enzyme_display_name: cellulose 1,4-beta-cellobiosidase (reducing end)

organism: Acetivibrio thermocellus

substrate_name: cellopentaose

sequence_source: UniProt REST accession A3DH67; canonical sequence checked on 2026-06-16

proof_lines: pH 5.7, temperature not specified in the publication

substrate: cellopentaose


organism: Dictyostelium discoideum

substrate_name: 4-nitrophenyl beta-D-lactoside

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

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

proof_lines: pH 5.0, 45°C, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker

source_databases_merged: brenda skid

enzyme: cellulose 1,4-beta-cellobiosidase (reducing end)

substrate: 4-nitrophenyl beta-D-lactoside

source: brenda


organism: Dictyostelium purpureum

km_display: Not reported


organism: Geotrichum candidum

source_db: oed

source_license: CC BY 4.0

source: oed


substrate_name: 4-nitrophenyl beta-D-cellobioside

substrate: 4-nitrophenyl beta-D-cellobioside


proof_lines:
catalyticdomain, pH 5.0, 37°C
Raw SKiD Env: Temp=37°C, pH=5


organism: Limnoria quadripunctata

substrate_name: Unknown

kcat_display: Not reported

ki_unit: mM

proof_lines:
pH 4.5, 30°C
at pH 4.5 and 30°C

substrate: Unknown


organism: Melanocarpus albomyces

substrate_name: 2-chloro-4-nitrophenyl beta-D-lactoside

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

substrate: 2-chloro-4-nitrophenyl beta-D-lactoside


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


mutation_type: substitution


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Phialemonium thermophilum

assay_conditions_summary: pH 5.7; 295.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer, pH 5.7, at 22°C

proof_lines: in 50 mM sodium acetate buffer, pH 5.0, at 22°C


organism: Rasamsonia emersonii

substrate_name: 4-methylumbelliferyl beta-D-lactoside

substrate: 4-methylumbelliferyl beta-D-lactoside


proof_lines:
pH 5.0, 60°C, wild-type
pH 5.0, 45°C, wild-type
pH 5.0, 22°C, wild-type


proof_lines: pH 5.0, 22°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module

proof_lines: pH 5.0, 45°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module


organism: Talaromyces funiculosus

substrate_name: 4-nitrophenyl beta-D-lactopyranoside

proof_lines:
at pH 4.0 and 60°C
Raw SKiD Env: Temp=60°C, pH=4

substrate: 4-nitrophenyl beta-D-lactopyranoside


enzyme_display_name: protein O-GlcNAcase

organism: Unknown

enzyme: protein O-GlcNAcase


organism: Thermoascus aurantiacus

assay_conditions_summary: pH 5; 295.15 K; buffer 50 mM sodium acetate

proof_lines: pH 5.0, 50°C, presence of 1 mM mannobiose


organism: Thermochaetoides thermophila


organism: Thermothelomyces thermophilus

proof_lines: at 50°C in 50 mM sodium acetate (pH 5.0)


organism: Thermothielavioides terrestris


organism: Trichoderma harzianum

proof_lines:
pH 5.0, 50°C
Raw SKiD Env: Temp=50°C, pH=5


organism: Trichoderma reesei


proof_lines: pH 5.0, 27°C, recombinant mutant W40A enzyme catalytic domain


proof_lines: pH 5.0, 27°C, recombinant wild-type enzyme catalytic domain


substrate_name: Avicel

substrate: Avicel


substrate_name: 4-nitrophenyl lactopyranoside

proof_lines:
pH 5.0, 25°C, wild-type enzyme
25°C, pH 7, wild-type
25°C, pH 5, wild-type

substrate: 4-nitrophenyl lactopyranoside


proof_lines: pH 5.0, 25°C, substrate: 4-nitrophenyl lactopyranoside, mutant enzyme R251A


proof_lines: pH 5.0, 25°C, substrate: 4-nitrophenyl lactopyranoside, mutant enzyme R394A


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=25°C, pH=5


enzyme_display_name: carnitine O-acetyltransferase

substrate_name: CoASH

enzyme: carnitine O-acetyltransferase

substrate: CoASH


enzyme_display_name: xanthine phosphoribosyltransferase

substrate_name: xanthine

enzyme: xanthine phosphoribosyltransferase

substrate: xanthine


enzyme_display_name: alanine--glyoxylate transaminase

organism: Canis lupus familiaris

substrate_name: glyoxylate

proof_lines: pH 8.2, 37°C, isoenzyme 1, alanine as amino donor

proof_lines: pH 8.2, 37°C, isoenzyme 1, glyoxylate as amino acceptor

enzyme: alanine--glyoxylate transaminase

substrate: glyoxylate


organism: Felis catus


organism: Mus musculus

substrate_name: L-alanine

proof_lines: pH 8.2, 37°C, isoenzyme 2, glyoxylate as amino acceptor

substrate: L-alanine


organism: Rattus norvegicus

proof_lines: pH 8.0, 37°C, pyruvate as amino acceptor


organism: Saccharomyces cerevisiae

proof_lines: pH 8.2, 37°C, glyoxylate as amino acceptor

proof_lines: pH 8.2, 37°C, isoenzyme 2, alanine as amino donor


organism: Suncus murinus

proof_lines: GPT 1, alanine:2-oxoglutarate aminotransferase AGT activity


enzyme_display_name: UMP/CMP kinase

substrate_name: UMP

enzyme: UMP/CMP kinase

substrate: UMP


enzyme_display_name: nucleoside-diphosphate kinase

organism: Homo sapiens

substrate_name: Cidofovir monophosphate; ATP

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

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines:
isozyme B6, 25°C
cosubstrate ADP
isozyme A6, 25°C

enzyme: nucleoside-diphosphate kinase

substrate: Cidofovir monophosphate; ATP


organism: Oryza sativa

substrate_name: GTP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

proof_lines: isozyme NDPK2, in 4 mM Tris-HCl, pH 7.5, 100 mM KCl, 25 mM MgCl2, at 25°C

proof_lines: isozyme NDPK3, in 4 mM Tris-HCl, pH 7.5, 100 mM KCl, 25 mM MgCl2, at 25°C

proof_lines: isozyme NDPK1, in 4 mM Tris-HCl, pH 7.5, 100 mM KCl, 25 mM MgCl2, at 25°C

substrate: GTP


substrate_name: acetyl-CoA

source_db: uniprot

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

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA

source: uniprot


organism: Caenorhabditis elegans

substrate_name: beta-xylose nitrophenyl (at 17 degrees Celsius)


organism: Bacillus subtilis (strain 168)


organism: Enterococcus faecalis (strain ATCC 700802 / V583)


substrate_name: CMP-NeuAc

substrate: CMP-NeuAc


organism: Arabidopsis thaliana

substrate_name: glutamate

substrate: glutamate


substrate_name: L-alanine (with the His-AGXT construct)

substrate: L-alanine (with the His-AGXT construct)


substrate_name: D-beta-aminoisobutyrate

substrate: D-beta-aminoisobutyrate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Bos taurus

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Gallus gallus


substrate_name: IDP

substrate: IDP


substrate_name: AMP with ATP as phosphate donor

substrate: AMP with ATP as phosphate donor


substrate_name: AMP

substrate: AMP


substrate_name: AMP (with ATP as phosphate donor)

substrate: AMP (with ATP as phosphate donor)


substrate_name: CMP

substrate: CMP


substrate_name: ADP

substrate: ADP


enzyme_display_name: coagulation factor VIIa

substrate_name: H-D-Ile-Pro-Arg-p-nitroanilide; H2O

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

proof_lines: SABIO-RK modifier species: coagulation factor VIIa(Enzyme) mutant C164V/V299C-FVIIa

enzyme: coagulation factor VIIa

substrate: H-D-Ile-Pro-Arg-p-nitroanilide; H2O


substrate_name: H2O; H-D-Ile-Pro-Arg-p-nitroanilide

proof_lines: presence of 200 mM NaCl, pH 7.4, temperature not specified in the publication

proof_lines: presence of 5 mM Ca2+, pH 7.4, temperature not specified in the publication

substrate: H2O; H-D-Ile-Pro-Arg-p-nitroanilide


proof_lines: SABIO-RK modifier species: coagulation factor VIIa(Enzyme) mutant L280I/V299M-FVIIa


proof_lines: SABIO-RK modifier species: coagulation factor VIIa(Enzyme) mutant V299M-FVIIa


substrate_name: Unknown

proof_lines: mutant G372 + soluble tissue factor for induced allosteric activation of factor VIIa

substrate: Unknown


substrate_name: Factor X

proof_lines: mutant G372A + lipidated tissue factor for induced allosteric activation of factor VIIa, pH 7.4

proof_lines: mutant G372A + soluble tissue factor for induced allosteric activation of factor VIIa, pH 7.4

substrate: Factor X


kcat_over_km_origin: calculated

sequence_source: UniProtKB:P08709 direct REST lookup 2026-06-16

data_origin: experimental


proof_lines: wild type enzyme, in the absence of soluble tissue factor (1-219), at pH 7.4 and 25°C

proof_lines: wild-type FVIIa + lipidated tissue factor for induced allosteric activation of factor VIIa, pH 7.4

proof_lines: wild type enzyme, in the presence of soluble tissue factor (1-219), at pH 7.4 and 25°C


enzyme_display_name: coagulation factor XIa

enzyme: coagulation factor XIa


sequence_source: UniProtKB:P03951 direct REST lookup 2026-06-16

proof_lines: recombinant wild-type enzyme, pH 7.5, 37°C


enzyme_display_name: dihydropyrimidinase

organism: Geobacillus stearothermophilus

substrate_name: DL-p-hydroxyphenylhydantoin

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q45515 canonical sequence with row-specific mutation reconstruction (M63H/F159N) and applied mutation signature M63H/F159N to reconstruct the assayed variant sequence.

enzyme: dihydropyrimidinase

substrate: DL-p-hydroxyphenylhydantoin


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (T418I) and applied mutation signature T418I to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme T418I


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (R118Q) and applied mutation signature R118Q to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme R118Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (H365Y) and applied mutation signature H365Y to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme H365Y


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (T513A) and applied mutation signature T513A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme T513A


sequence_source: UniProtKB:Q14117 canonical accession sequence from direct lookup

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (Y448H) and applied mutation signature Y448H to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme Y448H


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (G410S) and applied mutation signature G410S to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme G410S


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (H295R) and applied mutation signature H295R to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme H295R


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (A189V) and applied mutation signature A189V to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme A189V


organism: Jannaschia sp. CCS1

sequence_source: UniProtKB:Q28SA7 direct lookup returned Inactive/deleted; no live replacement accession was present in the selected evidence.


organism: Lachancea kluyveri

sequence_source: UniProtKB:Q9P903 canonical sequence found, but selected source notes a C-terminal Strep-Tag construct.

