sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature Δ170 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme DELTA170-171, at pH 7.5 and 20°C


enzyme_display_name: dUTP diphosphatase

organism: white spot syndrome virus

substrate_name: dUTP

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature R158A to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTR158A'; column 'kcat (s-1)' = 3.2; column 'Km (uM)' = 2.6; column 'kcat/Km (M-1 s-1)' = 1.2 x 10^6; column 'Relative efficiency (%)' = 28. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.2 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.2 s^(-1). Km: printed Table 1 cell 2.6 in a column headed Km (uM); 1 uM is 0.001 mM, so 2.6 / 1000 = 0.0026 mM. kcat/Km: printed Table 1 cell 1.2 x 10^6 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1200000 / 1000 = 1200 s^-1 mM^-1. The exported values are kcat 3.2 s^(-1) and Km 0.0026 mM and kcat_over_km 1230.769230769231 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTR158A': kcat = 3.2 s-1; Km = 2.6 uM; printed kcat/Km = 1.2 x 10^6 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTR158A'

table_label: Table 1: Enzyme kinetics data (J. Biol. Chem. 2018, 293(3):1088-1099). Printed column heads: Enzyme; kcat (s-1); Km (uM); kcat/Km (M-1 s-1); Relative efficiency (%).

data_origin: experimental

enzyme: dUTP diphosphatase

substrate: dUTP

status: corrected

source: oed


mutation_signature: Unknown

sequence_source: UniProtKB Q77J78 FASTA direct lookup

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

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTWT'; column 'kcat (s-1)' = 7.4; column 'Km (uM)' = 1.7; column 'kcat/Km (M-1 s-1)' = 4.4 x 10^6; column 'Relative efficiency (%)' = 100. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.4 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 7.4 s^(-1). Km: printed Table 1 cell 1.7 in a column headed Km (uM); 1 uM is 0.001 mM, so 1.7 / 1000 = 0.0017 mM. kcat/Km: printed Table 1 cell 4.4 x 10^6 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4400000 / 1000 = 4400 s^-1 mM^-1. The exported values are kcat 7.4 s^(-1) and Km 0.0017 mM and kcat_over_km 4352.941176470588 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTWT': kcat = 7.4 s-1; Km = 1.7 uM; printed kcat/Km = 4.4 x 10^6 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTWT'


source_db: brenda

kcat_over_km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature R158A to reconstruct the assayed variant sequence.

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature S115R to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTS115R'; column 'kcat (s-1)' = 2.6; column 'Km (uM)' = 4.5; column 'kcat/Km (M-1 s-1)' = 5.8 x 10^5; column 'Relative efficiency (%)' = 13. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.6 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.6 s^(-1). Km: printed Table 1 cell 4.5 in a column headed Km (uM); 1 uM is 0.001 mM, so 4.5 / 1000 = 0.0045 mM. kcat/Km: printed Table 1 cell 5.8 x 10^5 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 580000 / 1000 = 580 s^-1 mM^-1. The exported values are kcat 2.6 s^(-1) and Km 0.0045 mM and kcat_over_km 577.7777777777778 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTS115R': kcat = 2.6 s-1; Km = 4.5 uM; printed kcat/Km = 5.8 x 10^5 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTS115R'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature D170G to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTD170G'; column 'kcat (s-1)' = 6.2; column 'Km (uM)' = 2.1; column 'kcat/Km (M-1 s-1)' = 3.0 x 10^6; column 'Relative efficiency (%)' = 68. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.2 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 6.2 s^(-1). Km: printed Table 1 cell 2.1 in a column headed Km (uM); 1 uM is 0.001 mM, so 2.1 / 1000 = 0.0021 mM. kcat/Km: printed Table 1 cell 3.0 x 10^6 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3000000 / 1000 = 3000 s^-1 mM^-1. The exported values are kcat 6.2 s^(-1) and Km 0.0021 mM and kcat_over_km 2952.3809523809527 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTD170G': kcat = 6.2 s-1; Km = 2.1 uM; printed kcat/Km = 3.0 x 10^6 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTD170G'


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature S115R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature R161K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature D170G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature F166Y to reconstruct the assayed variant sequence.


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Dictyostelium discoideum

source_db: uniprot

proof_lines: kcat is 9.3 sec(-1) with dUTP as substrate.

source: uniprot


organism: Escherichia coli (strain K12)

proof_lines: kcat is 21 sec(-1) with dUTP as substrate, and 15 sec(-1) with dTTP as substrate.


kcat_display: Not reported


organism: Homo sapiens

proof_lines: kM is identical for both isoform 2 and isoform 3.


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


organism: Human gammaherpesvirus 4

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P03195 (2026-07-01) and applied mutation signature C4S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C4S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


kcat_over_km_origin: calculated

sequence_source: UniProtKB direct accession lookup P03195 (2026-07-01)


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P03195 (2026-07-01) and applied mutation signature D131N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D131N, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


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


organism: Leishmania major

substrate_name: dUDP

sequence_source: UniProtKB direct accession lookup O15826 (2026-07-01)

substrate: dUDP


substrate_name: dATP

substrate: dATP


substrate_name: H2O; dUTP

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

substrate: H2O; dUTP


substrate_name: dGTP

substrate: dGTP


substrate_name: dTTP

substrate: dTTP


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB direct accession lookup Q58502 (2026-07-01)


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


organism: Mycobacterium tuberculosis

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P9WNS5 (2026-07-01) and applied mutation signature D28N/H145W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D28N/H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


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

proof_lines: DELTA-loop mutant enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20°C


sequence_source: UniProtKB direct accession lookup P9WNS5 (2026-07-01)

proof_lines: wild type enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20°C

proof_lines: pH 7.5, 25°C, recombinant wild-type and mutant enzymes


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P9WNS5 (2026-07-01) and applied mutation signature H145W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


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

proof_lines: mutant enzyme D49N/F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


proof_lines: mutant enzyme F158A, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


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

proof_lines: wild type enzyme, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


proof_lines: at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0

proof_lines: pH and temperature not specified in the publication


organism: Human alphaherpesvirus 1

proof_lines: enzyme from herpes simplex virus type 1 infected KB cells


organism: Human alphaherpesvirus 2


proof_lines: pH 7.6, 25°C, recombinant enzyme, in presence of 1 mM MgCl2


proof_lines:
pH 8, 25°C
above


organism: Orthopoxvirus vaccinia


organism: Paramecium bursaria Chlorella virus 1


organism: Plasmodium falciparum


organism: Shrimp white spot syndrome virus


organism: Spbetavirus SPbeta


organism: Thermococcus pacificus


proof_lines:
wild-type, pH 7.5, 75°C
wild-type, pH 7.5, 95°C


organism: Trypanosoma brucei


organism: Trypanosoma cruzi


organism: Acholeplasma laidlawii

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


organism: Allium cepa


organism: Bacillus subtilis


organism: Campylobacter jejuni


organism: Drosophila melanogaster


organism: Dugesia ryukyuensis

proof_lines: in the presence of 5 mM Mg2+, at pH 8.2 and 25°C

proof_lines: in the presence of 5 mM Mn2+, at pH 8.2 and 25°C


organism: equine infectious anemia virus


organism: Escherichia coli


proof_lines: mutant enzyme T22R/R116S, at pH 7.5 and 20°C


proof_lines: pH 7.5, 25°C, in the presence of VO2+ or bis(acetylacetonato)oxovanadium(IV)

proof_lines: pH 7.5, 25°C, in the absence of added metal ions


organism: Homo sapiens

proof_lines: mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


organism: white spot syndrome virus

sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature V160D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R24T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature R161K to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTR161K'; column 'kcat (s-1)' = 0.053; column 'Km (uM)' = 5.4; column 'kcat/Km (M-1 s-1)' = 9.8 x 10^3; column 'Relative efficiency (%)' = 0.23. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.053 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.053 s^(-1). Km: printed Table 1 cell 5.4 in a column headed Km (uM); 1 uM is 0.001 mM, so 5.4 / 1000 = 0.0054 mM. kcat/Km: printed Table 1 cell 9.8 x 10^3 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9800 / 1000 = 9.8 s^-1 mM^-1. The exported values are kcat 0.053 s^(-1) and Km 0.0054 mM and kcat_over_km 9.814814814814815 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTR161K': kcat = 0.053 s-1; Km = 5.4 uM; printed kcat/Km = 9.8 x 10^3 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTR161K'


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature D34N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R24T/S115R/D170G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R24T/S115R/D170G, at pH 7.5 and 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature R24T/S115R to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTR24T/S115R'; column 'kcat (s-1)' = 0.51; column 'Km (uM)' = 6.7; column 'kcat/Km (M-1 s-1)' = 7.6 x 10^4; column 'Relative efficiency (%)' = 1.8. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.51 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.51 s^(-1). Km: printed Table 1 cell 6.7 in a column headed Km (uM); 1 uM is 0.001 mM, so 6.7 / 1000 = 0.0067 mM. kcat/Km: printed Table 1 cell 7.6 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 76000 / 1000 = 76 s^-1 mM^-1. The exported values are kcat 0.51 s^(-1) and Km 0.0067 mM and kcat_over_km 76.11940298507463 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTR24T/S115R': kcat = 0.51 s-1; Km = 6.7 uM; printed kcat/Km = 7.6 x 10^4 in a column headed kcat/Km (M-1 s-1).


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature D170L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature F166Y to reconstruct the assayed variant sequence.


mutation_type: deletion

proof_lines: mutant enzyme DELTA134-153, at pH 7.5 and 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature R158W to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTR158W'; column 'kcat (s-1)' = 3.1; column 'Km (uM)' = 3.2; column 'kcat/Km (M-1 s-1)' = 9.7 x 10^5; column 'Relative efficiency (%)' = 22. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.1 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.1 s^(-1). Km: printed Table 1 cell 3.2 in a column headed Km (uM); 1 uM is 0.001 mM, so 3.2 / 1000 = 0.0032 mM. kcat/Km: printed Table 1 cell 9.7 x 10^5 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 970000 / 1000 = 970 s^-1 mM^-1. The exported values are kcat 3.1 s^(-1) and Km 0.0032 mM and kcat_over_km 968.75 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTR158W': kcat = 3.1 s-1; Km = 3.2 uM; printed kcat/Km = 9.7 x 10^5 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTR158W'


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R158W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R24T/S115R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R24T/S115R, at pH 7.5 and 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature D34N to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTD34N'; column 'kcat (s-1)' = 0.92; column 'Km (uM)' = 13; column 'kcat/Km (M-1 s-1)' = 7.1 x 10^4; column 'Relative efficiency (%)' = 1.6. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.92 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.92 s^(-1). Km: printed Table 1 cell 13 in a column headed Km (uM); 1 uM is 0.001 mM, so 13 / 1000 = 0.013 mM. kcat/Km: printed Table 1 cell 7.1 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 71000 / 1000 = 71 s^-1 mM^-1. The exported values are kcat 0.92 s^(-1) and Km 0.013 mM and kcat_over_km 70.76923076923077 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTD34N': kcat = 0.92 s-1; Km = 13 uM; printed kcat/Km = 7.1 x 10^4 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTD34N'


verification_status: verified

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

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.4 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 7.4 s^(-1). Km: printed Table 1 cell 1.7 in a column headed Km (uM); 1 uM is 0.001 mM, so 1.7 / 1000 = 0.0017 mM. kcat/Km: printed Table 1 cell 4.4 x 10^6 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4400000 / 1000 = 4400 s^-1 mM^-1. The exported values are kcat 7.4 s^(-1) and Km 0.0017 mM; this export row stores no kcat_over_km field.

