organism: Pseudomonas aeruginosa

substrate_name: cyclic-di-GMP

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature T267A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 100 mM Tris

proof_lines: mutant enzyme T267A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2

substrate: cyclic-di-GMP


source_db: brenda

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 REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature Q372A to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant enzyme Q372A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature D296A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D296A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


verification_status: verified

mutation_signature: Unknown

sequence_source: UniProtKB REST direct lookup for Q9HX69 on 2026-06-17

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

assay_conditions_summary: pH 8; 296.15 K; buffer 100 mM Tris

column_label: Table 1 carries five columns, printed in this order: Enzyme, kcat (s^-1), Km (uM), kcat/Km (s^-1 uM^-1) and Decrease in kcat (fold). The cited cell set is the Table 1, enzyme row RocR, the wild-type enzyme: kcat (s^-1) = 0.67; Km (uM) = 3.2; kcat/Km (s^-1 uM^-1) = 0.21; the Decrease in kcat (fold) cell is blank on the wild-type row, which is itself the reference of that column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.67 under the column head kcat (s^-1); that column is already per second, so no unit conversion applies and the paper value is 0.67 s^(-1). Km: printed Table 1 cell 3.2 under the column head Km (uM); 1 uM is 0.001 mM, so 3.2 / 1000 = 0.0032 mM. kcat/Km: printed Table 1 cell 0.21 under the column head kcat/Km (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.21 x 1000 = 210.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme row RocR, the wild-type enzyme: kcat = 0.67 under the column head kcat (s^-1); Km = 3.2 under the column head Km (uM); the printed kcat/Km cell = 0.21 under the column head kcat/Km (s^-1 uM^-1).

table_label: Table 1: Steady-state kinetic parameters for RocR and its mutants (J. Bacteriol. 2008, 190(10):3622-3631)

status: verified


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature E352D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E352D, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature E268Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E268Q, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature Q161A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q161A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature R179A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R179A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature E352Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E352Q, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature D318A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D318A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature E355A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E355A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


substrate_name: cyclic di-3',5'-guanylate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HV27 on 2026-06-17 and applied mutation signature E314A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant enzyme E314A

substrate: cyclic di-3',5'-guanylate


sequence_source: UniProtKB REST direct lookup for Q9HV27 on 2026-06-17

proof_lines: pH 8.0, 30°C, recombinant wild-type enzyme


sequence_source: UniProtKB REST direct lookup for Q9HWS0 on 2026-06-17


organism: Ruminococcus albus

source_db: oed

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

source: oed


substrate_name: sophorose

substrate: sophorose


substrate_name: N,N'-diacetylchitobiose

substrate: N,N'-diacetylchitobiose


substrate_name: laminaribiose

substrate: laminaribiose


substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


substrate_name: D-Mannose

substrate: D-Mannose


substrate_name: D-glucose

sequence_source: UniProtKB reviewed E6UIS7 direct REST lookup on 2026-06-17

substrate: D-glucose


verification_status: unverified

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed E6UIS7 canonical sequence plus H245A reconstruction by direct residue check on 2026-06-17 and applied mutation signature H245A to reconstruct the assayed variant sequence.

data_origin: experimental

status: unverified


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


sequence_source: UniProtKB reviewed E6UIS7 canonical sequence plus H245A reconstruction by direct residue check on 2026-06-17


enzyme_display_name: sulfate adenylyltransferase

organism: Desulfovibrio piger

substrate_name: ATP

kcat_display: Not reported

assay_conditions_summary: pH 8; 308.15 K; cofactor ATP

enzyme: sulfate adenylyltransferase

substrate: ATP


organism: Euglena gracilis

substrate_name: diphosphate

proof_lines:
pH 8.8, enzyme form ATPSm
pH 8.8, enzyme form ATPSc

substrate: diphosphate


organism: Geobacillus stearothermophilus

substrate_name: dATP

assay_conditions_summary: pH 6; 313.15 K; cofactor ATP

substrate: dATP


organism: Penicillium chrysogenum

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, 30°C, at saturating concentrations of MoO42-

proof_lines: pH 8.0, 30°C, at saturating concentrations of SO42-


organism: Penicillium duponti


organism: Pyropia yezoensis

assay_conditions_summary: cofactor ATP

proof_lines:
ATP in form of MgATP2-
less than


organism: Rattus norvegicus

proof_lines:
30°C, pH 8.0
30°C, pH 8.0, reaction with CrO42-
ATP in form of MgATP2-


organism: Rhodovulum sulfidophilum


organism: Saccharomyces cerevisiae

proof_lines:
pH 8.0, 30°C
ATP in form of MgATP2-


organism: Spinacia oleracea

substrate_name: Diphosphate; Adenylylsulfate

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

ki_unit: mM

proof_lines: pH 8.0, 30°C, chloroplastic enzyme, reaction with MoO42-

proof_lines: pH 8.0, 30°C, cytosolic enzyme, reaction with MoO42-

substrate: Diphosphate; Adenylylsulfate


organism: Synechococcus sp.

substrate_name: adenosine 5'-phosphosulfate

substrate: adenosine 5'-phosphosulfate


organism: Zea mays


organism: Unknown


enzyme_display_name: (2E,6E)-farnesyl diphosphate synthase

organism: Abies grandis

substrate_name: Isopentenyl diphosphate; Dimethylallyl diphosphate

enzyme: (2E,6E)-farnesyl diphosphate synthase


organism: Bacillus subtilis

substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Cucurbita sp.

substrate_name: Geranyl diphosphate; Isopentenyl diphosphate

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


substrate_name: isopentenyl diphosphate

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

proof_lines:
C73F mutant enzyme at 45°C
C73F mutant enzyme at 55°C

substrate: isopentenyl diphosphate


substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


proof_lines:
wild-type enzyme at 45°C
wild-type enzyme at 55°C


organism: Homo sapiens

substrate_name: Unknown

km_display: Not reported

substrate: Unknown


organism: Leishmania major

proof_lines: pH and temperature not specified in the publication


organism: Mycobacterium tuberculosis


organism: Phaedon cochleariae

proof_lines: fixed substrate geranyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Co2+

proof_lines: fixed substrate isopentenyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+

proof_lines: fixed substrate geranyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+


organism: Anabaena cylindrica


organism: Archaeoglobus fulgidus


organism: Astragalus bisulcatus

assay_conditions_summary: pH 9


organism: Astragalus racemosus


organism: Astragalus sinicus


organism: Brassica capitata

proof_lines: pH 8.0, 30°C, synthesis of adenosine 5-phosphosulfate


organism: Desulfomicrobium sp.


enzyme_display_name: Cyclic di-GMP phosphodiesterase RocR

organism: Pseudomonas aeruginosa

substrate_name: cyclic di-3',5'-guanylate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature D296A to reconstruct the assayed variant sequence.

proof_lines: mutant RocR enzyme D296A, in 100 mM Tris buffer (pH 8.0) (23°C), 20 mM KCl, and 25 mM MgCl2

enzyme: Cyclic di-GMP phosphodiesterase RocR

substrate: cyclic di-3',5'-guanylate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature Q161A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature Q372A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature Q372A/D318A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 23°C, recombinant mutants Q372A and D318A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature E268Q to reconstruct the assayed variant sequence.

proof_lines: mutant RocR enzyme E268Q, in 100 mM Tris buffer (pH 8.0) (23°C), 20 mM KCl, and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature E352Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature D318A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature R179A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature E352D/T267A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 23°C, recombinant mutants E352D and T267A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature E355A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature T267A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature S302A to reconstruct the assayed variant sequence.

proof_lines: mutant RocR enzyme S302A, in 100 mM Tris buffer (pH 8.0) (23°C), 20 mM KCl, and 25 mM MgCl2


enzyme_display_name: peptidyl-tRNA hydrolase

organism: Saccharolobus solfataricus

substrate_name: diacetyl-lysyl-tRNALys

enzyme: peptidyl-tRNA hydrolase

substrate: diacetyl-lysyl-tRNALys


organism: Saccharomyces cerevisiae

substrate_name: N-acetyl-phenylalanyl-tRNA

substrate: N-acetyl-phenylalanyl-tRNA


organism: Borreliella burgdorferi


organism: Caulobacter vibrioides


organism: Escherichia coli


organism: Klebsiella pneumoniae

proof_lines: mutant enzyme R93S, at pH 7.5, 20°C, under dark conditions

proof_lines: mutant enzyme R93S, at pH 7.5, 20°C, under light conditions


proof_lines: wild type enzyme, at pH 7.5, 20°C, under dark conditions

proof_lines: wild type enzyme, in the presence of 10 mM Mn2+, at pH 7.5, 20°C, under dark conditions

proof_lines: wild type enzyme, in the presence of 10 mM Mn2+, at pH 7.5, 20°C, under light conditions


proof_lines: mutant enzyme L128C/G353C, at pH 7.5, 20°C, under light conditions

proof_lines: mutant enzyme L128C/G353C, at pH 7.5, 20°C, under dark conditions


proof_lines: mutant RocR enzyme D56N, in 100 mM Tris buffer (pH 8.0) (23°C), 20 mM KCl, and 25 mM MgCl2


proof_lines: mutant RocR enzyme F297A, in 100 mM Tris buffer (pH 8.0) (23°C), 20 mM KCl, and 25 mM MgCl2


proof_lines: mutant RocR enzyme D56N/D296A, in 100 mM Tris buffer (pH 8.0) (23°C), 20 mM KCl, and 25 mM MgCl2


proof_lines: mutant PA2567 enzyme E464A, in 100 mM Tris buffer (pH 8.0) (23°C), 50 mM KCl, and 10 mM MgCl2


proof_lines: wild type PA2567 enzyme, in 100 mM Tris buffer (pH 8.0) (23°C), 50 mM KCl, and 10 mM MgCl2

proof_lines: pH 8.0, 23°C, recombinant wild-type RocR

proof_lines: wild type RocR enzyme, in 100 mM Tris buffer (pH 8.0) (23°C), 20 mM KCl, and 25 mM MgCl2


organism: Vibrio cholerae serotype O1


enzyme_display_name: glutamate carboxypeptidase II

organism: Homo sapiens

substrate_name: N-acetyl-alpha-L-aspartyl-L-glutamate

enzyme: glutamate carboxypeptidase II

substrate: N-acetyl-alpha-L-aspartyl-L-glutamate


organism: Mus musculus


organism: Rattus norvegicus

substrate_name: N-Acetyl-L-Asp-L-Glu

proof_lines:
no addition of Zn2+ to assay medium
addition of Zn2+ to assay medium
i.e. gamma-Glu-Cys-Gly

substrate: N-Acetyl-L-Asp-L-Glu


enzyme_display_name: pyroglutamyl-peptidase I

organism: Bacillus amyloliquefaciens

substrate_name: L-pyroglutamyl-beta-naphthylamide

enzyme: pyroglutamyl-peptidase I

substrate: L-pyroglutamyl-beta-naphthylamide


enzyme_display_name: methionyl-tRNA formyltransferase

organism: Unknown

substrate_name: L-methionyl-tRNAfMet

enzyme: methionyl-tRNA formyltransferase

substrate: L-methionyl-tRNAfMet


organism: Bos taurus

substrate_name: L-methionyl-tRNA(fMet)

source_db: uniprot

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

substrate: L-methionyl-tRNA(fMet)

source: uniprot


sequence_variant_note: Resolved canonical sequence from uniprot:P46107 direct REST sequence; F142A applied at UniProt residue 142 and applied mutation signature F142A to reconstruct the assayed variant sequence.