proof_lines: pH 7.0, 25°C, dihydropyrimidinase with a C-terminal Strep-Tag


organism: Pseudomonas aeruginosa

substrate_name: 5,6-Dihydrouracil; H2O

sequence_source: UniProtKB:Q9I676 canonical accession sequence from direct lookup

substrate: 5,6-Dihydrouracil; H2O


organism: Pseudomonas fluorescens

substrate_name: isobutylhydantoin

verification_status: verified

sequence_source: UniProtKB:S5MPT0 canonical accession sequence from direct lookup

column_label: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'Isobutylhydantoin'; column 'Km [mM]' = 4.42; column 'kcat [s^-1]' = 391; column 'kcat/Km [s^-1 mM^-1]' = 88.5; the remaining column of the table, 'Structural formula', holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.42 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 4.42 mM. kcat: printed Table 2 cell 391 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 391.0 s^(-1). kcat/Km: the exported value 88.46153846153847 s^(-1)*mM^(-1) is the full-precision quotient of the same Table 2 row's own printed cells, 391 / 4.42 = 88.46153846153847; Table 2 also prints its own efficiency cell 88.5 s^-1 mM^-1, which is that same quotient stated to the precision the table uses, so the exported ratio stands unchanged.

raw_value_unit_evidence: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'Isobutylhydantoin': column 'Km [mM]' = 4.42; column 'kcat [s^-1]' = 391; column 'kcat/Km [s^-1 mM^-1]' = 88.5.

row_label: Table 2, substrate row 'Isobutylhydantoin'

table_label: Table 2: Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins (Appl Biochem Biotechnol 2016, 179(1):1-15)

substrate: isobutylhydantoin

status: verified


substrate_name: indolmethylhydantoin

column_label: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'Indolmethylhydantoin'; column 'Km [mM]' = 4.64; column 'kcat [s^-1]' = 1.43; column 'kcat/Km [s^-1 mM^-1]' = 0.31; the remaining column of the table, 'Structural formula', holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.64 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 4.64 mM. kcat: printed Table 2 cell 1.43 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 1.43 s^(-1). kcat/Km: the exported value 0.3081896551724138 s^(-1)*mM^(-1) is the full-precision quotient of the same Table 2 row's own printed cells, 1.43 / 4.64 = 0.3081896551724138; Table 2 also prints its own efficiency cell 0.31 s^-1 mM^-1, which is that same quotient stated to the precision the table uses, so the exported ratio stands unchanged.

raw_value_unit_evidence: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'Indolmethylhydantoin': column 'Km [mM]' = 4.64; column 'kcat [s^-1]' = 1.43; column 'kcat/Km [s^-1 mM^-1]' = 0.31.

row_label: Table 2, substrate row 'Indolmethylhydantoin'

substrate: indolmethylhydantoin


substrate_name: isopropylhydantoin

column_label: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'Isopropylhydantoin'; column 'Km [mM]' = 7.63; column 'kcat [s^-1]' = 77.3; column 'kcat/Km [s^-1 mM^-1]' = 10.1; the remaining column of the table, 'Structural formula', holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 7.63 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 7.63 mM. kcat: printed Table 2 cell 77.3 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 77.3 s^(-1). kcat/Km: the exported value 10.131061598951508 s^(-1)*mM^(-1) is the full-precision quotient of the same Table 2 row's own printed cells, 77.3 / 7.63 = 10.131061598951508; Table 2 also prints its own efficiency cell 10.1 s^-1 mM^-1, which is that same quotient stated to the precision the table uses, so the exported ratio stands unchanged.

raw_value_unit_evidence: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'Isopropylhydantoin': column 'Km [mM]' = 7.63; column 'kcat [s^-1]' = 77.3; column 'kcat/Km [s^-1 mM^-1]' = 10.1.

row_label: Table 2, substrate row 'Isopropylhydantoin'

substrate: isopropylhydantoin


sequence_source: UniProtKB REST direct lookup for S5MPT0 on 2026-06-16

column_label: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row '2-Chlorobenzenehydantoin'; column 'Km [mM]' = 8.57; column 'kcat [s^-1]' = 0.37; column 'kcat/Km [s^-1 mM^-1]' = 0.04; the remaining column of the table, 'Structural formula', holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 8.57 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 8.57 mM. kcat: printed Table 2 cell 0.37 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 0.37 s^(-1). kcat/Km: the exported value 0.043173862310385065 s^(-1)*mM^(-1) is the full-precision quotient of the same Table 2 row's own printed cells, 0.37 / 8.57 = 0.043173862310385065; Table 2 also prints its own efficiency cell 0.04 s^-1 mM^-1, which is that same quotient stated to the precision the table uses, so the exported ratio stands unchanged.

raw_value_unit_evidence: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row '2-Chlorobenzenehydantoin': column 'Km [mM]' = 8.57; column 'kcat [s^-1]' = 0.37; column 'kcat/Km [s^-1 mM^-1]' = 0.04.

row_label: Table 2, substrate row '2-Chlorobenzenehydantoin'


substrate_name: phenylmethylhydantoin

column_label: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'Phenylmethylhydantoin'; column 'Km [mM]' = 9.49; column 'kcat [s^-1]' = 2.91; column 'kcat/Km [s^-1 mM^-1]' = 0.31; the remaining column of the table, 'Structural formula', holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 9.49 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 9.49 mM. kcat: printed Table 2 cell 2.91 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 2.91 s^(-1). kcat/Km: the exported value 0.30663856691253955 s^(-1)*mM^(-1) is the full-precision quotient of the same Table 2 row's own printed cells, 2.91 / 9.49 = 0.30663856691253955; Table 2 also prints its own efficiency cell 0.31 s^-1 mM^-1, which is that same quotient stated to the precision the table uses, so the exported ratio stands unchanged.

raw_value_unit_evidence: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'Phenylmethylhydantoin': column 'Km [mM]' = 9.49; column 'kcat [s^-1]' = 2.91; column 'kcat/Km [s^-1 mM^-1]' = 0.31.

row_label: Table 2, substrate row 'Phenylmethylhydantoin'

substrate: phenylmethylhydantoin


column_label: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'p-Hydroxyphenylhydantoin'; column 'Km [mM]' = 7.52; column 'kcat [s^-1]' = 74.2; column 'kcat/Km [s^-1 mM^-1]' = 9.87; the remaining column of the table, 'Structural formula', holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 7.52 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 7.52 mM. kcat: printed Table 2 cell 74.2 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 74.2 s^(-1). kcat/Km: the exported value 9.867021276595745 s^(-1)*mM^(-1) is the full-precision quotient of the same Table 2 row's own printed cells, 74.2 / 7.52 = 9.867021276595745; Table 2 also prints its own efficiency cell 9.87 s^-1 mM^-1, which is that same quotient stated to the precision the table uses, so the exported ratio stands unchanged.

raw_value_unit_evidence: Table 2 (Steady-state kinetic constants of purified D-PfHYD toward 5'-monosubstituted hydantoins), substrate row 'p-Hydroxyphenylhydantoin': column 'Km [mM]' = 7.52; column 'kcat [s^-1]' = 74.2; column 'kcat/Km [s^-1 mM^-1]' = 9.87.

row_label: Table 2, substrate row 'p-Hydroxyphenylhydantoin'


organism: Rattus norvegicus

substrate_name: H2O; 5,6-Dihydrouracil

sequence_source: UniProtKB REST direct lookup for Q63150 on 2026-06-16

substrate: H2O; 5,6-Dihydrouracil


organism: Saccharomyces kluyveri

sequence_source: UniProtKB REST direct lookup for Q9P903 on 2026-06-16


organism: Aspergillus niger

substrate_name: CoASH

proof_lines:
mitochondrial enzyme
cytosolic enzyme

substrate: CoASH


substrate_name: O-acetyl-L-carnitine

proof_lines:
heart enzyme
sperm enzyme

substrate: O-acetyl-L-carnitine


organism: Camelus dromedarius

substrate_name: butyryl-CoA

substrate: butyryl-CoA


organism: Candida albicans

substrate_name: acetyl-CoA

proof_lines:
mitochondrial enzyme
peroxisomal enzyme

substrate: acetyl-CoA


organism: Candida tropicalis

substrate_name: propionyl-CoA

proof_lines: peroxisomal enzyme, second substrate propionyl-CoA

substrate: propionyl-CoA


organism: Cavia porcellus

substrate_name: L-carnitine

substrate: L-carnitine


organism: Columba livia

substrate_name: carnitine

substrate: carnitine


organism: Columba sp.


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines:
cosubstrate propionyl-CoA
peroxisomal enzyme, at pH 7.4 and 37°C
cosubstrate hexanoyl-CoA


organism: Mus musculus

substrate_name: hexanoyl-CoA

proof_lines:
cosubstrate butanoyl-CoA
cosubstrate decanoyl-CoA
cosubstrate hexanoyl-CoA

substrate: hexanoyl-CoA


organism: Oryctolagus cuniculus

substrate_name: choline

proof_lines:
brain enzyme
heart enzyme

substrate: choline


proof_lines: above, mutant enzyme A106M/T465V/T467N/R518N


proof_lines: presence of 25 microM of inhibitor 3_4_21-27_2-1, pH 7.4, 37°C

proof_lines: presence of 100 microM of inhibitor 3_4_21-27_2-1, pH 7.4, 37°C


enzyme_display_name: cathepsin H

organism: Capra hircus

substrate_name: Unknown

proof_lines: pH 6.0, 37°C, 1 mM, 25.40% activity remaining

enzyme: cathepsin H

substrate: Unknown


organism: Sus scrofa


organism: Bacillus sp. (in: firmicutes)

substrate_name: dihydrouracil

substrate: dihydrouracil


organism: Geobacillus stearothermophilus

substrate_name: DL-p-hydroxyphenylhydantoin

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q45515 FASTA direct lookup plus reconstructed substitutions M63I/F159S and applied mutation signature M63I/F159S to reconstruct the assayed variant sequence.

substrate: DL-p-hydroxyphenylhydantoin


substrate_name: hydantoin

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q45515 FASTA direct lookup plus reconstructed substitutions M63H/F159N and applied mutation signature M63H/F159N to reconstruct the assayed variant sequence.

substrate: hydantoin


sequence_source: UniProtKB:Q45515 FASTA direct lookup 2026-06-16


sequence_source: UniProtKB:Q45515 FASTA direct lookup plus reconstructed substitutions M63H/F159N


sequence_source: UniProtKB:Q45515 FASTA direct lookup plus reconstructed substitutions M63I/F159S


substrate_name: 3',5'-Cyclic AMP

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed D811A variant during review. and applied mutation signature D811A to reconstruct the assayed variant sequence.

substrate: 3',5'-Cyclic AMP

status: unverified


substrate_name: 3',5'-Cyclic AMP; H2O

sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed D812A variant during review. and applied mutation signature D812A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant D812A

substrate: 3',5'-Cyclic AMP; H2O


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed T810A variant during review. and applied mutation signature T810A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant T810A


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed H796A variant during review. and applied mutation signature H796A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed S804A variant during review. and applied mutation signature S804A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant S804A


sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed S804A variant during review.


