organism: Beta vulgaris

substrate_name: ascorbic acid

proof_lines:
electron donor ascorbic acid
vs. O2
vs. p-coumaric acid

substrate: ascorbic acid


enzyme_display_name: tyrosinase

organism: Brassica oleracea

substrate_name: 4-methyl catechol

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 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: polyphenol oxidase shows the best activity toward catechol and 4-methyl catechol

enzyme: tyrosinase

substrate: 4-methyl catechol

source: brenda


organism: Camellia sinensis

substrate_name: catechol

substrate: catechol


organism: Charybdis japonica

substrate_name: L-Dopa

assay_conditions_summary: pH 7.1; buffer pH 7

substrate: L-Dopa


organism: Colocasia esculenta

proof_lines:
at pH 6.5 and 25°C
pH 6.5, 30°C


organism: Crocus sativus

substrate_name: pyrogallol

substrate: pyrogallol


organism: Pholiota microspora

substrate_name: p-Cresol

protein_accession_database: UniProt

sequence_source: UniProtKB:A7BHQ9 direct REST lookup

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

substrate: p-Cresol


organism: Priestia megaterium

sequence_variant_note: Resolved canonical sequence from UniProtKB:B2ZB02 canonical sequence with checked V218F substitution applied and applied mutation signature V218F to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 301.15 K; buffer 50 mM Tris HCl

proof_lines: mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C


substrate_name: L-tyrosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:B2ZB02 canonical sequence with checked V218G substitution applied and applied mutation signature V218G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C

substrate: L-tyrosine


sequence_source: UniProtKB:B2ZB02 direct REST lookup

proof_lines: wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C


organism: Ralstonia solanacearum

substrate_name: D-tyrosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8Y2J8 canonical sequence with checked V153A substitution applied and applied mutation signature V153A to reconstruct the assayed variant sequence.

proof_lines: random mutant enzyme 145-V153A, at pH 7.0 and 30°C

substrate: D-tyrosine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8Y2J8 canonical sequence with checked F185Y substitution applied and applied mutation signature F185Y to reconstruct the assayed variant sequence.

proof_lines: random mutant enzyme C10-F185Y, at pH 7.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8Y2J8 canonical sequence with checked D317Y substitution applied and applied mutation signature D317Y to reconstruct the assayed variant sequence.

proof_lines: random mutant enzyme 145-D317Y, at pH 7.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8Y2J8 canonical sequence with checked L330V substitution applied and applied mutation signature L330V to reconstruct the assayed variant sequence.

proof_lines: random mutant enzyme 145-L330V, at pH 7.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8Y2J8 canonical sequence with checked T359M substitution applied and applied mutation signature T359M to reconstruct the assayed variant sequence.

proof_lines: random mutant enzyme C10-T359M, at pH 7.0 and 30°C


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

proof_lines: random mutant enzyme RV145, at pH 7.0 and 30°C

proof_lines: random mutant enzyme RVC10, at pH 7.0 and 30°C


sequence_source: UniProtKB:Q8Y2J8 direct REST lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8Y2J8 canonical sequence with checked N322S substitution applied and applied mutation signature N322S to reconstruct the assayed variant sequence.

proof_lines: random mutant enzyme C10-N322S, at pH 7.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8Y2J8 canonical sequence with checked Y119F substitution applied and applied mutation signature Y119F to reconstruct the assayed variant sequence.

proof_lines: random mutant enzyme 145-Y119F, at pH 7.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8Y2J8 canonical sequence with checked T183I substitution applied and applied mutation signature T183I to reconstruct the assayed variant sequence.

proof_lines: random mutant enzyme C10-T183I, at pH 7.0 and 30°C


organism: Streptomyces antibioticus

sequence_source: UniProtKB:P07524 direct REST lookup


organism: Cydonia oblonga


organism: Dactylis glomerata

substrate_name: 2-caffeoylisocitric acid

substrate: 2-caffeoylisocitric acid


organism: Dioscorea alata


organism: Dioscorea bulbifera

substrate_name: DL-dopa

proof_lines:
noncompetitive vs. pyrogallol
mixed inhibition vs. catechol
competitive vs. pyrogallol

substrate: DL-dopa


organism: Dioscorea cayenensis subsp. rotundata


organism: Dioscorea polystachya

substrate_name: Coke gallic acid

substrate: Coke gallic acid


organism: Dioscorea praehensilis


organism: Fagopyrum esculentum


organism: Helix vulgaris

proof_lines: the Km value is very close to those of Helix pomatia and Sepia officinalis Hcs, but several times higher compared to those of Rapana and Octopus Hcs


organism: Homo sapiens

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

proof_lines: human tyrosinase source TXM13 pigment cell


organism: Lactarius salmonicolor

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines:
at 25°C
noncompetitive inhibition, at 25°C
competitive inhibition, at 25°C

substrate: Unknown


organism: Lactuca sativa

proof_lines: at an inhibitor concentration of 0.133 mM, with 4-methylcatechol as a substrate, mixed inhibition

proof_lines: at an inhibitor concentration of 0.1 mM, with catechol as a substrate, mixed inhibition

proof_lines: at an inhibitor concentration of 0.0082 mM, with pyrogallol as a substrate, mixed inhibition


organism: Musca domestica

substrate_name: N-beta-alanyldopamine

substrate: N-beta-alanyldopamine


organism: Mushroom

substrate_name: L-tyrosinase

assay_conditions_summary: pH 7; buffer MOPS

proof_lines:
under 100 kPa O2
under 21 kPa O2
in H2O

substrate: L-tyrosinase


organism: Neoboletus erythropus


organism: Olea europaea


organism: Palinurus elephas

substrate_name: tyramine

proof_lines:
inhibitor is mimosine
inhibitor is phenylthiourea
with dopamine as substrate

substrate: tyramine


organism: Papaver somniferum


organism: Penaeus vannamei

proof_lines: in 15 mM Tris-HCl at pH 7.8, with 5 mM CaCl2 and 5 mM MgCl2


organism: Persea americana


organism: Pieris rapae


organism: Populus nigra


organism: Aeromonas media

sequence_source: UniProtKB direct accession lookup: B2Z3P7

proof_lines: endogenous enzyme, in 50 mM Tris-HCl (pH 7.0), at 30°C

proof_lines: recombinant enzyme, in 50 mM Tris-HCl (pH 7.0), at 30°C


organism: Agaricus bisporus

substrate_name: Dopa

sequence_source: UniProtKB direct accession lookup: O42713

proof_lines: Sigma mushroom tyrosinase (SMT, crude powder, lot 105k7026)

proof_lines: Worthington mushroom tyrosinase (WMT, crude powder, lot 33H6588Q)

substrate: Dopa


substrate_name: phenol

sequence_source: UniProtKB direct accession lookup: C7FF05

substrate: phenol


substrate_name: deoxyarbutin

sequence_source: UniProtKB direct accession lookup: C7FF04

proof_lines: pH and temperature not specified in the publication

proof_lines: in the presence of quercetin-7-oleate, at pH 6.8 and 25°C

proof_lines: in the presence of quercetin-7-linoleate, at pH 6.8 and 25°C

substrate: deoxyarbutin


organism: Armillaria ostoyae

sequence_source: UniProtKB direct accession lookup: A0A284RME6


proof_lines: mutant enzyme D262N/D266N, at pH 6.0 and 25°C


organism: Camellia sinensis

sequence_source: UniProtKB direct accession lookup: C0L3S4


organism: Homo sapiens

sequence_source: UniProtKB direct accession lookup: P14679


organism: Illex argentinus

substrate_name: D-Tyr

sequence_source: UniProtKB direct accession lookup: Q76DU0

substrate: D-Tyr


organism: Juglans regia

sequence_source: UniProtKB direct accession lookup: C0LU17


organism: Nelumbo nucifera

substrate_name: catechol

sequence_source: UniProtKB direct accession lookup: A0A1U7Z3Y9

substrate: catechol


organism: Lentinula boryana

substrate_name: L-Dopa

proof_lines: preparation shows substrate inhibition kinetics with L-dopa (3,4-dihydroxy-L-phenylalanine)

substrate: L-Dopa


organism: Litchi chinensis

substrate_name: (-)-epicatechin

substrate: (-)-epicatechin


organism: Lonicera confusa

substrate_name: pyrogallate

substrate: pyrogallate


organism: Macrolepiota gracilenta

substrate_name: 4-hydroxyphenylpropionic acid

substrate: 4-hydroxyphenylpropionic acid


organism: Malpighia glabra


organism: Malus sp.

