direct REST lookup; W263F reconstructed from canonical sequence and applied mutation signature W263F to reconstruct the assayed variant sequence.


organism: Sulfolobus acidocaldarius

sequence_source: UniProtKB Q4J6Z8 direct REST lookup

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


organism: Vulcanisaeta moutnovskia

substrate_name: octanoyl-L-homoserine lactone

sequence_source: UniProtKB F0QXN6 direct REST lookup

proof_lines: pH 8.3, temperature not specified in the publication

substrate: octanoyl-L-homoserine lactone


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA direct accession check and applied mutation signature H115Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 1,4-lactonase(Enzyme) mutant H115Q


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA direct accession check and applied mutation signature H115W to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST FASTA direct accession check


substrate_name: 3-oxo-dodecanoyl L-homoserine lactone

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA direct accession check and applied mutation signature S311C to reconstruct the assayed variant sequence.

substrate: 3-oxo-dodecanoyl L-homoserine lactone


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA direct accession check and applied mutation signature A148G to reconstruct the assayed variant sequence.


proof_lines: 25°C, pH not specified in the publication, mutant enzyme E14K


organism: Agrobacterium tumefaciens

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


substrate_name: patulin

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

substrate: patulin


substrate_name: gamma-hydroxybutyrate

substrate: gamma-hydroxybutyrate


organism: synthetic construct

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris

proof_lines: recombinant lactonase, in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C


organism: uncultured marine bacterium

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

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


enzyme_display_name: manganese peroxidase

organism: Moniliophthora roreri

substrate_name: veratryl alcohol

sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.

enzyme: manganese peroxidase

substrate: veratryl alcohol


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W/F259M with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W/A269R with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W/K168V with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


substrate_name: Reactive Black 5

sequence_source: UniProtKB:V2XS39 plus row mutation_signature reconstruction

substrate: Reactive Black 5


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W/I171V with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


organism: Irpex lacteus

sequence_variant_note: Resolved canonical sequence from UniProtKB:S4W784 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Irpex lacteus, EMBL AGO86670.2 evidence and applied mutation signature E166Q to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 30°C, recombinant mutant E166Q, in absence of Mn2+


sequence_source: UniProtKB:S4W784 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Irpex lacteus, EMBL AGO86670.2 evidence


sequence_variant_note: Resolved canonical sequence from UniProtKB:S4W784 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Irpex lacteus, EMBL AGO86670.2 evidence and applied mutation signature E166D to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 30°C, recombinant mutant E166D, in absence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence and applied mutation signature A172W/A269R with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence and applied mutation signature A172W/F259M with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence and applied mutation signature A172W/K168V with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence and applied mutation signature A172W with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence


organism: Gelatoporia subvermispora

sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/M2REM6 (retrieved 2026-06-03) and applied mutation signature S168W with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


substrate_name: Mn(II)

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

substrate: Mn(II)


sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/M2REM6 (retrieved 2026-06-03) and applied mutation signature T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


verification_status: verified

smiles: OO

column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'H2O2', Il-MnP6 block; column 'pH' = 4.5; column 'Temperature' = 30; the 'Kinetic constants' column of that block prints 'Km' = 194 (uM), 'kcat' = 879 (s^-1) and 'kcat/Km' = 4.5 x 10^6 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 194 uM; 194 / 1000 = 0.194 mM; the exported value is 0.194 mM. kcat: printed Table 2 cell 879 s^-1; already in s^-1, no unit conversion applies; the exported value is 879.0 s^(-1). kcat/Km: the exported value 4530.927835051546 s^(-1)*mM^(-1) is the full-precision quotient 879.0 / 0.194 of the two printed component cells; the paper's printed efficiency cell is 4.5 x 10^6 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 4500.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'H2O2': Km = 194 uM; kcat = 879 s^-1; printed kcat/Km = 4.5 x 10^6 s^-1 M^-1; printed pH = 4.5; printed temperature = 30 C.