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed H798A variant during review. and applied mutation signature H798A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed D811A variant during review.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant D811A


sequence_source: UniProt Q14432 canonical sequence version 3, direct REST/FASTA check during review.

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


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed H782A variant during review. and applied mutation signature H782A to reconstruct the assayed variant sequence.


substrate_name: H2O; 3',5'-Cyclic AMP

sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed H782A variant during review.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant H782A

substrate: H2O; 3',5'-Cyclic AMP


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed C816S variant during review. and applied mutation signature C816S to reconstruct the assayed variant sequence.


sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed T810A variant during review.


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed Y807A variant during review. and applied mutation signature Y807A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed Y807A variant during review.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant Y807A


enzyme_display_name: ubiquitinyl hydrolase 1

substrate_name: ubiquitin 7-amido-4-methylcoumarin

sequence_source: UniProt Q9Y5K5 sequence, direct UniProt REST lookup on 2026-06-16

enzyme: ubiquitinyl hydrolase 1

substrate: ubiquitin 7-amido-4-methylcoumarin


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


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P15374 canonical sequence, direct UniProt REST lookup on 2026-06-16 and applied mutation signature Q89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P09936 canonical sequence, direct UniProt REST lookup on 2026-06-16 and applied mutation signature Q84A to reconstruct the assayed variant sequence.


sequence_source: UniProt P09936 sequence, direct UniProt REST lookup on 2026-06-16

proof_lines: recombinant wild-type isozyme L1, pH 7.8, room temperature


substrate_name: Ubiquitin-AMC; H2O

sequence_source: UniProt Q6R6M4 sequence, direct UniProt REST lookup on 2026-06-16

substrate: Ubiquitin-AMC; H2O


substrate_name: H2O; Ubiquitin-AMC

sequence_source: UniProt Q93009 sequence, direct UniProt REST lookup on 2026-06-16

substrate: H2O; Ubiquitin-AMC


sequence_source: UniProt Q96RU2 sequence, direct UniProt REST lookup on 2026-06-16


substrate_name: Arg-Leu-Arg-Gly-Gly-AMC; H2O

sequence_source: UniProt Q96AP4 sequence, direct UniProt REST lookup on 2026-06-16

substrate: Arg-Leu-Arg-Gly-Gly-AMC; H2O


organism: Middle East respiratory syndrome-related coronavirus

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


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

proof_lines: SABIO-RK modifier species: ubiquitinyl hydrolase 1(Enzyme) mutant PLpro-deltaUbl2-domain (aa 1545-1801)


substrate_name: H2O; Ubiquitin-AFC

substrate: H2O; Ubiquitin-AFC


sequence_source: UniProt Q9R0P9 sequence, direct UniProt REST lookup on 2026-06-16


organism: Porcine epidemic diarrhea virus

substrate_name: Ubiquitin-AFC; H2O

substrate: Ubiquitin-AFC; H2O


organism: porcine epidemic diarrhea virus

substrate_name: Dabcyl-FKKKGGGDVKE-Edans

substrate: Dabcyl-FKKKGGGDVKE-Edans


organism: Rattus norvegicus

substrate_name: 3',5'-Cyclic AMP; H2O; 3',5'-Cyclic AMP; H2O; AMP


substrate_name: H2O; 3',5'-Cyclic AMP; H2O; 3',5'-Cyclic AMP; AMP


sequence_source: UniProtKB:Q01062 direct REST lookup on 2026-06-16

substrate: 3',5'-Cyclic AMP; H2O; 3',5'-Cyclic AMP; H2O; AMP


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P22434 direct REST lookup on 2026-06-16


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

proof_lines:
pH 7.5, 22°C
pH 7.5, 22°C, presence of 10 mM MgCl2
pH 7.5, 22°C, presence of 10 mM MnCl2


organism: Thermotoga maritima

substrate_name: 5'-pApG; 5'-pApA

sequence_source: UniProtKB:Q9X1T1 direct REST lookup on 2026-06-16

proof_lines:
pH 8.5, 23°C
Raw SKiD Env: Temp=23°C, pH=8.5

substrate: 5'-pApG; 5'-pApA


organism: Thermus thermophilus


substrate_name: 3',5'-Cyclic GMP

substrate: 3',5'-Cyclic GMP


substrate_name: H2O; 3',5'-Cyclic AMP; H2O; 3',5'-Cyclic AMP; AMP; H2O; 3',5'-Cyclic GMP; 3',5'-Cyclic GMP; GMP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09936 direct REST lookup on 2026-06-16 plus selected mutation signature and applied mutation signature S18Y to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant S18Y isozyme L1, pH 7.8, room temperature


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09936 direct REST lookup on 2026-06-16 plus selected mutation signature and applied mutation signature I93M to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant I93M isozyme L1, pH 7.8, room temperature


substrate_name: H2O; Ubiquitin fused C-terminal to tryptophan; H2O; Ubiquitin fused C-terminal to tryptophan; Ubiquitin; Tryptophan; Ubiquitin fused C-terminal to tryptophan; H2O; H2O; Ubiquitin fused C-terminal to alanine-tryptophan; Ubiquitin fused C-terminal to alanine-tryptophan; Ala-Trp; H2O; Ubiquitin fused C-terminal to tryptophan-alanine; Ubiquitin fused C-terminal to tryptophan-alanine; Trp-Ala


substrate_name: Ubiquitin fused C-terminal to tryptophan; H2O; Ubiquitin fused C-terminal to tryptophan; H2O; Tryptophan; Ubiquitin; H2O; Ubiquitin fused C-terminal to tryptophan; H2O; Ubiquitin fused C-terminal to alanine-tryptophan; Ubiquitin fused C-terminal to alanine-tryptophan; Ala-Trp; Ubiquitin fused C-terminal to tryptophan-alanine; H2O; Ubiquitin fused C-terminal to tryptophan-alanine; Trp-Ala

sequence_source: UniProtKB:P09936 direct REST lookup on 2026-06-16


sequence_source: UniProtKB:P15374 direct REST lookup on 2026-06-16


enzyme_display_name: pyridoxal kinase

organism: Bacillus subtilis

substrate_name: Pyridoxal

sequence_source: UniProtKB reviewed accession P39610 / PDXK_BACSU, REST check 2026-06-16

enzyme: pyridoxal kinase

substrate: Pyridoxal


substrate_name: ATP; Pyridoxal

substrate: ATP; Pyridoxal


organism: Bombyx mori

substrate_name: pyridoxal

sequence_source: UniProtKB reviewed accession Q1PCB1 / PDXK_BOMMO, REST check 2026-06-16

substrate: pyridoxal


substrate_name: ATP

assay_conditions_summary: pH 5.5; 310.15 K; cofactor ATP

substrate: ATP


proof_lines: in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C


organism: Dictyostelium discoideum

sequence_source: UniProtKB reviewed accession Q55EK9 / PDXK_DICDI, REST check 2026-06-16


organism: Homo sapiens

sequence_source: UniProtKB reviewed accession O00764 / PDXK_HUMAN, REST check 2026-06-16


proof_lines: SABIO-RK modifier species: pyridoxal kinase(Enzyme) mutant D235A


proof_lines: SABIO-RK modifier species: pyridoxal kinase(Enzyme) mutant D235N


assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP


substrate_name: 3',5'-Cyclic AMP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation D812A applied after residue check and applied mutation signature D812A to reconstruct the assayed variant sequence.

substrate: 3',5'-Cyclic AMP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation G815A applied after residue check and applied mutation signature G815A to reconstruct the assayed variant sequence.


substrate_name: 3',5'-Cyclic AMP; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation Y807C applied after residue check and applied mutation signature Y807C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant Y807C

substrate: 3',5'-Cyclic AMP; H2O


substrate_name: H2O; 3',5'-Cyclic AMP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation C816S applied after residue check and applied mutation signature C816S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant C816S

substrate: H2O; 3',5'-Cyclic AMP


sequence_source: UniProtKB Q14432 canonical sequence with selected-batch mutation G815A applied after residue check

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant G815A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation K805A applied after residue check and applied mutation signature K805A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation H798A applied after residue check and applied mutation signature H798A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant H798A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation Y814A applied after residue check and applied mutation signature Y814A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q14432 canonical sequence with selected-batch mutation Y807C applied after residue check


sequence_source: UniProtKB Q9Y233 canonical sequence context only; selected row describes a tagged/truncated construct

mutation_type: truncation

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) wildtype PDE10A2 truncated (aa 449-789), His-tagged


sequence_source: UniProtKB Q9Y233 canonical sequence from direct REST lookup on 2026-06-16

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


organism: Mus musculus

sequence_source: UniProtKB Q8CA95 canonical sequence from direct REST lookup on 2026-06-16


sequence_source: UniProtKB Q9Z0X4 canonical sequence context only; selected row describes a tagged/truncated construct

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant N-term truncation (del346), HA-tagged (C-term)


sequence_source: UniProtKB Q9Z0X4 canonical sequence from direct REST lookup on 2026-06-16


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB P9WP65 canonical sequence from direct REST lookup on 2026-06-16

proof_lines: pH and temperature not specified in the publication


sequence_source: UniProtKB Q9QYJ6 canonical sequence from direct REST lookup on 2026-06-16


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: pyridoxamine

sequence_source: UniProt REST accession A0A0F7J8S0; checked 2026-06-16

substrate: pyridoxamine


organism: Staphylococcus aureus

sequence_variant_note: Resolved canonical sequence from UniProt REST accession A0A0H3JTP0; checked 2026-06-16 and applied mutation signature C214D to reconstruct the assayed variant sequence.

proof_lines: mutant C214D, pH not specified in the publication, temperature not specified in the publication


substrate_name: pyridoxine

sequence_source: UniProt REST accession A0A0H3JTP0; checked 2026-06-16

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

substrate: pyridoxine


sequence_variant_note: Resolved canonical sequence from UniProt REST accession A0A0H3JTP0; checked 2026-06-16 and applied mutation signature C110A to reconstruct the assayed variant sequence.

proof_lines: mutant C110A, pH not specified in the publication, temperature not specified in the publication


organism: Trypanosoma cruzi

sequence_source: UniProt REST accession Q4D946; checked 2026-06-16

proof_lines: in the presence of K+, at pH 7.0 and 30°C


organism: Arthrobacter sp.