enzyme_display_name: signal peptidase I

substrate_name: FSASALAKI

enzyme: signal peptidase I

substrate: FSASALAKI


organism: Bacteroides fragilis

substrate_name: phosphate

sequence_source: UniProtKB:Q5LH68 reviewed entry

smiles: O=P(O)(O)O

assay_conditions_summary: pH 7; 303.15 K; buffer pH 7

substrate: phosphate


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

proof_lines:
pH 7.5, 30°C
Raw SKiD Env: Temp=30°C, pH=7.5

source_databases_merged: brenda skid


organism: Ruminococcus albus

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


substrate_name: gentiobiose

substrate: gentiobiose


substrate_name: methyl beta-D-glucoside

substrate: methyl beta-D-glucoside


substrate_name: methyl alpha-D-glucoside

substrate: methyl alpha-D-glucoside


substrate_name: maltose

substrate: maltose


substrate_name: cellobiose

substrate: cellobiose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-allose

substrate: D-allose


sequence_source: UniProtKB:E6UIS7 reviewed entry

proof_lines: pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate

proof_lines: pH 6.5, 37°C, phosphorolytic reaction, cosubstrate phosphate

proof_lines: pH 6.5, 37°C, synthetic reaction, cosubstrate D-glucose


proof_lines: apparent value, pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate


organism: Staphylococcus aureus

substrate_name: decanoyl-LTPTAKAASKIDD-OH

proof_lines: pH 8.0, 37°C, self-cleavage, full-length enzyme

substrate: decanoyl-LTPTAKAASKIDD-OH


substrate_name: SpsB

mutation_signature: truncated enzyme mutant

mutation_type: truncation

proof_lines: pH 8.0, 37°C, self-cleavage, truncated enzyme mutant

substrate: SpsB


organism: Thermococcus kodakarensis


substrate_name: E. coli L-methionyl-tRNAmMet

substrate: E. coli L-methionyl-tRNAmMet


proof_lines:
+ 10-formyltetrahydrofolate
pH 7.5


enzyme_display_name: streptopain

organism: Streptococcus pyogenes

enzyme: streptopain


enzyme_display_name: tyrosine decarboxylase

organism: Levilactobacillus brevis

substrate_name: L-tyrosine

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:J7GQ11 canonical sequence by applying H241N on 2026-06-17 and applied mutation signature H241N to reconstruct the assayed variant sequence.

proof_lines: mutant H241N, pH not specified in the publication, temperature not specified in the publication

enzyme: tyrosine decarboxylase

substrate: L-tyrosine


organism: Lycoris radiata

sequence_source: UniProtKB:A0A8F4Q3Q6 direct accession lookup on 2026-06-17


sequence_source: UniProtKB:A0A8F4Q3P6 direct accession lookup on 2026-06-17


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB:Q60358 direct accession lookup on 2026-06-17


organism: Papaver somniferum

substrate_name: L-Dopa

sequence_source: UniProtKB:P54768 direct accession lookup on 2026-06-17

substrate: L-Dopa


organism: Pyrococcus furiosus

sequence_source: UniProtKB:Q8U1P6 direct accession lookup on 2026-06-17


organism: Rhodiola sachalinensis

sequence_source: UniProtKB:Q1KLR8 direct accession lookup on 2026-06-17


enzyme_display_name: glycine N-acyltransferase

organism: Homo sapiens

substrate_name: glycine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q6IB77 canonical sequence with row-specific mutation S17N/N156S applied after residue checks (2026-06-17) and applied mutation signature S17N/N156S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: mutant S17N/N156S, S0.5 value, Hill coefficient 1.3, pH 8.0, 37°C

proof_lines: mutant S17N/N156S, S0.5 value, Hill coefficient 1.5, pH 8.0, 37°C

enzyme: glycine N-acyltransferase

substrate: glycine


sequence_variant_note: Resolved canonical sequence from UniProtKB Q6IB77 canonical sequence with row-specific mutation N156S applied after residue checks (2026-06-17) and applied mutation signature N156S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N156S, apparent value, at pH 8.0 and 37°C

proof_lines: mutant N156S, S0.5 value, Hill coefficient 1.6, pH 8.0, 37°C


substrate_name: Glycine; Salicyl-CoA

sequence_source: UniProtKB Q6IB77 canonical sequence direct lookup (2026-06-17)

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

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: K0.5 value at 5 mM gylcine, pH 8.0, temperature not specified in the publication

proof_lines: K0.5 value at 0.02 mM benzoyl-CoA, pH 8.0, temperature not specified in the publication

proof_lines: K0.5 value at 0.04 mM benzoyl-CoA, pH 8.0, temperature not specified in the publication

substrate: Glycine; Salicyl-CoA


organism: Mus musculus

substrate_name: butyryl-CoA

sequence_source: UniProtKB Q91XE0 canonical sequence direct lookup (2026-06-17)

proof_lines: apparent value, at pH 8.0, temperature not specified in the publication

substrate: butyryl-CoA


enzyme_display_name: laminaribiose phosphorylase

organism: Acholeplasma laidlawii

sequence_source: UniProtKB A9NG65 canonical sequence direct lookup (2026-06-17)

enzyme: laminaribiose phosphorylase


proof_lines:
pH 6.0, 40°C, reverse reaction
pH 7.5, 40°C, co-substrate: phosphate
pH 7.5, 40°C


organism: Paenibacillus sp.

substrate_name: laminaribiose

sequence_source: UniProtKB D7UT17 canonical sequence direct lookup (2026-06-17)

proof_lines:
co-substrate: phosphate, pH 7.0, 45°C
pH 7.0, 45°C
Raw SKiD Env: Temp=45°C, pH=7

substrate: laminaribiose


organism: Paenibacillus sp. YM1

substrate_name: alpha-D-glucose 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB D7UT17 canonical sequence with row-specific mutation E11I/Q12V/I186E/L199C/G725C/A522V/S285E/K582D applied after residue checks (2026-06-17) and applied mutation signature E11I/Q12V/I186E/L199C/G725C/A522V/S285E/K582D to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 60°C, recombinant mutant E11I/Q12V/I186E/L199C/G725C/A522V/S285E/K582D

substrate: alpha-D-glucose 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB D7UT17 canonical sequence with row-specific mutation E11I/Q12V/I186E/L199C/G725C/A522V/S285E/K582D/Q456E applied after residue checks (2026-06-17) and applied mutation signature E11I/Q12V/I186E/L199C/G725C/A522V/S285E/K582D/Q456E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB D7UT17 canonical sequence with row-specific mutation E11N/Q12N applied after residue checks (2026-06-17) and applied mutation signature E11N/Q12N to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 60°C, recombinant mutant E11N/Q12N


sequence_variant_note: Resolved canonical sequence from UniProtKB D7UT17 canonical sequence with row-specific mutation E11I/Q12V/I186E/L199C/G725C/A522V applied after residue checks (2026-06-17) and applied mutation signature E11I/Q12V/I186E/L199C/G725C/A522V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 60°C, recombinant mutant E11I/Q12V/I186E/L199C/G725C/A522V


proof_lines: pH 7.5, 60°C, recombinant wild-type enzyme

proof_lines: pH 7.5, 50°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB D7UT17 canonical sequence with row-specific mutation E11I/Q12V/I186E/L199C/G725C/A522V/S285E/K582D/Q456E/L361E applied after residue checks (2026-06-17) and applied mutation signature E11I/Q12V/I186E/L199C/G725C/A522V/S285E/K582D/Q456E/L361E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB D7UT17 canonical sequence with row-specific mutation E11I/Q12V/I186E/L199C/G725C/A522V/S285E applied after residue checks (2026-06-17) and applied mutation signature E11I/Q12V/I186E/L199C/G725C/A522V/S285E to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 60°C, recombinant mutant E11I/Q12V/I186E/L199C/G725C/A522V/S285E


sequence_variant_note: Resolved canonical sequence from UniProtKB D7UT17 canonical sequence with row-specific mutation E11N/Q12N/I186E applied after residue checks (2026-06-17) and applied mutation signature E11N/Q12N/I186E to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 60°C, recombinant mutant E11N/Q12N/I186E


sequence_source: UniProtKB J7GQ11 REST FASTA/JSON direct check


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB J7GQ11 canonical sequence plus selected BRENDA note H98M and applied mutation signature H98M to reconstruct the assayed variant sequence.

proof_lines: mutant H98M, pH not specified in the publication, temperature not specified in the publication


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


organism: Bos taurus

sequence_source: UniProtKB:O77480 direct accession lookup on 2026-06-17

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


organism: Enterococcus faecalis

sequence_source: UniProtKB:Q82ZD8 direct accession lookup on 2026-06-17


organism: Escherichia coli

substrate_name: L-methionyl-tRNAfMet

sequence_source: UniProtKB:P23882 canonical sequence with selected DeltaC20 truncation reconstructed on 2026-06-17

sequence_variant_note: Mutation signature ΔC20 could not be applied safely because the resolved sequence does not match the expected reference residue(s).

mutation_type: deletion

substrate: L-methionyl-tRNAfMet


sequence_source: UniProtKB:P23882 direct accession lookup on 2026-06-17

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

proof_lines: Escherichia coli tRNA2fMet, pH 7.6, 37°C, wild-type enzyme


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

proof_lines: Escherichia coli tRNA2fMet, pH 7.6, 37°C, mutant A172L


proof_lines: Escherichia coli tRNA2fMet, pH 7.6, 37°C, mutant A89L


sequence_source: UniProtKB:Q2KIR7 direct accession lookup on 2026-06-17

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
recombinant wild-type, pH 8.0, 30°C
wild-type, pH 8.0, 30°C


substrate_name: benzoyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q2KIR7 canonical sequence with selected E226Q substitution(s) reconstructed on 2026-06-17 and applied mutation signature E226Q to reconstruct the assayed variant sequence.