status: verified


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R158E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P06968 direct lookup on 2026-07-01 and applied mutation signature D90N to reconstruct the assayed variant sequence.

proof_lines: D90N mutant enzyme, pH 7.8, room temperature


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

sequence_source: UniProtKB reviewed accession P06968 direct lookup on 2026-07-01

source_databases_merged: brenda skid


sequence_source: UniProtKB reviewed accession P33316 direct lookup on 2026-07-01

proof_lines: recombinant wild-type and mutant enzymes

proof_lines: pH 7.4, 20°C, recombinant wild-type enzyme


sequence_source: UniProtKB reviewed accession P33316-2 direct lookup on 2026-07-01


sequence_source: UniProtKB reviewed accession P33316-1 direct lookup on 2026-07-01


assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.2 M Tris

proof_lines: in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C


organism: Human gammaherpesvirus 4

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P03195 direct lookup on 2026-07-01 and applied mutation signature R268A to reconstruct the assayed variant sequence.

status: unverified


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P03195 direct lookup on 2026-07-01 and applied mutation signature D131S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D131S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P03195 direct lookup on 2026-07-01 and applied mutation signature D131S/G78D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D131S/G78D, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


sequence_source: UniProtKB reviewed accession P03195 direct lookup on 2026-07-01

proof_lines: wild type enzyme, without MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C

proof_lines: wild type enzyme, without MgCl2, with dithiothreitol, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C

proof_lines: wild type enzyme, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P03195 direct lookup on 2026-07-01 and applied mutation signature D131N to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme R268A, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


organism: African swine fever virus (strain Badajoz 1971 Vero-adapted)

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


organism: Bacillus subtilis (strain 168)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: dITP

substrate: dITP


enzyme_display_name: arylamine N-acetyltransferase

substrate_name: Acetyl-CoA; 2-Aminofluorene

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: using control cholangiocarcinoma KKU-100 cells after treatment with the mixture of inflammatory cytokines for 48 h, Vmax: 135.7 pmol/min/mg. A significant decrease in Vmax is shown but without affecting Km, implying a change in the amount o

enzyme: arylamine N-acetyltransferase

substrate: Acetyl-CoA; 2-Aminofluorene


enzyme_display_name: pyruvate kinase

organism: Rattus norvegicus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 7.1; 310.15 K; cofactor ADP

proof_lines:
apparent value
pH 7.1, 37°C
R-type isozyme, pH 7.4, 37°C

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Escherichia coli (strain K12)

substrate_name: aniline

substrate: aniline


substrate_name: 2-aminofluorene (measured with the enzyme encoded by allele NAT2*4)


organism: Mycolicibacterium smegmatis

substrate_name: isoniazid

substrate: isoniazid


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

substrate_name: acetyl-CoA (in the presence of N-hydroxy-Glu-P-1)

assay_conditions_summary: cofactor CoA


organism: Enterobius vermicularis

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


proof_lines:
strain 54.8, pH 7.4, 37°C
strain K-12, pH 7.4, 37°C


organism: Gallus gallus

substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Helicobacter pylori


substrate_name: sulfamethazine

substrate: sulfamethazine


organism: Klebsiella aerogenes

substrate_name: 3-aminobenzoic acid

substrate: 3-aminobenzoic acid


organism: Anisakis simplex


organism: Bacillus cereus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: mutant enzyme E123D, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C

proof_lines: mutant enzyme E123D, apparent value, at pH 7.5 and 25°C


proof_lines: wild type enzyme, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C

proof_lines: wild type enzyme, apparent value, at pH 7.5 and 25°C


proof_lines:
Vmax: 2.1 micromol/min/mg
Vmax: 0.17 micromol/min/mg


organism: Bacteroides sp.

substrate_name: p-Aminobenzoic acid

substrate: p-Aminobenzoic acid


organism: Bos taurus


organism: Candida albicans


organism: Citrobacter amalonaticus


organism: Citrobacter farmeri


organism: Citrobacter freundii

substrate_name: 4-aminosalicylic acid

substrate: 4-aminosalicylic acid


organism: Citrobacter koseri

substrate_name: 5-aminosalicylic acid

substrate: 5-aminosalicylic acid


organism: Columba sp.

substrate_name: serotonin

substrate: serotonin


organism: Serratia marcescens


organism: Vibrio vulnificus

proof_lines: pH 7.5, temperature not specified in the publication


organism: Wickerhamomyces ciferrii

substrate_name: dodecylamine

substrate: dodecylamine


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 94 sec(-1) with 3-amino-4-hydroxybenzoic acid as substrate. kcat is 66 sec(-1) with 4-amino-3-hydroxybenzoic acid as substrate. kcat is 44 sec(-1) with hydralazine as substrate. kcat is 70 sec(-1) with 2-amino-4-methylphenol as subs


organism: Klebsiella oxytoca


organism: Klebsiella pneumoniae


organism: Klebsiella pneumoniae subsp. rhinoscleromatis


organism: Lactobacillus acidophilus


organism: Mesocricetus auratus

substrate_name: anisidine

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

proof_lines: cosubstrate acetyl-CoA, mutant Y190A, pH 7.0, 25°C

proof_lines: cosubstrate 4-nitrophenyl acetate, mutant Y190A, pH 7.0, 25°C

substrate: anisidine


substrate_name: 4-nitrophenyl acetate

proof_lines: cosubstrate 4-nitrophenyl acetate, wild-type, pH 7.0, 25°C

proof_lines: cosubstrate acetyl-CoA, wild-type, pH 7.0, 25°C

substrate: 4-nitrophenyl acetate


substrate_name: 4-aminobenzoyl glutamic acid

proof_lines: cosubstrate acetyl-CoA, mutant Y190F, pH 7.0, 25°C

proof_lines: cosubstrate 4-nitrophenyl acetate, mutant Y190F, pH 7.0, 25°C

substrate: 4-aminobenzoyl glutamic acid


proof_lines: cosubstrate 4-nitrophenyl acetate, mutant Y190I, pH 7.0, 25°C

proof_lines: cosubstrate acetyl-CoA, mutant Y190I, pH 7.0, 25°C


organism: Mesorhizobium loti

substrate_name: PAS

substrate: PAS


substrate_name: p-Aminosalicylic acid

substrate: p-Aminosalicylic acid


organism: Morganella morganii


organism: Musca domestica

substrate_name: tyramine

substrate: tyramine


organism: Mycobacterium marinum

assay_conditions_summary: pH 8; 301.15 K; cofactor CoA

proof_lines: chimeric enzyme, replacement of the third domain of Mycobacterium marinum enzyme with that from Mycobacterium tuberculosis, pH 8.0, 28°C

proof_lines: chimeric enzyme, replacement of the third domain of Mycobacterium tuberculosis enzyme with that from Mycobacterium marinum, pH 8.0, 28°C


organism: Mycobacterium tuberculosis


organism: Mycobacteroides abscessus


organism: Nocardia farcinica


organism: Pseudomonas aeruginosa

proof_lines: concentration p-anisidine: 200 nM, reaction: acetyl-CoA + p-anisidine


organism: Rattus norvegicus

substrate_name: Phenylethylamine

proof_lines: liver brain

substrate: Phenylethylamine


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines:
strain 60.62, pH 7.4, 37°C
strain YG1024, pH 7.4, 37°C
strain TA98, pH 7.4, 37°C


organism: Mesorhizobium japonicum


organism: Mycobacterium smegmatis

substrate_name: Acetyl-CoA; Isoniazid

substrate: Acetyl-CoA; Isoniazid


organism: Mycolicibacterium smegmatis


substrate_name: isoniazid

substrate: isoniazid


proof_lines:
recombinant isozyme Nat3
recombinant isozyme Nat2
recombinant isozyme Nat1


organism: Streptomyces griseus


organism: Tsukamurella paurometabola

substrate_name: malonyl-CoA

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: cosubstrate 5-aminosalicylate, pH 7.5, temperature not specified in the publication

substrate: malonyl-CoA


organism: African swine fever virus

substrate_name: dUTP

proof_lines:
at pH 8.0 and 37°C
Raw SKiD Env: Temp=37°C, pH=8

substrate: dUTP


proof_lines: mutant Q120A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant R149A, 25°C, pH 7.5, presence of K+, Mg2+


organism: Arabidopsis thaliana

proof_lines:
at pH 7.6 and 25°C
Raw SKiD Env: Temp=25°C, pH=7.6


organism: Dictyostelium discoideum

substrate_name: H2O; dUTP

substrate: H2O; dUTP


proof_lines: full-length protein, pH not specified in the publication, temperature not specified in the publication

proof_lines: core protein lacking N-terminal residues 1-37, pH not specified in the publication, temperature not specified in the publication


organism: Drosophila virilis


organism: Escherichia coli

proof_lines: wild-type enzyme, pH 7.8, room temperature


proof_lines: mutant L89A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant I90A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: wild-type, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant D29A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant F154A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant S73A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant S72A, 25°C, pH 7.5, presence of K+, Mg2+


organism: Aquifex aeolicus

proof_lines:
wild-type, pH 7.5, 75°C
wild-type, pH 7.5, 95°C


organism: Mesocricetus auratus

proof_lines: pH 7.0, 25°C, with cofactor 4-nitrophenyl acetate, recombinant wild-type enzyme

proof_lines: pH 7.0, 25°C, with cofactor acetyl-CoA, recombinant wild-type enzyme


proof_lines: pH 7.0, 25°C, recombinant mutant R64W, with 4-aminobenzoic acid

proof_lines: pH 7.0, 25°C, recombinant mutant R64W, with 4-nitrophenyl acetate


proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme, with 4-aminobenzoic acid

proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme, with 4-nitrophenyl acetate


proof_lines: pH 7.0, 23°C, isozyme NAT2, with 4-nitrophenyl acetate


organism: Fusarium verticillioides

substrate_name: acetyl-CoA

proof_lines: pH 7.5, temperature not specified in the publication

substrate: acetyl-CoA


organism: Homo sapiens

substrate_name: 4-amino-3-methylbenzoic acid

assay_conditions_summary: pH 7; 296.15 K; cofactor ATP

proof_lines: pH 7.0, 23°C, isozyme NAT1, with 4-nitrophenyl acetate

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

substrate: 4-amino-3-methylbenzoic acid


substrate_name: 4-Aminobenzoic acid

proof_lines: Hep-G2 cells, presence of alpha-solanine, pH 7.5, 37°C

substrate: 4-Aminobenzoic acid


proof_lines: variant NAT2 4, pH 7.4, temperature not specified in the publication


organism: Bacillus anthracis

proof_lines:
apparent KM
isoenzyme BanatC


proof_lines:
apparent KM
isoenzyme BanatB


substrate_name: hydralazine

substrate: hydralazine


proof_lines: artificial full-length enzyme, pH 7.5, 37°C


organism: Rattus norvegicus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 7.1; 310.15 K; cofactor ATP

proof_lines:
apparent value
pH 7.1, 37°C
R-type isozyme, pH 7.4, 37°C

substrate: Phosphoenolpyruvate; ADP


organism: Saccharomyces cerevisiae

assay_conditions_summary: cofactor ATP


enzyme_display_name: prostaglandin-endoperoxide synthase

substrate_name: linoleic acid

assay_conditions_summary: pH 7.4; 297.15 K; buffer 100 mM Tris-HCl

proof_lines: isozyme PGHS-2, in 100 mM Tris-HCl buffer (pH 7.4), at 24°C

proof_lines: purified isoform PGHS-1, method: direct, O2

proof_lines: purified isoform PGHS-1, method: direct, arachidonate

enzyme: prostaglandin-endoperoxide synthase

substrate: linoleic acid


organism: Mus musculus

substrate_name: arachidonate

substrate: arachidonate


smiles: CCCCC/C=C\C/C=C\C/C=C\C/C=C\CCCC(=O)O


enzyme_display_name: dye decolorizing peroxidase

organism: Amycolatopsis sp.