sequence_source: UniProt REST accession M9W6G9; checked 2026-06-16


organism: Bos taurus


organism: Helicobacter pylori

sequence_source: UniProt REST accession O25683; checked 2026-06-16


substrate_name: Bis-4-nitrophenyl phosphate; H2O

substrate: Bis-4-nitrophenyl phosphate; H2O


substrate_name: Bis-4-nitrophenyl phosphate

substrate: Bis-4-nitrophenyl phosphate


column_label: Table 1: Kinetic parameters of native pure proteins directly isolated from Helicobacter pylori (PLoS ONE 2013, 8(6):e66605, page 5), enzyme block HP1042, body row 'cGMP'; column 'Km (mM)' = 0.82 ± 0.15; column 'Vmax (µmol ml^-1 min^-1)' = 5.13 ± 0.20; column 'kcat (min^-1)' = 957 ± 82; column 'kcat/Km (s^-1 mM^-1)' = 19.5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 957 under the column head kcat (min^-1); 1 min^-1 is 1/60 s^-1, so 957 / 60 = 15.95 s^(-1) exactly; the exported value is 15.95 s^(-1). Km: printed Table 1 cell 0.82 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.82 mM; the exported value is 0.82 mM. kcat/Km: printed Table 1 cell 19.5 under the column head kcat/Km (s^-1 mM^-1); the printed unit is the canonical unit, so no unit conversion applies and the printed efficiency is 19.5 s^(-1)*mM^(-1); the exported value 19.451219512195124 s^(-1)*mM^(-1) is the full-precision quotient 15.95 / 0.82 of the same two printed cells, and the printed cell is that quotient at the table's one-decimal precision.

raw_value_unit_evidence: Table 1, enzyme HP1042, substrate row 'cGMP': Km = 0.82 ± 0.15 mM; kcat = 957 ± 82 min^-1; printed kcat/Km = 19.5 s^-1 mM^-1; Vmax = 5.13 ± 0.20 µmol ml^-1 min^-1.

row_label: Table 1, enzyme HP1042, substrate row cGMP


sequence_source: UniProt REST accession Q9Y233; checked 2026-06-16


substrate_name: cAMP

substrate: cAMP


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q14432; checked 2026-06-16 and applied mutation signature K805A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant K805A


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q14432; checked 2026-06-16 and applied mutation signature Y814A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant Y814A


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q14432; checked 2026-06-16 and applied mutation signature H796A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant H796A


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed variant sequence from selected mutation signature and applied mutation signature D87H to reconstruct the assayed variant sequence.

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed H246Q sequence from selected mutation signature and applied mutation signature H246Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O00764 FASTA direct check

proof_lines: pH 7.3, 37°C recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed variant sequence from selected mutation signature and applied mutation signature H246Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O00764 FASTA; reconstructed variant sequence from selected mutation signature


sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed A243G sequence from selected mutation signature and applied mutation signature A243G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed V128I sequence from selected mutation signature and applied mutation signature V128I to reconstruct the assayed variant sequence.


substrate_name: ATP; Pyridoxine

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

assay_conditions_summary: pH 6.2; 310.15 K; buffer 70 mM potassium phosphate; cofactor ATP

proof_lines: in 70 mM potassium phosphate buffer, pH 6.2

source_databases_merged: sabio_rk brenda skid

substrate: ATP; Pyridoxine


organism: Leishmania donovani

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

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


proof_lines: recombinant wild-type enzyme, pH 7.2, 37°C


substrate_name: ginkgotoxin

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

substrate: ginkgotoxin


organism: Plasmodium vivax

sequence_source: UniProtKB A5K1Z8 FASTA direct check

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


sequence_source: UniProtKB A0A0F7J8S0 FASTA direct check

assay_conditions_summary: pH 6.6; 310.15 K; cofactor ATP

proof_lines:
with pyridoxal, pH 6.6, 37°C
pH 6.6, 37°C
with pyridoxamine, pH 8.5, 37°C


organism: porcine epidemic diarrhea virus

substrate_name: Dabcyl-FRLKGGAPIKGV-Edans

sequence_source: UniProtKB:A0A075ECV2 canonical sequence with D195-N196 deletion reconstructed from UniProt PDB 7F0U chain A/B=1686-1922 mapping

sequence_variant_note: Mutation signature N196del could not be applied safely because the resolved sequence does not match the expected reference residue(s).

mutation_type: deletion

substrate: Dabcyl-FRLKGGAPIKGV-Edans


substrate_name: Dabcyl-FKKKGGGDVKE-Edans

sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A075ECV2 canonical sequence with N138A reconstructed from UniProt PDB 7F0U chain A/B=1686-1922 mapping and applied mutation signature N138A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

substrate: Dabcyl-FKKKGGGDVKE-Edans


sequence_source: UniProtKB:A0A075ECV2 canonical sequence retrieved by direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A075ECV2 canonical sequence with E99A reconstructed from UniProt PDB 7F0U chain A/B=1686-1922 mapping and applied mutation signature E99A to reconstruct the assayed variant sequence.


organism: SARS coronavirus

substrate_name: Ubiquitin-AMC; H2O

substrate: Ubiquitin-AMC; H2O


organism: Schizosaccharomyces pombe

substrate_name: H2O; Arg-Leu-Arg-Gly-Gly-AMC

sequence_source: UniProtKB:O13979 canonical reviewed sequence

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

substrate: H2O; Arg-Leu-Arg-Gly-Gly-AMC


substrate_name: 3',5'-cyclic AMP

substrate: 3',5'-cyclic AMP


substrate_name: 3',5'-cyclic AMP (isoform 1)

substrate: 3',5'-cyclic AMP (isoform 1)


organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)


organism: Rattus norvegicus


substrate_name: 3',5'-cyclic AMP (at pH 7.5)

substrate: 3',5'-cyclic AMP (at pH 7.5)


organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

substrate_name: p-nitrophenyl-O-GlcNAc (pNP-O-GlcNAc) (at pH 7.4)


organism: Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)


organism: Homo sapiens

substrate_name: pNP-GlcNAc

substrate: pNP-GlcNAc


organism: Mus musculus


organism: Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516)

substrate_name: p-nitrophenyl-GlcNAc

substrate: p-nitrophenyl-GlcNAc


substrate_name: pNP-O-GlcNAc

substrate: pNP-O-GlcNAc


organism: Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)

substrate_name: Ub-AMC

substrate: Ub-AMC


substrate_name: cGMP

proof_lines:
stimulation with Mg2+ or Mn2+
two forms of phosphodiesterase
30 C, pH 8.0, PDE3A

substrate: cGMP


substrate_name: wild-type di-ubiquitin

proof_lines:
pH 8.0, 37 C
pH 8.0, 37 C, isozyme L2
pH 8.0, 37 C, isozyme H2

substrate: wild-type di-ubiquitin


proof_lines: below, pH 7.5, 25 C, inhibition kinectis


sequence_source: UniProtKB:Q9R0P9 direct accession check; UniProt references PMID 12913066

proof_lines: recombinant wild-type isozyme L1, pH 7.5, 25 C

proof_lines: pH 7.5, 25 C, recombinant wild-type isozyme L1


organism: Arabidopsis thaliana

substrate_name: ATP

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

substrate: ATP


organism: Bacillus subtilis (strain 168)

substrate_name: HMP

substrate: HMP


organism: Dictyostelium discoideum

substrate_name: pyridoxal (at 37 degrees Celsius)

substrate: pyridoxal (at 37 degrees Celsius)


organism: Spinacia oleracea

substrate_name: GDP

assay_conditions_summary: cofactor ADP

substrate: GDP


organism: Sus scrofa

substrate_name: ThDP

substrate: ThDP


organism: Bos taurus

substrate_name: Unknown

substrate: Unknown


organism: Drosophila melanogaster

substrate_name: 3',5'-cyclic GMP

substrate: 3',5'-cyclic GMP


substrate_name: cAMP

substrate: cAMP


substrate_name: 3',5'-cyclic AMP

substrate: 3',5'-cyclic AMP


organism: Dugbe virus (isolate ArD44313)


substrate_name: ubiquitin vinyl sulfone (in presence of WDR48)


substrate_name: ubiquitin-rhodamine

substrate: ubiquitin-rhodamine


organism: Turnip yellow mosaic virus


organism: Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651)

substrate_name: dihydrouracil

substrate: dihydrouracil


organism: Escherichia coli (strain K12)

substrate_name: guanine (at pH 8.5)

proof_lines: kcat is 112.0 sec(-1) with guanine as substrate. kcat is 150.1 sec(-1) with xanthine as substrate. kcat is 54.8 sec(-1) with hypoxanthine as substrate (at pH 8.5).

substrate: guanine (at pH 8.5)


organism: Rattus norvegicus

proof_lines: kcat is 35.6 min(-1) for the donor CMP-Neu5Ac (at pH 6.5 and 37 degrees Celsius). kcat is 40.3 min(-1) for the acceptor beta-Gal1,4-GlcNAc (at pH 6.5 and 37 degrees Celsius).


organism: Aedes aegypti

substrate_name: 3-hydroxykynurenine (at 50 degrees Celsius and pH 7.0)

assay_conditions_summary: pH 7

proof_lines: kcat is 2424 min(-1) for 3-hydroxykynurenine (at 50 degrees Celsius and pH 7) (PubMed:11880382). kcat is 1640 min(-1) for L-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate) (PubMed:11880382). kcat is 1200 min(-1) f


proof_lines: kcat is 117 sec(-1) for alanine (at 45 degrees Celsius, pH 7.5 and with glyoxylate as cosubstrate).


organism: Anopheles gambiae

proof_lines: kcat is 988.5 min(-1) for D,L-3-hydroxykynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate) (PubMed:16262702). kcat is 1077.2 min(-1) for D,L-kynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate)


substrate_name: alanine (with recombinant enzyme, in the presence of 20 mM glyoxylate)

proof_lines: kcat is 6.4 sec(-1) for L-serine. kcat is 2.86 sec(-1) for L-alanine.


proof_lines: kcat is 6800 min(-1) for glyoxylate (at 50 degrees Celsius, pH 7 and with alanine as cosubstrate) (PubMed:12220660). kcat is 7880 min(-1) for alanine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate) (PubMed:12220660).


organism: Bombyx mori

substrate_name: ATP (in the presence of 0.5 mM ZnCl(2), at pH 5.5 and 37 degrees Celsius)

assay_conditions_summary: pH 5.5; cofactor ATP

proof_lines: kcat is 1.23 sec(-1) for ATP. kcat is 1.35 sec(-1) for PL.