substrate_name: caffeic acid

assay_conditions_summary: pH 4

proof_lines: at pH 4.0, slight increase in Km above pH 5.0

proof_lines: at pH 4.0, slight increase in Km above pH 4.0

proof_lines: at pH 3.5-5.0, strong increase in Km above pH 5.0

substrate: caffeic acid


organism: Mangifera indica

substrate_name: pyrogallol

substrate: pyrogallol


organism: Mesocricetus auratus


organism: Mucuna pruriens


organism: Mus musculus

substrate_name: tyrosine

proof_lines:
enzyme from normal melanocytes
enzyme from malignant melanocytes
in B16/C3 tumor cell homogenates

substrate: tyrosine


organism: Musa acuminata

substrate_name: dicatechol

proof_lines:
free enzyme, at pH 6.8 and 25°C
immobilized enzyme, at pH 6.8 and 25°C

substrate: dicatechol


organism: Musa x paradisiaca


organism: Priestia megaterium

substrate_name: D-Dopa

assay_conditions_summary: pH 7; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.0), with 30% (v/v) DMSO

substrate: D-Dopa


assay_conditions_summary: pH 7; 301.15 K; buffer pH 7

proof_lines: mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C


substrate_name: L-tyrosine

proof_lines: wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C

substrate: L-tyrosine


organism: Prunus domestica subsp. insititia


organism: Prunus persica

proof_lines: membrane-bound (PPO-B) peach polyphenol oxidase without SDS

proof_lines: membrane-bound (PPO-B) peach polyphenol oxidase with 2 mM SDS

proof_lines: soluble (PPO-S) peach polyphenol oxidase without SDS


organism: Pseudomonas putida


organism: Pyrus pyrifolia

assay_conditions_summary: pH 6.8; 303.15 K; buffer 0.2 mM phosphate

proof_lines: in 0.2 mM phosphate buffer at pH 6.8 and 30°C


organism: Ralstonia solanacearum

proof_lines: mutant enzyme Y119F/V153A/D317Y/L330V, at pH 7.0 and 30°C


proof_lines: mutant enzyme T183I/F185Y/N322S/T359M, at pH 7.0 and 30°C


organism: Rapana venosa

substrate_name: o-Diphenol

proof_lines:
Rapana venosa RvH2 (subunits)
Rapana venosa native (didecamers)

substrate: o-Diphenol


organism: Sarcophaga bullata


organism: Solanum lycocarpum


organism: Solanum melongena


organism: Solanum tuberosum

assay_conditions_summary: pH 6.8; 298.15 K; buffer contexts

proof_lines: with catechol as a substrate, at pH 6.8 and 25°C

proof_lines: with 4-methylcatechol as a substrate, at pH 6.8 and 25°C


organism: Spinacia oleracea

substrate_name: esculetin

substrate: esculetin


organism: Streptomyces antibioticus

substrate_name: dopamine

assay_conditions_summary: pH 6.8; 298.15 K; buffer aqueous

proof_lines: in 100 mM phosphate buffer, pH 6.8, at 25°C

proof_lines: pH 6.8, 10°C, in methanol-glycerol cryosolvent

substrate: dopamine


organism: Streptomyces castaneoglobisporus


organism: Streptomyces glaucescens


organism: Streptomyces refuineus


organism: Streptomyces sp.

substrate_name: phenol

proof_lines:
non-competitive vs. L-tyrosine
non-competitive vs. L-dopa

substrate: phenol


organism: Terfezia arenaria

proof_lines: with L-tyrosine as substrate, at pH 7.0 and 40°C


organism: Theobroma cacao


organism: Urtica dioica

substrate_name: trans-cinnamic acid

substrate: trans-cinnamic acid


organism: Vaccinium corymbosum

proof_lines:
isoform PPO-4, at pH 6.0 and 25°C
isoform PPO-3, at pH 6.0 and 25°C
isoform PPO-2, at pH 6.0 and 25°C


organism: Vanilla planifolia

substrate_name: chlorogenic acid

substrate: chlorogenic acid


organism: Vitis vinifera

substrate_name: tyramine

proof_lines: in poly-(10)-oxyethylene oleyl ether-cyclohexane reverse micelles

substrate: tyramine


organism: Xenopus laevis

substrate_name: Dopa

proof_lines:
dopa oxidase activity
tyrosine hydroxylase activity
dopa oxidase inhibition

substrate: Dopa


organism: Thermomicrobium roseum

substrate_name: L-Dopa

substrate: L-Dopa


organism: Thermothelomyces thermophilus


proof_lines: mutant enzyme G292N/Y296V, at pH 7.0 and 40°C


substrate_name: guaiacol

proof_lines: mutant enzyme G292N/L306A, at pH 7.0 and 40°C

proof_lines: mutant enzyme G292N/L306A N, at pH 7.0 and 40°C

substrate: guaiacol


substrate_name: catechin

substrate: catechin


organism: Trametes sanguinea

substrate_name: L-Tyr

substrate: L-Tyr


organism: Trapa acornis

proof_lines:
at pH 5.8, 30°C
at pH 7.0, 30°C
at pH 6.0, 20°C


organism: Trichoderma reesei

substrate_name: L-Tyr-Gly-Gly

assay_conditions_summary: pH 7; 298.15 K; buffer 0.1M sodium phosphate

proof_lines: in 0.1M sodium phosphate buffer (pH 7.0) at 25°C

substrate: L-Tyr-Gly-Gly


organism: uncultured bacterium

substrate_name: p-coumaric acid

substrate: p-coumaric acid


enzyme_display_name: laccase

organism: Agrobacterium sp. S5-1

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

enzyme: laccase


organism: Bacillus pumilus


proof_lines: 22°C, pH 7.0, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)

proof_lines: 21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)

proof_lines: 21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I/V482G 2.06 (variant L9 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I/V482G substitutions)


proof_lines: 21-23°C, pH not specified in the publication, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)

proof_lines: 22°C, pH 7.0, mutant enzyme L386Q/G417I (variant L2 harbours the insertion of two amino acids (Ser and Pro) after the N-terminal methionine, in addition to the L386Q/G417I substitutions)


proof_lines: 21-23°C, pH not specified in the publication, wild-type enzyme


organism: Bacillus sp. (in: firmicutes)

substrate_name: syringaldazine

proof_lines:
pH 6.5, 37°C, recombinant enzyme
pH 5.0, 25°C, recombinant enzyme

substrate: syringaldazine


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9W2C5 canonical sequence with selected-row mutation E188V and applied mutation signature E188V to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 22°C, mutant enzyme E188V, in aqueous solution


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9W2C5 canonical sequence with selected-row mutation E188A and applied mutation signature E188A to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 22°C, mutant enzyme E188A, in aqueous solution


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9W2C5 canonical sequence with selected-row mutation E188L and applied mutation signature E188L to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 22°C, mutant enzyme E188L, in aqueous solution


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

proof_lines: pH 4.0, 22°C, wild-type enzyme, in aqueous solution


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9W2C5 canonical sequence with selected-row mutation E188I and applied mutation signature E188I to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 22°C, mutant enzyme E188I, in aqueous solution


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9W2C5 canonical sequence with selected-row mutation E188R and applied mutation signature E188R to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 22°C, mutant enzyme E188R, in aqueous solution


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9W2C5 canonical sequence with selected-row mutation E188K and applied mutation signature E188K to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 22°C, mutant enzyme E188K, in aqueous solution


organism: basidiomycete PM1

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication, wild-type PM1 laccase

proof_lines: pH 3.0, temperature not specified in the publication, wild-type PM1 laccase

proof_lines: pH 4.0, temperature not specified in the publication, wild-type PM1 laccase


substrate_name: 4-hydroxybenzoic acid

sequence_source: UniProtKB:Q12571 canonical sequence only

proof_lines: pH 5.0, temperature not specified in the publication, engineered enzyme 7D5

proof_lines: pH 3.0, temperature not specified in the publication, engineered enzyme 7D5

proof_lines: pH 4.0, temperature not specified in the publication, engineered enzyme 7D5

substrate: 4-hydroxybenzoic acid


organism: Cerrena sp.

substrate_name: catechol

proof_lines: pH and temperature not specified in the publication

substrate: catechol


organism: Trametes sp.

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


proof_lines: 30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)) and 6His tagged (C(DELTA)6H)

proof_lines: 30°C, pH 6.0, a variant of laccase 3 deleted of the last 13 residues (C(DELTA)), 6His tagged (C(DELTA)6H) and hyper-glycosylated


proof_lines:
30°C, pH 6.0, deglycosylated enzyme
30°C, pH 6.0, C-6His tagged laccase 3


organism: Trametes versicolor

proof_lines:
pH 3.0, 30°C, recombinant mutant D206N
pH 3.4, 30°C, recombinant mutant D206N


proof_lines:
pH 3.0, 30°C, recombinant mutant D206A
pH 3.4, 30°C, recombinant mutant D206A


proof_lines:
pH 3.0, 30°C, recombinant mutant D206E
pH 3.4, 30°C, recombinant mutant D206E


proof_lines: pH 3.0, 30°C, recombinant wild-type enzyme

proof_lines: pH 3.4, 30°C, recombinant wild-type enzyme


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


proof_lines: pH and temperature not specified in the publication, mutant enzyme V281A/P309L/S318G/D232V