proof_lines: pH and temperature not specified in the publication

enzyme: dye decolorizing peroxidase


organism: Auricularia auricula-judae

substrate_name: veratrylglycerol-beta-guaiacyl ether

substrate: veratrylglycerol-beta-guaiacyl ether


organism: Anabaena sp.

assay_conditions_summary: pH 4; 310.15 K; buffer 50 mM citrate

proof_lines: in 50 mM citrate buffer (pH 4.0-4.4), at 37°C


substrate_name: pyrogallol

proof_lines:
at pH 4.0 and 25°C
at pH 3.0 and 25°C

substrate: pyrogallol


organism: Bjerkandera adusta

substrate_name: Reactive Blue 19

substrate: Reactive Blue 19


organism: Irpex lacteus


organism: Amycolatopsis sp. ATCC 39116

proof_lines:
at pH 5.0 and 25°C
at pH 3.0 and 25°C


proof_lines:
wild type enzyme, at pH 3.0 and 25°C
wild type enzyme, at pH 3.5 and 25°C
wild type enzyme, at pH 3.0 and 30°C


substrate_name: Reactive Blue 5

proof_lines:
mutant enzyme W377S, at pH 3.5 and 25°C
mutant enzyme W377S, at pH 3.0 and 25°C
mutant enzyme W377S, at pH 2.5 and 25°C

substrate: Reactive Blue 5


organism: Saccharomonospora viridis

substrate_name: Reactive Yellow 2

substrate: Reactive Yellow 2


organism: Pseudomonas aeruginosa


organism: Thermobifida fusca YX

assay_conditions_summary: pH 3.5; 298.15 K; buffer 25 mM citrate

proof_lines: in 25 mM citrate buffer (pH 3.5), at 25°C


organism: Pleurotus sapidus

proof_lines:
at pH 4.0 and 30°C
at pH 4.5 and 30°C
at pH 3.8 and 30°C


organism: Shewanella oneidensis MR-1

assay_conditions_summary: pH 3.2; 298.15 K; buffer 25 mM citrate

proof_lines: in 25 mM citrate buffer, pH 3.2, at 25°C


organism: Thermomonospora curvata

substrate_name: guaiacol

proof_lines: with guaiacol as cosubstrate, mutant enzyme H312C, at pH 3.0 and 22°C

substrate: guaiacol


organism: Homo sapiens

substrate_name: O2; Arachidonate; Reduced acceptor

substrate: O2; Arachidonate; Reduced acceptor


substrate_name: Arachidonic acid; O2

substrate: Arachidonic acid; O2


substrate_name: Reactive Blue 4

proof_lines: with hydroquinone as cosubstrate, wild type enzyme, at pH 3.0 and 22°C

proof_lines: with guaiacol as cosubstrate, wild type enzyme, at pH 3.0 and 22°C

substrate: Reactive Blue 4


proof_lines: purified isoform PGHS-2, method: coupled, homo-vanilic acid

proof_lines: purified isoform PGHS-2, method: direct, O2

proof_lines: purified isoform PGHS-2, method: direct, arachidonate


proof_lines: pH 8.0, 25°C, COX-2 wild-type COX-2 and mutant N580A


proof_lines: with guaiacol as cosubstrate, mutant enzyme D220A, at pH 3.0 and 22°C


organism: Ovis aries

substrate_name: t-Butylhydroperoxide

smiles: CC(C)(C)OO

substrate: t-Butylhydroperoxide


substrate_name: Ethyl hydroperoxide

smiles: CCOO

substrate: Ethyl hydroperoxide


substrate_name: 15-HPETE; Guaiacol

substrate: 15-HPETE; Guaiacol


smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)O)OO


smiles: OO


proof_lines: purified isoform PGHS-1, method: direct, O2

proof_lines: purified isoform PGHS-1, method: direct, arachidonate

proof_lines: purified isoform PGHS-1, method: coupled, homo-vanilic acid


organism: Salvelinus fontinalis

substrate_name: O2; alpha-Linolenate; Reduced acceptor

substrate: O2; alpha-Linolenate; Reduced acceptor


organism: Dictyostelium discoideum


enzyme_display_name: abscisate beta-glucosyltransferase

organism: Solanum lycopersicum

substrate_name: UDPglucose; Abscisate

enzyme: abscisate beta-glucosyltransferase

substrate: UDPglucose; Abscisate


enzyme_display_name: beta-galactosidase

organism: Aspergillus niger

substrate_name: 2-nitrophenyl beta-D-galactopyranoside

enzyme: beta-galactosidase

substrate: 2-nitrophenyl beta-D-galactopyranoside


substrate_name: H2O; Lactose

substrate: H2O; Lactose


organism: Aspergillus oryzae

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

proof_lines:
pH 4.5, 60°C
Raw SKiD Env: Temp=60°C, pH=4.5
Raw SKiD Env: Temp=60°C, pH=5

source_databases_merged: sabio_rk brenda skid


substrate_name: 2-nitrophenyl beta-D-galactoside

substrate: 2-nitrophenyl beta-D-galactoside


organism: Bacillus coagulans

substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


organism: Bacillus subtilis

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

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


organism: Bacteroides ovatus


organism: Arthrobacter sp.


substrate_name: o-nitrophenyl beta-D-galactopyranoside

proof_lines:
at 5°C
at 18°C
at 10°C

substrate: o-nitrophenyl beta-D-galactopyranoside


proof_lines:
at 10°C
at 50°C
at 20°C


enzyme_display_name: lipid IVA 3-deoxy-D-manno-octulosonic acid transferase

organism: Escherichia coli


substrate_name: Protein N-phosphohistidine; D-Fructose

substrate: Protein N-phosphohistidine; D-Fructose


enzyme_display_name: DNA primase DnaG

substrate_name: rNTP

enzyme: DNA primase DnaG

substrate: rNTP


organism: Saccharolobus solfataricus

substrate_name: NTP

substrate: NTP


proof_lines: KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, in presence of M13 ssDNA as template, wild-type enzyme

proof_lines: KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, 1 mM Mn2+, in presence of M13 ssDNA as template, wild-type enzyme


proof_lines: KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, in presence of M13 ssDNA as template, mutant enzyme E175Q


organism: Alicyclobacillus acidocaldarius


substrate_name: lactulose

substrate: lactulose


organism: Arabidopsis thaliana


organism: Arthrobacter psychrolactophilus


organism: Bifidobacterium bifidum

substrate_name: Lactose; H2O

substrate: Lactose; H2O


organism: Bispora sp.

substrate_name: lactose

assay_conditions_summary: pH 1.5; buffer note 'in glycine-HCl

substrate: lactose


organism: Caldicellulosiruptor saccharolyticus

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: 2-phospho-L-lactate transferase

organism: Methanocaldococcus jannaschii

enzyme: 2-phospho-L-lactate transferase


organism: Kluyveromyces lactis

substrate_name: alpha-Lactose; H2O

substrate: alpha-Lactose; H2O


organism: Kluyveromyces marxianus


organism: Lacticaseibacillus casei

substrate_name: 4-nitrophenyl beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


organism: Haloferax volcanii

proof_lines: pH 7.2, 22°C, the enzyme also shows beta-fucosidase activity


organism: Lactobacillus delbrueckii subsp. bulgaricus


organism: Limosilactobacillus reuteri

proof_lines:
recombinant enzyme, pH 6.5, 30°C
native enzyme, pH 6.5, 30°C


organism: Lactobacillus acidophilus


organism: Lactobacillus delbrueckii

proof_lines: wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C


proof_lines: mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C


organism: Escherichia coli


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

proof_lines: mutant enzyme H418F, in 30 mM TES buffer, 10 mM Mg2+, 150 mM Na+, pH 7.0 at 25°C


proof_lines: wild type enzyme, in 30 mM TES buffer, 145 mM NaCl, pH 7.0 at 25°C

proof_lines: wild type enzyme, in 30 mM TES buffer, 145 mM NaCl, 0.01 mM Mg2+, pH 7.0 at 25°C


proof_lines: mutant enzyme H418N, in 30 mM TES buffer, 0.01 mM Mg2+, 150 mM Na+, pH 7.0 at 25°C

proof_lines: mutant enzyme H418N, in 30 mM TES buffer, 145 mM NaCl, 0.01 mM Mg2+, pH 7.0 at 25°C


proof_lines: mutant enzyme H418E, in 30 mM TES buffer, 0.01 mM Mg2+, 150 mM Na+, pH 7.0 at 25°C

proof_lines: mutant enzyme H418E, in 30 mM TES buffer, 145 mM NaCl, 0.01 mM Mg2+, pH 7.0 at 25°C


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


enzyme_display_name: L-arabinonolactonase

organism: Halobacterium volcanii

substrate_name: H2O; L-Arabinono-1,4-lactone

enzyme: L-arabinonolactonase

substrate: H2O; L-Arabinono-1,4-lactone


substrate_name: D-xylono-gamma-lactone

substrate: D-xylono-gamma-lactone


organism: Mus musculus


organism: Oryza sativa

proof_lines: pH 3.5, 60°C, recombinant isozyme OsGal1


organism: Pantoea agglomerans


organism: Pediococcus pentosaceus


organism: Planococcus sp. (in: firmicutes)


organism: Priestia megaterium


organism: Pseudoalteromonas haloplanktis


organism: Putranjiva roxburghii

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

proof_lines:
pH 4.6, 37°C, native enzyme
pH 4.6, 37°C, recombinant enzyme

substrate: 4-nitrophenyl beta-D-glucopyranoside


organism: Raphanus sativus


organism: Saccharolobus solfataricus


proof_lines: pH 7.5, 80°C, recombinant mutant enzyme F441Y


proof_lines:
Raw SKiD Env: Temp=30°C, pH=6.5
Raw SKiD Env: Temp=80°C, pH=7.5


enzyme_display_name: maleylpyruvate hydrolase

organism: Aquipseudomonas alcaligenes

enzyme: maleylpyruvate hydrolase


organism: Sphingobium sp. SYK-6

proof_lines:
pH 7.2, 23°C
Raw SKiD Env: Temp=23°C, pH=7.2


enzyme_display_name: histidine decarboxylase

organism: Clostridium perfringens

substrate_name: L-Histidine

enzyme: histidine decarboxylase

substrate: L-Histidine


enzyme_display_name: asparaginase

organism: Saccharomyces cerevisiae

substrate_name: H2O; L-Asparagine

enzyme: asparaginase

substrate: H2O; L-Asparagine


organism: Solanum lycopersicum


organism: Synechocystis sp.