table_label: Table 2: Kinetic parameters - Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1) of Il-DyP4 and Il-MnP6 for substrates oxidation obtained based on the optimal pH and temperature (C) (AMB Express 2018, 8:119)

status: verified


substrate_name: Reactive Blue 19

sequence_source: UniProt REST/FASTA direct lookup for A0A2P1C6N7

proof_lines: pH 3.0, 35°C, recombinant His6-tagged enzyme

proof_lines: pH 3.5, 45°C, recombinant His6-tagged enzyme

proof_lines: pH 4.0, 45°C, recombinant His6-tagged enzyme

substrate: Reactive Blue 19


column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'ABTS', Il-MnP6 block; column 'pH' = 3.5; column 'Temperature' = 45; the 'Kinetic constants' column of that block prints 'Km' = 83 (uM), 'kcat' = 245 (s^-1) and 'kcat/Km' = 3.0 x 10^6 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 83 uM; 83 / 1000 = 0.083 mM; the exported value is 0.083 mM. kcat: printed Table 2 cell 245 s^-1; already in s^-1, no unit conversion applies; the exported value is 245.0 s^(-1). kcat/Km: the exported value 2951.8072289156626 s^(-1)*mM^(-1) is the full-precision quotient 245.0 / 0.083 of the two printed component cells; the paper's printed efficiency cell is 3.0 x 10^6 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 3000.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'ABTS': Km = 83 uM; kcat = 245 s^-1; printed kcat/Km = 3.0 x 10^6 s^-1 M^-1; printed pH = 3.5; printed temperature = 45 C.


column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'Mn2+', Il-MnP6 block; column 'pH' = 4.5; column 'Temperature' = 30; the 'Kinetic constants' column of that block prints 'Km' = 129 (uM), 'kcat' = 369 (s^-1) and 'kcat/Km' = 2.9 x 10^6 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 129 uM; 129 / 1000 = 0.129 mM; the exported value is 0.129 mM. kcat: printed Table 2 cell 369 s^-1; already in s^-1, no unit conversion applies; the exported value is 369.0 s^(-1). kcat/Km: the exported value 2860.4651162790697 s^(-1)*mM^(-1) is the full-precision quotient 369.0 / 0.129 of the two printed component cells; the paper's printed efficiency cell is 2.9 x 10^6 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 2900.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'Mn2+': Km = 129 uM; kcat = 369 s^-1; printed kcat/Km = 2.9 x 10^6 s^-1 M^-1; printed pH = 4.5; printed temperature = 30 C.


column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'DMP', Il-MnP6 block; column 'pH' = 4.5; column 'Temperature' = 55; the 'Kinetic constants' column of that block prints 'Km' = 53 (uM), 'kcat' = 989 (s^-1) and 'kcat/Km' = 1.9 x 10^7 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 53 uM; 53 / 1000 = 0.053 mM; the exported value is 0.053 mM. kcat: printed Table 2 cell 989 s^-1; already in s^-1, no unit conversion applies; the exported value is 989.0 s^(-1). kcat/Km: the exported value 18660.377358490565 s^(-1)*mM^(-1) is the full-precision quotient 989.0 / 0.053 of the two printed component cells; the paper's printed efficiency cell is 1.9 x 10^7 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 19000.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'DMP': Km = 53 uM; kcat = 989 s^-1; printed kcat/Km = 1.9 x 10^7 s^-1 M^-1; printed pH = 4.5; printed temperature = 55 C.


substrate_name: guaiacol

column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'Guaiacol', Il-MnP6 block; column 'pH' = 4; column 'Temperature' = 45; the 'Kinetic constants' column of that block prints 'Km' = 2.6 (uM), 'kcat' = 184 (s^-1) and 'kcat/Km' = 7.1 x 10^7 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 2.6 uM; 2.6 / 1000 = 0.0026 mM; the exported value is 0.0026 mM. kcat: printed Table 2 cell 184 s^-1; already in s^-1, no unit conversion applies; the exported value is 184.0 s^(-1). kcat/Km: the exported value 70769.23076923077 s^(-1)*mM^(-1) is the full-precision quotient 184.0 / 0.0026 of the two printed component cells; the paper's printed efficiency cell is 7.1 x 10^7 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 71000.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'Guaiacol': Km = 2.6 uM; kcat = 184 s^-1; printed kcat/Km = 7.1 x 10^7 s^-1 M^-1; printed pH = 4; printed temperature = 45 C.