substrate_name: pyridoxal (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius)

proof_lines: kcat is 140 min(-1) for the phosphorylation of PL with MgATP. kcat is 120 min(-1) for the phosphorylation of PL with ZnATP. kcat is 20 min(-1) for the phosphorylation of PN with MgATP. kcat is 40 min(-1) for the phosphorylation of PM with M


organism: Homo sapiens

substrate_name: pyridoxal (in the presence of K(+))

proof_lines: KM is <10 uM for pyridoxal (in the presence of K(+)) (PubMed:17766369). KM is <25 uM for MgATP (in the presence of K(+)) (PubMed:17766369). kcat is 200 min(-1) for phosphorylase activity using PL as substrate in the presence of Na(+). kcat

substrate: pyridoxal (in the presence of K(+))


organism: Acanthamoeba polyphaga mimivirus

substrate_name: dGDP

proof_lines: KM values are below 10 uM for dCDP, dCTP and dUTP.

substrate: dGDP


organism: Schistosoma mansoni

substrate_name: GDP (at pH 7.6)

proof_lines: kcat is 0.68 sec(-1) with GDP as substrate.

substrate: GDP (at pH 7.6)


proof_lines: kcat is 10 min(-1) for cleavage after 'Arg-191' in F9 (in the presence of 5 mM CaCl(2), from initial velocities). kcat is 7.1 min(-1) for cleavage after 'Arg-226' in F9 cleaved at 'Arg-191' (in the presence of 5 mM CaCl(2), from initial vel


enzyme_display_name: ADP-specific glucose/glucosamine kinase

organism: Methanohalobium evestigatum

substrate_name: ADP

sequence_source: UniProtKB REST exact accession lookup: D7E8P3

assay_conditions_summary: pH 7.8; 313.15 K; cofactor ADP

enzyme: ADP-specific glucose/glucosamine kinase

substrate: ADP


proof_lines:
MgADP, pH 7.8, 40°C
pH 7.8, 40°C


organism: Methanosarcina mazei

substrate_name: D-glucose

sequence_source: UniProtKB REST exact accession lookup: Q8PZL9

substrate: D-glucose


proof_lines:
pH 7.8, 40°C
MgADP, pH 7.8, 40°C


organism: Mus musculus

substrate_name: D-Glucose; ADP

sequence_source: UniProtKB REST exact accession lookup: Q8VDL4

assay_conditions_summary: pH 7; 310.15 K; cofactor ADP

proof_lines: at 0.8 mM and an ADP:Mg2+ ratio of 1:1, pH 7.0, 37°C

substrate: D-Glucose; ADP


organism: Pyrococcus furiosus

substrate_name: ADP; D-Glucose

sequence_source: UniProtKB REST exact accession lookup: Q9V2Z6

proof_lines:
versus ADP
Raw SKiD Env: Temp=40°C, pH=7.8

substrate: ADP; D-Glucose


organism: Pyrococcus horikoshii

sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession lookup: O58328 and applied mutation signature F272A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ADP-specific glucokinase(Enzyme) mutant F272A N-terminal His6-tag


sequence_source: UniProtKB REST exact accession lookup: O58328

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ADP

proof_lines:
pH 7.4, 37°C
Raw SKiD Env: Temp=37°C, pH=7.4


organism: Thermococcus kodakarensis

substrate_name: D-glucosamine

sequence_source: UniProtKB REST exact accession lookup: Q5JE39

assay_conditions_summary: pH 7.5; 343.15 K; cofactor ADP

substrate: D-glucosamine


assay_conditions_summary: pH 7.5; 353.15 K; cofactor ADP


substrate_name: D-Glucosamine

substrate: D-Glucosamine


organism: Thermococcus litoralis

sequence_source: UniProtKB REST exact accession lookup: Q7M537


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession lookup: Q7M537 and applied mutation signature E279D to reconstruct the assayed variant sequence.


organism: Caldanaerobacter subterraneus subsp. tengcongensis

assay_conditions_summary: pH 8; 348.15 K; cofactor ADP


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


sequence_source: UniProtKB REST direct accession lookup Q9BRR6, accessed 2026-06-16


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB REST direct accession lookup Q58999, accessed 2026-06-16


organism: Methanococcoides burtonii

sequence_source: UniProtKB REST direct accession lookup Q12WB9, accessed 2026-06-16

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ADP


organism: Methanococcus maripaludis

sequence_source: UniProtKB REST direct accession lookup Q6LXQ3, accessed 2026-06-16

assay_conditions_summary: pH 6.5; 303.15 K; cofactor ADP

proof_lines: pH 6.5, 30°C, phosphopfructokinase activity

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


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


assay_conditions_summary: pH 7; 303.15 K; cofactor ADP


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


sequence_source: UniProtKB REST direct accession lookup D7E8P3, accessed 2026-06-16


enzyme_display_name: non-specific protein-tyrosine kinase

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: non-specific protein-tyrosine kinase

substrate: ATP


substrate_name: phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0)

assay_conditions_summary: pH 8; cofactor ADP


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


substrate_name: D-glucose (at 37 degrees Celsius)

substrate: D-glucose (at 37 degrees Celsius)


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


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: glucose

substrate: glucose


organism: Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)


organism: Rattus norvegicus

substrate_name: carnitine

substrate: carnitine


substrate_name: choline

substrate: choline


substrate_name: palmitoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: palmitoyl-CoA


substrate_name: CoASH

proof_lines: supplementation with R-alpha-lipoic acid

proof_lines: substrate hexanoylcarnitine, enzyme from liver homogenate

substrate: CoASH


organism: Saccharomyces cerevisiae

substrate_name: L-(-)-carnitine

substrate: L-(-)-carnitine


organism: Sus scrofa

substrate_name: (-)carnitine

substrate: (-)carnitine


organism: Drosophila melanogaster

substrate_name: UDPgalactose

substrate: UDPgalactose


organism: Gallus gallus


organism: Homo sapiens

substrate_name: UDP-galactose

assay_conditions_summary: pH 7.4; 310.15 K; buffer 100 mM sodium cacodylate

proof_lines: wild type enzyme, in 100 mM sodium cacodylate buffer (pH 7.4) containing 10 mM MnCl2, at 37°C

proof_lines: DELTA1-81, wild-type, pH and temperature not specified in the publication

proof_lines: wild type enzyme, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, temperature not specified in the publication

substrate: UDP-galactose


assay_conditions_summary: pH 7; buffer 100 mM cacodylate

proof_lines: DELTA1-81, mutant L206P, pH and temperature not specified in the publication

proof_lines: mutant enzyme L206P, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, temperature not specified in the publication


proof_lines: DELTA1-81, mutant R270C, pH and temperature not specified in the publication

proof_lines: mutant enzyme R270C, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, temperature not specified in the publication


proof_lines: DELTA1-81, mutant A186D, pH and temperature not specified in the publication

proof_lines: mutant enzyme A186D, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, temperature not specified in the publication


proof_lines: mutant L206A, pH and temperature not specified in the publication


assay_conditions_summary: pH 5; 298.15 K; buffer sodium acetate; cofactor ATP

proof_lines: recombinant enzyme, in sodium acetate buffer (25 mM, pH 5.0), 20 mM MnCl2, 50 mM KCl, at 25°C

proof_lines: pH 5.5, 37°C before preincubation with ATP

proof_lines: pH 5.5, 37°C after preincubation with ATP


organism: Mus musculus


organism: Enterococcus faecalis

substrate_name: xanthine

substrate: xanthine


organism: Lacticaseibacillus casei


organism: Leishmania donovani

substrate_name: hypoxanthine

substrate: hypoxanthine


assay_conditions_summary: pH 7.5; 298.15 K; buffer TM

proof_lines: wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine

proof_lines: wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine


substrate_name: guanine

proof_lines: mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine

proof_lines: mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine

substrate: guanine


proof_lines: mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine

proof_lines: mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine


proof_lines: mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine

proof_lines: mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine


proof_lines: mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine

proof_lines: mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine


organism: Plasmodium falciparum

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: unactivated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication

proof_lines: IMP-activated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


organism: Thermococcus litoralis

substrate_name: ADP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q7M537 direct REST/FASTA lookup plus selected source accession evidence and applied mutation signature E279Q to reconstruct the assayed variant sequence.

substrate: ADP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7M537 direct REST/FASTA lookup plus selected source accession evidence and applied mutation signature E279L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q7M537 direct REST/FASTA lookup plus selected source accession evidence


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7M537 direct REST/FASTA lookup plus selected source accession evidence and applied mutation signature E308Q to reconstruct the assayed variant sequence.


substrate_name: D-glucose

substrate: D-glucose


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


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 7.6; 323.15 K; cofactor ADP

proof_lines: 50°C, pH not specified in the publication


organism: Pyrococcus furiosus

assay_conditions_summary: pH 7.8; 313.15 K; cofactor ADP

proof_lines: in the presence of 1 mM Mg2+, pH 7.8, 40°C

proof_lines: in the presence of 1 mM Mn2+, pH 7.8, 40°C

proof_lines: in the presence of 1 mM Co2+, pH 7.8, 40°C


organism: Pyrococcus horikoshii

assay_conditions_summary: pH 6.5; 323.15 K; cofactor ADP

proof_lines: in the presence of 1 mM Mn2+, pH 6.5, 50°C

proof_lines: in the presence of 1 mM Mg2+, pH 6.5, 50°C

proof_lines: in the presence of 1 mM Co2+, pH 6.5, 50°C


organism: Thermococcus kodakarensis

substrate_name: D-glucosamine

substrate: D-glucosamine


organism: uncultured bacterium


proof_lines:
pH 7.8, 60°C
MgADP, pH 7.8, 60°C


organism: Bacillus subtilis


organism: Escherichia coli

substrate_name: pyridoxamine

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

proof_lines: kinase 1 with ZnATP2- as substrate, pH 7.3, 37°C

proof_lines: kinase 1 with MgATP2- as substrate, pH 7.3, 37°C

proof_lines: kinase 1 with pyridoxal as substrate, pH 7.3, 37°C

substrate: pyridoxamine


substrate_name: pyridoxal

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

proof_lines: in the presence of Zn2+, at pH 6.5 and 37°C

proof_lines: in the presence of K+, at pH 7.0 and 30°C

substrate: pyridoxal


organism: Ovis aries

substrate_name: ATP

assay_conditions_summary: pH 5.8; 310.15 K; cofactor ATP

proof_lines: pH 5.8, 37°C, with MnATP2- as the second substrate

substrate: ATP


assay_conditions_summary: pH 6.5; 303.15 K; cofactor ATP


organism: Photobacterium sp.