organism: Homo sapiens

substrate_name: L-histidine

proof_lines: pH and temperature not specified in the publication

substrate: L-histidine


proof_lines: mutant C179S/Y334F/C417S, product imidazole acetaldehyde, pH 6.5, 37°C


proof_lines: mutant C179S/C417S, product histamine, pH 6.5, 37°C


organism: Lactobacillus buchneri


organism: Sulfolobus solfataricus


organism: Trichoderma reesei

substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


organism: uncultured microorganism

substrate_name: 4-nitrophenyl beta-D-fucopyranoside

proof_lines: pH 6.0, 60°C, additive: 25 mM cellobiose

proof_lines: pH 6.0, 60°C, additive: 250 mM D-galactose

substrate: 4-nitrophenyl beta-D-fucopyranoside


organism: Arabidopsis thaliana


organism: Escherichia coli

substrate_name: L-Aspartyl-beta-hydroxamate; H2O

substrate: L-Aspartyl-beta-hydroxamate; H2O


organism: Mycobacterium tuberculosis


organism: Nostoc sp.


organism: Rattus norvegicus

substrate_name: H2O; L-Aspartic acid beta-(7-amido-4-methylcoumarin)


organism: Lactobacillus sp.


assay_conditions_summary: pH 7


organism: Morganella morganii

proof_lines: mutant C53S/C330S/C340S, product histamine, pH 6.5, 37°C


proof_lines: mutant C53S/Y260F/C330S/C340S, product imidazole acetaldehyde, pH 6.5, 37°C


organism: Staphylococcus epidermidis


organism: Azospirillum brasilense


organism: Mus musculus


organism: Oenococcus oeni


organism: Variovorax paradoxus


organism: Homo sapiens

substrate_name: arachidonic acid

proof_lines:
isozyme 1 and 2
isozyme 2
native enzyme

substrate: arachidonic acid


organism: Kluyveromyces lactis

substrate_name: o-nitrophenyl-beta-D-galactoside

proof_lines:
isoenzyme betaG41
isoenzyme betaG630
isoenzyme betaG550

substrate: o-nitrophenyl-beta-D-galactoside


proof_lines:
pH 7.5, 30°C, isozyme BGT I
pH 7.5, 35°C, isozyme BGT I
pH 7.5, 30°C, isozyme BGT II


organism: Unknown


organism: Irpex lacteus

substrate_name: veratryl alcohol

assay_conditions_summary: pH 2

proof_lines: pH 2.0, temperature not specified in the publication

proof_lines: pH 3.0, temperature not specified in the publication

proof_lines: pH 4.0, temperature not specified in the publication

substrate: veratryl alcohol


proof_lines: native wild type enzyme, at pH 2.0 and 25°C

proof_lines: recombinant wild type enzyme, at pH 4.5 and 25°C

proof_lines: recombinant wild type enzyme, at pH 2.0 and 25°C


organism: Physeter macrocephalus

substrate_name: guaiacol

substrate: guaiacol


organism: Pleurotus ostreatus

proof_lines:
at pH 6.0 and 28°C
at pH 4.0 and 30°C


organism: Pseudomonas putida

substrate_name: Acid Blue 62

proof_lines: with 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 5.0 and 30°C

substrate: Acid Blue 62


proof_lines: mutant enzyme E188K/A142V, at pH 5.5 and 25°C


proof_lines: mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C

proof_lines: mutant enzyme E188K/A142V/H125Y, at pH 8.0 and 25°C

proof_lines: mutant enzyme E188K/A142V/H125Y, at pH 8.5 and 25°C


proof_lines: mutant enzyme E188K/H125R, at pH 4.3 and 25°C


organism: Dictyostelium discoideum

substrate_name: UDP-GlcNAc

proof_lines: The low Vmax value suggests that the enzyme may be down-regulated under the assay conditions.

substrate: UDP-GlcNAc


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: NTPs

substrate: NTPs


organism: Arabidopsis thaliana

substrate_name: para-nitrophenyl-beta-D-galactoside

proof_lines: Measured at pH 4.5 and 37 degrees Celsius for all experiments.

substrate: para-nitrophenyl-beta-D-galactoside


organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)

substrate_name: lactose

substrate: lactose


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

substrate_name: Gal-beta-PNP

substrate: Gal-beta-PNP


organism: Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL)

substrate_name: p-nitrophenyl beta-D-galactopyranoside (pNPGal) (at pH 5.5 and 75 degrees Celsius)

proof_lines: kcat is 4522 sec(-1) with pNPGal as substrate. kcat is 3750.6 sec(-1) with pNPGlu as substrate. kcat is 944.3 sec(-1) with pNPC as substrate. kcat is 652.6 sec(-1) with pNPX as substrate. kcat is 2149 sec(-1) with cellobiose as substrate.


organism: Escherichia coli (strain K12)

substrate_name: p-nitrophenyl beta-D-galactoside

proof_lines: The values for the enzymatic assays using manganese as cofactor are very close.

substrate: p-nitrophenyl beta-D-galactoside


organism: Auricularia auricula-judae

substrate_name: Reactive Black 5

assay_conditions_summary: pH 3; 293.15 K; buffer sodium tartrate

proof_lines: manganese-independent peroxidase I, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C

proof_lines: manganese-independent peroxidase II, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C

proof_lines: manganese-independent peroxidase II, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C

substrate: Reactive Black 5


organism: Bacillus subtilis

proof_lines: pH and temperature not specified in the publication

proof_lines: with 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 4.0 and 30°C


organism: Basidiomycota sp.


proof_lines: mutant enzyme D222E/R390K, at pH 3.0 and 25°C


organism: Bjerkandera adusta

proof_lines:
at pH 4.0 and 30°C
at pH 4.0 and 50°C
at pH 3.0 and 70°C


organism: Cellulomonas bogoriensis

substrate_name: Reactive Blue 19

assay_conditions_summary: pH 5

proof_lines: wild type enzyme, at pH 5.0, temperature not specified in the publication

proof_lines: wild type enzyme, with Reactive Blue 19 as cosubstrate, at pH 5.0, temperature not specified in the publication

substrate: Reactive Blue 19


proof_lines: mutant enzyme E201D, at pH 5.0, temperature not specified in the publication

proof_lines: mutant enzyme E201D, with Reactive Blue 19 as cosubstrate, at pH 5.0, temperature not specified in the publication


organism: Geotrichum candidum

proof_lines: using AQ2 as cosubstrate, at pH 3.2 and 30°C

proof_lines: using Reactive Blue 5 as cosubstrate, at pH 3.2 and 30°C


organism: Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)

substrate_name: ONPG (at 30 degrees Celsius and pH 6.5)

substrate: ONPG (at 30 degrees Celsius and pH 6.5)


organism: Bacillus subtilis (strain 168)

substrate_name: p-nitrophenyl beta-D-galactopyranoside (at pH 7.0 and 37 degrees Celsius)


organism: Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)

substrate_name: Gal(beta1-4)Gal (at 37 degrees Celsius and pH 6.0)


organism: Carnobacterium maltaromaticum

substrate_name: o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 30 degrees Celsius)


organism: Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B)

substrate_name: pNPAp (at 37 degrees Celsius and pH 6.0)


organism: Enterobacter agglomerans

substrate_name: o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius)


organism: Geobacillus kaustophilus

substrate_name: ONPG (at 55 degrees Celsius and pH 7.0)

substrate: ONPG (at 55 degrees Celsius and pH 7.0)


organism: Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)

substrate_name: ONPG (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)


organism: Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)

substrate_name: o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 37 degrees Celsius and pH 6.0)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Planococcus sp. (strain L4)

substrate_name: ONPG (at 5 degrees Celsius and at pH 6.8)


organism: Pseudomonas putida


organism: Streptomyces albidoflavus


organism: Streptomyces avermitilis

proof_lines:
at pH 4.0 and 25°C
at pH 4.5 and 30°C
at pH 4.5 and 25°C


organism: Streptomyces griseosporeus

substrate_name: o-Dianisidine

substrate: o-Dianisidine


organism: Streptomyces lividans


organism: Vibrio cholerae

proof_lines:
mutant enzyme D138V, at pH 4.0 and 25°C
mutant enzyme D138V, at pH 6.5 and 25°C


proof_lines:
wild type enzyme, at pH 4.5 and 25°C
wild type enzyme, at pH 7.0 and 25°C


organism: Xylaria grammica


organism: Bos taurus

substrate_name: arachidonic acid


organism: Homo sapiens

substrate_name: (5Z,8Z,11Z,14Z)-eicosatetraenoate (in absence of sodium nitroprusside NO donor)

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


substrate_name: arachidonate

substrate: arachidonate


organism: Ovis aries


organism: Solanum lycopersicum

substrate_name: abscisic acid

substrate: abscisic acid


organism: Escherichia coli (strain K12)

substrate_name: lipid IV(A) (at pH 8)

assay_conditions_summary: pH 8

enzyme: lipid IVA 3-deoxy-D-manno-octulosonic acid transferase

substrate: lipid IV(A) (at pH 8)


substrate_name: fructose

substrate: fructose


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

substrate_name: FO

substrate: FO


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

substrate_name: L-arabino-gamma-lactone

substrate: L-arabino-gamma-lactone


organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA)

substrate_name: ONPG (at 60 degrees Celsius and pH 6.0)

assay_conditions_summary: pH 6

substrate: ONPG (at 60 degrees Celsius and pH 6.0)


organism: Arthrobacter sp

substrate_name: ONPG (at 10 degrees Celsius)

substrate: ONPG (at 10 degrees Celsius)


substrate_name: ONPG

substrate: ONPG


organism: Bifidobacterium bifidum

substrate_name: lactose

proof_lines: hydrolysis transgalactosylation

substrate: lactose


organism: Bifidobacterium longum


organism: Bifidobacterium longum subsp. infantis

substrate_name: o-nitrophenyl beta-D-galactopyranoside

substrate: o-nitrophenyl beta-D-galactopyranoside


organism: Caldariella acidophila

substrate_name: 4-nitrophenyl beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


organism: Caldicellulosiruptor saccharolyticus

proof_lines:
at pH 6.0 and 80°C
at 80°C and pH 6.0


organism: Clostridium perfringens

assay_conditions_summary: pH 6; 310.15 K; buffer 20 mM sodium acetate

proof_lines: mutant enzyme E467A, in 20 mM sodium acetate buffer at pH 6.0, 37°C


proof_lines: mutant enzyme E354A, in 20 mM sodium acetate buffer at pH 6.0, 37°C


proof_lines: wild type enzyme, in 20 mM sodium acetate buffer at pH 6.0, 37°C


proof_lines: mutant enzyme D429A, in 20 mM sodium acetate buffer at pH 6.0, 37°C


organism: Corynebacterium murisepticum

substrate_name: o-nitrophenyl-beta-D-galactoside

substrate: o-nitrophenyl-beta-D-galactoside


organism: Enterobacter cloacae

substrate_name: 2-nitrophenyl beta-D-galactopyranoside

substrate: 2-nitrophenyl beta-D-galactopyranoside


organism: Kluyveromyces lactis


organism: Kluyveromyces marxianus

assay_conditions_summary: pH 6.8; 298.15 K; buffer mixture

proof_lines:
pH 6.8
dimeric enzyme, 25°C
strain A60


organism: Kluyveromyces sp.