substrate: guaiacol


column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'RBlack 5', Il-MnP6 block; column 'pH' = 3; column 'Temperature' = 35; the 'Kinetic constants' column of that block prints 'Km' = 4.4 (uM), 'kcat' = 0.06 (s^-1) and 'kcat/Km' = 1.5 x 10^4 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 4.4 uM; 4.4 / 1000 = 0.0044 mM; the exported value is 0.0044 mM. kcat: printed Table 2 cell 0.06 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.06 s^(-1). kcat/Km: printed Table 2 cell 1.5 x 10^4 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 1.5 x 10^4 / 1000 = 15.0 s^-1 mM^-1, which is the value proposed for the efficiency metric.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'RBlack 5': Km = 4.4 uM; kcat = 0.06 s^-1; printed kcat/Km = 1.5 x 10^4 s^-1 M^-1; printed pH = 3; printed temperature = 35 C.


column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'RBlue 19', Il-MnP6 block; column 'pH' = 3; column 'Temperature' = 35; the 'Kinetic constants' column of that block prints 'Km' = 81 (uM), 'kcat' = 7.3 (s^-1) and 'kcat/Km' = 9.0 x 10^4 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 81 uM; 81 / 1000 = 0.081 mM; the exported value is 0.081 mM. kcat: printed Table 2 cell 7.3 s^-1; already in s^-1, no unit conversion applies; the exported value is 7.3 s^(-1). kcat/Km: the exported value 90.12345679012346 s^(-1)*mM^(-1) is the full-precision quotient 7.3 / 0.081 of the two printed component cells; the paper's printed efficiency cell is 9.0 x 10^4 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 90.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'RBlue 19': Km = 81 uM; kcat = 7.3 s^-1; printed kcat/Km = 9.0 x 10^4 s^-1 M^-1; printed pH = 3; printed temperature = 35 C.


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct lookup for S4W784 plus local E166D reconstruction and applied mutation signature E166D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:S4W784 / NCBI Protein:AGO86670.2 with E166G and applied mutation signature E166G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:S4W784 / NCBI Protein:AGO86670.2 with E166D and applied mutation signature E166D to reconstruct the assayed variant sequence.


sequence_source: reconstructed from UniProtKB:S4W784 / NCBI Protein:AGO86670.2 with E166G


sequence_source: UniProtKB:S4W784 / NCBI Protein:AGO86670.2

proof_lines: pH 4.0, 30°C, recombinant wild-type enzyme, in presence of Mn2+

proof_lines: pH 7.4, 30°C, recombinant wild-type enzyme, in absence of Mn2+

proof_lines: pH 7.4, 30°C, recombinant wild-type enzyme, in presence of Mn2+


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:S4W784 / NCBI Protein:AGO86670.2 with E166Q and applied mutation signature E166Q to reconstruct the assayed variant sequence.


proof_lines: pH 4.0, 30°C, recombinant mutant E166G, in absence of Mn2+


organism: Phanerochaete chrysosporium

substrate_name: Hexacyanoferrate(II); H2O2; H+

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

proof_lines: SABIO-RK modifier species: manganese peroxidase(Enzyme) mutant R177K

substrate: Hexacyanoferrate(II); H2O2; H+


sequence_source: UniProtKB Q02567 REST/FASTA direct check


proof_lines: SABIO-RK modifier species: manganese peroxidase(Enzyme) mutant R177A


organism: Phanerodontia chrysosporium

substrate_name: Phenol red

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

proof_lines:
isoenzyme H3
isoenzyme H5
isoenzyme H4

substrate: Phenol red


organism: Agrocybe praecox

proof_lines: 0.1 mM H2O2, Mn2+-independent activity, MnP1


organism: Bjerkandera adusta

proof_lines:
Mn2+-dependent activity
Mn2+-independent activity


organism: Bjerkandera sp.

proof_lines:
Mn2+-dependent activity, BOS2
isoform BOS2, at pH 5.0 and 30°C
0.1 mM Mn2+, BOS1


organism: Deuteromycotina sp.