proof_lines: pH 5.0, 37°C, cosubstrate: CMP-9-benzamido-Neu5Ac

proof_lines: pH 5.0, 37°C, cosubstrate: CMP-9-phenylacetamido-Neu5Ac


organism: Photobacterium sp. JT-ISH-224

substrate_name: CMP-N-acetyl-beta-neuraminate

substrate: CMP-N-acetyl-beta-neuraminate


organism: Rattus norvegicus

substrate_name: CMP-N-acetylneuraminate

proof_lines:
with asialo-alpha1-acid glycoprotein
pH 5.0, 37°C
pH 6.5, 37°C

substrate: CMP-N-acetylneuraminate


organism: Aedes aegypti

substrate_name: glyoxylate

proof_lines: pH 7.0, 50°C, glyoxylate as amino acceptor

substrate: glyoxylate


organism: Arabidopsis thaliana

proof_lines:
cosubstrate L-alanine, pH 7.5, 25°C
cosubstrate L-glutamate, pH 7.5, 25°C
pH 7.5, 25°C


organism: Canis familiaris

substrate_name: Glyoxylate; L-Alanine

substrate: Glyoxylate; L-Alanine


organism: Homo sapiens

substrate_name: L-alanine

proof_lines: G82E, pH not specified in the publication, temperature not specified in the publication

substrate: L-alanine


proof_lines: major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication

proof_lines: pH 8.0, 37°C, recombinant AGT-His, L-alanine as amino donor


proof_lines: P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication


proof_lines: P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication


proof_lines: F152I, pH not specified in the publication, temperature not specified in the publication


proof_lines: P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication


proof_lines: G41V, pH not specified in the publication, temperature not specified in the publication


proof_lines: G41R, pH not specified in the publication, temperature not specified in the publication


organism: Spinacia oleracea

proof_lines: pH 7.0, 27°C, glyoxylate as amino acceptor


organism: Thermococcus litoralis


substrate_name: asialo-transferrin

proof_lines: expressed as concentration of terminal galactosyl residues

substrate: asialo-transferrin


organism: Mus musculus


organism: Photobacterium damselae

substrate_name: 4-methylumbelliferyl beta-D-lactoside

proof_lines: pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N)

substrate: 4-methylumbelliferyl beta-D-lactoside


proof_lines: pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N)

proof_lines: alpha2,6-trans-sialidase activity of DELTA15Pd2,6ST


substrate_name: lactose

proof_lines: mutant enzyme I411T/L433T, at pH 8.0 and 22°C

substrate: lactose


proof_lines: mutant enzyme I411T/L433S, at pH 8.0 and 22°C


organism: Photobacterium leiognathi

mutation_signature: 6-sialyltransferase activity of the truncated recombinant enzyme alpha2 / 6-sialyltransferase activity of the truncated recombinant enzyme

proof_lines: alpha2,6-sialyltransferase activity of the truncated recombinant enzyme


organism: Plasmodium falciparum

proof_lines: unactivated wild type enzyme, at pH 7.4, temperature not specified in the publication

proof_lines: IMP-activated wild type enzyme, at pH 7.4, temperature not specified in the publication


proof_lines: IMP-activated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication

proof_lines: unactivated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication


proof_lines: IMP-activated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication

proof_lines: unactivated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication


organism: Toxoplasma gondii

substrate_name: xanthine

substrate: xanthine


organism: Bombyx mori


organism: Bos taurus

substrate_name: asialo-thyroglobulin glycopeptides

substrate: asialo-thyroglobulin glycopeptides


organism: Capra hircus

proof_lines:
with N-acetyllactosamine
with lactose


organism: Cavia porcellus


organism: Drosophila sp. (in: flies)

proof_lines: non-reducing terminus of asialofetuin glycans


organism: Helicobacter cetorum


organism: Penicillium digitatum

substrate_name: carboxymethyl cellulose

substrate: carboxymethyl cellulose


organism: Phanerodontia chrysosporium

substrate_name: bacterial cellulose

proof_lines: in 50 mM sodium acetate, pH 5.0, at 30°C

substrate: bacterial cellulose


organism: Rasamsonia emersonii


organism: Thermoascus aurantiacus


organism: Trametes versicolor

substrate_name: p-nitrophenyl beta-D-cellobioside

substrate: p-nitrophenyl beta-D-cellobioside


organism: Trichoderma harzianum

substrate_name: 2-chloro-4-nitrophenyl beta-D-lactoside

proof_lines: 50 mM sodium acetate buffer, pH 5.0, at 50°C

substrate: 2-chloro-4-nitrophenyl beta-D-lactoside


organism: Trichoderma reesei

assay_conditions_summary: pH 5; 303.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium acetate with 2 mM CaCl2 and pH 5.0 at 25°C


substrate_name: 4-nitrophenyl beta-lactoside

proof_lines:
pH 5.7, 37°C, wild-type enzyme
wild type enzyme, at pH 5.0 and 27°C

substrate: 4-nitrophenyl beta-lactoside


substrate_name: 4-methylumbelliferyl beta-lactoside

substrate: 4-methylumbelliferyl beta-lactoside


substrate_name: 2,4-dinitrophenyl beta-lactoside

substrate: 2,4-dinitrophenyl beta-lactoside


organism: Tetrahymena pyriformis

substrate_name: ATP

substrate: ATP


organism: Acanthamoeba polyphaga Mimivirus

substrate_name: dTDP

assay_conditions_summary: pH 7.5; cofactor ATP

substrate: dTDP


organism: Avena sativa

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 8.0
cosubstrate dTDP, 30°C, pH 8.0
cosubstrate ATP, 30°C, pH 8.0


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C
cosubstrate ATP, pH 7.5, 37°C


organism: Halomonas sp.

substrate_name: GTP

assay_conditions_summary: pH 8

proof_lines:
pH 8.0
pH 8.0, presence of 0.2 M NaCl
pH 8.0, presence of 0.5 M NaCl

substrate: GTP


organism: Lathyrus oleraceus

assay_conditions_summary: cofactor ATP


organism: Plasmodium falciparum


organism: Pseudomonas sp.

proof_lines:
pH 8.0
pH 8.0, presence of 0.5 M NaCl
pH 8.0, presence of 0.2 M NaCl


organism: Rattus norvegicus

substrate_name: UDP

proof_lines: cosubstrate ATP, membrane-associated kinase

substrate: UDP


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines:
cosubstrate ATP, 37°C, pH 7.6
37°C, pH 7.6
cosubstrate ATP


organism: Saccharum officinarum


organism: Spinacia oleracea

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: cosubstrate GDP, NDP-kinase II, 37°C, pH 7.4

proof_lines: cosubstrate ATP, NDP-kinase I and II, 37°C, pH 7.4


enzyme_display_name: oleoyl-[acyl-carrier-protein] hydrolase

organism: Helianthus annuus

substrate_name: palmitoleoyl-[acyl-carrier protein]

enzyme: oleoyl-[acyl-carrier-protein] hydrolase

substrate: palmitoleoyl-[acyl-carrier protein]


organism: Mangifera indica

substrate_name: oleoyl-[acyl-carrier protein]

substrate: oleoyl-[acyl-carrier protein]


organism: Umbellularia californica

substrate_name: decanoyl-[acyl-carrier protein]

substrate: decanoyl-[acyl-carrier protein]


organism: Anabaena sp.

proof_lines: pH and temperature not specified in the publication


organism: Corynebacterium glutamicum


organism: Dictyostelium discoideum

substrate_name: cAMP

proof_lines:
isoform PDE7, 22°C, pH 7.0
isoform PDE3, 22°C, pH 7.0
isoform PDE2, 22°C, pH 7.0

substrate: cAMP


organism: Drosophila melanogaster


organism: Homo sapiens

proof_lines: catalytic domain of PDE2A (PDE2A residues 578-919), enzyme expressed in Escherichia coli


organism: Mus musculus

proof_lines:
soluble enzyme
particulate enzyme


organism: Mycobacterium tuberculosis


organism: Myxococcus xanthus

assay_conditions_summary: pH 8; 313.15 K; cofactor ATP

proof_lines: PdeB, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C

proof_lines: PdeA, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C

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


organism: Pseudomonas aeruginosa

sequence_source: RCSB:5B6A; UniProt:Q9HT57

sequence_variant_note: Resolved canonical sequence from RCSB:5B6A; UniProt:Q9HT57 and applied mutation signature C124A to reconstruct the assayed variant sequence.


substrate_name: pyridoxal

substrate: pyridoxal


organism: Sus scrofa

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


organism: Trypanosoma brucei

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: recombinant enzyme, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C


organism: Dictyostelium sp.

substrate_name: dCMP

substrate: dCMP


substrate_name: UMP

substrate: UMP


organism: Escherichia coli

substrate_name: CMP; ATP

substrate: CMP; ATP


proof_lines:
pH 7.4, 37°C, His-tagged UMP-CMP kinase
pH 7.4, 37°C, GST fusion UMP-CMP kinase
pH 7.4, 37°C, GST fusion UMP/CMP kinase


organism: Rattus norvegicus

assay_conditions_summary: pH 7.1; 310.15 K; cofactor ATP

proof_lines:
reaction with dATP, liver enzyme
reaction with ATP, liver enzyme
pH 7.1, 37°C


organism: Saccharomyces cerevisiae


proof_lines:
pH 7.0, 25°C, AUA chimeric enzyme
pH 7.0, 25°C, UMP-CMP kinase
pH 7.0, 25°C, UAU chimeric enzyme


substrate_name: 3',5'-Cyclic AMP; H2O

substrate: 3',5'-Cyclic AMP; H2O


organism: Sinorhizobium fredii


organism: Trypanosoma cruzi


organism: Xenopus laevis


sequence_source: UniProtKB reviewed accession O60502 (direct EC 3.2.1.169 + Homo sapiens lookup)


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O60502 with D174A reconstructed from selected source note and PMID 16533067 and applied mutation signature D174A to reconstruct the assayed variant sequence.

proof_lines:
D174A mutant (pH 7.4)
D174A mutant (pH 5.0)


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O60502 with D175A reconstructed from selected source note and PMID 16533067 and applied mutation signature D175A to reconstruct the assayed variant sequence.