organism: Haloferax volcanii

proof_lines: 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02

proof_lines: 45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02


organism: Manduca sexta

substrate_name: N-acetyldopamine

mutation_type: truncation

proof_lines: pH 5.0-5.5, recombinant N-terminally truncated enzyme

substrate: N-acetyldopamine


substrate_name: N-beta-alanyldopamine

proof_lines: pH 5.0-5.5, recombinant full-length enzyme

substrate: N-beta-alanyldopamine


organism: Marinomonas mediterranea

proof_lines: recombinant wild-type enzyme MmPPOA-695, pH 5.0, 25°C


proof_lines: recombinant mutant enzyme MmPPOA-637, pH 5.0, 25°C

proof_lines: recombinant His-tagged mutant enzyme MmPPOA-637, pH 5.0, 25°C


proof_lines: recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C


organism: Melanocarpus albomyces

proof_lines: pH 4.5, 25°C, recombinant wild-type enzyme, versus 2,6-dimethoxyphenol

proof_lines: pH 4.5, 25°C, recombinant wild-type enzyme versus 2,2-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid


proof_lines: pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae versus 2,2-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid

proof_lines: pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae, versus 2,6-dimethoxyphenol


proof_lines: pH 4.5, 22°C, recombinant enzyme expressed in Saccharomyces cerevisiae

proof_lines: pH 4.5, 25°C, recombinant enzyme expressed in Trichoderma reesei


organism: Pestalotiopsis sp. KF079

substrate_name: o-Dianisidine

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

substrate: o-Dianisidine


organism: Pleurotus eryngii

sequence_variant_note: Resolved canonical sequence from UniProtKB:B0JDP9 canonical sequence with K532A reconstruction and applied mutation signature K532A to reconstruct the assayed variant sequence.

proof_lines:
pH 6.5, 25°C, mutant K532A
pH 3.0, 25°C, mutant K532A
pH 4.5, 25°C, mutant K532A


sequence_variant_note: Resolved canonical sequence from UniProtKB:B0JDP9 canonical sequence with K532E reconstruction and applied mutation signature K532E to reconstruct the assayed variant sequence.

proof_lines:
pH 6.5, 25°C, mutant K532E
pH 3.0, 25°C, mutant K532E
pH 4.5, 25°C, mutant K532E


proof_lines:
pH 3.0, 25°C, mutant P530A
pH 6.5, 25°C, mutant P530A
pH 4.5, 25°C, mutant P530A


organism: Pleurotus ostreatus

mutation_signature: Δ4

mutation_type: deletion

proof_lines: pH 3.0, 22°C, recombinant truncated mutant POXA1bDELTA4

proof_lines: pH 6.0, 22°C, recombinant truncated mutant POXA1bDELTA4

proof_lines: pH 5.3, 22°C, recombinant truncated mutant POXA1bDELTA4


proof_lines: pH 3.0, 22°C, recombinant truncated mutant POXA1bDELTA16

proof_lines: pH 6.0, 22°C, recombinant truncated mutant POXA1bDELTA16

proof_lines: pH 5.3, 22°C, recombinant truncated mutant POXA1bDELTA16


proof_lines: pH 3.0, 22°C, recombinant truncated mutant POXA1bD205R

proof_lines: pH 5.3, 22°C, recombinant truncated mutant POXA1bD205R


proof_lines: pH 5.3, 22°C, recombinant wild-type enzyme

proof_lines: pH 6.0, 22°C, recombinant wild-type enzyme

proof_lines: pH 3.0, 22°C, recombinant wild-type enzyme


organism: Streptomyces cyaneus

proof_lines: pH and temperature not specified in the publication


organism: Streptomyces griseoflavus

proof_lines: mutant enzyme M199A, 30°C, pH not specified in the publication


proof_lines: mutant enzyme H165A/M199G, 30°C, pH not specified in the publication


proof_lines: mutant enzyme M199G, 30°C, pH not specified in the publication


proof_lines: mutant enzyme M199G/R240H, 30°C, pH not specified in the publication


proof_lines: mutant enzyme Y230A, 30°C, pH not specified in the publication


proof_lines: wild-type enzyme, 30°C, pH not specified in the publication


proof_lines: mutant enzyme H165A/R240H, 30°C, pH not specified in the publication


organism: Streptomyces viridochromogenes

proof_lines: pH 4.0, temperature not specified in the publication

proof_lines: pH 8.5, temperature not specified in the publication


organism: Thermus thermophilus


proof_lines: wild-type, presence of 0.5 mM Cu2+, 30°C, pH 5


organism: Fomes sclerodermeus

proof_lines:
pH 5.0, isozyme Lac II
pH 5.0, isozyme Lac I


organism: Pleurotus floridanus


proof_lines:
pH 7.0, 25°C
pH 6.0, 25°C
25°C, isozyme POXA3a


organism: Populus x canadensis

substrate_name: coniferaldehyde

substrate: coniferaldehyde


organism: Acer pseudoplatanus


organism: Agaricus bisporus


organism: Agaricus blazei


organism: Agaricus sinodeliciosus


organism: Agroathelia rolfsii

substrate_name: Diamond Black PV 200

substrate: Diamond Black PV 200


organism: Agrocybe pediades

proof_lines: pH 4, temperature not specified in the publication, mutant enzyme V159E/N398D

proof_lines: pH 5, temperature not specified in the publication, mutant enzyme V159E/N398D

proof_lines: pH 3, temperature not specified in the publication, mutant enzyme V159E/N398D


assay_conditions_summary: pH 3

proof_lines: pH 3, temperature not specified in the publication, mutant enzyme V159E

proof_lines: pH 5, temperature not specified in the publication, mutant enzyme V159E

proof_lines: pH 4, temperature not specified in the publication, mutant enzyme V159E


organism: Aquisalibacillus elongatus


organism: Aureobasidium pullulans


organism: Bacillus pumilus

proof_lines: pH 7.0, 22°C, recombinant enzyme, with 25% v/v DMSO

proof_lines: pH 6.5, 22°C, recombinant enzyme, with 0.8% v/v DMSO


organism: Bacillus sp. (in: firmicutes)

proof_lines: at 22°C, pH not specified in the publication


organism: Cerrena sp. WR1

sequence_source: UniProtKB E7BLR0 REST accessions endpoint, release 2026_02 (10-June-2026)


organism: Coprinopsis cinerea

sequence_source: UniProtKB A8N3P5 REST accessions endpoint, release 2026_02 (10-June-2026)


sequence_source: UniProtKB Q08AC1 REST accessions endpoint, release 2026_02 (10-June-2026)


organism: Coprinus comatus

sequence_source: UniProtKB H9C4A3 REST accessions endpoint, release 2026_02 (10-June-2026)


sequence_source: UniProtKB X5JAK9 REST accessions endpoint, release 2026_02 (10-June-2026)


sequence_source: UniProtKB X5JA14 REST accessions endpoint, release 2026_02 (10-June-2026)


organism: Coptotermes formosanus

substrate_name: hydroquinone

sequence_source: UniProtKB A0A1C9EFW4 REST accessions endpoint, release 2026_02 (10-June-2026)

substrate: hydroquinone


organism: Coriolopsis trogii

sequence_source: UniProtKB A0A140CWW4 REST accessions endpoint, release 2026_02 (10-June-2026)


organism: Daucus carota

sequence_source: UniProtKB A0A0U2US60 REST accessions endpoint, release 2026_02 (10-June-2026)

proof_lines: laccase DcLac1, pH 2.8, temperature not specified in the publication


sequence_source: UniProtKB A0A0U2LZJ6 REST accessions endpoint, release 2026_02 (10-June-2026)

proof_lines: laccase DcLac2, pH 2.8, temperature not specified in the publication


organism: Desulfovibrio sp. A2


organism: Escherichia coli

substrate_name: enterobactin

proof_lines:
pH 5, 30°C
presence of 0.25 mM Cu2+, pH 5, 30°C
presence of 0.1 mM Cu2+, pH 5, 30°C

substrate: enterobactin


proof_lines: region Pro357-His406 deletion plus P444G mutant, pH 5.5, 25°C


proof_lines: region Pro357-His406 deletion plus P444A mutant, pH 5.5, 25°C

proof_lines: mutant P444A, pH 5.5, temperature not specified in the publication


mutation_signature: region Pro357-His406 deletion mutant

proof_lines: region Pro357-His406 deletion mutant, pH 5.5, 25°C

proof_lines: region Pro357-His406 deletion mutant, presence of 1 mM Cu2+, pH 5.5, 25°C


organism: Chaetomiaceae


organism: Collybia mongolica

assay_conditions_summary: pH 4.5; 303.15 K; buffer 67 mM sodium acetate

proof_lines: in 67 mM sodium acetate buffer (pH 4.5), at 30°C


organism: Collybiopsis quercophila


organism: Coriolisimus fulvocinerea

substrate_name: ferulic acid

substrate: ferulic acid


organism: Cubamyces flavidus


organism: Deconica castanella


organism: Didymosphaeria variabile

assay_conditions_summary: pH 4.5; 310.15 K; buffer 100 mM citrate

proof_lines: in 100 mM citrate buffer, pH 4.5, at 37°C


organism: Fomes fomentarius

substrate_name: syringic acid

substrate: syringic acid


organism: Fomitopsis pinicola


organism: Fomitopsis quercina


organism: Fusarium solani

assay_conditions_summary: pH 4.5; 303.15 K; buffer 100 mM sodium tartrate

proof_lines: at 30°C in 100 mM sodium tartrate buffer (pH 4.5)


organism: Ganoderma lucidum


organism: Gelatoporia subvermispora


organism: Geobacillus sp. JS12


organism: Hexagonia tenuis


organism: Klebsiella pneumoniae


organism: Lactiplantibacillus plantarum


organism: Lentinula edodes

substrate_name: pyrogallol

substrate: pyrogallol


organism: Lentinus tigrinus


organism: Leptographium qinlingense (nom. inval.)