organism: Dichomitus squalens


organism: Klebsiella pneumoniae


sequence_variant_note: Resolved canonical sequence from UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19 and applied mutation signature A172W/A273T with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_source: UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19


sequence_variant_note: Resolved canonical sequence from UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19 and applied mutation signature A172W/I171V with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19 and applied mutation signature A172W with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19 and applied mutation signature A172W/A269R with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P19136 direct FASTA lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02567 direct FASTA lookup plus mature-chain offset from UniProt feature table and applied mutation signature R177Q with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


organism: Lentinus tigrinus

proof_lines: with 1.5 mM Mn2+ as cosubstrate, pH 5.5, 45°C

proof_lines: in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C

proof_lines: in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C


organism: Musa x paradisiaca


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

proof_lines: A48C/A63C double mutant MnP after thermal treatment at 37°C for 15 min

proof_lines: recombinant MnP and A48C/A63C double mutant MnP


organism: Pleurotus eryngii

assay_conditions_summary: cofactor NADH

proof_lines:
0.1 mM Mn2+, 0.1 mM H2O2
0.1 mM 2,6-dimethoxyphenol, 0.1 mM H2O2
below


organism: Pleurotus ostreatus


organism: Schizophyllum commune


organism: Schizophyllum sp.


organism: Stropharia coronilla


organism: Trichophyton rubrum

proof_lines:
reaction with Mn2+
reactioin with H2O2
reaction with H2O2


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature R177E with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature R177Q with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature R177D with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature R177K with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature E35Q with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


substrate_name: ferrocyanide

sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature F190A with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

proof_lines:
MnP1 from mutant F190A
mutant enzyme F190A, at pH 4.5 and 25°C

substrate: ferrocyanide


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02567 plus PMID:9100022 F190I mutation note and applied mutation signature F190I with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02567 plus PMID:9100022 F190L mutation note and applied mutation signature F190L with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F190L, at pH 4.5 and 25 °C


proof_lines: MnP1 from mutants F190Y, F190L, F190I and F190A


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

proof_lines:
wild-type MnP1
wild-type MnP
wild-type enzyme


organism: Phlebiopsis flavidoalba


organism: Gelatoporia subvermispora

sequence_variant_note: Resolved canonical sequence from UniProt REST M2REM6 FASTA; variant reconstructed from PMID 25788979 mutation context with +21 offset and applied mutation signature T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_source: UniProt REST M2REM6 FASTA; variant reconstructed from PMID 25788979 mutation context with +21 offset


sequence_source: UniProt REST M2REM6 FASTA


sequence_variant_note: Resolved canonical sequence from UniProt REST M2REM6 FASTA; variant reconstructed from PMID 25788979 mutation context with +21 offset and applied mutation signature S168W with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST M2REM6 FASTA; variant reconstructed from PMID 25788979 mutation context with +21 offset and applied mutation signature S168W with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


enzyme_display_name: cystathionine beta-synthase

organism: Unknown

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

enzyme: cystathionine beta-synthase


organism: Rattus norvegicus

substrate_name: L-Homocysteine; L-Serine

sequence_source: UniProtKB:P32232 direct REST lookup on 2026-06-03

substrate: L-Homocysteine; L-Serine


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P32582 direct REST lookup on 2026-06-03


substrate_name: L-Serine

substrate: L-Serine


substrate_name: L-Homocysteine

substrate: L-Homocysteine


substrate_name: L-Cystathionine; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P32582 direct REST lookup on 2026-06-03 and applied mutation signature Y158F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant Y158F His-tagged

substrate: L-Cystathionine; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32582 direct REST lookup on 2026-06-03 and applied mutation signature T85A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant T85A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32582 direct REST lookup on 2026-06-03 and applied mutation signature Q157H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant Q157H His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32582 direct REST lookup on 2026-06-03 and applied mutation signature S82A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant S82A His-tagged


organism: Bacillus anthracis

substrate_name: L-homocysteine

sequence_variant_note: Resolved canonical sequence from Reconstructed A72S from UniProt A0A6L8PXK0 canonical sequence; A0A1J9VES8 is a secondary/merged accession and RCSB 5XW3 maps to A0A6L8PXK0. and applied mutation signature A72S to reconstruct the assayed variant sequence.

substrate: L-homocysteine


organism: Homo sapiens

substrate_name: L-Serine; L-Homocysteine

sequence_variant_note: Resolved canonical sequence from Reconstructed deltaN69 by deleting residues 1-69 from UniProt P35520 canonical human CBS sequence. and applied mutation signature ΔN69 with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant deltaN69

substrate: L-Serine; L-Homocysteine


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

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant deltaN69/K119A

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant K119A


substrate_name: L-Cysteine

sequence_source: Canonical wild-type sequence from UniProt P35520 reviewed human cystathionine beta-synthase.