proof_lines: free enzyme, substrate is milk, pH 7.5, 41°C

proof_lines: immobilized enzyme MP-MCC-Gal, substrate is milk, pH 7.5, 41°C

proof_lines: immobilized enzyme Fe-ALK-Gal, pH 7.5, 41°C


organism: Lactiplantibacillus pentosus


organism: Lactiplantibacillus plantarum


organism: Lactiplantibacillus plantarum WCFS1

proof_lines:
at pH 7.5 and 55°C
at pH 7.0 and 60°C


organism: Lactobacillus acidophilus


organism: Lactobacillus crispatus


organism: Lactobacillus delbrueckii


organism: Alicyclobacillus acidocaldarius

proof_lines:
pH 6.0, 65°C
strain HM-1
strain 11-1O


organism: Arthrobacter psychrolactophilus


organism: Arthrobacter sp.

sequence_source: UniProtKB Q7WTU5; BRENDA EC 3.2.1.23 page links Q7WTU5 to Arthrobacter sp. SB and PMID 16736094


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTU5; BRENDA EC 3.2.1.23 page links Q7WTU5 to Arthrobacter sp. SB and PMID 16736094 and applied mutation signature E229D/V405A to reconstruct the assayed variant sequence.

proof_lines: 15°C, recombinant mutant BgaS7, i.e. E229D/V405A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTU5; BRENDA EC 3.2.1.23 page links Q7WTU5 to Arthrobacter sp. SB and PMID 16736094 and applied mutation signature E229D/V405A/G803D to reconstruct the assayed variant sequence.

proof_lines: 15°C, recombinant mutant BgaS6, i.e.E229D/V405A/G803D


organism: Aspergillus aculeatus


organism: Aspergillus carbonarius


organism: Aspergillus niger

proof_lines: enzyme immobilized on sucrose sulfate-polyacrolein


organism: Aspergillus oryzae

assay_conditions_summary: pH 4.5; 310.15 K; buffer mixture

proof_lines:
cross-linked enzyme, pH 4.5, 37°C
free enzyme, pH 4.5, 37°C
adsorbed enzyme, pH 4.5, 37°C


organism: Averrhoa carambola

substrate_name: nitrophenyl beta-D-galactoside

proof_lines:
37°C, pH 4.1,beta-galactosidase IV
37°C, pH 4.1,beta-galactosidase III
37°C, pH 4.1,beta-galactosidase II

substrate: nitrophenyl beta-D-galactoside


organism: Bacillus sp. (in: firmicutes)

proof_lines:
pH 7.6 enzyme
pH 10.2 enzyme


organism: Bacteroides polypragmatus


organism: Erythrina variegata


organism: Escherichia coli

assay_conditions_summary: pH 7.3; 298.15 K; buffer mixture

proof_lines:
dimeric enzyme, 25°C
tetrameric enzyme, 25°C
with 0.05 M NaCl


organism: Felis catus

substrate_name: ganglioside GM1

substrate: ganglioside GM1


organism: Geobacillus stearothermophilus


substrate_name: lactosucrose

substrate: lactosucrose


organism: Hamamotoa singularis


organism: Heyndrickxia coagulans

proof_lines:
at 55°C
at 30°C


organism: Hymenaea courbaril

substrate_name: Unknown

substrate: Unknown


organism: Irpex lacteus


organism: Planococcus sp. (strain 'SOS Orange')

substrate_name: ONPG (at 1.9 degrees Celsius and at pH 6.5)


organism: Pseudoalteromonas haloplanktis

substrate_name: lactose (at pH 7.5 and at 25 degrees Celsius)


organism: Thermus sp

substrate_name: pNPGal (at 70 degrees Celsius and pH 7.0)


substrate_name: ONPG (at 70 degrees Celsius and pH 7.0)

substrate: ONPG (at 70 degrees Celsius and pH 7.0)


organism: Thermus thermophilus

substrate_name: lactose (at pH 6.5 and at 70 degrees Celsius)


organism: Aquipseudomonas alcaligenes

substrate_name: maleylpyruvate

substrate: maleylpyruvate


organism: Homo sapiens

substrate_name: arachidonic acid

proof_lines:
mutant Y348F, cyclooxygenase activity
mutant enzyme Y348F

substrate: arachidonic acid


proof_lines:
mutant Y504F, cyclooxygenase activity
mutant enzyme Y504F
mutant Y504F, cyclooxygenase inhibition


proof_lines: mutant Y348F/Y504F, cyclooxygenase activity

proof_lines: mutant Y348F/Y504F, cyclooxygenase inhibition


organism: Oryctolagus cuniculus


organism: Ovis aries

substrate_name: cis-5,8,11,14-eicosatetraenoic acid

substrate: cis-5,8,11,14-eicosatetraenoic acid


organism: Dictyostelium sp.


organism: Macleaya microcarpa

substrate_name: abscisic acid

proof_lines: apparent value, at pH 5.0, temperature not specified in the publication

substrate: abscisic acid


organism: Escherichia coli


organism: Pseudomonas aeruginosa

substrate_name: D-fructose[side 1]

substrate: D-fructose[side 1]


organism: Salmonella typhimurium


organism: Achatina achatina

substrate_name: 2-nitrophenyl beta-D-galactoside

substrate: 2-nitrophenyl beta-D-galactoside


organism: Actinomyces viscosus

substrate_name: lactose


organism: Cavia porcellus


substrate_name: arachidonate

substrate: arachidonate


proof_lines:
pH 7.2, 30°C, mutant enzyme N382L
pH 8.0, 23°C, mutant enzyme N382L


proof_lines:
pH 8.0, 23°C, wild-type enzyme
wild-type, cyclooxygenase activity
pH 7.2, 30°C, PGHS-2 wild-type enzyme


organism: Rhizomucor sp.

substrate_name: p-nitrophenyl beta-D-galactopyranoside

substrate: p-nitrophenyl beta-D-galactopyranoside


organism: Saccharolobus solfataricus

proof_lines:
pH 6.5, 30°C
pH 6.5, 75°C
at 75°C and pH 6.5

substrate: lactose


organism: Saccharomyces fragilis

substrate_name: o-nitrophenyl-beta-D-galactoside

proof_lines: enzyme immobilized on sucrose-polyacrolein


organism: Saccharopolyspora rectivirgula


organism: Sterigmatomyces elviae


organism: Streptococcus pneumoniae


organism: Streptococcus sp.


organism: Streptococcus thermophilus

substrate_name: 2-nitrophenyl beta-D-galactopyranoside

proof_lines: in presence of 0.05 mM Mg2+ and 50 mM K+

proof_lines: in presence of 0.25 mM Mg2+, 50 mM K+ and 50 mM Na+


organism: Tenebrio molitor

substrate_name: 4-methylumbelliferyl beta-D-galactoside

proof_lines: hydrolysis of p-nitrophenyl beta-D-galactoside

proof_lines: hydrolysis of 4-methylumbellipheryl beta-D-galactoside

proof_lines: hydrolysis of 4-methylumbelliferyl beta-D-galactoside

substrate: 4-methylumbelliferyl beta-D-galactoside


organism: Thermoanaerobacter sp.

substrate: o-nitrophenyl-beta-D-galactoside


substrate_name: p-nitrophenyl-beta-D-galactoside

proof_lines:
at 25°C, in presence of 10 mM Mg2+
at 50°C, in presence of 10 mM Mg2+

substrate: p-nitrophenyl-beta-D-galactoside


organism: Thermomyces dupontii

proof_lines: native enzyme, substrate 2-nitrophenyl beta-D-galactoside, pH 6.5, 40°C


organism: Raoultella planticola

substrate_name: L-His

substrate: L-His


organism: Rattus norvegicus

substrate_name: L-Histidine

proof_lines:
membrane-bound enzyme
enzyme form 1
soluble enzyme

substrate: L-Histidine


organism: Tetragenococcus muriaticus

substrate_name: L-histidine

substrate: L-histidine


organism: Cupriavidus necator


organism: Herbaspirillum seropedicae


organism: Roseateles saccharophilus


organism: Paenibacillus macerans


organism: Papiliotrema laurentii


organism: Penicillium canescens


organism: Penicillium chrysogenum

substrate_name: o-nitrophenyl beta-D-galactopyranoside

substrate: o-nitrophenyl beta-D-galactopyranoside


organism: Penicillium citrinum


organism: Penicillium multicolor


organism: Petunia x hybrida

proof_lines:
enzyme form H3
enzyme form H4
enzyme form H2


organism: Phaseolus vulgaris


organism: Prunus persica


organism: Pseudarthrobacter oxydans

substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


organism: Raphanus sativus


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

assay_conditions_summary: pH 3; buffer presence of 50 mM glycine/HCl

proof_lines: 97000 da enzyme form and 84000 Da enzyme form

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


organism: Lactobacillus helveticus


organism: Lactococcus lactis subsp. lactis


organism: Lathyrus oleraceus

proof_lines: in 50 mM sodium acetate-acetic acid, pH 4.0, at 37°C

proof_lines: enzyme immobilized on Amberlite MB-150 beads


organism: Limosilactobacillus reuteri

proof_lines: pH 6.5, 30°C, substrate: o-nitrophenyl-beta-D-galactoside, strain L461


organism: Macrotyloma geocarpum

substrate_name: Unknown

substrate: Unknown


organism: Marchantia polymorpha


organism: Mus musculus

proof_lines:
in presence of inhibitor
without inhibitor


organism: Neurospora crassa

proof_lines: beta-D-galactoside galactohydrolase pH 4.2

proof_lines: beta-D-galactoside galactohydrolase pH 4.5


organism: Niallia circulans


organism: Oreochromis niloticus


organism: Oryctolagus cuniculus


organism: Paecilomyces variotii


organism: Aquipseudomonas alcaligenes

proof_lines: pH and temperature not specified in the publication


organism: Clostridium perfringens


organism: Homo sapiens

proof_lines: pH 6.8, 37°C, recombinant enzyme, versus L-histidine


organism: Klebsiella aerogenes


organism: Lactobacillus sp.