substrate_name: guaiacol

substrate: guaiacol


organism: Leucaena leucocephala


organism: Loweporus lividus

substrate_name: m-cresol

assay_conditions_summary: pH 4.5; 310.15 K; buffer 50 mM sodium malonate

proof_lines: in 50 mM sodium malonate buffer, pH 4.5 at 37°C

substrate: m-cresol


organism: Loweporus lividus MTCC-1178


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical sequence reconstructed as M502F and applied mutation signature M502F to reconstruct the assayed variant sequence.

proof_lines:
pH 7.6, 37°C, mutant M502F
mutant enzyme M502F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical sequence reconstructed as M502L and applied mutation signature M502L to reconstruct the assayed variant sequence.

proof_lines:
pH 7.6, 37°C, mutant M502L
mutant enzyme M502L


proof_lines:
pH 7, holoCotA
pH 3, holoCotA
pH 7.5, 37°C


proof_lines:
pH 7.0, 25°C, wild-type CotA
pH 7.6, 37°C, wild-type enzyme
pH 4.0, 25°C, wild-type CotA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical sequence reconstructed as I494A and applied mutation signature I494A to reconstruct the assayed variant sequence.

proof_lines:
pH 8.0, 25°C, mutant I494A
pH 4.0, 25°C, mutant I494A
pH 9.0, 25°C, mutant I494A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical sequence reconstructed as L386A and applied mutation signature L386A to reconstruct the assayed variant sequence.

proof_lines:
pH 7.0, 25°C, mutant L386A
pH 4.0, 25°C, mutant L386A


organism: Bacillus tequilensis


organism: Bacillus vallismortis


organism: Basidiomycota


organism: Botrytis cinerea

proof_lines:
laccase 1
extracellular enzyme
intracellular enzyme


organism: Carica papaya


organism: Cerrena unicolor


organism: Escherichia coli

proof_lines: region Pro357-His406 deletion plus D439A/P444A mutant, pH 5.5, 25°C

proof_lines: mutant D439A/P444A, pH 5.5, temperature not specified in the publication


proof_lines: mutant D439A, pH 5.5, temperature not specified in the publication

proof_lines: region Pro357-His406 deletion plus D439A mutant, pH 5.5, 25°C


proof_lines: wild-type, pH 5.5, temperature not specified in the publication

proof_lines: wild-type, presence of 1 mM Cu2+, pH 5.5, 25°C


proof_lines: mutant P444A/M510Q, pH 5.5, temperature not specified in the publication


proof_lines: mutant D439A/P444A/M510Q, pH 5.5, temperature not specified in the publication


proof_lines: mutant D439A/M510L, pH 5.5, temperature not specified in the publication


proof_lines: mutant D439A/M510Q, pH 5.5, temperature not specified in the publication


proof_lines: mutant M510L, pH 5.5, temperature not specified in the publication


organism: Ganoderma fornicatum


organism: Ganoderma lucidum


organism: Polyporus pinsitus


organism: Prunus persica


organism: Pseudomonas putida

proof_lines: enzyme has a higher affinity for syringaldazine than for L-dopa


organism: Rhizoctonia solani


organism: Schinus molle

substrate_name: quinol

substrate: quinol


organism: Shigella dysenteriae

proof_lines:
pH 4.0, 25°C, recombinant mutant WlacS
pH 4.0, 25°C, recombinant mutant WlacD


proof_lines: pH 4.0, 25°C, recombinant wild-type enzyme


organism: Sphingobacterium sp. ksn-11


organism: Sporothrix carnis


organism: Stenotrophomonas maltophilia


organism: Streptomyces griseorubens


organism: Trametes sanguinea


organism: Trametes sp.

proof_lines: pH 5.0, 30°C, surface display laccase (SDL) biocatalyst (where the enzyme laccase is displayed on the surface of biological cells through synthetic biology)


organism: Trametes versicolor

proof_lines: enzyme conjugated with chitosan of 214 kDa

proof_lines: enzyme conjugated with chitosan of 505 kDa


organism: Trametes villosa

proof_lines: soluble enzyme in presence of 1-hydroxybenzotriazole

proof_lines: immobilized enzyme in presence of 1-hydroxybenzotriazole


organism: Trichoderma harzianum

proof_lines: pH 6, 25°C,laccase immobilized in sol–gel matrix


organism: Trichophyton rubrum

substrate_name: methyl syringate

substrate: methyl syringate


organism: Tropicoporus linteus

proof_lines: pH and temperature not specified in the publication


organism: Truncospora tephropora


organism: Volvariella volvacea


organism: Mycetinis scorodonius


organism: Mycothermus thermophilus


organism: Myrioconium sp.

proof_lines:
25°C, pH 4
25°C, pH 6


organism: Naganishia albida


organism: Obba rivulosa

proof_lines:
pH 3.0, 25°C, laccase Lac-4.8
pH 3.0, 25°C, laccase Lac-3.5
pH 3.0, 25°C,laccase Lac-4.8


organism: Perenniporia fraxinea


organism: Phellinus ribis

substrate_name: syringaldazine

substrate: syringaldazine


organism: Phlebia fascicularia

proof_lines:
Lac II, 70°C, pH 2.2
Lac I, 70°C, pH 2.2
Lac I, 70°C, pH 4.0


organism: Phlebia floridensis


organism: Pleurotus pulmonarius


organism: Thermus thermophilus

sequence_variant_note: Resolved canonical sequence from UniProtKB Q72HW2 REST canonical sequence with M455L reconstructed after confirming residue 455 is M and applied mutation signature M455L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72HW2 REST canonical sequence with M456A reconstructed after confirming residue 456 is M and applied mutation signature M456A to reconstruct the assayed variant sequence.

proof_lines: mutant M456A, presence of 0.5 mM Cu2+, 30°C, pH 5


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


organism: Trametes cinnabarina

sequence_source: UniProtKB Q9UVQ2 REST canonical sequence

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

proof_lines: recombinant wild-type enzyme, pH 3.0, temperature not specified in the publication


organism: Trametes hirsuta

sequence_source: UniProtKB Q02497 REST canonical sequence

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

proof_lines: pH 5.0, temperature not specified in the publication


organism: Trametes sanguinea

sequence_source: UniProtKB C1JCL7 REST canonical sequence

proof_lines:
pH 4.5, 22°C, deglycosylated enzyme
pH 4.5, 22°C, native enzyme


organism: Streptomyces griseus

substrate_name: N,N-dimethyl-p-phenylenediamine sulfate

verification_status: corrected

protein_accession_database: NCBI Protein

sequence_source: NCBI Protein BAB64332.1 linked from PMID 12801920

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

data_origin: experimental

substrate: N,N-dimethyl-p-phenylenediamine sulfate

status: corrected


organism: Thermochaetoides thermophila

substrate_name: gallic acid

substrate: gallic acid


organism: Thielavia sp.


organism: Toxicodendron vernicifluum


proof_lines: pH 4.5, 50°C, enzyme conjugated with 1.1 kDa PEG


organism: Trametes polyzona

substrate_name: catechol

substrate: catechol


organism: Trametes pubescens


enzyme_display_name: purine-nucleoside phosphorylase

organism: Unknown

substrate_name: phosphate

enzyme: purine-nucleoside phosphorylase

substrate: phosphate


organism: Halalkalibacterium halodurans

substrate_name: guanosine

substrate: guanosine


organism: Helicobacter pylori

proof_lines:
pH 7.0, 25°C
pH 7.0, 25°C, with guanosine
pH 7.0, 25°C, with 7-methylguanosine


organism: Homo sapiens

substrate_name: hypoxanthine

proof_lines:
recombinant erythrocyte enzyme
pH 7.5, 37°C
pH 7.5, 25°C

substrate: hypoxanthine


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature H257D to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.4, mutant enzyme H257D, measured in slow-onset tight-binding phase

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature H257G to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.4, mutant enzyme H257G, measured in slow-onset tight-binding phase


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature H257F to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.4, mutant enzyme H257F, measured in slow-onset tight-binding phase


substrate_name: Inosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88W to reconstruct the assayed variant sequence.

substrate: Inosine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00491 and applied mutation signature Y88Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00491 canonical sequence plus one-based mutation reconstruction from selected signature Y88S. and applied mutation signature Y88S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P00491 direct accession sequence; reviewed Homo sapiens purine nucleoside phosphorylase, EC 2.4.2.1.