substrate: benzoyl-CoA


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


substrate_name: Oleoyl-CoA; Glycine

sequence_source: UniProtKB:Q8WU03 direct accession lookup on 2026-06-17

assay_conditions_summary: cofactor CoA

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

substrate: Oleoyl-CoA; Glycine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6IB77 canonical sequence with selected R131H substitution(s) reconstructed on 2026-06-17 and applied mutation signature R131H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R131H, apparent value, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6IB77 canonical sequence with selected F168L substitution(s) reconstructed on 2026-06-17 and applied mutation signature F168L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F168L, apparent value, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6IB77 canonical sequence with selected K16N substitution(s) reconstructed on 2026-06-17 and applied mutation signature K16N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K16N, apparent value, at pH 8.0 and 37°C


sequence_source: UniProtKB:Q6IB77 direct accession lookup on 2026-06-17

proof_lines: wild type enzyme, apparent value, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6IB77 canonical sequence with selected S17T substitution(s) reconstructed on 2026-06-17 and applied mutation signature S17T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S17T, apparent value, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6IB77 canonical sequence with selected N156S/R199C substitution(s) reconstructed on 2026-06-17 and applied mutation signature N156S/R199C to reconstruct the assayed variant sequence.

proof_lines: mutant N156S/R199C, S0.5 value, Hill coefficient 3.5, pH 8.0, 37°C

proof_lines: mutant N156S/R199C, S0.5 value, Hill coefficient 1.4, pH 8.0, 37°C


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


organism: Arabidopsis thaliana

substrate_name: ATP

substrate: ATP


organism: Pisum sativum


organism: Pneumocystis carinii


enzyme_display_name: endo-polygalacturonase

organism: Solanum lycopersicum

substrate_name: polygalacturonic acid (for PG2 at pH 4.6 and 35 degrees Celsius)

enzyme: endo-polygalacturonase


organism: Lophophora williamsii

substrate_name: L-tyrosine (at pH 7.5 and 30 degrees Celsius)


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


organism: Psilocybe cubensis

substrate_name: L-phenylalanine

substrate: L-phenylalanine


sequence_variant_note: Resolved canonical sequence from UniProtKB:D7UT17 FASTA direct lookup on 2026-06-17 and applied mutation signature E11I/Q12V/I186E/L199C/G725C to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 60°C, recombinant mutant E11I/Q12V/I186E/L199C/G725C


organism: Paenibacillus sp. YM-1

substrate_name: D-glucose

sequence_source: UniProtKB:D7UT17 FASTA direct lookup on 2026-06-17

substrate: D-glucose


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


sequence_source: UniProtKB:Q1ENB6 FASTA direct lookup on 2026-06-17


sequence_source: UniProtKB:P26281 FASTA direct lookup on 2026-06-17


organism: Francisella tularensis

sequence_source: UniProtKB:Q5NGA7 FASTA direct lookup on 2026-06-17

assay_conditions_summary: pH 8.3; 303.15 K; cofactor ATP


sequence_source: UniProtKB:O04862 FASTA direct lookup on 2026-06-17


organism: Plasmodium falciparum

substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 FASTA direct lookup on 2026-06-17 and applied mutation signature S436F/A613T to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 FASTA direct lookup on 2026-06-17 and applied mutation signature A613T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 FASTA direct lookup on 2026-06-17 and applied mutation signature A613S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 FASTA direct lookup on 2026-06-17 and applied mutation signature A437G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 FASTA direct lookup on 2026-06-17 and applied mutation signature S436A/A437G/A613S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 FASTA direct lookup on 2026-06-17 and applied mutation signature S436A/A437G/A613T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 FASTA direct lookup on 2026-06-17 and applied mutation signature S436F/A613S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check Q25704; row-specific variant reconstructed from validated substitutions. and applied mutation signature A437G/K540E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check Q25704; row-specific variant reconstructed from validated substitutions. and applied mutation signature S436A/A437G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check Q25704; row-specific variant reconstructed from validated substitutions. and applied mutation signature K540E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check Q25704; row-specific variant reconstructed from validated substitutions. and applied mutation signature A581G to reconstruct the assayed variant sequence.


sequence_source: UniProt REST direct check Q25704.

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


sequence_source: UniProt REST direct check P29251.


organism: Saccharomyces cerevisiae

sequence_source: UniProt REST direct check P53848.


enzyme_display_name: carboxymethylenebutenolidase

organism: Pseudomonas knackmussii

substrate_name: 4-nitrophenyl acetate

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

enzyme: carboxymethylenebutenolidase

substrate: 4-nitrophenyl acetate


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check P0A115; row-specific variant reconstructed from validated substitutions. and applied mutation signature Q35H/F38L/Q110L/C123S/Y145C/E199G/S208G/G211D to reconstruct the assayed variant sequence.


sequence_source: UniProt REST direct check P0A115; row-specific variant reconstructed from validated substitutions.


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check P0A115; row-specific variant reconstructed from validated substitutions. and applied mutation signature Q35H/F38L/C123S/Y137C/Y145C/E199G/S208G/G211D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check P0A115; row-specific variant reconstructed from validated substitutions. and applied mutation signature Q35H/F38L/C123S/Y145C/E199G/S208G/G211D to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed P0A115 direct REST lookup on 2026-06-17; row-specific variant sequence not populated because residue-coordinate validation failed


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0A115 plus direct residue substitution reconstruction on 2026-06-17 and applied mutation signature Q35H/F38L/C123S/Y137C/Y145C/E199G/S208G/G211D to reconstruct the assayed variant sequence.


organism: Saccharolobus solfataricus

substrate_name: trans-dienelactone

sequence_source: UniProtKB B9WPN8 direct REST lookup on 2026-06-17 returned Inactive/Deleted; no sequence populated

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

substrate: trans-dienelactone


organism: Aspergillus luchuensis

substrate_name: poly-D-galacturonic acid

sequence_source: UniProtKB unreviewed A0A146FN71 direct REST lookup on 2026-06-17

substrate: poly-D-galacturonic acid


organism: Chondrostereum purpureum

substrate_name: Pectin

sequence_source: UniProtKB unreviewed P79074 direct REST lookup on 2026-06-17; row sequence not populated because source snapshots mix mature enzyme and pro-enzyme contexts

proof_lines:
mature enzyme, at pH 4.5 and 30°C
pro-enzyme, at pH 4.5 and 30°C
pro-enzyme, at pH 4.0 and 30°C

substrate: Pectin


organism: Gibberella fujikuroi

substrate_name: Pectate

sequence_source: UniProtKB reviewed Q07181 direct REST lookup on 2026-06-17

substrate: Pectate


organism: Rhizopus arrhizus

substrate_name: trigalacturonate

sequence_source: UniProtKB unreviewed Q5W9U0 direct REST lookup on 2026-06-17; sequence not accepted because UniProt has no EC/protein-family support for EC 3.2.1.15

substrate: trigalacturonate


organism: Arabidopsis thaliana

substrate_name: L-Tyrosine

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 Q8RY79 direct REST lookup on 2026-06-17; sequence not populated as accepted evidence because EC 4.1.1.25 contradicts the accession annotation

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

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----

source_databases_merged: sabio_rk brenda skid

substrate: L-Tyrosine


organism: Enterococcus faecalis

substrate_name: L-Dopa

sequence_source: UniProtKB reviewed Q838D6 direct REST lookup on 2026-06-17

substrate: L-Dopa


sequence_source: UniProtKB reviewed P0DTQ4 direct REST lookup on 2026-06-17


organism: Enterococcus faecium

sequence_source: UniProtKB reviewed A0A481NV25 direct REST lookup on 2026-06-17


organism: Levilactobacillus brevis

substrate_name: L-tyrosine

sequence_source: UniProtKB reviewed J7GQ11 direct REST lookup on 2026-06-17

substrate: L-tyrosine


organism: Unknown


enzyme_display_name: kynurenine 3-monooxygenase

organism: Aedes aegypti

substrate_name: L-kynurenine

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

assay_conditions_summary: cofactor NADPH

enzyme: kynurenine 3-monooxygenase

substrate: L-kynurenine


organism: Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465)


organism: Rattus norvegicus


enzyme_display_name: aryl-acylamidase

organism: Rhodococcus erythropolis

substrate_name: Gly-para-nitroanilide

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

enzyme: aryl-acylamidase

substrate: Gly-para-nitroanilide


enzyme_display_name: memapsin 2

organism: Homo sapiens

substrate_name: APP cleaved by PSEN1 (at pH4)

assay_conditions_summary: pH 4

proof_lines: kcat is 0.67 sec(-1) and 2.45 sec(-1) for APP cleaved by PSEN1 and APP Swedish variant, respectively (PubMed:10677483).

enzyme: memapsin 2

substrate: APP cleaved by PSEN1 (at pH4)


organism: Enterococcus faecalis (strain ATCC 700802 / V583)

substrate_name: L-tyrosine (at pH 5.0)

assay_conditions_summary: pH 5

proof_lines: kcat is 6963 min(-1) for the decarboxylation of L-tyrosine. kcat is 3531 min(-1) for the decarboxylation of L-dopa (at pH 5.0).

proof_lines: kcat is 63.6 sec(-1) for the decarboxylation of L-tyrosine. kcat is 55.5 sec(-1) for the decarboxylation of L-dopa (at pH 5.5).

substrate: L-tyrosine (at pH 5.0)


proof_lines: kcat is 435.6 min(-1) for the decarboxylation of L-tyrosine. kcat is 342.4 min(-1) for the decarboxylation of L-dopa (at pH 5.0).


proof_lines: kcat is 343.1 sec(-1) for the decarboxylation of L-tyrosine (PubMed:24211777). kcat is 124.8 sec(-1) for the decarboxylation of L-tyrosine. kcat is 76.5 sec(-1) for the decarboxylation of L-dopa (PubMed:27292129).


organism: Ephestia kuehniella

substrate_name: NADPH

substrate: NADPH


substrate_name: kynurenine

substrate: kynurenine


organism: Meriones unguiculatus


organism: Pseudomonas fluorescens

assay_conditions_summary: pH 7.5; 278.15 K; cofactor NADPH

proof_lines:
recombinant enzyme, pH 7.5, 5°C
recombinant enzyme, pH 7.5, 25°C


substrate_name: FAD

substrate: FAD


organism: Saccharomyces cerevisiae

proof_lines:
under unaerobic conditions
under aerobic conditions


organism: Saccharomyces pastorianus

substrate_name: Unknown

proof_lines:
inhibition for L-kynurenine
inhibition for NADPH

substrate: Unknown


organism: Escherichia coli

substrate_name: L-methionyl-tRNAfMet

substrate: L-methionyl-tRNAfMet


organism: Euglena gracilis


organism: Haemophilus influenzae

substrate_name: E. coli L-methionyl-tRNAfMet

substrate: E. coli L-methionyl-tRNAfMet


substrate_name: L-kynurenine (at 25 degrees Celsius)

substrate: L-kynurenine (at 25 degrees Celsius)


enzyme_display_name: protein-histidine N-methyltransferase

substrate_name: beta-actin

proof_lines: kcat is 0.65 min(-1) with beta-actin as substrate (PubMed:30526847). kcat is 0.809 min(-1) with beta-actin as substrate (PubMed:30785395). kcat is 0.61 min(-1) with S-adenosyl-L-methionine as substrate (PubMed:30526847). kcat is 0.673 min(-

enzyme: protein-histidine N-methyltransferase

substrate: beta-actin


proof_lines: kcat is 0.8 min(-1) with beta-actin as substrate (PubMed:30526847). kcat is 0.57 min(-1) with S-adenosyl-L-methionine as substrate (PubMed:30526847).