substrate: L-Cysteine


sequence_source: Reconstructed delta411-551 by retaining residues 1-410 from UniProt P35520 canonical human CBS sequence.

sequence_variant_note: Mutation signature Δ411 references residue 411, which is outside the resolved sequence length.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant delta411-551


proof_lines: wild-type, 37°C, pH not specified in the publication


substrate_name: L-serine

sequence_variant_note: Resolved canonical sequence from Reconstructed S500L from UniProt P35520 canonical human CBS sequence. and applied mutation signature S500L to reconstruct the assayed variant sequence.

proof_lines: mutant S500L, 37°C, pH not specified in the publication

substrate: L-serine


sequence_variant_note: Resolved canonical sequence from Reconstructed D444N from UniProt P35520 canonical human CBS sequence. and applied mutation signature D444N to reconstruct the assayed variant sequence.

proof_lines: mutant D444N, 37°C, pH not specified in the publication


organism: Aeropyrum pernix

sequence_source: UniProtKB:Q9YBL2 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A6L8PXK0 canonical sequence queried via secondary accession A0A1J9VES8; variant reconstructed from source mutation_signature A72S and applied mutation signature A72S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A6L8PXK0 canonical sequence queried via secondary accession A0A1J9VES8; variant reconstructed from source mutation_signature E220R and applied mutation signature E220R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A6L8PXK0 canonical sequence queried via secondary accession A0A1J9VES8

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

proof_lines: wild-type, production of H2S, pH 8.2, 37°C


sequence_source: UniProtKB:A0A6L8PXK0 canonical sequence queried via secondary accession A0A1J9VES8; variant reconstructed from source mutation_signature E220R


substrate_name: H2O; L-Cystathionine

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

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant Q157E His-tagged

substrate: H2O; L-Cystathionine


proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant Q157A His-tagged


proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant T81A His-tagged


organism: Toxoplasma gondii

mutation_type: truncation

assay_conditions_summary: pH 9

proof_lines: cosubstrate L-serine, C-terminally truncated R353* CBS, pH 9, 37Â°C

proof_lines: cosubstrate O-acetyl-L-serine, C-terminally truncated R353* CBS, pH 9, 37Â°C


substrate_name: O-acetyl-L-serine

sequence_source: UniProtKB A0A125YSJ9 REST accession lookup on 2026-06-03

proof_lines: cosubstrate O-acetyl-L-serine, wild-type, pH 9, 37Â°C

proof_lines: cosubstrate L-serine, wild-type, pH 9, 37Â°C

substrate: O-acetyl-L-serine


organism: Trypanosoma cruzi

substrate_name: Sulfide; O-Acetyl-L-serine

substrate: Sulfide; O-Acetyl-L-serine


substrate_name: 2-Mercaptoethanol; L-Cysteine

substrate: 2-Mercaptoethanol; L-Cysteine


sequence_variant_note: Resolved canonical sequence from UniProtKB P35520 direct lookup on 2026-06-03 and applied mutation signature P427L to reconstruct the assayed variant sequence.

proof_lines: mutant P427L, 37°C, pH not specified in the publication


proof_lines: mutant K523Sfs?18, 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P35520 direct lookup on 2026-06-03 and applied mutation signature L540Q to reconstruct the assayed variant sequence.

proof_lines: mutant L540Q, 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P35520 direct lookup on 2026-06-03 and applied mutation signature V449G to reconstruct the assayed variant sequence.