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

proof_lines:
wild-type, pH 7.0, 25°C
pH 7.4, 25°C, wild-type light PNP
pH 7.4, 25°C, wild-type heavy PNP


sequence_variant_note: Resolved canonical sequence from UniProtKB P00491 canonical sequence plus one-based mutation reconstruction from selected signature Y88A. and applied mutation signature Y88A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00491 canonical sequence plus one-based mutation reconstruction from selected signature Y88T. and applied mutation signature Y88T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00491 canonical sequence plus one-based mutation reconstruction from selected signature Y88V. and applied mutation signature Y88V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00491 canonical sequence plus one-based mutation reconstruction from selected signature Y88H. and applied mutation signature Y88H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P00491 canonical sequence plus one-based mutation reconstruction from selected signature F159Y. and applied mutation signature F159Y to reconstruct the assayed variant sequence.

proof_lines:
pH 7.4, 25°C, mutant F159Y heavy PNP
pH 7.4, 25°C, mutant F159Y light PNP


verification_status: unverified

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

proof_lines: pH and temperature not specified in the publication

status: unverified


organism: Kluyveromyces lactis

substrate_name: Xanthosine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q6CSZ6 canonical sequence plus one-based mutation reconstruction from selected signature N256D. and applied mutation signature N256D to reconstruct the assayed variant sequence.

substrate: Xanthosine


sequence_source: UniProtKB Q6CSZ6 direct accession sequence; unreviewed Kluyveromyces lactis purine nucleoside phosphorylase, EC 2.4.2.1.

proof_lines: recombinant wild-type enzyme, pH 7.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q6CSZ6 canonical sequence plus one-based mutation reconstruction from selected signature N256E. and applied mutation signature N256E to reconstruct the assayed variant sequence.


organism: Plasmodium falciparum

sequence_source: UniProtKB Q8T9Z7 direct accession sequence; reviewed Plasmodium falciparum purine nucleoside phosphorylase, EC 2.4.2.1/2.4.2.44.

proof_lines: pH 7.4, inhibition constant during slow-onset phase

proof_lines: pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8T9Z7 canonical sequence plus one-based mutation reconstruction from selected signature V73I/Y160F. and applied mutation signature V73I/Y160F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V73I/Y160F, at pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8T9Z7 canonical sequence plus one-based mutation reconstruction from selected signature V73I. and applied mutation signature V73I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V73I, at pH 7.4, temperature not specified in the publication


sequence_source: UniProtKB Q8T9Z7 canonical sequence checked directly; selected variant was not reconstructed.

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

proof_lines: mutant enzyme V66I/Y73I/Y160F, at pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8T9Z7 canonical sequence plus one-based mutation reconstruction from selected signature V66I/Y160F. and applied mutation signature V66I/Y160F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V66I/Y160F, at pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q8T9Z7 canonical sequence after direct REST lookup on 2026-06-19 and applied mutation signature V66I/V73I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V66I/V73I, at pH 7.4, temperature not specified in the publication


sequence_source: UniProtKB:Q8T9Z7 direct REST lookup on 2026-06-19

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


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q8T9Z7 canonical sequence after direct REST lookup on 2026-06-19 and applied mutation signature Y160F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y160F, at pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q8T9Z7 canonical sequence after direct REST lookup on 2026-06-19 and applied mutation signature V66I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V66I, at pH 7.4, temperature not specified in the publication


proof_lines: native enzyme subunits fused with the same peptide linker, at pH 7.4 and 25°C


sequence_source: UniProtKB:Q8I3X4 direct REST lookup on 2026-06-19


proof_lines: native enzyme subunits fused with subunits of mutant enzyme M183L, at pH 7.4 and 25°C


organism: Pseudoalteromonas sp.

sequence_source: UniProtKB:A3F8V1 direct REST lookup on 2026-06-19


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


organism: Pyrococcus furiosus

sequence_source: UniProtKB Q8U2I1 direct accession lookup

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


organism: Thermus thermophilus


organism: Toxoplasma gondii

sequence_source: UniProtKB Q2HXR2 direct accession lookup

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

proof_lines: Ki above 0.05 mM, pH 7.4, temperature not specified in the publication


proof_lines:
presence of 50 mM phosphate, pH 7.0
presence of 100 mM phosphate, pH 7.0
native enzyme, at pH 7.4 and 25°C


proof_lines: reaction with inosine, mutant enzyme S33A


proof_lines: reaction with inosine, mutant enzyme T242A


proof_lines: reaction with inosine, mutant enzyme N243A


proof_lines: reaction with inosine, mutant enzyme M219A


proof_lines: reaction with inosine, mutant enzyme F200A


proof_lines: reaction with inosine, mutant enzyme R84A


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: deoxyribose 1-phosphate

proof_lines:
reaction with adenine
reaction with inosine

substrate: deoxyribose 1-phosphate


organism: Schistosoma mansoni

proof_lines: free enzyme, at pH 7.4, temperature not specified in the publication

proof_lines: immobilized enzyme, at pH 7.4, temperature not specified in the publication


organism: Serratia marcescens


substrate_name: adenosine

proof_lines: wild type trimeric enzyme, at pH 8.0 and 70°C

proof_lines: wild type hexameric enzyme, at pH 8.0 and 70°C

substrate: adenosine


proof_lines: mutant hexameric enzyme N204D, at pH 8.0 and 70°C


proof_lines: mutant trimeric enzyme A196E/D238N, at pH 8.0 and 70°C


proof_lines: pH and temperature not specified in the publication


organism: Trichomonas vaginalis


organism: Mus musculus

assay_conditions_summary: pH 6

proof_lines: mutant enzyme N243D/K244Q, with adenosine as substrate


assay_conditions_summary: pH 7

proof_lines: wild-type enzyme, with inosine as substrate


organism: Mycobacterium tuberculosis

proof_lines: cosubstrate 2-amino-6-mercapto-7-methylpurine ribonucleoside, pH 7.0, 25°C


organism: Oryctolagus cuniculus


organism: Pectobacterium carotovorum


proof_lines: with 2-amino-6-mercapto-7-methylpurine ribonucleoside as cosubstrate, at pH 7.5 and 25°C


organism: Plasmodium lophurae


organism: Plasmodium yoelii


organism: Proteus vulgaris

proof_lines:
reaction with inosine
reaction with guanosine


organism: Rattus norvegicus


organism: Aeropyrum pernix


organism: Agaricus bisporus var. burnettii

sequence_source: UniProtKB:K5WSX5 direct lookup, release 2026_02


organism: Aneurinibacillus migulanus


organism: Anopheles gambiae

sequence_source: UniProtKB:A4Q998 direct lookup, release 2026_02


organism: Bos taurus

sequence_source: UniProtKB:P55859 direct lookup, release 2026_02

proof_lines:
pH 7.0, 25°C, recombinant enzyme
pH 5.7
pH 6.0


proof_lines: about, pH 6.5, 25°C, recombinant wild-type enzyme


proof_lines: about, pH 6.5, 25°C, recombinant mutant N243D

proof_lines: above, pH 6.5, 25°C, recombinant mutant N243D


organism: Cellulomonas sp.

sequence_source: UniProtKB:P81989 direct lookup, release 2026_02

proof_lines: 25°C, pH 7.0, cosubstrate: 7-methylguanosine


organism: Escherichia coli

sequence_source: UniProtKB:P0ABP8 direct lookup, release 2026_02


sequence_source: UniProtKB:P45563 direct lookup, release 2026_02


proof_lines: above, pH 6.5, 25°C, recombinant wild-type enzyme and mutant D204N


organism: Homo sapiens

proof_lines: reaction with inosine, mutant enzyme Y88F


proof_lines: reaction with inosine, mutant enzyme K244A


proof_lines: reaction with inosine, mutant enzyme E89A


proof_lines: reaction with inosine, mutant enzyme H86A


proof_lines: reaction with inosine, mutant enzyme E201A


proof_lines: reaction with inosine, mutant enzyme F159A


proof_lines: reaction with inosine, mutant enzyme H257A


organism: Hyalomma dromedarii


organism: Klebsiella aerogenes


organism: Mesomycoplasma hyorhinis


organism: Mus musculus

proof_lines:
mutant enzyme N243D, pH 6.0
mutant enzyme N243D, pH 7.0
mutant enzyme N243D, pH 6.0 ot pH 7.0


organism: Bacillus cereus

proof_lines:
enzyme from spores
enzyme from vegetative cells


organism: Bacillus subtilis

proof_lines: isoform of 816 amino acids, pH 7.0, 37°C

proof_lines: isoform of 702 amino acids, pH 7.0, 37°C


substrate_name: alpha-D-ribose 1-phosphate

proof_lines:
reaction with guanine
pH 7.4, 25°C
reaction with hypoxanthine

substrate: alpha-D-ribose 1-phosphate


proof_lines: mutant F200W, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant F159W, pH not specified in the publication, temperature not specified in the publication