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: L-methionyl-tRNA(fMet)

proof_lines: kcat is 0.13 sec(-1) with L-methionyl-tRNA(fMet) as substrate.

substrate: L-methionyl-tRNA(fMet)


enzyme_display_name: (2E,6E)-farnesyl diphosphate synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: IPP

proof_lines: kcat is 0.3 min(-1) with GPP as substrate. kcat is 0.7 min(-1) with FPP as substrate. kcat is 0.17 min(-1) with DMAPP as substrate.

enzyme: (2E,6E)-farnesyl diphosphate synthase

substrate: IPP


organism: Escherichia coli (strain K12)

substrate_name: N-acyl-leucyl-tRNA(Leu)

proof_lines: kcat is 3.6 sec(-1) for di-acyl-lysyl-tRNA(Lys).

substrate: N-acyl-leucyl-tRNA(Leu)


substrate_name: diacetyl-lysyl-tRNA(Lys)

substrate: diacetyl-lysyl-tRNA(Lys)


substrate_name: c-di-GMP

substrate: c-di-GMP


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


organism: Streptococcus pyogenes

substrate_name: a substrate peptide

substrate: a substrate peptide


organism: Pseudomonas knackmussii


organism: Pseudomonas putida


organism: Pseudomonas reinekei


organism: Pseudomonas sp.

substrate_name: trans-dienelactone

substrate: trans-dienelactone


substrate_name: E-dienelactone

substrate: E-dienelactone


organism: Rhodococcus opacus


organism: Acrocylindrium sp.


organism: Aspergillus foetidus

substrate_name: Pectin

substrate: Pectin


organism: Aspergillus fumigatus

substrate_name: Polygalacturonate

substrate: Polygalacturonate


organism: Aspergillus japonicus

proof_lines:
polygalacturonase I
polygalacturonase II


organism: Aspergillus niger


organism: Trichoderma harzianum

substrate_name: polygalacturonic acid

substrate: polygalacturonic acid


enzyme_display_name: glycosylceramidase

organism: Cricetinae

substrate_name: phlorizin

enzyme: glycosylceramidase

substrate: phlorizin


organism: Homo sapiens

proof_lines: both mannose-rich precursor form and mature form

proof_lines: in non infected cells, in brush border-membrane enriched fraction


organism: Macaca radiata

proof_lines: from brain, competitive inhibition of lactase activity


organism: Mus musculus


organism: Oryctolagus cuniculus

substrate_name: Unknown

substrate: Unknown


organism: Ovis aries

substrate_name: H2O; Quercetin 4'-O-glucoside

substrate: H2O; Quercetin 4'-O-glucoside


organism: Ovis aries aries


organism: Rattus norvegicus


organism: Rattus sp.

substrate_name: phloretin-beta-D-galactoside

proof_lines: from proximal intestine isolated phlorizin hydrolase activity

proof_lines: from distal intestine isolated phlorizin hydrolase activity

proof_lines: from proximal intestine isolated lactase

substrate: phloretin-beta-D-galactoside


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

substrate_name: D-erythro-dihydrosphingosine

substrate: D-erythro-dihydrosphingosine


organism: Sus scrofa

proof_lines: slightly higher catalytic efficiency than for the human enzyme


organism: Plasmodium chabaudi

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP


organism: Plasmodium falciparum


organism: Pneumocystis carinii

assay_conditions_summary: pH 8.2; buffer 50 mM Tris


organism: Burkholderia cepacia


organism: Cupriavidus necator

proof_lines: Alcaligenes eutrophus JMP134, cell-free extract, not with purified enzyme


organism: Escherichia coli

substrate_name: Alpha-naphthyl acetate

assay_conditions_summary: pH 7

substrate: Alpha-naphthyl acetate


proof_lines: E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0


proof_lines: E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0


substrate_name: lenampicillin

proof_lines: native enzyme from liver cytosol, Vmax: 19.7 nmol/min/mg

proof_lines: recombinant CMBL, Vmax: 24.6 nmol/min/mg

substrate: lenampicillin


organism: Pseudomonas knackmussii


substrate_name: FSASALAKI

substrate: FSASALAKI


substrate_name: pro-ompA-nuclease

substrate: pro-ompA-nuclease


organism: Pseudomonas aeruginosa

substrate_name: Val-Leu-Lys-p-nitroanilide

substrate: Val-Leu-Lys-p-nitroanilide


organism: Streptococcus pyogenes


organism: Streptococcus sp.


enzyme_display_name: cathepsin E

organism: Cavia porcellus

substrate_name: acidic fibroblast growth factor

enzyme: cathepsin E

substrate: acidic fibroblast growth factor


organism: Homo sapiens

assay_conditions_summary: pH 5.8; 298.15 K; cofactor ATP

proof_lines:
with ATP, pH 5.8
without ATP, pH 5
with ATP, pH 6.2


substrate_name: tRNAfMet

substrate: tRNAfMet


organism: Saccharomyces cerevisiae

substrate_name: L-valyl-tRNAfMet

substrate: L-valyl-tRNAfMet


organism: Bos taurus

substrate_name: glycine

proof_lines:
acyl donor benzoyl-CoA
acyl donor salicyl-CoA
cosubstrate glycine

substrate: glycine


proof_lines:
acyl donor benzoyl-CoA
cosubstrate glycine
cosubstrate alanine


organism: Macaca mulatta

substrate_name: salicyl-CoA

proof_lines:
cosubstrate glycine
acyl donor salicyl-CoA
acyl donor butyryl-CoA

substrate: salicyl-CoA


organism: Oryctolagus cuniculus

proof_lines:
acyl donor phenylacetyl-CoA
cosubstrate glycine


organism: Ovis aries

substrate_name: Glycine; Salicyl-CoA

substrate: Glycine; Salicyl-CoA


organism: Acholeplasma laidlawii


organism: Euglena gracilis

substrate_name: D-glucose

proof_lines:
at pH 6.0 and 35°C
with laminaribiose addition
with glucose addition

substrate: D-glucose


organism: Paenibacillus sp. YM1


substrate_name: ATP

assay_conditions_summary: pH 8.6; 310.15 K; cofactor ATP

substrate: ATP


organism: Lathyrus oleraceus

assay_conditions_summary: cofactor ATP

proof_lines: recombinant bifunctional enzyme 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase expressed in Escherichia coli

proof_lines: bifunctional enzyme 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase from Pisum sativum and recombinant enzyme expressed in Escherichia coli


organism: Aspergillus sojae

substrate_name: Unknown

substrate: Unknown


organism: Borassus flabellifer

substrate_name: poly-D-galacturonic acid

substrate: poly-D-galacturonic acid


organism: Fusarium verticillioides

substrate_name: Polygalacturonate

substrate: Polygalacturonate


organism: Geotrichum klebahnii


organism: Geotrichum reessii

substrate_name: polygalacturonic acid

substrate: polygalacturonic acid


organism: Kluyveromyces marxianus

substrate_name: Pectin

proof_lines: apple pectin, 75% degree of esterification

substrate: Pectin


organism: Penicillium oxalicum

proof_lines: pH 5.0, 50°C, recombinant catalytic polygalacturonase domain


proof_lines: pH 5.0, 50°C, recombinant wild-type full-length enzyme


organism: Penicillium rolfsii


organism: Sclerotinia sclerotiorum


organism: Solanum lycopersicum

substrate_name: pectate

substrate: pectate


organism: Tetracoccosporium sp.


organism: Aedes aegypti

substrate_name: NADH

sequence_source: UniProtKB:Q86PM2 direct accession lookup 2026-06-17; reviewed; EC 1.14.13.9; sequence length 476

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines: recombinant enzyme, with respect to L-kynurenine, pH 7.5, 37°C

proof_lines: recombinant enzyme, with respect to NADPH, pH 7.5, 37°C

substrate: NADH


organism: Cytophaga hutchinsonii

substrate_name: L-Kynurenine; O2; H+; NADPH

sequence_source: UniProtKB:Q11PP7 direct accession lookup 2026-06-17; reviewed; EC 1.14.13.9; sequence length 449

assay_conditions_summary: cofactor NADP+

proof_lines: pH and temperature not specified in the publication

substrate: L-Kynurenine; O2; H+; NADPH


organism: Homo sapiens

substrate_name: H+; L-Kynurenine; NADPH; O2

sequence_source: UniProtKB:O15229 direct accession lookup 2026-06-17; reviewed; EC 1.14.13.9; sequence length 486

assay_conditions_summary: pH 7; 310.15 K; cofactor NADP+

proof_lines: pH 7, 37°C, full length 6His-tagged enzyme

proof_lines: pH 7, 37°C, full length 12His-tagged enzyme, FLAG tag removed during affinity purification

substrate: H+; L-Kynurenine; NADPH; O2


organism: Pseudomonas fluorescens

substrate_name: L-Kynurenine; O2; NADPH; H+

sequence_source: UniProtKB:Q84HF5 direct accession lookup 2026-06-17; reviewed; EC 1.14.13.9; sequence length 461

substrate: L-Kynurenine; O2; NADPH; H+


organism: Rattus norvegicus

substrate_name: L-Kynurenine; H+; NADPH; O2

sequence_source: UniProtKB:O88867 direct accession lookup 2026-06-17; reviewed; EC 1.14.13.9; sequence length 478

substrate: L-Kynurenine; H+; NADPH; O2


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P38169 direct accession lookup 2026-06-17; reviewed; EC 1.14.13.9; sequence length 460


organism: Cryptococcus neoformans


organism: Rhodococcus sp. M-777

proof_lines: mutant enzyme D314Y, hydrolysis reaction, at pH 4.0 and 37°C


proof_lines: mutant enzyme D311Y, hydrolysis reaction, at pH 4.0 and 37°C


proof_lines: wild type enzyme, hydrolysis reaction, at pH 4.0 and 37°C


proof_lines: 40°C, pH 4.0, erythrocyte cathepsin E, hydrolysis of (7-methoxycoumarin-4-yl)acetyl-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2


proof_lines:
40°C, pH 4.0, wild-type cathepsin E
pH 3.5, 40°C, wild-type


substrate_name: SEVNLDAEFR

assay_conditions_summary: pH 3.8; 310.15 K; buffer 50 mM sodium acetate

proof_lines: in 44 mM acetic acid/6 mM Na-acetate pH 3.8, 10 mM beta-mercaptoethanol, at 37°C

substrate: SEVNLDAEFR


organism: Perilla frutescens


enzyme_display_name: acetylspermidine deacetylase

sequence_source: UniProtKB reviewed Q969S8 / HDA10_HUMAN direct EC+organism lookup

enzyme: acetylspermidine deacetylase


organism: Rattus sp.