organism: Lactobacillus sp. (strain 30a)


organism: Morganella morganii


organism: Oenococcus oeni


enzyme_display_name: 7,8-dihydroneopterin oxygenase

organism: Mycobacterium tuberculosis

enzyme: 7,8-dihydroneopterin oxygenase


enzyme_display_name: 2,5-dihydroxypyridine 5,6-dioxygenase

organism: Pseudomonas putida

substrate_name: O2; 2,5-Dihydroxypyridine

enzyme: 2,5-dihydroxypyridine 5,6-dioxygenase

substrate: O2; 2,5-Dihydroxypyridine


organism: Streptomyces avermitilis

substrate_name: (+/-)-1-deoxypentalenic acid

proof_lines: pH 6.0, temperature not specified in the publication

substrate: (+/-)-1-deoxypentalenic acid


enzyme_display_name: pyridinium-3,5-biscarboxylic acid mononucleotide synthase

organism: Lactiplantibacillus plantarum

substrate_name: deamido-NAD+

assay_conditions_summary: pH 8; 295.15 K; cofactor NAD+

proof_lines:
pH 8.0, 22°C
Raw SKiD Env: Temp=22°C, pH=8

substrate: deamido-NAD+


enzyme_display_name: cysteine transaminase

organism: Rattus norvegicus

substrate_name: L-Cysteine; 2-Oxoglutarate

enzyme: cysteine transaminase

substrate: L-Cysteine; 2-Oxoglutarate


enzyme_display_name: putrescine--2-oxoglutarate transaminase

organism: Escherichia coli

substrate_name: 2-Oxoglutarate; Putrescine

enzyme: putrescine--2-oxoglutarate transaminase

substrate: 2-Oxoglutarate; Putrescine


enzyme_display_name: 2-phospho-L-lactate guanylyltransferase

organism: Methanocaldococcus jannaschii

substrate_name: (2S)-2-Phospholactate; GTP

enzyme: 2-phospho-L-lactate guanylyltransferase

substrate: (2S)-2-Phospholactate; GTP


enzyme_display_name: (S)-nandinine synthase

organism: Eschscholzia californica

substrate_name: H+; NADPH; O2; (S)-Scoulerine

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH

enzyme: (S)-nandinine synthase

substrate: H+; NADPH; O2; (S)-Scoulerine


enzyme_display_name: sulfite reductase (coenzyme F420)

substrate_name: sulfite

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: sulfite reductase (coenzyme F420)

substrate: sulfite


organism: Methanosarcina barkeri


enzyme_display_name: 3-oxoadipyl-CoA thiolase

organism: Pseudomonas sp.

substrate_name: Coenzyme A; 3-Oxoadipyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: 3-oxoadipyl-CoA thiolase

substrate: Coenzyme A; 3-Oxoadipyl-CoA


organism: Gentiana triflora


enzyme_display_name: jasmonate O-methyltransferase

organism: Populus trichocarpa

substrate_name: benzoate

enzyme: jasmonate O-methyltransferase

substrate: benzoate


substrate_name: jasmonate

substrate: jasmonate


enzyme_display_name: [phosphatase 2A protein]-leucine-carboxy methyltransferase

organism: Homo sapiens

substrate_name: S-Adenosyl-L-methionine; [phosphatase 2A protein]-leucine


enzyme_display_name: molybdopterin adenylyltransferase

organism: Arabidopsis thaliana

substrate_name: ATP

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: 10 mM MgCl2, pH 7.2, temperature not specified in the publication

enzyme: molybdopterin adenylyltransferase

substrate: ATP


enzyme_display_name: undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate

organism: Campylobacter jejuni


enzyme_display_name: ent-cassa-12,15-diene 11-hydroxylase

organism: Oryza sativa

proof_lines: in 0.1 M Tris-HCl, pH 7.2, 20% (v/v) glycerol, 0.5 mM EDTA, 1 mM dithiothreitol, temperature not specified in the publication

enzyme: ent-cassa-12,15-diene 11-hydroxylase


enzyme_display_name: monacolin L hydroxylase

organism: Aspergillus terreus

substrate_name: Monacolin L acid; O2; [reduced NADPH-hemoprotein reductase]

assay_conditions_summary: cofactor NADPH

enzyme: monacolin L hydroxylase


enzyme_display_name: tryptophan N-monooxygenase

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

assay_conditions_summary: pH 7.9; 307.15 K; cofactor NADPH

proof_lines:
in 100 mM Tricine, pH 7.9, at 34°C
recombinant enzyme, pH 7.9, 34°C

enzyme: tryptophan N-monooxygenase

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


enzyme_display_name: Glutarate 2-hydroxylase

sequence_source: UniProtKB:P76621 direct REST accession check (identity context only; sequence not emitted)

proof_lines:
pH 7.2, 30°C
Raw SKiD Env: Temp=30°C, pH=7.2

enzyme: Glutarate 2-hydroxylase


enzyme_display_name: Benzoyl-CoA oxygenase component A

organism: Aromatoleum evansii

substrate_name: benzoyl-CoA

sequence_source: UniProtKB:Q9AIX6 direct REST accession check (identity context only; sequence not emitted)

assay_conditions_summary: pH 8; 295.15 K; cofactor CoA

proof_lines: pH 8, 22°C, addition of the putative ring cleaving enzyme BoxC leads to a several-fold acceleration of the initial rate and completes conversion of benzoyl-CoA. Because of this complex behaviour of the oxygenase system, the apparent Km valu

enzyme: Benzoyl-CoA oxygenase component A

substrate: benzoyl-CoA


enzyme_display_name: benzoyl-CoA 2,3-epoxidase

organism: Azoarcus evansii

substrate_name: H+; NADPH; O2; Benzoyl-CoA

enzyme: benzoyl-CoA 2,3-epoxidase

substrate: H+; NADPH; O2; Benzoyl-CoA


enzyme_display_name: Ent-cassadiene C11-alpha-hydroxylase 1

substrate_name: O2; ent-Cassadiene; NADPH; H+

sequence_source: UniProtKB:Q69X58 direct REST accession check (identity context only; sequence not emitted)

enzyme: Ent-cassadiene C11-alpha-hydroxylase 1

substrate: O2; ent-Cassadiene; NADPH; H+


organism: Picea abies

proof_lines:
pH 7.0, 18°C, isozyme PtJAMT2
pH 7.0, 18°C, isozyme PtJAMT3
pH 6.5, 27°C, isozyme PtJAMT1


organism: Mycobacterium tuberculosis

substrate_name: alpha-ribazole 5'-phosphate

proof_lines:
full length protein
maltose binding protein fusion protein
Raw SKiD Env: Temp=-----, pH=-----

substrate: alpha-ribazole 5'-phosphate


organism: Campylobacter jejuni subsp. jejuni serotype O:2


enzyme_display_name: acyl-lysine deacylase

organism: Thermus thermophilus

enzyme: acyl-lysine deacylase


substrate_name: H2O; N2-Acetyl-L-ornithine

substrate: H2O; N2-Acetyl-L-ornithine


enzyme_display_name: cAMP deaminase

organism: Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130

substrate_name: 3',5'-cyclic AMP

enzyme: cAMP deaminase

substrate: 3',5'-cyclic AMP


enzyme_display_name: 2,5-dihydroxypyridine 5,6-dioxygenase

organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

enzyme: 2,5-dihydroxypyridine 5,6-dioxygenase


enzyme_display_name: glutarate dioxygenase

organism: Escherichia coli (strain K12)

substrate_name: glutarate

enzyme: glutarate dioxygenase

substrate: glutarate


organism: Oryza sativa subsp. japonica


substrate_name: monacolin L acid

substrate: monacolin L acid


organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)


substrate_name: tryptophan

substrate: tryptophan


enzyme_display_name: (S)-nandinine synthase

organism: Eschscholzia californica

substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


enzyme_display_name: sulfite reductase (coenzyme F420)

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

substrate_name: sulfite


enzyme_display_name: columbamine O-methyltransferase

organism: Coptis japonica

substrate_name: columbamine

enzyme: columbamine O-methyltransferase

substrate: columbamine


enzyme_display_name: jasmonate O-methyltransferase

organism: Arabidopsis thaliana

substrate_name: methyl jasmonate

substrate: methyl jasmonate


enzyme_display_name: 3-oxoadipate CoA-transferase

organism: Pseudomonas knackmussii (strain DSM 6978 / CCUG 54928 / LMG 23759 / B13)

enzyme: 3-oxoadipate CoA-transferase


enzyme_display_name: 3-O-acetylpapaveroxine carboxylesterase

organism: Papaver somniferum

enzyme: 3-O-acetylpapaveroxine carboxylesterase


organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)

substrate_name: cAMP

substrate: cAMP


organism: Pseudomonas knackmussii

substrate_name: succinyl-CoA

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

substrate: succinyl-CoA


organism: Pseudomonas sp.

substrate_name: Succinyl-CoA; 3-Oxoadipate

substrate: Succinyl-CoA; 3-Oxoadipate


substrate_name: 3-O-Acetylpapaveroxine; H2O

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

substrate: 3-O-Acetylpapaveroxine; H2O


enzyme_display_name: [phosphatase 2A protein]-leucine-carboxy methyltransferase

organism: Homo sapiens


enzyme_display_name: [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M

organism: Methanosarcina barkeri


organism: Methanosarcina barkeri (strain Fusaro / DSM 804)

substrate_name: dimethylamine

substrate: dimethylamine


enzyme_display_name: 3-oxoadipyl-CoA thiolase

enzyme: 3-oxoadipyl-CoA thiolase


organism: Gentiana triflora

substrate_name: delphinidin 3,5-di-O-glucoside

substrate: delphinidin 3,5-di-O-glucoside


enzyme_display_name: pyridinium-3,5-biscarboxylic acid mononucleotide synthase

organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)

substrate_name: nicotinic acid adenine dinucleotide

substrate: nicotinic acid adenine dinucleotide


enzyme_display_name: cysteine transaminase

organism: Rattus norvegicus

substrate_name: L-cysteine

enzyme: cysteine transaminase

substrate: L-cysteine


enzyme_display_name: 2-phospho-L-lactate guanylyltransferase

enzyme: 2-phospho-L-lactate guanylyltransferase


enzyme_display_name: molybdopterin adenylyltransferase

substrate_name: ATP for domain G

assay_conditions_summary: cofactor ATP

enzyme: molybdopterin adenylyltransferase

substrate: ATP for domain G


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: ATP

substrate: ATP


enzyme_display_name: undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate

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

substrate_name: uridine 5'-diphosphobacillosamine

substrate: uridine 5'-diphosphobacillosamine


organism: Pseudomonas putida

proof_lines: pH 8.0, 25°C, strict substrate specificity


enzyme_display_name: tryptophan N-monooxygenase

substrate_name: L-tryptophan

proof_lines: CYP79B2, pH and temperature not specified in the publication

substrate: L-tryptophan


organism: Sinapis alba


organism: Berberis wilsoniae

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Eutrema japonicum

substrate_name: jasmonate

enzyme: jasmonate O-methyltransferase

substrate: jasmonate


organism: Fragaria x ananassa


organism: Sus scrofa

substrate_name: S-Adenosyl-L-methionine; [phosphatase 2A protein]-leucine

enzyme: [phosphatase 2A protein]-leucine-carboxy methyltransferase


substrate_name: Unknown

substrate: Unknown


substrate_name: CoA

substrate: CoA


enzyme_display_name: putrescine--2-oxoglutarate transaminase

organism: Escherichia coli

substrate_name: putrescine

enzyme: putrescine--2-oxoglutarate transaminase

substrate: putrescine


organism: Campylobacter jejuni

substrate_name: UDP-bacillosamine

enzyme: undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate

substrate: UDP-bacillosamine


enzyme_display_name: beta-galactosidase

organism: Thermomyces lanuginosus

substrate_name: beta-lactose

enzyme: beta-galactosidase

substrate: beta-lactose


organism: Thermotoga maritima

substrate_name: o-nitrophenyl-beta-D-galactoside

substrate: o-nitrophenyl-beta-D-galactoside


organism: Thermus aquaticus

substrate_name: lactose

proof_lines: calculated from glucose liberated from lactose

proof_lines: calculated from disappearance from lactose

substrate: lactose


organism: Thermus sp.