proof_lines: mutant V449G, 37°C, pH not specified in the publication


sequence_source: UniProtKB P35520 direct lookup on 2026-06-03


sequence_variant_note: Resolved canonical sequence from UniProtKB P35520 direct lookup on 2026-06-03 and applied mutation signature H2S with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

proof_lines: cosubstrate H2S, presence of S-adenosyl-L-methionine, pH 7.4, 37°C


smiles: S


organism: Haemonchus contortus

substrate_name: L-Cys

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

substrate: L-Cys


proof_lines: pH 6.8, 37°C, deltaC143 mutant after homocysteine pre-treatment

proof_lines: pH 6.8, 37°C, deltaC143 mutant after L-serine pre-treatment


proof_lines: I435T mutant, 37°C, presence of S-adenosyl-L-methionine

proof_lines: I435T mutant, 37°C, absence of S-adenosyl-L-methionine


substrate_name: homocysteine

proof_lines: S466L mutant, 37°C, absence of S-adenosyl-L-methionine

proof_lines: mutant enzyme S466L, in the presence of 0.25 mM S-adenosyl-L-methionine

substrate: homocysteine


substrate_name: L-cysteine

proof_lines: pH 8.0, 37°C, reaction with cysteamine, continous UV assay

proof_lines: pH 6.8, 37°C, full length enzyme after L-serine pre-treatment

substrate: L-cysteine


substrate_name: L-cystathionine

proof_lines: reverse reaction (L-cystathionine hydrolysis), mutant S289A

proof_lines: cosubstrate: L-homocysteine, mutant S289A

substrate: L-cystathionine


proof_lines:
37°C, pH 8.6, mutant enzyme R266K
mutant R266K


proof_lines: 37°C, pH 8.0, wild-type enzyme, without S-adenosyl-L-methionine

proof_lines: 37°C, pH 8.0, wild-type enzyme, with S-adenosyl-L-methionine


organism: Panagrellus redivivus


substrate_name: DL-homocysteine

proof_lines:
cosubstrate L-Ser
cosubstrate L-Cys
enzyme composed of MW 48000 subunits

substrate: DL-homocysteine


proof_lines:
pH 8.6, 37°C
37°C, homocysteine pre-treatment
37°C


proof_lines: presence of S-adenosyl-L-methionine, pH 8.6, 37°C

proof_lines: cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C


organism: Lactiplantibacillus plantarum


sequence_variant_note: Resolved canonical sequence from UniProtKB:F9UT54 plus reviewed mutation signature E223G and applied mutation signature E223G to reconstruct the assayed variant sequence.


proof_lines: formation of (2R,2R)-3,3-sulfanediylbis(2-aminopropanoic acid), wild-type, pH 7.5, 37°C

proof_lines: formation of L-cystathionine, wild-type, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:F9UT54 plus reviewed mutation signature A70S and applied mutation signature A70S to reconstruct the assayed variant sequence.

proof_lines: formation of L-cystathionine, mutant A70S, pH 7.5, 37°C


sequence_source: UniProtKB:F9UT54 plus reviewed mutation signature E223G

proof_lines: formation of L-cystathionine, mutant E223G, pH 7.5, 37°C

proof_lines: formation of (2R,2R)-3,3-sulfanediylbis(2-aminopropanoic acid), mutant E223G, pH 7.5, 37°C


sequence_source: UniProtKB:F9UT54 plus reviewed mutation signature A70S


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


proof_lines:
wild-type enzyme, pH 8.6, 37°C
cosubstrate: L-homocysteine, wild-type
cosubstrate: L-serine, wild-type


enzyme_display_name: 3-mercaptopyruvate sulfurtransferase

organism: Arabidopsis thaliana

substrate_name: thiosulfate

enzyme: 3-mercaptopyruvate sulfurtransferase

substrate: thiosulfate


substrate_name: 2-Mercaptoethanol; 3-Mercaptopyruvate

sequence_source: UniProtKB:P97532 direct REST lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:P97532 direct REST lookup and applied mutation signature R187G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant R187G

substrate: 2-Mercaptoethanol; 3-Mercaptopyruvate


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P97532 direct REST lookup and applied mutation signature S249A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P97532 direct REST lookup and applied mutation signature R196G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant R196G