proof_lines: non-competitive inhibition, i.e.ammonium, (2-mercaptoethyl)trimethyl-, S-ester with O,O-diethyl phosphorothioate


enzyme_display_name: mandelamide amidase

organism: Pseudomonas putida

substrate_name: (S)-(+)-mandelamide

sequence_source: UniProtKB reviewed Q84DC4 / MANHY_PSEPU; PubMed 12670968 names Pseudomonas putida ATCC 12633 mandelamide hydrolase

enzyme: mandelamide amidase

substrate: (S)-(+)-mandelamide


substrate_name: (S)-lactamide

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q84DC4 / MANHY_PSEPU with selected batch mutation signature reconstructed after residue-position check and applied mutation signature T31I/I437N to reconstruct the assayed variant sequence.

substrate: (S)-lactamide


substrate_name: (S)-mandelamide

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q84DC4 / MANHY_PSEPU with selected batch mutation signature reconstructed after residue-position check and applied mutation signature G202S/Q207H/R236C/R369M/Q382E to reconstruct the assayed variant sequence.

substrate: (S)-mandelamide


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q84DC4 / MANHY_PSEPU with selected batch mutation signature reconstructed after residue-position check and applied mutation signature G202A/Q207H/Q382E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q84DC4 / MANHY_PSEPU with selected batch mutation signature reconstructed after residue-position check and applied mutation signature Q207H/S316N/I437N to reconstruct the assayed variant sequence.


enzyme_display_name: methenyltetrahydrofolate cyclohydrolase

enzyme: methenyltetrahydrofolate cyclohydrolase


organism: Bos taurus


organism: Clostridium formicaceticum


substrate_name: methenyltetrahydrofolate

proof_lines: forward reaction, recombinant mutant R173E

proof_lines: reverse reaction, recombinant mutant R173E, substrate 10-formyltetrahydrofolate

substrate: methenyltetrahydrofolate


proof_lines: forward reaction, recombinant mutant R173A and R173K


proof_lines: forward reaction, recombinant mutant S197D

proof_lines: reverse reaction, recombinant mutant S197D, substrate 10-formyltetrahydrofolate


proof_lines: forward reaction, recombinant mutant S197R

proof_lines: reverse reaction, recombinant mutant S197R, substrate 10-formyltetrahydrofolate


proof_lines: forward reaction, recombinant wild-type enzyme

proof_lines: reverse reaction, recombinant wild-type enzyme, substrate 10-formyltetrahydrofolate


proof_lines: forward reaction, recombinant mutant R173A

proof_lines: reverse reaction, recombinant mutant R173A, substrate 10-formyltetrahydrofolate


enzyme_display_name: ornithine decarboxylase

organism: Mus musculus

substrate_name: L-Orn

enzyme: ornithine decarboxylase

substrate: L-Orn


organism: Neurospora crassa

sequence_source: UniProtKB:P27121 direct EC+organism lookup on 2026-06-17


organism: Oenococcus oeni

substrate_name: L-ornithine

substrate: L-ornithine


organism: Panagrellus redivivus


organism: Pelophylax nigromaculatus


organism: Physarum polycephalum

substrate_name: L-Ornithine

substrate: L-Ornithine


organism: Phytomonas sp.


organism: Plasmodium falciparum

proof_lines:
recombinant PfODC domain
recombinant Pf-Hinge-ODC
recombinant PfODC


organism: Pseudomonas savastanoi pv. phaseolicola


organism: Rattus norvegicus

sequence_source: UniProtKB:P09057 direct EC+organism lookup on 2026-06-17

assay_conditions_summary: pH 7; buffer 10 mM sodium phosphate

proof_lines: in 10 mM sodium phosphate buffer, pH 7.0


organism: Homo sapiens

proof_lines: forward reaction, recombinant mutant S197T

proof_lines: reverse reaction, recombinant mutant S197T, substrate 10-formyltetrahydrofolate


proof_lines: forward reaction, recombinant mutant S197A

proof_lines: reverse reaction, recombinant mutant S197A, substrate 10-formyltetrahydrofolate


proof_lines: forward reaction, recombinant mutant R173K

proof_lines: reverse reaction, recombinant mutant R173K, substrate 10-formyltetrahydrofolate


organism: Lathyrus oleraceus


organism: Methylorubrum extorquens


organism: Oryctolagus cuniculus

substrate_name: 5,10-Methenyltetrahydrofolate; H2O

substrate: 5,10-Methenyltetrahydrofolate; H2O


organism: Ovis aries


organism: Photobacterium phosphoreum


organism: Sus scrofa


organism: Anastrepha fraterculus

proof_lines:
larva, 37°C, pH 7.1
pupa, 37°C, pH 7.1
ovaries of young females, 37°C, pH 7.1


organism: Saccharomyces cerevisiae

proof_lines:
CO2 assay, pH 7.8, 25°C
circular dichroism assay, pH 7.8, 25°C
pH 7.8, 25°C


organism: Tetrahymena pyriformis

substrate_name: L-Lys

substrate: L-Lys


organism: Tetrahymena thermophila


organism: Thermus thermophilus


organism: Trichomonas vaginalis


organism: Trypanosoma brucei


proof_lines:
native enzyme
recombinant enzyme
pH 7.0


organism: Xenopus laevis

substrate_name: L-lysine

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

substrate: L-lysine


enzyme_display_name: lysine decarboxylase

organism: Bacterium cadaveris

enzyme: lysine decarboxylase


organism: Burkholderia sp.


organism: Escherichia coli

substrate_name: delta-hydroxylysine

substrate: delta-hydroxylysine


organism: Glycine max

substrate_name: L-Lysine

substrate: L-Lysine


organism: Hafnia alvei

proof_lines: pH 6.0, 37°C, recombinant wild-type enzyme


organism: Heimia salicifolia


organism: Leptospirillum ferriphilum


organism: Ligilactobacillus saerimneri 30a


organism: Lupinus polyphyllus


organism: Serratia marcescens


organism: Vibrio parahaemolyticus


organism: Aspergillus terreus

substrate_name: L-arginine

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

substrate: L-arginine


organism: Badhamia polycephala


organism: Caenorhabditis elegans

sequence_source: UniProtKB reviewed P41931 from direct EC 4.1.1.17 + Caenorhabditis elegans lookup


proof_lines:
biosynthetic ornithine decarboxylase
degradative ornithine decarboxylase


organism: Fusobacterium necrophorum


organism: Hordeum vulgare

proof_lines:
enzyme from chromatin
cytosolic enzyme


organism: Lactobacillus sp.


organism: Lactobacillus sp. 30a

substrate_name: alpha-Methylornithine

sequence_source: UniProtKB reviewed P43099 from direct EC 4.1.1.17 + Lactobacillus sp. strain 30a lookup

substrate: alpha-Methylornithine


organism: Leishmania donovani

substrate_name: Unknown

sequence_source: UniProtKB reviewed P27116; direct UniProt reference cites PMID 17407445 / DOI 10.1042/bj20070188

substrate: Unknown


organism: Mammalia


organism: Mus musculus

proof_lines:
enzyme from epidermis
in presence of 0.25 M NaCl
in absence of NaCl


enzyme_display_name: glycerol dehydratase

organism: Klebsiella pneumoniae

enzyme: glycerol dehydratase


substrate_name: glycerol

substrate: glycerol


proof_lines: mutant I498W, pH 8.0, 42°C. Mutant Q42D, pH 9.5, 42°C, mutant Q42E, pH 8.0, 42°C. Mutant Q42F, pH 9.5, 47°C. Mutant Q42N, pH 9.5, 42°C. Mutant Q42Y, pH 7.5, 42°C


enzyme_display_name: branched-chain-2-oxoacid decarboxylase

organism: Homo sapiens

substrate_name: thiamine diphosphate

proof_lines: mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction

proof_lines: mutant Y300F, pH 7.5, 30°C, overall reaction

enzyme: branched-chain-2-oxoacid decarboxylase

substrate: thiamine diphosphate


organism: Lactococcus lactis

assay_conditions_summary: pH 6.8; buffer 50 mM potassium phosphate

proof_lines: pH and temperature not specified in the publication

proof_lines: in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate


organism: Psychrobacter arcticus


organism: Psychrobacter cryohalolentis


organism: Rattus norvegicus


enzyme_display_name: propanediol dehydratase

organism: Clostridium glycolicum

substrate_name: Glycol

enzyme: propanediol dehydratase

substrate: Glycol


organism: Klebsiella oxytoca


proof_lines:
pH 8.0, 37°C, mutant Halpha143Q
pH 8.0, 37°C, mutant Salpha224A
pH 8.0, 37°C, mutant Kbeta135E


substrate_name: CN-cobalamin

proof_lines: pH 8.0, 37°C, wild-type enzyme and mutant Salpha224A

substrate: CN-cobalamin


proof_lines: wild-type, pH 9.0, 45°C. Mutant I498C, pH 9.0, 40°C. Mutant Q42G, pH 7.5, 42°C. Mutant Q42N, pH 9.5, 42°C


proof_lines: both cytosolic and membrane associated enzymes

proof_lines: cytosolic and membrane-associated enzymes


organism: Lentilactobacillus diolivorans


organism: Levilactobacillus brevis


organism: Secundilactobacillus collinoides

substrate_name: coenzyme B12

substrate: coenzyme B12


organism: Terrisporobacter glycolicus


assay_conditions_summary: 310.15 K; buffer the presence of 0.1 M potassium phosphate

proof_lines: 37°C, recombinant enzyme, purification method 2

proof_lines: 37°C, recombinant enzyme, purification method 1 and 2


enzyme_display_name: tyrosine decarboxylase

organism: Periplaneta americana

substrate_name: L-Tyrosine

enzyme: tyrosine decarboxylase

substrate: L-Tyrosine


organism: Rehmannia glutinosa

substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Thalictrum rugosum

substrate_name: L-Dopa

proof_lines: no details of experimental conditions given

substrate: L-Dopa


enzyme_display_name: phenylpyruvate decarboxylase

organism: Acinetobacter sp.