proof_lines: at 70°C and pH 6.5, using 4-nitrophenyl-beta-D-galactopyranoside as substrate


organism: Torulopsis sphaerica


organism: Trametes cinnabarina


organism: Treponema phagedenis

substrate_name: p-nitrophenyl-beta-D-galactoside

substrate: p-nitrophenyl-beta-D-galactoside


organism: uncultured soil bacterium

substrate_name: 2-nitrophenyl beta-D-galactopyranoside

proof_lines:
pH 7, 20°C
pH 7, 10°C
pH 7, 5°C

substrate: 2-nitrophenyl beta-D-galactopyranoside


organism: Vigna radiata

proof_lines:
beta-galactosidase I
beta-galactosidase II
beta-galactosidase III


organism: Wickerhamiella versatilis


organism: Xanthomonas phaseoli pv. manihotis

proof_lines: pH 7.0, 30°C, mutant E184A, glycohydrolase activity


enzyme_display_name: 7,8-dihydroneopterin oxygenase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 7,8-dihydroneopterin in the aldolase reaction

proof_lines: kcat is 0.0054 sec(-1) for the aldolase reaction with 7,8-dihydroneopterin as substrate. kcat is 0.006 sec(-1) for the aldolase reaction with 7,8-dihydromonapterin as substrate. kcat is 0.0015 sec(-1) for the epimerization of 7,8-dihydroneo

enzyme: 7,8-dihydroneopterin oxygenase


organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)

substrate_name: 1-deoxypentalenic acid

proof_lines: kcat is 4.2 sec(-1) with 1-deoxypentalenic acid.

substrate: 1-deoxypentalenic acid


enzyme_display_name: ent-cassa-12,15-diene 11-hydroxylase

organism: Oryza sativa subsp. japonica

substrate_name: ent-cassadiene

proof_lines: kcat is 0.011 sec(-1) with ent-sandaracopimaradien as substrate. kcat is 0.009 sec(-1) with ent-pimaradiene as substrate. kcat is 0.015 sec(-1) with ent-isokaurene as substrate. kcat is 0.006 sec(-1) with ent-cassadiene as substrate. kcat i

enzyme: ent-cassa-12,15-diene 11-hydroxylase

substrate: ent-cassadiene


enzyme_display_name: (S)-nandinine synthase

organism: Argemone mexicana

proof_lines: kcat is 13.8 min(-1) for (S)-cheilanthifoline.

enzyme: (S)-nandinine synthase


substrate_name: a hybrid RNA/DNA substrate

proof_lines: Vmax value for RNase H activity is identical to that for dsRNase activity.

substrate: a hybrid RNA/DNA substrate


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

substrate_name: CDP-L-glutamine

substrate: CDP-L-glutamine


sequence_source: UniProtKB:P48982 direct lookup from the PMID 16844121 BgaX organism/enzyme anchor

proof_lines: pH 7.0, 30°C, wild-type enzyme, glycohydrolase activity


enzyme_display_name: acyl-lysine deacylase

organism: Achromobacter pestifer

enzyme: acyl-lysine deacylase


organism: Papaver somniferum

substrate_name: (S)-1-Hydroxy-N-methylcanadine; O2; NADPH; H+


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

substrate: (S)-1-Hydroxy-N-methylcanadine; O2; NADPH; H+


enzyme_display_name: emodin O-methyltransferase

organism: Aspergillus terreus

substrate_name: Emodin; S-Adenosyl-L-methionine

enzyme: emodin O-methyltransferase

substrate: Emodin; S-Adenosyl-L-methionine


organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)

substrate_name: emodin

assay_conditions_summary: pH 7

substrate: emodin


enzyme_display_name: sulfopyruvate decarboxylase

organism: Methanocaldococcus jannaschii

substrate_name: sulfopyruvate

enzyme: sulfopyruvate decarboxylase

substrate: sulfopyruvate


enzyme_display_name: deoxynucleotide 3'-phosphatase

organism: Rattus norvegicus

substrate_name: deoxythymidine 5'-phosphate

enzyme: deoxynucleotide 3'-phosphatase

substrate: deoxythymidine 5'-phosphate


organism: Paenarthrobacter nicotinovorans

sequence_source: UniProtKB/Swiss-Prot Q93NG6 FASTA; reviewed entry DHPON_PAENI; PMID 16321959 evidence

assay_conditions_summary: pH 7.5; buffer 75 mM phosphate

proof_lines: in 75 mM phosphate buffer, pH 7.5, temperature not specified in the publication


enzyme_display_name: maleamate amidohydrolase

organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: Unknown

enzyme: maleamate amidohydrolase

substrate: Unknown


organism: Bacteriophage T4

substrate_name: Deoxythymidine 3'-phosphate; H2O

substrate: Deoxythymidine 3'-phosphate; H2O


organism: Bordetella bronchiseptica

substrate_name: Maleamate

substrate: Maleamate


organism: Pseudomonas putida

substrate_name: H2O; Maleamate

substrate: H2O; Maleamate


organism: Arthrobacter nicotinovorans

substrate_name: 2,6-Dihydroxypseudooxynicotine; H2O

substrate: 2,6-Dihydroxypseudooxynicotine; H2O


enzyme_display_name: linoleate 10R-lipoxygenase

organism: Aspergillus fumigatus

substrate_name: O2; Linoleate

proof_lines: pH and temperature not specified in the publication

enzyme: linoleate 10R-lipoxygenase

substrate: O2; Linoleate


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


enzyme_display_name: glycine betaine--corrinoid protein Co-methyltransferase

organism: Desulfitobacterium hafniense

substrate_name: glycine betaine

proof_lines:
at pH 6.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=6.5

substrate: glycine betaine


organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: linoleic acid

smiles: CCCCC/C=C\C/C=C\CCCCCCCC(=O)O

substrate: linoleic acid


organism: Desulfitobacterium hafniense (strain Y51)

enzyme: glycine betaine--corrinoid protein Co-methyltransferase


organism: Escherichia coli (strain K12)

substrate_name: UDP-glucose (for hydrolysis reaction)

proof_lines: kcat is 0.013 sec(-1) for UDP-glucose hydrolysis.

substrate: UDP-glucose (for hydrolysis reaction)


organism: Escherichia coli

substrate_name: UDPglucose; Lipopolysaccharide

substrate: UDPglucose; Lipopolysaccharide


enzyme_display_name: homogentisate geranylgeranyltransferase

organism: Hordeum vulgare

enzyme: homogentisate geranylgeranyltransferase


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


enzyme_display_name: glucosinolate gamma-glutamyl hydrolase

organism: Arabidopsis thaliana

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

enzyme: glucosinolate gamma-glutamyl hydrolase


substrate_name: phenylacetohydroximoyl-glutathione

substrate: phenylacetohydroximoyl-glutathione


enzyme_display_name: coagulation factor IXa

organism: Homo sapiens

substrate_name: Factor X

enzyme: coagulation factor IXa

substrate: Factor X


organism: Bos taurus

proof_lines: factor IXabeta, 0.1 mg/ml phospholipids, factor VIIIa in activating mixture

proof_lines: factor IXabeta, 0.1 mg/ml phospholipids in activating mixture

proof_lines: Gla-domainless factor IXabeta in activating mixture


proof_lines: pH 7.4, 22°C, recombinant mutant N129A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant N129A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: mutant enzyme N129A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: pH 7.4, 22°C, recombinant mutants N129A and K132A, each in the intrinsic tenase complex, in absence of ethylene glycol


proof_lines: pH 7.4, 22°C, recombinant mutant R165A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant R165A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: mutant enzyme R165A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: pH 7.4, 22°C, recombinant mutant N178A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant N178A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: mutant enzyme N178A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: pH 7.4, 22°C, recombinant mutant K132A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant K132A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: mutant enzyme K132A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: pH 7.4, 22°C, recombinant mutant K126A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant K126A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: mutant enzyme K126A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: mutant Y94F/K98T/Y177F/I213V/E219, FX activation in presence of FVIIIa

proof_lines: mutant Y94F/K98T/Y177F/I213V/E219, FX activation in absence of FVIIIa


proof_lines: mutant Y94F/K98T, FX activation in presence of FVIIIa

proof_lines: mutant Y94F/K98T, FX activation in absence of FVIIIa


proof_lines: mutant Y94F/K98T/Y177F, FX activation in absence of FVIIIa

proof_lines: mutant Y94F/K98T/Y177F, FX activation in presence of FVIIIa


substrate_name: Factor X; H2O

proof_lines: in the presence of 0.1 mM phospholipid and 5 mM Ca2+

proof_lines: plasma-derived FIXa, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C

proof_lines: plasma-derived FIXa, 5 units/ml FVIIIa and extruded phosphatidylcholine-phosphatidylserine phospholipid vesicles supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C

substrate: Factor X; H2O


proof_lines: mutant enzyme rFIXa107A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C

proof_lines: mutant enzyme rFIXa105A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C

proof_lines: mutant enzyme rFIXa91A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C


proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme, in presence of 0.2 M NaCl

proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme, in absence of NaCl

proof_lines: wild type enzyme FIXa, in presence of 200 mM Na+


proof_lines: mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in presence of FVIIIa

proof_lines: mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in absence of FVIIIa


assay_conditions_summary: pH 7.5; 295.15 K; buffer containing 0

proof_lines: wild type enzyme, in 0.02 M Tris-HCl (pH 7.5) buffer containing 0.1 M NaCl, 0.1 mg/ml bovine serum albumin, 33% ethylene glycol, and 5 mM Ca2+, at 22°C

proof_lines: pH 7.4, 22°C, recombinant wild-type enzyme the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: wild type FIXa, FX activation in presence of FVIIIa


proof_lines: FIXa/FXa chimera in which the 39-loop of the protease is replaced with the corresponding loop of FXa, in TBS containing 0.1 mg/ml bovine serum albumin, 0.1% polyethylene glycol (PEG) 8000, and 5 mM Ca2+, at 22°C, pH not specified in the pub

proof_lines: in the presence of factor VIIIa, pH and temperature not specified in the publication

proof_lines: chimera enzyme FIXaN, in the presence of SFLLRN-activated platelets


proof_lines: mutant enzyme R233A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: mutant enzyme R170A, using factor X as substrate, at pH 7.4, 22°C