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


proof_lines: pH and temperature not specified in the publication


organism: Cricetulus griseus


organism: Enterobacter cloacae


organism: Geobacillus stearothermophilus


proof_lines:
wild-tpe, pH 7.4, 25°C
wild-type enzyme
reaction with inosine, wild-type enzyme


enzyme_display_name: mannan-binding lectin-associated serine protease-2

substrate_name: complement component C4 P4-P4' fragment

substrate: complement component C4 P4-P4' fragment


substrate_name: H2O; N-Acetyl-Gly-Lys methyl ester

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

proof_lines:
MASP-2 CCP1-CCP2-SP
chimera C1s(MASP-2CCP1/2), 37°C
chimera C1s(MASP-2SP), 37°C

enzyme: mannan-binding lectin-associated serine protease-2

substrate: H2O; N-Acetyl-Gly-Lys methyl ester


substrate_name: p-Tosyl-L-arginine methyl ester

source_db: oed

kcat_over_km_origin: calculated

substrate: p-Tosyl-L-arginine methyl ester

source: oed


substrate_name: Complement component C4; H2O

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

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

substrate: Complement component C4; H2O


substrate_name: N-Acetyl-Gly-Lys methyl ester

substrate: N-Acetyl-Gly-Lys methyl ester


substrate_name: Complement component C2; H2O

substrate: Complement component C2; H2O


substrate_name: Complement component C4

substrate: Complement component C4


organism: Rattus norvegicus

proof_lines: SABIO-RK modifier species: mannan-binding lectin-associated serine protease-2(Enzyme) mutant R424K (activated MASP-2K)


enzyme_display_name: N,N'-diacetylchitobiose non-reducing end deacetylase

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

substrate_name: GlcNAc2 (at pH 8 and at 70 degrees Celsius)

source_db: uniprot

assay_conditions_summary: pH 8

source: uniprot


organism: Pyrococcus horikoshii

substrate_name: N,N'-diacetylchitobiose

sequence_variant_note: Resolved canonical sequence from UniProtKB O58235 REST lookup on 2026-06-19 plus row-specific R157T reconstruction and applied mutation signature R157T to reconstruct the assayed variant sequence.

enzyme: N,N'-diacetylchitobiose non-reducing end deacetylase

substrate: N,N'-diacetylchitobiose


sequence_source: UniProtKB O58235 REST lookup on 2026-06-19


substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


organism: Thermococcus chitonophagus

sequence_source: UniProtKB A0A160VQZ8 REST lookup on 2026-06-19


organism: Thermococcus kodakaraensis

substrate_name: H2O; N-Acetylglucosamine

sequence_source: UniProtKB Q6F4N1 REST lookup on 2026-06-19; matches source_record cache sequence

substrate: H2O; N-Acetylglucosamine


organism: Thermococcus kodakarensis


organism: Euglena sp.

substrate_name: oleoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: oleoyl-CoA


organism: Homo sapiens

substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: stearoyl-CoA as an acyl donor reveals only 33% of the activity observed under the standard assay conditions

substrate: palmitoyl-CoA


substrate_name: 1-acyl-sn-glycerol 3-phosphate

proof_lines: in the incorporation of palmitate and linoleate

substrate: 1-acyl-sn-glycerol 3-phosphate


organism: Spinacia oleracea


substrate_name: palmitoyl-CoA (in the presence of 1-palmitoyl-LPC as cosubstrate)


substrate_name: arachidonoyl-CoA (20:4) for LPIAT activity


substrate_name: 1-oleoyl-lysophosphatidic acid

substrate: 1-oleoyl-lysophosphatidic acid


substrate_name: LPA sn-1 C18:1

substrate: LPA sn-1 C18:1


substrate_name: triacylglycerol

substrate: triacylglycerol


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: arachidonoyl-CoA

substrate: arachidonoyl-CoA


substrate_name: Oleoyl-CoA; 1-Oleoyl-lysophosphatidate

sequence_source: UniProtKB REST exact accession lookup

substrate: Oleoyl-CoA; 1-Oleoyl-lysophosphatidate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q99943 canonical sequence plus selected-row mutation reconstruction and applied mutation signature T180S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q99943 canonical sequence plus selected-row mutation reconstruction and applied mutation signature P207L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q99943 canonical sequence plus selected-row mutation reconstruction and applied mutation signature R149K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q99943 canonical sequence plus selected-row mutation reconstruction and applied mutation signature I208A 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.


substrate_name: 1-Oleoyl-lysophosphatidate; Oleoyl-CoA

substrate: 1-Oleoyl-lysophosphatidate; Oleoyl-CoA


assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


substrate_name: 1-oleoyl-sn-glycerol 3-phosphate

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

substrate: 1-oleoyl-sn-glycerol 3-phosphate


substrate_name: docosahexaenoyl-CoA

sequence_source: UniProtKB REST lookup of C4B4E7 secondary accession resolving to Q9D517

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

substrate: docosahexaenoyl-CoA


organism: Mycobacterium tuberculosis

assay_conditions_summary: 301.15 K; cofactor CoA

proof_lines: 28°C, pH not specified in the publication, cosubstrate: pamitoleoyl-CoA

proof_lines: 28°C, pH not specified in the publication, cosubstrate: oleoyl-CoA

proof_lines: 28°C, pH not specified in the publication, cosubstrate: 1-acyl-sn-glycerol 3-phosphate


substrate_name: LPA C16:0

substrate: LPA C16:0


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: oleoyl-CoA (with lysophosphoethanolamine as cosubstrate)


enzyme_display_name: gamma-butyrobetaine dioxygenase

organism: Bos taurus

enzyme: gamma-butyrobetaine dioxygenase


proof_lines: co-substrate: (3S)-3-fluoro-4-(trimethylammonio)butanoate, pH 7.5, 25°C, fluoride assay

proof_lines: co-substrate: 2-oxoglutarate, pH 7.5, 25°C, NMR assay

proof_lines: co-substrate: 2-oxoglutarate, pH 7.5, 25°C, fluoride assay


organism: Mus musculus

sequence_source: UniProtKB reviewed Q924Y0 (BODG_MOUSE)

assay_conditions_summary: pH 7.4; buffer 20mM potassium phosphate

proof_lines: in 20mM potassium phosphate buffer (pH 7.4) containing 50 mM KCl, 3mM 2-oxoglutarate, 10 mM sodium ascorbate, 0.5 mM DTT, 0.5 mM ammonium iron sulfate, 2.5 mg/ml bovine serum albumin, 0.01% (w/v) Triton X-100 and 2 mM 6-N-trimethyllysine


organism: Pseudomonas sp.

substrate_name: gamma-butyrobetaine

sequence_source: UniProtKB reviewed P80193 (BODG_PSESK), anchored by PMID 861203 strain AK 1

substrate: gamma-butyrobetaine


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

sequence_source: UniProtKB:O75936 reviewed; direct accession lookup on 2026-06-19

proof_lines: pH 7.5, temperature not specified in the publication

source_databases_merged: sabio_rk brenda skid


sequence_source: UniProtKB:P80193 reviewed; direct accession lookup on 2026-06-19

proof_lines: pH 7.5, temperature not specified in the publication, only the Michaelis-Menten range is fitted


sequence_source: UniProtKB:Q9QZU7 reviewed; direct accession lookup on 2026-06-19


organism: Sus scrofa

sequence_source: UniProtKB:A0A4X1SZK1 unreviewed; source accession F1SGL4 is a secondary/merged accession in direct lookup on 2026-06-19

proof_lines: apparent kinetic constant (Km), in liver of 210-day-old domestic pig, pH 7.4, 37°C

proof_lines: apparent kinetic constant (Km), in kidney of 21-day-old domestic pig, pH 7.4, 37°C

proof_lines: apparent kinetic constant (Km), in liver of 1-day-old domestic pig, pH 7.4, 37°C


organism: Plasmodium falciparum

substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: H+; Acetoacetyl-[acp]; NADPH

assay_conditions_summary: cofactor NADP+

substrate: H+; Acetoacetyl-[acp]; NADPH


organism: Streptococcus pneumoniae

substrate_name: NADPH

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH

substrate: NADPH


organism: Xanthomonas campestris pv. campestris

substrate_name: 3-oxododecanoyl-[acyl-carrier protein]

proof_lines: pH and temperature not specified in the publication

substrate: 3-oxododecanoyl-[acyl-carrier protein]


organism: Brassica napus

substrate_name: acetoacetyl-[acyl-carrier protein]

assay_conditions_summary: cofactor NADPH

substrate: acetoacetyl-[acyl-carrier protein]


organism: Carthamus tinctorius


organism: Lactococcus lactis

substrate_name: beta-ketobutyryl-CoA

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

proof_lines:
pH 7.0, 30°C, FabG1
pH 7.0, 30°C, FabG2

substrate: beta-ketobutyryl-CoA


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: in the presence of 1 M urea, pH 7.0, 25°C


organism: Cupriavidus necator

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


substrate_name: Acetoacetyl-CoA; NADPH; H+

proof_lines: SABIO-RK modifier species: 3-oxoacyl-[acyl-carrier-protein] reductase(Enzyme) mutant K1699A BKR

substrate: Acetoacetyl-CoA; NADPH; H+


substrate_name: NADPH; H+; Acetoacetyl-CoA

proof_lines: SABIO-RK modifier species: 3-oxoacyl-[acyl-carrier-protein] reductase(Enzyme) mutant K1699Q BKR

substrate: NADPH; H+; Acetoacetyl-CoA


organism: Mycolicibacterium smegmatis

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADPH


organism: Pseudomonas aeruginosa

proof_lines: with acetoacetyl-CoA as cosubstrate, pH and temperature not specified in the publication

proof_lines: with 3-hydroxydecanoyl-N-acetylcysteamine as cosubstrate, pH and temperature not specified in the publication