substrate_name: phenylpyruvate

enzyme: phenylpyruvate decarboxylase

substrate: phenylpyruvate


organism: Azospirillum brasilense

substrate_name: 4-phenyl-2-oxobutanoic acid

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

proof_lines: in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30°C

substrate: 4-phenyl-2-oxobutanoic acid


organism: Enterobacter sp. CGMCC 5087


organism: Saccharomyces cerevisiae

proof_lines:
strain CEN.PK 608-4B
strain CEN.PK 555-4A
strain CEN.PK 113-7D


organism: Bacillus subtilis

proof_lines: and 2-oxoisopentanoate, 2-oxoisohexanoate, value below, 30°C, pH 7.5


organism: Homo sapiens

proof_lines: mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction

proof_lines: mutant Y300A, pH 7.5, 30°C, overall reaction


proof_lines: mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction

proof_lines: mutant R301A, pH 7.5, 30°C, overall reaction


proof_lines: mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction

proof_lines: mutant D295A, pH 7.5, 30°C, overall reaction


proof_lines: wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction

proof_lines: wild-type, pH 7.5, 30°C, overall reaction


organism: Enterococcus faecalis

substrate_name: L-Tyr

substrate: L-Tyr


organism: Enterococcus faecium


organism: Eschscholzia californica


proof_lines:
pH 5, 25°C, IOEB 9809, crude extract
pH 5, 25°C, ATCC 367, crude extract
pH 5, 25°C


proof_lines: purified recombinant mutant Y398A, pH 5.0-7.4, 40°C


proof_lines: purified recombinant mutant S586A, pH 5.0-7.4, 40°C


proof_lines: purified recombinant mutant K240A, pH 5.0-7.4, 40°C


proof_lines: purified recombinant mutants S586A and Y398F, pH 5.0-7.4, 40°C


proof_lines: purified recombinant His-tagged wild-type enzyme, pH 5.0-7.4, 40°C


proof_lines: purified recombinant mutant Y398F, pH 5.0-7.4, 40°C


organism: Locusta migratoria


organism: Lycoris aurea


enzyme_display_name: cathepsin G

substrate_name: Z-Lys-SBzl

enzyme: cathepsin G

substrate: Z-Lys-SBzl


enzyme_display_name: aryl-acylamidase

organism: Oryza sativa

enzyme: aryl-acylamidase


organism: Pseudomonas fluorescens

substrate_name: p-nitroacetanilide

substrate: p-nitroacetanilide


organism: Pseudomonas sp.

proof_lines:
strain RA2
strain RB4


organism: Rattus norvegicus


organism: Rhodococcus erythropolis

substrate_name: acetaminophen

substrate: acetaminophen


organism: Taraxacum officinale


organism: Limosilactobacillus reuteri


enzyme_display_name: phosphatidate phosphatase

organism: Eimeria tenella

substrate_name: lysophosphatidate

sequence_source: UniProt REST accession lookup A0A0A7H9C0

enzyme: phosphatidate phosphatase

substrate: lysophosphatidate


sequence_source: UniProt REST accession lookup A0A0A7H6F4


substrate_name: diacylglycerol diphosphate

sequence_source: UniProt REST accession lookup Q8NEB5

substrate: diacylglycerol diphosphate


sequence_source: UniProt REST accession lookup Q5VZY2


substrate_name: phosphatidate

proof_lines: truncated protein lacking NDR and CDR regions, pH 7.5, 30Â°C

substrate: phosphatidate


mutation_signature: truncated protein 1-591

sequence_source: reconstructed from UniProt REST accession lookup P32567 residues 1-591

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.


sequence_source: UniProt REST accession lookup P32567


organism: bacterium CSBL00001

sequence_source: UniProt REST accession lookup C3UWD1

proof_lines:
pH 9.0, 37°C
Raw SKiD Env: Temp=37°C, pH=9


organism: Paracoccus sp. M1-1

sequence_source: UniProt REST accession lookup F6N111

proof_lines:
pH 7.0, 35°C, recombinant enzyme
pH 7.0, 35°C


organism: Starkeya sp.


organism: Bos taurus

substrate_name: o-nitroacetanilide

substrate: o-nitroacetanilide


organism: Glycine max

substrate_name: Nalpha-benzoyl-DL-Arg 2-naphthylamide

substrate: Nalpha-benzoyl-DL-Arg 2-naphthylamide


organism: Homo sapiens

proof_lines: assays performed at high albumin concentrations, spectrophotometric assay


substrate_name: Unknown

proof_lines: wild type, substrate: o-nitroacetanilide

proof_lines: wild type, substrate: m-(acetamido)N,N,N-trimethylanilinium, inhibition depends on substrate concentration

substrate: Unknown


proof_lines: value above 0.3 mM, mutant D70G, substrate: o-nitroacetanilide, inhibition depends on substrate concentration

proof_lines: mutant D70G, substrate: m-(acetamido)N,N,N-trimethylanilinium


organism: Mesocricetus auratus


organism: Oncorhynchus mykiss

substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


organism: Vigna radiata var. radiata


substrate_name: phosphatidic acid

substrate: phosphatidic acid


organism: Momordica charantia


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: phosphatidate dispersed in sonicated microsomal lipid

proof_lines: phosphatidate bound to microsomal membrane


organism: Saccharomyces cerevisiae

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


organism: Lysinibacillus sphaericus


organism: Nocardia farcinica

substrate_name: hexanoamide

substrate: hexanoamide


organism: Oryza alta


organism: Oryza coarctata


organism: Oryza collina


organism: Oryza grandiglumis


organism: Oryza longiglumis


organism: Oryza longistaminata


organism: Oryza officinalis


organism: Oryza punctata


organism: Oryza ridleyi


organism: Oryza rufipogon


organism: Homo sapiens

substrate_name: UDP-alpha-D-GlcNAc

sequence_variant_note: Resolved canonical sequence from UniProtKB Q10469 REST lookup on 2026-06-17; row-specific variant reconstructed from the canonical sequence. and applied mutation signature E259A to reconstruct the assayed variant sequence.

substrate: UDP-alpha-D-GlcNAc


sequence_variant_note: Resolved canonical sequence from UniProtKB Q10469 REST lookup on 2026-06-17; row-specific variant reconstructed from the canonical sequence. and applied mutation signature N318A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q10469 REST lookup on 2026-06-17; row-specific variant reconstructed from the canonical sequence. and applied mutation signature D217A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q10469 REST lookup on 2026-06-17; row-specific variant reconstructed from the canonical sequence. and applied mutation signature Y344A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q10469 REST lookup on 2026-06-17; row-specific variant reconstructed from the canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q10469 REST lookup on 2026-06-17; row-specific variant reconstructed from the canonical sequence. and applied mutation signature R198A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q10469 REST lookup on 2026-06-17; row-specific variant reconstructed from the canonical sequence. and applied mutation signature W346A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q10469 REST lookup on 2026-06-17; row-specific variant reconstructed from the canonical sequence. and applied mutation signature Y294A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q10469 REST lookup on 2026-06-17.

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

proof_lines: pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293S cells

proof_lines: pH 7.0, 37°C, recombinant wild-type mutant expressed from HEK-293F cells


organism: Eimeria tenella

sequence_source: UniProtKB A0A0A7H9U0 REST lookup on 2026-06-17.


enzyme_display_name: nitric oxide dioxygenase

organism: Cupriavidus necator

substrate_name: Nitric oxide; O2; NADH

sequence_source: UniProtKB:P39662 reviewed record, fetched 2026-06-17

assay_conditions_summary: cofactor NADPH

proof_lines:
apparent KM
Raw SKiD Env: Temp=-----, pH=-----

enzyme: nitric oxide dioxygenase

substrate: Nitric oxide; O2; NADH


substrate_name: NADH

assay_conditions_summary: pH 7.8; 310.15 K; cofactor NADPH

substrate: NADH


organism: Escherichia coli

substrate_name: NADH; O2; Nitric oxide

sequence_variant_note: Resolved canonical sequence from UniProtKB:P24232 reviewed record plus Y29F substitution reconstructed from selected SABIO-RK mutation note, fetched/computed 2026-06-17 and applied mutation signature Y29F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: nitric oxide dioxygenase(Enzyme) mutant Phe(B10) (Y29F)

substrate: NADH; O2; Nitric oxide


sequence_source: UniProtKB:P24232 reviewed record, fetched 2026-06-17


smiles: O=O

assay_conditions_summary: pH 7; 283.15 K; cofactor NADPH


substrate_name: H+; Cumene hydroperoxide; NADH

substrate: H+; Cumene hydroperoxide; NADH


organism: Giardia lamblia

sequence_source: UniProtKB:E2RTZ4 reviewed record, fetched 2026-06-17

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH


organism: Saccharomyces cerevisiae

substrate_name: O2; Nitric oxide; NADH

sequence_source: UniProtKB:P39676 reviewed record, fetched 2026-06-17

substrate: O2; Nitric oxide; NADH


enzyme_display_name: choline O-acetyltransferase

substrate_name: Acetyl-CoA; Choline

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

assay_conditions_summary: cofactor CoA

proof_lines: SABIO-RK modifier species: choline O-acetyltransferase(Enzyme) mutant R482G

enzyme: choline O-acetyltransferase

substrate: Acetyl-CoA; Choline


substrate_name: Choline

smiles: C[N+](C)(C)CCO

substrate: Choline


substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession:P28329 and applied mutation signature I305T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

substrate: Acetyl-CoA


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession:P28329 and applied mutation signature L210P to reconstruct the assayed variant sequence.


substrate_name: Choline; Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession:P28329 and applied mutation signature P211A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: choline O-acetyltransferase(Enzyme) mutant P211A

substrate: Choline; Acetyl-CoA


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession:P28329 and applied mutation signature V506L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: choline O-acetyltransferase(Enzyme) mutant V506L


proof_lines: SABIO-RK modifier species: choline O-acetyltransferase(Enzyme) mutant R560H


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession:P28329 and applied mutation signature R420C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: choline O-acetyltransferase(Enzyme) mutant R420C


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession:P28329 and applied mutation signature S498L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: choline O-acetyltransferase(Enzyme) mutant S498L


proof_lines: SABIO-RK modifier species: choline O-acetyltransferase(Enzyme) mutant L210P


sequence_source: UniProtKB:P39662 direct accession lookup


assay_conditions_summary: pH 7.8; 310.15 K; cofactor NADH


sequence_variant_note: Resolved canonical sequence from UniProtKB:P24232 direct accession lookup and applied mutation signature Y29F to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+


substrate_name: NADPH

sequence_source: UniProtKB:P24232 direct accession lookup

substrate: NADPH


sequence_source: UniProtKB:E2RTZ4 direct accession lookup


sequence_source: UniProtKB:P39676 direct accession lookup


enzyme_display_name: ureidoglycolate dehydrogenase (NAD(+))

substrate_name: (S)-ureidoglycolate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P77555 direct accession lookup and applied mutation signature S43A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S43A, pH and temperature not specified in the publication

enzyme: ureidoglycolate dehydrogenase (NAD(+))

substrate: (S)-ureidoglycolate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77555 direct accession lookup and applied mutation signature R259A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R259A, pH and temperature not specified in the publication


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from UniProtKB:P77555 direct accession lookup and applied mutation signature D141E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D141E, pH and temperature not specified in the publication

substrate: NAD+


sequence_source: UniProtKB:P77555 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77555 direct accession lookup and applied mutation signature D141N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D141N, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77555 canonical sequence with validated D141A substitution reconstructed during review. and applied mutation signature D141A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D141A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77555 canonical sequence with validated M251A substitution reconstructed during review. and applied mutation signature M251A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M251A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77555 canonical sequence with validated Y52F substitution reconstructed during review. and applied mutation signature Y52F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y52F, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77555 canonical sequence with validated H44A substitution reconstructed during review. and applied mutation signature H44A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H44A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77555 canonical sequence with validated S140A substitution reconstructed during review. and applied mutation signature S140A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S140A, pH and temperature not specified in the publication


sequence_source: UniProtKB:P77555 direct accession lookup during review.