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

proof_lines:
OGA-FL
OGA-NV
for OGA-FL


proof_lines: compared to the control, pancreas of rats treated with saline

proof_lines: compared to the control, muscles of rats treated with saline


organism: Acetivibrio thermocellus

substrate_name: Avicel

substrate: Avicel


enzyme_display_name: glutamyl aminopeptidase

organism: Tetragenococcus halophilus

substrate_name: Glu-p-nitroanilide

enzyme: glutamyl aminopeptidase

substrate: Glu-p-nitroanilide


substrate_name: Unknown

substrate: Unknown


organism: Oryctolagus cuniculus

proof_lines:
at 0.0006 mM ubiquitin, pH 7.8, 25°C
in absence of ubiquitin, pH 7.8, 25°C


organism: Oryza sativa

proof_lines: pH 8.0, temperature not specified in the publication, ubiquitin C-terminal hydrolase OsUCH3


organism: synthetic construct

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

proof_lines:
with UCH-L3
with UCH-L1


organism: Bos taurus


organism: Homo sapiens

substrate_name: Factor X

proof_lines: mutant enzyme E154A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles

substrate: Factor X


proof_lines: mutant enzyme L192A or E154A, tissue factor/phosphatidylcholine vesicles


proof_lines: mutant enzyme L144A, tissue factor/phosphatidylcholine vesicles

proof_lines: mutant enzyme L144A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles


proof_lines: mutant enzyme K192A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles

proof_lines: mutant enzyme K192A, tissue factor/phosphatidylcholine vesicles


proof_lines: mutant enzyme L192A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles


proof_lines: pH 8.0, 37°C, mutant enzyme M156Q, addition of tissue factor


proof_lines: wild-type enzyme VIIa, tissue factor/phosphatidylcholine-phosphatidylserine vesicles


substrate_name: D-Ile-Pro-Arg-p-nitroanilide

proof_lines: pH 8.0, 30°C, mutant enzyme DELTA360-329, without tissue factor

proof_lines: pH 8.0, 30°C, mutant enzyme DELTA360-329, activated by tissue factor

substrate: D-Ile-Pro-Arg-p-nitroanilide


proof_lines: mutant enzyme L305V, in absence of tissue factor


proof_lines: mutant enzyme L305V/M306D/D309S, in absence of tissue factor


proof_lines: 37°C, mutant enzyme N100A/H101A/Y179A/F256A


organism: Gallus gallus

substrate_name: Glu-beta-naphthylamide

substrate: Glu-beta-naphthylamide


proof_lines: recombinant enzyme, pH 7.5, 37°C, in absence of Ca2+

proof_lines: recombinant enzyme, pH 7.5, 37°C, in presence of 1 mM Ca2+


proof_lines: mutant D221N, in the presence of 1.0 mM CaCl2


proof_lines: mutant D221E, in the presence of 1.0 mM CaCl2


proof_lines: mutant D221Q, in the presence of 1.0 mM CaCl2


proof_lines: mutant D221, in the presence of 1 mM CaCl2


substrate_name: angiotensin II

proof_lines: wild-type, in the presence of 1.0 mM CaCl2

proof_lines: wild-type enzyme, in the absence of CaCl2

substrate: angiotensin II


proof_lines: mutant D221A, in the presence of 1.0 mM CaCl2


organism: Lactococcus lactis

substrate_name: Asp-Ala

substrate: Asp-Ala


organism: Lactococcus lactis ssp. lactis


organism: Mus musculus


organism: Streptomyces coelicolor

substrate_name: ATP

sequence_source: UniProtKB P50589 from direct EC 2.7.4.6 + Streptomyces coelicolor lookup

assay_conditions_summary: 300.15 K; cofactor ATP

substrate: ATP


organism: Thermus thermophilus

substrate_name: GDP

substrate: GDP


organism: white spot syndrome virus

substrate_name: dTDP

proof_lines: pH 7.5, temperature not specified in the publication

substrate: dTDP


organism: Brassica rapa subsp. oleifera

substrate_name: oleoyl-[acyl-carrier protein]

substrate: oleoyl-[acyl-carrier protein]


organism: Camelina sativa

substrate_name: stearoyl-[acyl-carrier protein]

substrate: stearoyl-[acyl-carrier protein]


organism: Cuphea lanceolata

proof_lines:
medium-chain acyl-ACP thioesterase
oleoyl-ACP thioesterase


organism: Diploknema butyracea

substrate_name: palmitoyl-[acyl-carrier protein]

substrate: palmitoyl-[acyl-carrier protein]


organism: Helianthus annuus

proof_lines: pH 8.0, 22°C, recombinant His-tagged enzyme

proof_lines: isoform FatA, palmitoyl-[acyl-carrier protein] from Escherichia coli, at pH 8.0, temperature not specified in the publication

proof_lines: isoform FatB, palmitoyl-[acyl-carrier protein] from Escherichia coli, at pH 8.0, temperature not specified in the publication


substrate_name: palmitoleoyl-[acyl-carrier protein]

substrate: palmitoleoyl-[acyl-carrier protein]


proof_lines: mutant enzyme C164V/V299C FVIIa, in the presence of tissue factor, pH 7.4


proof_lines: mutant enzyme L280I/V299M-FVIIa, in the presence of tissue factor, pH 7.4


proof_lines: mutant enzyme V299M-FVIIa, in the presence of tissue factor, pH 7.4


organism: Rattus norvegicus


substrate_name: factor IX

proof_lines: in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C

substrate: factor IX


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

proof_lines: wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: kcat less than 0.2 s-1, mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


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

proof_lines: kcat is 27.23 min(-1) for lipopolysaccharide kinase activity.


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: ADP

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 248 sec(-1) with glucose as substrate. kcat is 120 sec(-1) with glucosamine as substrate. kcat is 210 sec(-1) with ADP as substrate.

substrate: ADP


organism: Helicobacter pylori (strain ATCC 700392 / 26695)

substrate_name: cAMP

proof_lines: kcat is 2008 min(-1) and 957 min(-1) with cAMP and cGMP as substrate, respectively.

substrate: cAMP


organism: Homo sapiens

substrate_name: 3',5'-cyclic GMP

proof_lines: kcat is 0.6 sec(-1) with 3',5'-cyclic GMP as substrate (PubMed:15938621). kcat is 0.12 sec(-1) with 3',5'-cyclic AMP as substrate (PubMed:15938621).

substrate: 3',5'-cyclic GMP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 2.8 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.55 sec(-1) with pNPP as substrate. kcat is 12.4 sec(-1) with bis(pNPP) as substrate.


substrate_name: linear diubiquitin

proof_lines: kcat is 6.3 sec(-1) with linear diubiquitin as substrate.

substrate: linear diubiquitin


substrate_name: Arg-Leu-Arg-Gly-Gly-AMC

proof_lines: kcat is 4.9 sec(-1) with Arg-Leu-Arg-Gly-Gly-AMC as substrate (PubMed:29476094). kcat is 0.084 sec(-1) with Ub-Rhodamine as substrate (PubMed:29576528).

substrate: Arg-Leu-Arg-Gly-Gly-AMC


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: ubiquitin-AMC

proof_lines: kcat is 3.2 sec(-1) with ubiquitin-AMC as substrate.

substrate: ubiquitin-AMC


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 0.17 sec(-1) with ubiquitin-AMC as substrate.


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

proof_lines: kcat is 7.2 sec(-1) with Arg-Leu-Arg-Gly-Gly-AMC as substrate.


organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

proof_lines: The kinetic parameters are studied for the 3C-like proteinase domain.

substrate: peptide TSAVLQSGFRK-NH(2)


substrate_name: Factor X

substrate: Factor X


proof_lines: pH 6.5, MES buffer, without tissue factor

proof_lines: in 50 mM HEPES, pH 7.4, with 0.1 M NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, and 0.01% Tween 80, at 37°C


proof_lines: pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q


proof_lines: pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/L305V


proof_lines: pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/K337A


substrate_name: spectrozyme fVIIa

substrate: spectrozyme fVIIa


proof_lines: pH 8.0, mutant enzyme V21N/E154I/M156Q, with addition of tissue factor

proof_lines: pH 8.0, mutant enzyme V21N/E154I/M156Q, without tissue factor

proof_lines: pH 8.0, mutant enzyme V21N/E154I/M156Q, chromozym tPA as substrate without addition of tissue factor


proof_lines:
mutant FVIIaVEAY
mutant FVIIaIIa-sTF
mutant FVIIaVEAY-sTF


enzyme_display_name: chymase

proof_lines:
in presence of heparin proteoglycan
in absence of heparin
pH 7.5, 37°C

enzyme: chymase


enzyme_display_name: tryptase

organism: Bos taurus

enzyme: tryptase


substrate_name: N-p-tosyl-Gly-Pro-Arg-p-nitroanilide

substrate: N-p-tosyl-Gly-Pro-Arg-p-nitroanilide


substrate_name: Bz-Arg-p-nitroanilide

proof_lines:
pH 7.6, 20°C, isoform L1
pH 6.0, 25°C, 200 ng protamine
pH 7.6, 20°C, isoform L2

substrate: Bz-Arg-p-nitroanilide


organism: Mus musculus

substrate_name: N-p-tosyl-Gly-Pro-Lys-p-nitroanilide

proof_lines:
pH 6.0, 25°C, 1200 ng polybrene
pH 6.0, 25°C, 1000 ng polybrene
pH 6.0, 25°C, 800 ng polybrene

substrate: N-p-tosyl-Gly-Pro-Lys-p-nitroanilide


substrate_name: bovine prothrombin

substrate: bovine prothrombin


organism: Bubalus bubalis

substrate_name: L-Leu-beta-naphthylamide

substrate: L-Leu-beta-naphthylamide


organism: Capra hircus

substrate_name: Unknown

assay_conditions_summary: pH 7; 310.15 K; buffer 0.1 M acetate

proof_lines:
pH 7, 37°C
at pH 7.0 and 37°C
pH 5, 37°C

substrate: Unknown


organism: Cyprinus carpio


proof_lines: mutant T11_E18del-cathepsin H, pH 6.8, 30°C

proof_lines: pH 6.5, 25°C, mutant lacking the mini chain


enzyme_display_name: nicotinamidase

organism: Arabidopsis thaliana

substrate_name: nicotinamide

enzyme: nicotinamidase

substrate: nicotinamide


organism: Aspergillus niger


organism: Borreliella burgdorferi

assay_conditions_summary: pH 7.3; 298.15 K; buffer 100 mM phosphate

proof_lines: wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C


proof_lines: in 100 mM phosphate buffer, pH 7.3 at 25°C


organism: Caenorhabditis elegans

proof_lines: wild type enzyme isoform PNC2, in 100 mM phosphate buffer, pH 7.3 at 25°C

proof_lines: wild type enzyme isoform PNC1, in 100 mM phosphate buffer, pH 7.3 at 25°C


proof_lines: isoform PNC1, in 100 mM phosphate buffer, pH 7.3 at 25°C

proof_lines: isoform PNC2, in 100 mM phosphate buffer, pH 7.3 at 25°C


organism: Escherichia coli


organism: Flavobacterium peregrinum


organism: Micrococcus luteus


organism: Mycobacterium tuberculosis

proof_lines: Ki about 0.1 mM, wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C


proof_lines: mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C


organism: Plasmodium falciparum


assay_conditions_summary: pH 7.5; 310.15 K; buffer 100 mM phosphate


organism: Pseudomonas sp.