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from UniProtKB:P35731 reconstructed from canonical sequence and applied mutation signature S40A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P35731 reconstructed from canonical sequence and applied mutation signature S36A to reconstruct the assayed variant sequence.


organism: Synechococcus elongatus PCC 7942 = FACHB-805

substrate_name: ethylbenzoylacetate

assay_conditions_summary: pH 7; buffer 0.1 M sodium phosphate; cofactor NADPH

proof_lines: with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0

substrate: ethylbenzoylacetate


enzyme_display_name: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

organism: Homo sapiens

substrate_name: Crotonoyl-CoA; NADPH

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: enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)(Enzyme) mutant K1699A ER

substrate: Crotonoyl-CoA; NADPH


substrate_name: NADPH; Crotonoyl-CoA

proof_lines: SABIO-RK modifier species: enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)(Enzyme) mutant K1699Q ER

enzyme: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

substrate: NADPH; Crotonoyl-CoA


verification_status: verified

sequence_source: UniProtKB REST canonical sequence for P49327, checked 2026-06-19

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: TABLE THREE enoyl reductase block, enzyme row WT; columns kcat (min^-1), KNADPH (uM) and kcat/KNADPH (uM^-1 min^-1); kcat cell = 20 min^-1; KNADPH cell = 3 uM; kcat/KNADPH cell = 7; author manuscript page 15 (PDF page 15). captured primary segment: NADPH | wild-type HFAS, recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE enoyl reductase block, enzyme row WT: Km NADPH 3 uM | kcat 20 min^-1 | kcat/Km NADPH printed cell 7 under the column head kcat/KNADPH (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE enoyl reductase block, enzyme row WT: KNADPH = 3 uM; kcat = 20 min^-1; printed kcat/KNADPH = 7 uM^-1 min^-1.

table_label: TABLE THREE (kinetic evaluation of the wild-type and Lys-1699 mutant HFAS enzymes), enoyl reductase block; printed column heads enzyme | kcat (min^-1) | KNADPH (uM) | KCRT (uM) | kcat/KNADPH (uM^-1 min^-1) | kcat/KCRT (uM^-1 min^-1)

status: verified


organism: Porphyromonas gingivalis

substrate_name: crotonyl-[acyl-carrier protein]

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

sequence_source: UniProtKB REST canonical sequence for Q7MAW0, checked 2026-06-19

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5

source_databases_merged: brenda skid

substrate: crotonyl-[acyl-carrier protein]


organism: Staphylococcus aureus

substrate_name: Crotonyl-N-acetyl-cysteamine

sequence_source: UniProtKB REST canonical sequence for Q9RMI3, checked 2026-06-19

substrate: Crotonyl-N-acetyl-cysteamine


organism: uncultured bacterium pBF1


organism: Bacillus cereus

substrate_name: Unknown

substrate: Unknown


organism: Bacillus subtilis


assay_conditions_summary: pH 7.8; 298.15 K; buffer 100 mM Na2HPO4; cofactor NADPH

proof_lines: wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)

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


substrate_name: dodecenoyl-[Staphylococcus aureus acyl carrier protein]

proof_lines: mutant enzyme A95V, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)


proof_lines: Km above 1 mM, mutant enzyme I193S, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)


proof_lines: mutant enzyme F204S, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)

substrate: dodecenoyl-[Staphylococcus aureus acyl carrier protein]


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

proof_lines: pH 6.5, 30°C, versus trans-2-octenoyl N-acetylcysteamine


proof_lines: mutant enzyme Y147F, pH and temperature not specified in the publication


proof_lines: mutant enzyme M99T, pH and temperature not specified in the publication


proof_lines: mutant enzyme Y147H, pH and temperature not specified in the publication


organism: Streptomyces collinus

sequence_source: NCBI Protein:AAC44655.1

assay_conditions_summary: cofactor CoA

proof_lines:
vmax 0.0053 mmol/mg/min
vmax 0.0075 mmol/mg/min


enzyme_display_name: tryptophan 5-halogenase

organism: Streptomyces rugosporus

substrate_name: L-tryptophan

sequence_source: UniProtKB A4D0H5 direct accession check; reviewed Swiss-Prot TRP5H_STRRG, EC 1.14.19.58, Streptomyces rugosporus.

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

enzyme: tryptophan 5-halogenase

substrate: L-tryptophan


sequence_variant_note: Resolved canonical sequence from UniProtKB A4D0H5 direct accession check; reviewed Swiss-Prot TRP5H_STRRG, EC 1.14.19.58, Streptomyces rugosporus. and applied mutation signature Y454F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 303.15 K; buffer potassium phosphate

proof_lines: mutant enzyme Y454F, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB A4D0H5 direct accession check; reviewed Swiss-Prot TRP5H_STRRG, EC 1.14.19.58, Streptomyces rugosporus. and applied mutation signature E46D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E46D, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB A4D0H5 direct accession check; reviewed Swiss-Prot TRP5H_STRRG, EC 1.14.19.58, Streptomyces rugosporus. and applied mutation signature E46Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E46Q, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB A4D0H5 direct accession check; reviewed Swiss-Prot TRP5H_STRRG, EC 1.14.19.58, Streptomyces rugosporus. and applied mutation signature F49A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F49A, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


proof_lines: wild type enzyme, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


organism: Streptomyces toxytricini

substrate_name: anthranilamide; kynurenine

sequence_source: UniProtKB E9P162 direct accession check found a reviewed Streptomyces toxytricini tryptophan 6-halogenase, EC 1.14.19.59; sequence not promoted for EC 1.14.19.58.

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

substrate: anthranilamide; kynurenine


organism: Xenorhabdus szentirmaii

sequence_source: UniProtKB W1J423 direct accession check; unreviewed TrEMBL tryptophan 5-halogenase, Xenorhabdus szentirmaii DSM 16338.

proof_lines: with chloride as cosubstrate, at pH 7.4 and 37°C


enzyme_display_name: NADH oxidase (H2O2-forming)

organism: Brevibacterium sp.

substrate_name: NADH

assay_conditions_summary: pH 8.8; 298.15 K; cofactor NADH

enzyme: NADH oxidase (H2O2-forming)

substrate: NADH


organism: Pseudothermotoga hypogea

assay_conditions_summary: pH 7; 353.15 K; cofactor NADH


organism: Thermotoga maritima

assay_conditions_summary: pH 7.8; 353.15 K; cofactor NADH


organism: Archaeoglobus fulgidus

sequence_source: UniProtKB O29852 direct accession lookup

assay_conditions_summary: pH 6.6; 328.15 K; cofactor NADH


sequence_source: UniProtKB O29794 direct accession lookup

assay_conditions_summary: pH 7; 343.15 K; cofactor NADH


sequence_source: UniProtKB O29985 direct accession lookup


organism: Escherichia coli

substrate_name: O2; H+; NADH

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

assay_conditions_summary: cofactor NADH

proof_lines: SABIO-RK modifier species: NADH oxidase (H2O2-forming)(Enzyme) mutant Phe(B10) (Y29F)

substrate: O2; H+; NADH


substrate_name: H+; NADH; O2

proof_lines: SABIO-RK modifier species: NADH oxidase (H2O2-forming)(Enzyme) mutant Glu(B10) (Y29E)

substrate: H+; NADH; O2


substrate_name: NADH; H+; O2

proof_lines: SABIO-RK modifier species: NADH oxidase (H2O2-forming)(Enzyme) mutant His(B10) (Y29H)

substrate: NADH; H+; O2


organism: Pyrococcus horikoshii

substrate_name: beta-NADH

proof_lines: pH and temperature not specified in the publication

substrate: beta-NADH


organism: Streptococcus mutans

sequence_source: UniProtKB O66266 direct accession lookup

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

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

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


enzyme_display_name: glutaminyl-peptide cyclotransferase

organism: Tannerella forsythia

proof_lines: pH and temperature not specified in the publication, secretory glutaminyl cyclase

enzyme: glutaminyl-peptide cyclotransferase


organism: Homo sapiens


substrate_name: QEDL

proof_lines: protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions

substrate: QEDL


proof_lines:
pH 8.0, 30°C
pH 6.0, 30°C, in absence of DMSO
pH 6.0, 30°C, 1% DMSO


organism: Mus musculus

substrate_name: Gln-Gly-Pro

proof_lines: protein expressed in Pichia pastoris, pH 8.0, 30°C

substrate: Gln-Gly-Pro


organism: Oryctolagus cuniculus

proof_lines: kcat less than 0.012 s-1, pH and temperature not specified in the publication