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:P28329 canonical sequence with validated I305T substitution reconstructed during review. and applied mutation signature I305T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: choline O-acetyltransferase(Enzyme) mutant I305T


sequence_source: UniProtKB:P28329 direct accession lookup during review.


enzyme_display_name: flavone 7-O-beta-glucosyltransferase

organism: Arabidopsis thaliana

substrate_name: eriodictyol

sequence_source: UniProtKB:Q8VZE9 direct accession lookup during review.

assay_conditions_summary: pH 7

enzyme: flavone 7-O-beta-glucosyltransferase

substrate: eriodictyol


organism: Bacillus licheniformis

substrate_name: TDP-glucose

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

assay_conditions_summary: pH 8

proof_lines: wild-type, pH 8.0, temperature not specified in the publication

substrate: TDP-glucose


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 R282W, pH 8.0, temperature not specified in the publication


substrate_name: corylifol A

proof_lines: pH 9.6, temperature not specified in the publication

substrate: corylifol A


organism: Erigeron breviscapus

substrate_name: 4-coumaric acid

sequence_source: UniProtKB:A0A4D6J6W7 direct accession lookup during review.

substrate: 4-coumaric acid


sequence_source: UniProtKB:A0A4D6J6N6 direct accession lookup during review.


organism: Zea mays

substrate_name: apigenin

sequence_source: UniProtKB:A0A1D6MY21 direct accession lookup during review.

substrate: apigenin


organism: Gallus gallus

proof_lines: recombinant ART4, in the presence of PNGase F


assay_conditions_summary: 310.15 K; cofactor NAD+

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

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: with protein L-arginine methyl ester as acceptor, at pH 7.5, temperature not specified in the publication

proof_lines: with protein Nalpha-acetyl-L-arginine methyl ester as acceptor, at pH 7.5, temperature not specified in the publication


organism: Mus musculus

substrate_name: NAD+; L-Arginine

substrate: NAD+; L-Arginine


assay_conditions_summary: pH 7.4; 310.15 K; buffer 50mM HEPES

proof_lines: at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl


enzyme_display_name: meprin B

substrate_name: Abz-VKMDAE-EDDnp

enzyme: meprin B

substrate: Abz-VKMDAE-EDDnp


proof_lines:
pH 7.5, 37°C
pH 7.5, 30°C, recombinant enzyme
pH 7.4, 30°C, recombinant enzyme


substrate_name: Abz-VNLDAE-EDDnp

substrate: Abz-VNLDAE-EDDnp


substrate_name: H2O; Xyloglucan

sequence_source: UniProt P93046 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).

substrate: H2O; Xyloglucan


organism: Aspergillus aculeatus

substrate_name: xyloglucan

sequence_source: UniProt O94218 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).

proof_lines:
from tamarind, pH 5, 37°C
pH 5, 37°C

substrate: xyloglucan


organism: Aspergillus fumigatus

sequence_source: UniProt Q4WB93 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).


organism: Aspergillus niger

sequence_source: UniProt A1XP58 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).


organism: Aspergillus oryzae

substrate_name: carboxymethyl cellulose

sequence_source: UniProt I8IVP5 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).

substrate: carboxymethyl cellulose


substrate_name: tamarind seed xyloglucan

sequence_source: UniProt Q2UK93 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).

substrate: tamarind seed xyloglucan


organism: Bacteroides ovatus

substrate_name: XXXG-beta-CNP; H2O

sequence_source: UniProt A7LXT7 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).

unit: onedivsecgl

substrate: XXXG-beta-CNP; H2O


organism: Cellvibrio japonicus

sequence_source: UniProt B3PKK9 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).


organism: Paenibacillus odorifer

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

proof_lines: xyloglucan from tamarind seed, pH 7.0, 37°C, recombinant mutant PoGH74catW406A

proof_lines: xyloglucan from tamarind seed, pH 7.0, 37°C, recombinant mutant PoGH74catW348A

proof_lines: xyloglucan from tamarind seed, pH 7.0, 37°C, recombinant mutant PoGH74catG476Y


proof_lines: xyloglucan from tamarind seed, pH 7.0, 37°C, recombinant wild-type enzyme PoGH74


organism: Paenibacillus sp.

sequence_source: UniProt Q3MUH7 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).


substrate_name: Xyloglucan; H2O

sequence_source: UniProt Q3MUH8 canonical sequence; UniProt REST lookup on 2026-06-18 (UniProt release 2026_02).

substrate: Xyloglucan; H2O


proof_lines: pH 6.0, 45°C, recombinant mutant W61A enzyme catalytic domain


proof_lines: pH 6.0, 45°C, recombinant mutant W64A enzyme catalytic domain


proof_lines: pH 6.0, 45°C, recombinant mutant W319A enzyme catalytic domain


proof_lines: pH 6.0, 45°C, recombinant wild-type enzyme catalytic domain


substrate_name: NAD for the NADase activity (in the presence of 0.03 mM DTT)

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

assay_conditions_summary: cofactor ADP


organism: Candida albicans

substrate_name: Unknown

substrate: Unknown


organism: Escherichia coli

substrate_name: NADH

assay_conditions_summary: 310.15 K; cofactor NADPH

proof_lines:
per heme at 37°C
per heme at 20°C
with 0.001 mM NO at 37°C

substrate: NADH


organism: Homo sapiens

substrate_name: NO

substrate: NO


organism: Hordeum vulgare

substrate_name: NADPH

substrate: NADPH


organism: Saccharomyces cerevisiae


organism: Vibrio vulnificus

substrate_name: nitric oxide

proof_lines:
at pH 7.8 and 30°C
at pH 7.8 and 37°C

substrate: nitric oxide


organism: Bos taurus

substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Cornu aspersum

substrate_name: choline

substrate: choline


organism: Doryteuthis pealeii


organism: Drosophila melanogaster

substrate_name: Acetylcholine

substrate: Acetylcholine


substrate_name: CoA

substrate: CoA


organism: Drosophila sp. (in: flies)


organism: Electrophorus electricus

substrate_name: Acetyl-CoA; Choline

substrate: Acetyl-CoA; Choline


organism: Limulus polyphemus


organism: Loligo sp.


organism: Mus musculus


organism: Oryctolagus cuniculus


organism: Periplaneta americana


organism: Platyrrhini


organism: Rattus norvegicus


organism: Unknown

substrate_name: Arginine methyl ester

substrate: Arginine methyl ester


organism: Paenibacillus sp.

proof_lines: pH 6.0, 45°C, recombinant mutant w318A enzyme catalytic domain


organism: uncultured bacterium

substrate_name: tamarind xyloglucan

proof_lines: pH and temperature not specified in the publication

substrate: tamarind xyloglucan


organism: Homo sapiens

substrate_name: Abz-MGWMDEIDK(Dnp)SG-OH

sequence_source: UniProtKB Q16820 direct lookup

substrate: Abz-MGWMDEIDK(Dnp)SG-OH


substrate_name: Abz-YVAEAPK(Dnp)G-OH

substrate: Abz-YVAEAPK(Dnp)G-OH


organism: Escherichia coli (strain K12)

substrate_name: NAD

proof_lines: kcat is 62.39 sec(-1) for dehydrogenase activity with NAD. kcat is 57.06 sec(-1) for dehydrogenase activity with (S)-ureidoglycolate.

substrate: NAD


organism: Punica granatum

substrate_name: gallic acid (at pH 5.0 and 30 degrees Celsius)

proof_lines: kcat is 0.52 sec(-1) with gallic acid as substrate. kcat is 0.61 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 0.76 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.64 sec(-1) with caffeic acid as substrate. kcat is


proof_lines: kcat is 0.55 sec(-1) with gallic acid as substrate. kcat is 0.6 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec(-1) with caffeic acid as substrate. kcat is

substrate: gallic acid (at pH 5.0 and 30 degrees Celsius)


organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

proof_lines: kcat is 0.11 min(-1) with DdGluD2 as substrate. kcat is 0.15 min(-1) with NAD(+) as substrate.


organism: Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)

substrate_name: NAD(+)

proof_lines: Measured on chicken skeletal alpha-actin.

substrate: NAD(+)


organism: Salmonella typhimurium

proof_lines: For a catalytic domain encompassing residues 375-591, measured on Drosophila melanogaster Act88F indirect flight muscle actin.


organism: Arabidopsis thaliana

substrate_name: XXXGol

proof_lines: KM for xyloglucan as donor substrate is 1.6 mg/ml. KM is quoted in mg/ml, not uM, because XTHs are able to utilise any segment of the polysaccharide chain equally well, not just one site per molecule as with the acceptor.

substrate: XXXGol


proof_lines: KM for xyloglucan as donor substrate is 2.87 mg/ml. KM is quoted in mg/ml, not uM, because XTHs are able to utilise any segment of the polysaccharide chain equally well, not just one site per molecule as with the acceptor.