proof_lines:
variant protein factor IXaCH
variant protein factor IXaAL


proof_lines: mutant enzyme E410A, in the absence of factor VIIIa, at pH 7.4 and 37°C

proof_lines: mutant enzyme E410A, in the presence of factor VIIIa, at pH 7.4 and 37°C


proof_lines: mutant enzyme E410L, in the absence of factor VIIIa, at pH 7.4 and 37°C

proof_lines: mutant enzyme E410L, in the presence of factor VIIIa, at pH 7.4 and 37°C


proof_lines: mutant enzyme E410N, in the absence of factor VIIIa, at pH 7.4 and 37°C

proof_lines: mutant enzyme E410N, in the presence of factor VIIIa, at pH 7.4 and 37°C


proof_lines: mutant enzyme E410H, in the absence of factor VIIIa, at pH 7.4 and 37°C

proof_lines: mutant enzyme E410H, in the presence of factor VIIIa, at pH 7.4 and 37°C


enzyme_display_name: plasmepsin II

organism: Unknown

enzyme: plasmepsin II


organism: Plasmodium falciparum

proof_lines: pH 4.5, temperature not specified in the publication


proof_lines:
pH 4.4, 37°C
autoactivated enzyme
pH 4.7


proof_lines: F244E mutant enzyme expressed by a system that bypasses the need for autoactivation


proof_lines: delF241 mutant enzyme expressed by a system that bypasses the need for autoactivation


proof_lines: F244A mutant enzyme expressed by a system that bypasses the need for autoactivation


proof_lines: F244K mutant enzyme expressed by a system that bypasses the need for autoactivation


assay_conditions_summary: pH 5

proof_lines: wild-type PMII, pH 5, temperature not specified in the publication


enzyme_display_name: matriptase

proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant L785S

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S

enzyme: matriptase


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant A757S

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S


proof_lines: above, pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant E712Y/A757S/L785S

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant A757S/L785S

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S


substrate_name: RQLRVVGG

assay_conditions_summary: pH 8; 310.15 K; buffer Tris saline

proof_lines: matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C

proof_lines: purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C

proof_lines: recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C

substrate: RQLRVVGG


organism: Mus musculus

substrate_name: Suc-Ala-Ala-Pro-Arg-p-nitroanilide

substrate: Suc-Ala-Ala-Pro-Arg-p-nitroanilide


organism: Rattus norvegicus

substrate_name: single-chain urokinase-type plasminogen activator

proof_lines: catalytic domain, Asp603 - Val855, after treatment with enteropeptidase

proof_lines: full-length rat matriptase with Myc-epitope-hexahistidine tag at its carboxyl-terminus

proof_lines: pseudozymogen His6t-S-CD consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase is used


proof_lines: construct consisting of the catalytic domain of matriptase bearing a N772Q mutation fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase


proof_lines: engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase)


substrate_name: Ile-Pro-Arg-p-nitroanilide

substrate: Ile-Pro-Arg-p-nitroanilide


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


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

proof_lines: matriptase-2, pH and temperature not specified in the publication


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant H665F

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged wild-type enzyme

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant


proof_lines: above, pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant E712Y

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y


enzyme_display_name: thrombin

substrate_name: GLVPRGVNL

assay_conditions_summary: pH 7.4; 298.15 K; buffer 10 mM imidazole

proof_lines:
pH 7.4, 25°C
alpha-thrombin
beta-thrombin

enzyme: thrombin

substrate: GLVPRGVNL


substrate_name: H2O; Sar-Pro-Arg p-nitroanilide dihydrochloride

assay_conditions_summary: pH 7.5; 298.15 K; buffer and 0

proof_lines:
pH 7.5, 25°C
pH 8.0, 25°C, absence of Na+
0.15 M KCl


proof_lines: mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 0.2 M choline chloride, at 22°C

proof_lines: mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 0.2 M NaCl, at 22°C

proof_lines: mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 1.0 M NaCl and dithiothreitol, at 22°C


proof_lines: mutant enzyme R67C/I82C, in Tris-HCl (pH 7.5) with 0.2 M NaCl, at 22°C

proof_lines: mutant enzyme R67C/I82C, in Tris-HCl (pH 7.5) with 0.2 M choline chloride, at 22°C


proof_lines: mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride

proof_lines: mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM NaCl

proof_lines: mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mN NaCl


proof_lines: wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride

proof_lines: wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM NaCl


substrate_name: fibrinogen

proof_lines: pH 7.0, 25°C, Kcat/KM values for diverse recombinant thrombin mutants, overview

substrate: fibrinogen


substrate_name: protein C

substrate: protein C


substrate_name: spectrozyme-TH

proof_lines: mutant K222D, pH 8.0, 25°C, absence of Na+

proof_lines: mutant K222D, pH 8.0, 25°C, presence of 0.2 M Na+

substrate: spectrozyme-TH


proof_lines: wild-type, pH 8.0, 25°C, presence of 0.2 M Na+


substrate_name: p-Tosyl-L-arginine methyl ester; H2O

substrate: p-Tosyl-L-arginine methyl ester; H2O


substrate_name: Coagulation Factor XIII; H2O

proof_lines: 37°C, pH not specified in the publication, plasma-derived human thrombin FII

proof_lines: 37°C, pH not specified in the publication, recombinant human thrombin FII

substrate: Coagulation Factor XIII; H2O


substrate_name: Fibrinopeptide A

substrate: Fibrinopeptide A


substrate_name: PAR1 peptide

substrate: PAR1 peptide


enzyme_display_name: aspartate kinase

substrate_name: ATP; L-Aspartate

enzyme: aspartate kinase

substrate: ATP; L-Aspartate


substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP


substrate_name: L-Aspartate

substrate: L-Aspartate


substrate_name: L-Malate

substrate: L-Malate


proof_lines: AK2, 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana


organism: Daucus carota


proof_lines: 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana


proof_lines: AK3, 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana


organism: Pseudomonas stutzeri


organism: Saccharomyces cerevisiae


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Methanocaldococcus jannaschii

substrate_name: L-aspartate

proof_lines:
at 37°C
at 70°C
Raw SKiD Env: Temp=37°C, pH=-----

substrate: L-aspartate


organism: Thermus thermophilus


assay_conditions_summary: pH 7.5; 333.15 K; cofactor ATP


substrate_name: L-Aspartate; ATP

substrate: L-Aspartate; ATP


organism: Streptomyces noursei

proof_lines: mutant M68V, recombinant enzyme purified to homogeneity


proof_lines: wild-type, recombinant enzyme purified to homogeneity


organism: Thermotoga maritima

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP


enzyme_display_name: trypanothione-disulfide reductase

organism: Leishmania donovani

substrate_name: trypanothione disulfide

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADPH

enzyme: trypanothione-disulfide reductase

substrate: trypanothione disulfide


organism: Leishmania infantum

proof_lines: in the presence of 0.01 mM 4-((1-(4-ethylphenyl)-2-methyl-5-(4-(methylthio)phenyl)-1H-pyrrol-3-yl)methyl)thiomorpholine, at 20°C, pH not specified in the publication

proof_lines: in the absence of 4-((1-(4-ethylphenyl)-2-methyl-5-(4-(methylthio)phenyl)-1H-pyrrol-3-yl)methyl)thiomorpholine, at 20°C, pH not specified in the publication

proof_lines: in the presence of 0.03 mM 4-((1-(4-ethylphenyl)-2-methyl-5-(4-(methylthio)phenyl)-1H-pyrrol-3-yl)methyl)thiomorpholine, at 20°C, pH not specified in the publication


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


proof_lines: mutant enzyme W81A, pH and temperature not specified in the publication


organism: Aspergillus japonicus

substrate_name: myo-inositol hexakisphosphate

proof_lines:
phytic acid sodium salt
phytic acid dipotassium salt

substrate: myo-inositol hexakisphosphate


organism: Aspergillus niger


organism: Bacillus sp. (in: firmicutes)


organism: Bacillus subtilis


proof_lines: mutant enzyme E436A, pH and temperature not specified in the publication


proof_lines: mutant enzyme Q439A, pH and temperature not specified in the publication


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines:
in 40 mM HEPES, pH 7.4, 1 mM EDTA
Raw SKiD Env: Temp=-----, pH=7.4


organism: Trypanosoma congolense

substrate_name: H+; NADPH; Oxidized trypanothione

assay_conditions_summary: cofactor NADPH

substrate: H+; NADPH; Oxidized trypanothione


organism: Burkholderia sp. a13(2014)


organism: Citrobacter amalonaticus

assay_conditions_summary: pH 4.5; 310.15 K; buffer sodium acetate

proof_lines: recombinant enzyme, in 0.1 M sodium acetate buffer (pH 4.5) at 37°C


organism: Debaryomyces castellii

proof_lines:
native protein
recombinant protein
Raw SKiD Env: Temp=-----, pH=-----


organism: Trypanosoma cruzi

substrate_name: Unknown

proof_lines: at 25°C, pH not specified in the publication

substrate: Unknown


enzyme_display_name: ADP-specific phosphofructokinase

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 6.5; 313.15 K; cofactor ADP

proof_lines:
pH 6.5, 40°C
pH 6.5, 50°C
Raw SKiD Env: Temp=40°C, pH=6.5

enzyme: ADP-specific phosphofructokinase

substrate: D-fructose 6-phosphate


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


organism: Methanosarcina mazei

substrate_name: ADP

substrate: ADP


proof_lines:
pH 6.5, 40°C
MgADP, pH 6.5, 40°C


organism: Pyrococcus horikoshii

assay_conditions_summary: 323.15 K; cofactor ADP


organism: Methanococcus maripaludis

assay_conditions_summary: pH 6.5; 303.15 K; cofactor ADP


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


substrate_name: D-glucose

substrate: D-glucose


proof_lines: pH 6.5, 30°C, phosphopfructokinase activity

proof_lines: pH 7.8, 30°C, reverse glucokinase reaction


organism: Methanococcoides burtonii

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ADP


substrate_name: D-fructose 1,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


organism: Methanohalobium evestigatum

substrate_name: ADP; D-fructose 6-phosphate

substrate: ADP; D-fructose 6-phosphate


enzyme_display_name: D-xylose reductase (NADPH)

organism: Saccharomyces cerevisiae

substrate_name: D-xylose

assay_conditions_summary: pH 5; 303.15 K; cofactor NADPH

proof_lines: pH 5.0, 30°C, recombinant wild-type enzyme

enzyme: D-xylose reductase (NADPH)

substrate: D-xylose


organism: Scheffersomyces stipitis

substrate_name: D-Xylose

substrate: D-Xylose


assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines: with NADH, with 150 mM NaCl, pH 8.0, 30°C


organism: Yamadazyma tenuis

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309D, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose

proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309D, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose


substrate_name: NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme D50A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose

proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme D50A, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose

substrate: NADPH


proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme W23Y, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose


organism: Zymomonas mobilis subsp. mobilis

substrate_name: benzaldehyde

proof_lines: pH 7.2, temperature not specified in the publication

substrate: benzaldehyde