sequence_source: UniProtKB:P25325 canonical FASTA, direct REST lookup

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

proof_lines: isoform TUM1-Iso1, with cyanide as cosubstrate, at pH 10.5 and 37°C

proof_lines: isoform TUM1-Iso2, with cyanide as cosubstrate, at pH 10.5 and 37°C


substrate_name: dithiothreitol

column_label: Table 2 (Summary of kinetic parameters of human MST), acceptor row 'DTT'; column 'Km A (mM)' = 4.6; column 'Km 3-MP (uM)' = 26; column 'Vmax (umol min^-1 mg^-1)' = 11; column 'kcat (s^-1)' = 6.1; column 'kcat/Km A (mM^-1 s^-1)' = 1.3.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.6 mM; the column head is already mM, so no unit conversion applies and the exported value is 4.6 mM. kcat: printed Table 2 cell 6.1 s^-1; the column head is already s^-1, so no unit conversion applies and the exported value is 6.1 s^(-1). kcat/Km: the exported value 1.3260869565217392 s^(-1)*mM^(-1) is the full-precision quotient of those two printed cells, 6.1 / 4.6. The paper's own printed efficiency cell is 1.3 mM^-1 s^-1; mM^-1 s^-1 is already the canonical s^(-1)*mM^(-1), so that cell reads 1.3 s^(-1)*mM^(-1), which is the same quotient carried to the precision printed in that column (its rounding interval is 1.25 to 1.35).

raw_value_unit_evidence: Table 2, acceptor row 'DTT': column 'Km A (mM)' = 4.6; column 'kcat (s^-1)' = 6.1; printed column 'kcat/Km A (mM^-1 s^-1)' = 1.3.

row_label: Table 2, acceptor row 'DTT'

table_label: Table 2: Summary of kinetic parameters of human MST (J. Biol. Chem. 2013, 288(27):20002-20013)

substrate: dithiothreitol


substrate_name: cyanide

smiles: C#N

column_label: Table 2 (Summary of kinetic parameters of human MST), acceptor row 'Cyanide'; column 'Km A (mM)' = 6; column 'Km 3-MP (uM)' = 350; column 'Vmax (umol min^-1 mg^-1)' = 4.3; column 'kcat (s^-1)' = 2.4; column 'kcat/Km A (mM^-1 s^-1)' = 0.4.

normalized_value_unit_evidence: Km: printed Table 2 cell 6 mM; the column head is already mM, so no unit conversion applies and the exported value is 6.0 mM. kcat: printed Table 2 cell 2.4 s^-1; the column head is already s^-1, so no unit conversion applies and the exported value is 2.4 s^(-1). kcat/Km: the exported value 0.39999999999999997 s^(-1)*mM^(-1) is the full-precision quotient of those two printed cells, 2.4 / 6. The paper's own printed efficiency cell is 0.4 mM^-1 s^-1; mM^-1 s^-1 is already the canonical s^(-1)*mM^(-1), so that cell reads 0.4 s^(-1)*mM^(-1), which is the same quotient carried to the precision printed in that column (its rounding interval is 0.35 to 0.45).

raw_value_unit_evidence: Table 2, acceptor row 'Cyanide': column 'Km A (mM)' = 6; column 'kcat (s^-1)' = 2.4; printed column 'kcat/Km A (mM^-1 s^-1)' = 0.4.

row_label: Table 2, acceptor row 'Cyanide'

substrate: cyanide


substrate_name: L-homocysteine

column_label: Table 2 (Summary of kinetic parameters of human MST), acceptor row 'L-Homocysteine'; column 'Km A (mM)' = 12.5; column 'Km 3-MP (uM)' = 30; column 'Vmax (umol min^-1 mg^-1)' = 1.6; column 'kcat (s^-1)' = 0.8; column 'kcat/Km A (mM^-1 s^-1)' = 0.06.

normalized_value_unit_evidence: Km: printed Table 2 cell 12.5 mM; the column head is already mM, so no unit conversion applies and the exported value is 12.5 mM. kcat: printed Table 2 cell 0.8 s^-1; the column head is already s^-1, so no unit conversion applies and the exported value is 0.8 s^(-1). kcat/Km: the exported value 0.064 s^(-1)*mM^(-1) is the full-precision quotient of those two printed cells, 0.8 / 12.5. The paper's own printed efficiency cell is 0.06 mM^-1 s^-1; mM^-1 s^-1 is already the canonical s^(-1)*mM^(-1), so that cell reads 0.06 s^(-1)*mM^(-1), which is the same quotient carried to the precision printed in that column (its rounding interval is 0.055 to 0.065).

raw_value_unit_evidence: Table 2, acceptor row 'L-Homocysteine': column 'Km A (mM)' = 12.5; column 'kcat (s^-1)' = 0.8; printed column 'kcat/Km A (mM^-1 s^-1)' = 0.06.