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


assay_conditions_summary: pH 7.3; 298.15 K; buffer notes


organism: Streptococcus pneumoniae


assay_conditions_summary: pH 7.3; 298.15 K; buffer notes but no substrate


organism: unidentified

substrate_name: ethylnicotinate

proof_lines: pH 7.3, temperature not specified in the publication, substrate: pyrazinamide

substrate: ethylnicotinate


enzyme_display_name: glutathionylspermidine amidase

organism: Crithidia fasciculata

substrate_name: glutathionylspermidine

assay_conditions_summary: pH 7.3; cofactor ATP

proof_lines:
pH 7.3, amidase activity
pH 7.3, synthetase activity

enzyme: glutathionylspermidine amidase

substrate: glutathionylspermidine


organism: Homo sapiens

proof_lines:
pH 6.0, enzyme from normal tissue
pH 6.0, enzyme from meningioma
pH 6.8, 22°C


organism: Oryctolagus cuniculus


organism: Sus scrofa

proof_lines:
pH 6.5, 25°C, native enzyme
similar value


enzyme_display_name: cathepsin K

enzyme: cathepsin K


assay_conditions_summary: pH 7.4; 298.15 K; buffer 100 mM sodium acetate

proof_lines: enzyme in the presence of 300 mM NaCl, in 50 mM HEPES, pH 7.4, containing 1 mM EDTA and 2.5 mM dithiothreitol, at 25°C

proof_lines: enzyme in the absence of NaCl, in 50 mM HEPES, pH 7.4, containing 1 mM EDTA and 2.5 mM dithiothreitol, at 25°C


proof_lines: tert-butyloxycarbonyl-Ala-Gly-Pro- Arg 4-methylcoumarin 7-amide


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: cruzipain

organism: Trypanosoma congolense

enzyme: cruzipain


organism: Trypanosoma cruzi

proof_lines: at pH 6.5 the propeptide of cruzipain inactivates cruzipain competitively


organism: Geobacillus stearothermophilus

substrate_name: DL-hydroxyphenylhydantoin

substrate: DL-hydroxyphenylhydantoin


substrate_name: dihydrouracil

substrate: dihydrouracil


organism: Geobacillus thermocatenulatus

substrate_name: p-hydroxyphenylhydantoin

substrate: p-hydroxyphenylhydantoin


organism: Niallia circulans

substrate_name: allantoin

substrate: allantoin


organism: Pseudomonas fluorescens


organism: Pseudomonas putida


substrate_name: H2O; 5,6-Dihydrouracil

substrate: H2O; 5,6-Dihydrouracil


organism: Sinorhizobium meliloti


organism: Vigna angularis


enzyme_display_name: arginine deiminase

organism: Aspergillus fumigatus

substrate_name: L-lysine

proof_lines: pH 7.0, 45°C, enzyme covalently immobilized on dextran

enzyme: arginine deiminase

substrate: L-lysine


organism: Aspergillus nidulans

substrate_name: L-arginine

substrate: L-arginine


organism: Bacillus cereus


organism: Burkholderia mallei

proof_lines:
pH 5.6, 25°C
at pH 5.6 and 25°C


organism: Escherichia coli

proof_lines:
pH 6.0, 25°C
at pH 6.0 and 25°C


organism: Giardia duodenalis

substrate_name: L-canavanine

substrate: L-canavanine


organism: Halobacterium salinarum


organism: Lactococcus lactis subsp. lactis


organism: Lentilactobacillus buchneri

assay_conditions_summary: pH 6


organism: Metamycoplasma arthritidis

substrate_name: L-Arg

proof_lines:
ammonium assay at 25°C
at pH 7.2, 25°C
ammonium assay at 37°C

substrate: L-Arg


organism: Metamycoplasma hominis

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


organism: Porphyromonas gingivalis

substrate_name: L-Pro-L-Phe-L-Arg

proof_lines: in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C

substrate: L-Pro-L-Phe-L-Arg


organism: Pseudomonas aeruginosa


organism: Agrobacterium sp.

substrate_name: hydantoin

substrate: hydantoin


organism: Agrobacterium tumefaciens

proof_lines:
at 25°C
at 40°C
at 20°C


organism: Blastobacter sp.

substrate_name: H2O; Hydantoin

substrate: H2O; Hydantoin


organism: Bos taurus

substrate_name: Hydrothymine

substrate: Hydrothymine


organism: Burkholderia cepacia

substrate_name: D,L-benzylhydantoin

proof_lines:
free enzyme, at pH 8.5 and 45°C
immobilized enzyme, at pH 8.5 and 45°C

substrate: D,L-benzylhydantoin


organism: Crystallibacter crystallopoietes

substrate_name: phenylhydantoin

substrate: phenylhydantoin


organism: Geobacillus stearothermophilus


substrate_name: Nomega-methyl-L-arginine

substrate: Nomega-methyl-L-arginine


organism: Pseudomonas plecoglossicida

assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.5 M phosphate

proof_lines: wild type enzyme, in 0.5 M phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme K5T/D44E/H404R, in 0.5 M phosphate buffer, pH 7.4, at 37°C


assay_conditions_summary: pH 7.4; 310.15 K; buffer phosphate

proof_lines: mutant enzyme H404R, in 0.5 M phosphate buffer, pH 7.4, at 37°C


proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R299K


proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R319K


proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R338K


proof_lines: pH 7.4, 55°C, M31 mutant enzyme R299K/R382K

proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R299K/R382K


proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R382K


proof_lines: pH 7.4, 55°C, PEGylated variant M31 (parent)

proof_lines: pH 7.4, 55°C, variant M31 (parent enzyme)


organism: Pseudomonas putida


organism: Streptococcus pyogenes

proof_lines: pH and temperature not specified in the publication


organism: Trichomonas vaginalis

proof_lines:
strain MR-5
strain MR-100
at pH 6.0 and 37°C


organism: Tritrichomonas foetus


enzyme_display_name: (R)-2-methylmalate dehydratase

organism: Pseudomonas sp.

enzyme: (R)-2-methylmalate dehydratase


enzyme_display_name: coagulation factor XIa

organism: Homo sapiens

proof_lines: mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C

enzyme: coagulation factor XIa


proof_lines: mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


substrate_name: factor IX

proof_lines: kcat less than 0.2 s-1, mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C

substrate: factor IX


proof_lines: kcat less than 0.2 s-1, mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: kcat less than 0.2 s-1, mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


organism: Canis lupus familiaris


proof_lines: in the presence of heparin, at pH 7.4 and 37°C

proof_lines: in the absence of heparin, at pH 7.4 and 37°C


organism: Mesocricetus auratus

substrate_name: angiotensin I

substrate: angiotensin I


organism: Mus musculus

proof_lines:
enzyme form 1A
enzyme form 1E
enzyme form 1B


enzyme_display_name: chitosanase

organism: Streptomyces sp. N174

substrate_name: chitosan

sequence_source: UniProtKB P33665 canonical precursor with mature-chain mutation reconstruction from PMID 19143844

sequence_variant_note: Mutation signature T45S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant T45S, assayed as the amount of D-glucosamine released from chitosan

enzyme: chitosanase

substrate: chitosan


sequence_variant_note: Resolved canonical sequence from UniProtKB P33665 canonical precursor with mature-chain mutation reconstruction from PMID 19143844 and applied mutation signature D40G/T45D with inferred residue-numbering offset +40 to reconstruct the assayed variant sequence.

proof_lines: mutant D40G/T45D, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature T45E could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant T45E, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Resolved canonical sequence from UniProtKB P33665 canonical precursor with mature-chain mutation reconstruction from PMID 19143844 and applied mutation signature E36Q/D40G with inferred residue-numbering offset +40 to reconstruct the assayed variant sequence.

proof_lines: mutant E36Q/D40G, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Resolved canonical sequence from UniProtKB P33665 canonical precursor with mature-chain mutation reconstruction from PMID 19143844 and applied mutation signature E36A/D40G with inferred residue-numbering offset +40 to reconstruct the assayed variant sequence.

proof_lines: mutant E36A/D40G, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature E36D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E36D, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature D40G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant D40G, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature E36A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E36A, assayed as the amount of D-glucosamine released from chitosan


organism: Bacillus subtilis


organism: Gynuella sunshinyii

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


sequence_variant_note: Mutation signature L117D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature N21W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -8, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature D236A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E206Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E149Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: uracil-DNA glycosylase

organism: Thermus thermophilus

substrate_name: double stranded DNA containing G-U mismatch

sequence_source: UniProtKB Q5SKC5 canonical protein sequence from direct accession lookup

enzyme: uracil-DNA glycosylase


substrate_name: DNA; H2O

sequence_source: UniProtKB Q5SKC5 canonical sequence used only as mutation-position context; row-specific variant sequence unresolved

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

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant E41Q-G42D C-terminal His6-tagged

proof_lines: mutant enzyme E41Q/G42D, at pH 7.6 and 60°C

substrate: DNA; H2O


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant E41Q C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant E47A C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant H155S C-terminal His6-tagged


substrate_name: H2O; DNA

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant E41A-G42D C-terminal His6-tagged

substrate: H2O; DNA


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant F54A C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant N89A C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant N80A C-terminal His6-tagged


organism: Vibrio cholerae

substrate_name: dUMP DNA

sequence_source: UniProtKB Q9KPK8 canonical sequence used only as mutation-position context; row-specific variant sequence unresolved

substrate: dUMP DNA


sequence_source: UniProtKB Q9KPK8 canonical protein sequence from direct accession lookup


enzyme_display_name: low-specificity L-threonine aldolase

organism: Aphanothece halophytica

substrate_name: L-erythro-phenylserine

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

enzyme: low-specificity L-threonine aldolase

substrate: L-erythro-phenylserine


organism: Arabidopsis thaliana

substrate_name: L-Threonine

sequence_source: UniProtKB Q8RXU4 canonical protein sequence from direct accession lookup

substrate: L-Threonine


sequence_source: UniProtKB Q9FPH3 canonical protein sequence from direct accession lookup


organism: Escherichia coli

sequence_source: UniProtKB:P12295 direct accession lookup


substrate_name: 5-hydroxymethyluracil-mismatched double-stranded DNA with U-G mismatch


substrate_name: uracil-mismatched double-stranded DNA with U-G mismatch

sequence_source: UniProtKB:Q53HV7 direct accession lookup


sequence_source: UniProtKB:P13051 direct accession lookup for canonical context only

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant H268N


sequence_source: UniProtKB:P13051 direct accession lookup

unit: Mswedgeone


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13051 direct accession lookup plus direct mutation reconstruction and applied mutation signature D145N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant D145N


substrate_name: uracil-containing calf thymus DNA

proof_lines:
mutant enzyme D183G, at pH 7.5 and 15°C
mutant enzyme D183G, at pH 7.5 and 22°C
mutant enzyme D183G, at pH 7.5 and 37°C

substrate: uracil-containing calf thymus DNA


proof_lines: mutant enzyme D183G/K302R, at pH 7.5 and 15°C

proof_lines: mutant enzyme D183G/K302R, at pH 7.5 and 22°C

proof_lines: mutant enzyme D183G/K302R, at pH 7.5 and 37°C


proof_lines:
wild type enzyme, at pH 7.5 and 15°C
wild type enzyme, at pH 7.5 and 22°C
wild type enzyme, at pH 7.5 and 37°C