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

substrate_name: XXXG-beta-CNP

proof_lines: kcat is 10.5 sec(-1) for XXXG-beta-CNP. kcat is 11.1 sec(-1) for XLLG-beta-CNP. kcat is 0.12 sec(-1) for GGGG-beta-CNP.

substrate: XXXG-beta-CNP


substrate_name: carnitine

proof_lines: enzyme mutant ChAT-R, cosubstrate acetyl-CoA

proof_lines: enzyme mutant ChAT-TET, cosubstrate acetyl-CoA

proof_lines: enzyme mutant ChAT-R, cosubstrate carnitine

substrate: carnitine


proof_lines:
cosubstrate acetyl-CoA
cosubstrate choline
cosubstrate carnitine


organism: Rhizoglyphus echinopus


organism: Torpedo sp.


organism: Arachis hypogaea

substrate_name: naringenin

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

substrate: naringenin


organism: Entada phaseoloides

substrate_name: luteolin

substrate: luteolin


organism: Glycine max

substrate_name: genistein

proof_lines: isoform UGT73C20, cosubstrate UDP-glucose, pH 7.5, 30°C

proof_lines: isoform UGT88E19, cosubstrate UDP-glucose, pH 7.5, 30°C

proof_lines: isoform UGT92G4, cosubstrate UDP-glucose, pH 7.5, 30°C

substrate: genistein


organism: Marchantia paleacea

substrate_name: quercetin

substrate: quercetin


organism: Petroselinum crispum

substrate_name: TDPglucose

substrate: TDPglucose


organism: Clostridium perfringens

substrate_name: NAD+

proof_lines: ADP-ribosyltransferase activity, mutant enzyme Y251A, cosubstrate: non-muscle actin from human platelets

substrate: NAD+


proof_lines: ADP-ribosyltransferase activity, mutant enzyme N255A, cosubstrate: rabbit muscle actin

proof_lines: ADP-ribosyltransferase activity, mutant enzyme N255A, cosubstrate: non-muscle actin from human platelets


proof_lines: ADP-ribosyltransferase activity, mutant enzyme Y246A, cosubstrate: non-muscle actin from human platelets

proof_lines: ADP-ribosyltransferase activity, mutant enzyme Y246A, cosubstrate: rabbit muscle actin


proof_lines: ADP-ribosyltransferase activity, mutant enzyme F349A, cosubstrate: rabbit muscle actin

proof_lines: ADP-ribosyltransferase activity, mutant enzyme F349A, cosubstrate: non-muscle actin from human platelets


proof_lines: ADP-ribosyltransferase activity, wild-type enzyme, cosubstrate: rabbit muscle actin

proof_lines: ADP-ribosyltransferase activity, wild-type enzyme, cosubstrate: non-muscle actin from human platelets


organism: Gallus gallus

substrate_name: beta/gamma-actin-L-arginine

proof_lines:
reaction with gamma-actin
reaction with alpha-actin
reaction with beta/gamma-actin

substrate: beta/gamma-actin-L-arginine


organism: Homo sapiens


organism: Lysinibacillus sphaericus

assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines:
pH 7.4, absence of peptide 265-285
pH 7.4, presence of peptide 265-285


organism: Meleagris gallopavo

proof_lines: in presence of 250 mM NaCl, NAD:arginine ADP-ribosyltransferase A


organism: Mus musculus

proof_lines: reaction with 20 mM agmatine, enzyme Yac-1


organism: Rattus norvegicus


organism: Tequatrovirus T4


organism: Vibrio splendidus

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: NADH-dependent peroxiredoxin

organism: Burkholderia thailandensis

sequence_source: UniProtKB:Q2SWT3 direct accession lookup

proof_lines: in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C

proof_lines: in the presence of AhpD as reducing system, at pH 7.4 and 25°C

enzyme: NADH-dependent peroxiredoxin


substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


smiles: OO


substrate_name: tert-butyl hydroperoxide

smiles: CC(C)(C)OO

substrate: tert-butyl hydroperoxide


organism: Salmonella enterica subsp. enterica serovar Typhimurium

sequence_source: UniProtKB:P0A251 canonical sequence plus PMID: 28375740; DOI: 10.1089/ars.2016.6922 mutation T43S with paper-numbering initiator-Met offset applied

sequence_variant_note: Mutation signature T43S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P0A251 direct accession lookup


sequence_source: UniProtKB:P0A251 canonical sequence plus PMID: 28375740; DOI: 10.1089/ars.2016.6922 mutation E49Q with paper-numbering initiator-Met offset applied

sequence_variant_note: Mutation signature E49Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A251 canonical sequence plus PMID: 28375740; DOI: 10.1089/ars.2016.6922 mutation W169F with paper-numbering initiator-Met offset applied and applied mutation signature W169F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A251 canonical sequence plus PMID: 28375740; DOI: 10.1089/ars.2016.6922 mutation W81F with paper-numbering initiator-Met offset applied and applied mutation signature W81F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A251 canonical sequence plus PMID: 28375740; DOI: 10.1089/ars.2016.6922 mutation C165S with paper-numbering initiator-Met offset applied and applied mutation signature C165S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0A251 canonical sequence plus PMID: 28375740; DOI: 10.1089/ars.2016.6922 mutation R119A with paper-numbering initiator-Met offset applied

sequence_variant_note: Mutation signature R119A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P0A251 canonical sequence plus PMID: 28375740; DOI: 10.1089/ars.2016.6922 mutation T77I with paper-numbering initiator-Met offset applied

sequence_variant_note: Mutation signature T77I could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P0A251 canonical sequence plus PMID: 28375740; DOI: 10.1089/ars.2016.6922 mutation T43V with paper-numbering initiator-Met offset applied

sequence_variant_note: Mutation signature T43V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P0A251 canonical sequence plus PMID: 28375740; DOI: 10.1089/ars.2016.6922 mutation T77V with paper-numbering initiator-Met offset applied

sequence_variant_note: Mutation signature T77V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P0A251 FASTA; variant reconstructed from selected mutation signature using mature-chain offset +1

sequence_variant_note: Mutation signature T43A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A251 FASTA; variant reconstructed from selected mutation signature using mature-chain offset +1 and applied mutation signature W81F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A251 FASTA; variant reconstructed from selected mutation signature using mature-chain offset +1 and applied mutation signature C165S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0A251 FASTA; variant reconstructed from selected mutation signature using mature-chain offset +1 and applied mutation signature W169F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

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

proof_lines: kcat is 55.1 sec(-1) with H(2)O(2) as substrate.


enzyme_display_name: inositol-polyphosphate 5-phosphatase

proof_lines: kcat is 0.026 sec(-1) with 1D-myo-inositol 1,4,5-trisphosphate.

enzyme: inositol-polyphosphate 5-phosphatase


substrate_name: 1D-myo-inositol 1,4,5-trisphosphate

proof_lines: kcat is 194.4 sec(-1) with 1D-myo-inositol 1,4,5-trisphosphate.

substrate: 1D-myo-inositol 1,4,5-trisphosphate


proof_lines: kcat is 26 sec(-1) with 1D-myo-inositol 1,4,5-trisphosphate.


organism: Arabidopsis thaliana


organism: Canis lupus familiaris

substrate_name: inositol 1,4,5- trisphosphate

substrate: inositol 1,4,5- trisphosphate


substrate_name: phosphatidylinositol 4,5-bisphosphate

substrate: phosphatidylinositol 4,5-bisphosphate


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

proof_lines: membrane associated enzyme, pH 7.2, 37°C


substrate_name: D-myo-inositol 1,4,5-trisphosphate

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

substrate: D-myo-inositol 1,4,5-trisphosphate


organism: Oryctolagus cuniculus

proof_lines:
membrane bound enzyme, pH 7.2, 30°C
soluble enzyme, pH 7.2, 30°C


substrate_name: D-myo-Inositol 1,4,5-trisphosphate; H2O

proof_lines:
type I enzyme, pH 7.1, 30°C
pH 7.2, 37°C
type II enzyme, pH 7.1, 30°C

substrate: D-myo-Inositol 1,4,5-trisphosphate; H2O


organism: Saccharomyces cerevisiae


proof_lines: pH 7.2, 30°C, recombinant truncated enzyme Siw14(116-281)


proof_lines: pH 7.2, 30°C, recombinant wild-type enzyme Siw14


organism: Phanerodontia chrysosporium

substrate_name: xyloglucan

proof_lines: 30°C, pH 5, enzyme with C-terminal carbohydrate binding module domain

proof_lines: 30°C, pH 5, enzyme without C-terminal carbohydrate binding module domain

substrate: xyloglucan


organism: Thermomonospora sp.

substrate_name: Unknown

substrate: Unknown


organism: Trichoderma reesei

substrate_name: phosphoric acid-swollen cellulose

substrate: phosphoric acid-swollen cellulose


organism: Tropaeolum majus

proof_lines: pH 4.8, isoform NXG1, hydrolysis of xyloglucan

proof_lines: pH 4.8, isoform NXG1, transglycosylation of xyloglucan


proof_lines: pH 4.8, mutant DELTAYNIIG of isoform NXG1, hydrolysis of xyloglucan

proof_lines: pH 4.8, mutant DELTAYNIIG of isoform NXG1, transglycosylation of xyloglucan


organism: Vigna angularis

assay_conditions_summary: pH 6


substrate_name: N-benzoyl-L-tyrosine ethyl ester

substrate: N-benzoyl-L-tyrosine ethyl ester


organism: Homo sapiens

assay_conditions_summary: pH 8; 310.15 K; buffer and 1

proof_lines: wild type enzyme, in PBS buffer, pH 8.0, 37°C

proof_lines: wild type enzyme, in 1.8 M NaCl, pH 8.0, 37°C


proof_lines: pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-4-nitroanilide


organism: Mus musculus


proof_lines: mutant enzyme S189A/A226E, in PBS buffer, pH 8.0, 37°C

proof_lines: mutant enzyme S189A/A226E, in 1.8 M NaCl, pH 8.0, 37°C


assay_conditions_summary: pH 8; 310.15 K; buffer PBS

proof_lines: mutant enzyme A226E, in 1.8 M NaCl, pH 8.0, 37°C

proof_lines: mutant enzyme A226E, in PBS buffer, pH 8.0, 37°C


organism: Schizosaccharomyces pombe


organism: Sus scrofa

proof_lines: with inositol 1,3,4,5-tetrakisphosphate as substrate


organism: Acetivibrio thermocellus

substrate_name: lichenan

substrate: lichenan


organism: Aspergillus japonicus


organism: Aspergillus niger


organism: Fragaria chiloensis

substrate_name: xyloglucan octasaccharide XXXGXXXG

substrate: xyloglucan octasaccharide XXXGXXXG


organism: Lathyrus oleraceus


organism: Paenibacillus polymyxa


organism: Salmonella enterica subsp. enterica serovar Typhimurium

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A251 plus row mutation C165S reconstructed after offset check against RCSB 4XS6/PDB numbering. and applied mutation signature C165S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C165S, at pH 8.5, temperature not specified in the publication


sequence_source: UniProtKB reviewed accession P0A251 plus row mutation T77V reconstructed after offset check against RCSB 4XS6/PDB numbering.

proof_lines: mutant enzyme T77V, at pH 8.5, temperature not specified in the publication


sequence_source: UniProtKB reviewed accession P0A251 plus row mutation T43A reconstructed after offset check against RCSB 4XS6/PDB numbering.

proof_lines: mutant enzyme T43A, at pH 8.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A251 plus row mutation W81F reconstructed after offset check against RCSB 4XS6/PDB numbering. and applied mutation signature W81F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W81F, at pH 8.0, temperature not specified in the publication


sequence_source: UniProtKB reviewed accession P0A251 plus row mutation T77I reconstructed after offset check against RCSB 4XS6/PDB numbering.

proof_lines: mutant enzyme T77I, at pH 8.5, temperature not specified in the publication


sequence_source: UniProtKB reviewed accession P0A251 plus row mutation R119A reconstructed after offset check against RCSB 4XS6/PDB numbering.

proof_lines: mutant enzyme R119A, at pH 8.5, temperature not specified in the publication