row_label: Table 2, acceptor row 'L-Homocysteine'

substrate: L-homocysteine


substrate_name: dihydrolipoic acid

smiles: O=C(O)CCCCC(S)CCS

column_label: Table 2 (Summary of kinetic parameters of human MST), acceptor row 'Dihydrolipoic acid'; column 'Km A (mM)' = 4.4; column 'Km 3-MP (uM)' = 25; column 'Vmax (umol min^-1 mg^-1)' = 3.1; column 'kcat (s^-1)' = 1.7; column 'kcat/Km A (mM^-1 s^-1)' = 0.39.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.4 mM; the column head is already mM, so no unit conversion applies and the exported value is 4.4 mM. kcat: printed Table 2 cell 1.7 s^-1; the column head is already s^-1, so no unit conversion applies and the exported value is 1.7 s^(-1). kcat/Km: the exported value 0.3863636363636363 s^(-1)*mM^(-1) is the full-precision quotient of those two printed cells, 1.7 / 4.4. The paper's own printed efficiency cell is 0.39 mM^-1 s^-1; mM^-1 s^-1 is already the canonical s^(-1)*mM^(-1), so that cell reads 0.39 s^(-1)*mM^(-1), which is the same quotient carried to the precision printed in that column (its rounding interval is 0.385 to 0.395).

raw_value_unit_evidence: Table 2, acceptor row 'Dihydrolipoic acid': column 'Km A (mM)' = 4.4; column 'kcat (s^-1)' = 1.7; printed column 'kcat/Km A (mM^-1 s^-1)' = 0.39.

substrate: dihydrolipoic acid


smiles: OCCS

column_label: Table 2 (Summary of kinetic parameters of human MST), acceptor row '2-Mercaptoethanol'; column 'Km A (mM)' = 108; column 'Km 3-MP (uM)' = 130; column 'Vmax (umol min^-1 mg^-1)' = 417; column 'kcat (s^-1)' = 229; column 'kcat/Km A (mM^-1 s^-1)' = 2.1.

normalized_value_unit_evidence: Km: printed Table 2 cell 108 mM; the column head is already mM, so no unit conversion applies and the exported value is 108.0 mM. kcat: printed Table 2 cell 229 s^-1; the column head is already s^-1, so no unit conversion applies and the exported value is 229.0 s^(-1). kcat/Km: the exported value 2.1203703703703702 s^(-1)*mM^(-1) is the full-precision quotient of those two printed cells, 229 / 108. The paper's own printed efficiency cell is 2.1 mM^-1 s^-1; mM^-1 s^-1 is already the canonical s^(-1)*mM^(-1), so that cell reads 2.1 s^(-1)*mM^(-1), which is the same quotient carried to the precision printed in that column (its rounding interval is 2.05 to 2.15).

raw_value_unit_evidence: Table 2, acceptor row '2-Mercaptoethanol': column 'Km A (mM)' = 108; column 'kcat (s^-1)' = 229; printed column 'kcat/Km A (mM^-1 s^-1)' = 2.1.


proof_lines: mitochondrial splice variant MPST2, Hill coefficient 1.4, pH 7.4, 37°C

proof_lines: cytosolic splice variant MPST1, Hill coefficient 1.6, pH 7.4, 37°C

proof_lines: cytosolic splice variant MPST1, Hill coefficient 1.4, pH 7.4, 37°C


substrate_name: N-acetyl-L-cysteine

substrate: N-acetyl-L-cysteine


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

proof_lines: mutant H66A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C


proof_lines: mutant S239A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C


proof_lines: wild-type, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C


organism: Leishmania major

substrate_name: reduced thioredoxin

proof_lines:
pH 7.3, 37°C
Raw SKiD Env: Temp=37°C, pH=7.3

substrate: reduced thioredoxin


organism: Mycobacterium tuberculosis


proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant R248G


sequence_source: UniProtKB reviewed accession P24329


substrate_name: 3-Mercaptopyruvate; 2-Mercaptoethanol

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant R248G K249S

substrate: 3-Mercaptopyruvate; 2-Mercaptoethanol


proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant K249S


sequence_source: UniProtKB reviewed accession P97532


sequence_source: UniProtKB reviewed accession P97532 FASTA, checked directly during review.