organism: Porphyromonas gingivalis


organism: Prevotella intermedia


organism: Rattus norvegicus


organism: Solanum tuberosum

substrate_name: L-Gln-Gly

substrate: L-Gln-Gly


sequence_source: UniProtKB REST direct lookup: Q16769

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: Q16769 and applied mutation signature Y115E/Y117E to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, with enzyme mutant Y115E/Y117E


organism: Ixodes scapularis

substrate_name: L-glutaminyl 2-naphthylamide

sequence_source: UniProtKB REST direct lookup: B7QK46

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

substrate: L-glutaminyl 2-naphthylamide


sequence_source: UniProtKB REST direct lookup: Q9CYK2


proof_lines: wild type enzyme, in 50 mM Tris, pH 8.0, at 30°C


organism: Myxococcus xanthus

substrate_name: QGGG

sequence_source: UniProtKB REST direct lookup: Q1DDS6

proof_lines: in 0.1 M MES, pH 7.5, temperature not specified in the publication

substrate: QGGG


substrate_name: QSVVPDSIGR

sequence_source: UniProtKB REST direct lookup: Q7MT37

substrate: QSVVPDSIGR


substrate_name: H-Gln-Gly-OH

sequence_source: UniProtKB REST direct lookup: M1AKD0

substrate: H-Gln-Gly-OH


sequence_source: UniProtKB REST direct lookup: G8UMP8


organism: Xanthomonas campestris

sequence_source: UniProtKB REST direct lookup: Q8P8M4


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: Q8P8M4 and applied mutation signature E45Q to reconstruct the assayed variant sequence.


organism: Zymomonas mobilis

sequence_source: UniProtKB REST direct lookup: Q5NLA9

assay_conditions_summary: pH 6

proof_lines: in 0.1 M MES, pH 6.0, temperature not specified in the publication


organism: Arabidopsis thaliana

sequence_source: UniProt Q84WV9 / QPCT_ARATH direct EC+organism lookup; UniProt cites PMID 17261077 for function and catalytic activity.


organism: Bos taurus

substrate_name: gonadotropin releasing hormone

substrate: gonadotropin releasing hormone


organism: Carica papaya

substrate_name: Gln-Tyr-Ala

sequence_source: UniProt O81226 / O81226_CARPA direct EC+organism lookup; accession is TrEMBL but is tied to Carica papaya glutamine cyclotransferase sequence AAC27745.1.

substrate: Gln-Tyr-Ala


organism: Drosophila melanogaster

substrate_name: H-Gln-beta-naphthylamide

sequence_source: UniProt Q86PD7 / QPCT2_DROME; selected source notes say isoDromeQC and UniProt cites PMID 17722885 for iso glutaminyl cyclase catalytic activity.

proof_lines:
30°C, isoDromeQC
pH 8, isoDromeQC
pH 7, isoDromeQC

substrate: H-Gln-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from UniProt Q16769 / QPCT_HUMAN canonical sequence plus PMID 11551224 H307Q mutation evidence. and applied mutation signature H307Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q16769 / QPCT_HUMAN canonical sequence plus PMID 11551224 H319Q mutation evidence. and applied mutation signature H319Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q16769 / QPCT_HUMAN canonical sequence plus PMID 18072935 D248Q mutation evidence. and applied mutation signature D248Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q16769 / QPCT_HUMAN canonical sequence plus PMID 18072935 S160G mutation evidence. and applied mutation signature S160G to reconstruct the assayed variant sequence.


sequence_source: UniProt Q16769 / QPCT_HUMAN; selected source notes say wild-type enzyme and PMID 18072935 is cited by UniProt for QPCT catalytic activity.

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


sequence_variant_note: Resolved canonical sequence from UniProt Q16769 / QPCT_HUMAN canonical sequence plus PMID 18072935 Asp-305 mutation context. and applied mutation signature D305N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q16769 / QPCT_HUMAN canonical sequence plus PMID 18072935 Glu-201 mutation evidence. and applied mutation signature E201D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q16769 / QPCT_HUMAN canonical sequence plus PMID 18072935 D305E mutation evidence. and applied mutation signature D305E to reconstruct the assayed variant sequence.


substrate_name: H-Gln-Gln-OH

sequence_source: UniProtKB REST direct lookup Q9VRQ9 (QPCT1_DROME) canonical sequence

proof_lines:
30°C
pH 8
pH 7

substrate: H-Gln-Gln-OH


substrate_name: DIM-10 protein

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q86PD7 (QPCT2_DROME); variant reconstructed from canonical sequence and applied mutation signature C136A/C158A to reconstruct the assayed variant sequence.

proof_lines: isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM MOPS (pH 7.0)

proof_lines: isoform isoDromeQC mutant C136A/C158A, at 30°C in 50 mM Tris (pH 8.0)

substrate: DIM-10 protein


substrate_name: MCCB protein

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q9VRQ9 (QPCT1_DROME); variant reconstructed from canonical sequence and applied mutation signature C113A/C136A to reconstruct the assayed variant sequence.

proof_lines: isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM MOPS (pH 7.0)

proof_lines: isoform DromeQC mutant C113A/C136A, at 30°C in 50 mM Tris (pH 8.0)

substrate: MCCB protein


sequence_source: UniProtKB REST direct lookup Q86PD7 (QPCT2_DROME) canonical sequence

proof_lines: isoform isoDromeQC, at 30°C in 50 mM Tris (pH 8.0)

proof_lines: isoform isoDromeQC, at 30°C in 50 mM MOPS (pH 7.0)

proof_lines: isoform isoDromeQC, at 30°C in 50 mM MES (pH 6.0)


substrate_name: Unknown

sequence_source: UniProtKB REST direct lookup Q16769 (QPCT_HUMAN) canonical sequence

proof_lines: pH and temperature not specified in the publication, secretory glutaminyl cyclase

substrate: Unknown


substrate_name: Gln-Gln

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q16769 (QPCT_HUMAN); variant reconstructed from canonical sequence and applied mutation signature Q304L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

substrate: Gln-Gln


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q16769 (QPCT_HUMAN); variant reconstructed from canonical sequence and applied mutation signature R54W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q16769 (QPCT_HUMAN); variant reconstructed from canonical sequence and applied mutation signature F325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q16769 (QPCT_HUMAN); variant reconstructed from canonical sequence and applied mutation signature W207F to reconstruct the assayed variant sequence.


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

proof_lines:
pH 7.0, wild-type enzyme
pH 8.0, wild-type enzyme
pH 7.5, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q16769 (QPCT_HUMAN); variant reconstructed from canonical sequence and applied mutation signature W207L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q16769 (QPCT_HUMAN); variant reconstructed from canonical sequence and applied mutation signature E201D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q16769 (QPCT_HUMAN); variant reconstructed from canonical sequence and applied mutation signature K144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q16769 (QPCT_HUMAN); variant reconstructed from canonical sequence and applied mutation signature W329A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q16769 (QPCT_HUMAN); variant reconstructed from canonical sequence and applied mutation signature F146A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct lookup Q9NXS2 (QPCTL_HUMAN) canonical sequence

proof_lines: Golgi-resident glutaminyl cyclase, at 25°C in 50 mM Tris-HCl, pH 8.0


enzyme_display_name: formate dehydrogenase

organism: Unknown

substrate_name: formate

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

enzyme: formate dehydrogenase

substrate: formate


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines: pH 7.5, 30°C, enzyme from DE-52 chromatography

proof_lines: pH 7.5, 30°C, enzyme expressed in tobacco


organism: [Candida] boidinii

substrate_name: NADP+

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

assay_conditions_summary: pH 7.5; buffer potassium phosphate; cofactor NADP+

proof_lines: mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5)

substrate: NADP+


proof_lines: mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5)


proof_lines: mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5)


substrate_name: NAD+

assay_conditions_summary: pH 9.7; 303.15 K; buffer 50 mM carbonate; cofactor NADP+

proof_lines: wild type enzyme, in the presence of 30% (v/v) 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30°C

proof_lines: wild type enzyme, in the absence of 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30°C

proof_lines: wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5)

substrate: NAD+


proof_lines: mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5)


proof_lines: mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5)


proof_lines: mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5)


proof_lines: mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5)


organism: Candida methanolica


organism: [Candida] methylica


sequence_variant_note: Resolved canonical sequence from UniProt REST O13437 sequence plus row-specific BRENDA mutation note and applied mutation signature V120S/N187D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+

proof_lines: mutant enzyme V120S/N187D, at pH 9.5 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProt REST O13437 sequence plus row-specific BRENDA mutation note and applied mutation signature V120S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST O13437 sequence plus row-specific BRENDA mutation note and applied mutation signature A10C/I239C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+

proof_lines: mutant enzyme A10C/I239C, at 30°C and pH 7.0


sequence_variant_note: Resolved canonical sequence from UniProt REST O13437 sequence plus row-specific BRENDA mutation note and applied mutation signature A10C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST O13437 sequence plus row-specific BRENDA mutation note and applied mutation signature I239C to reconstruct the assayed variant sequence.


sequence_source: UniProt REST A0A0A1EQY0 canonical sequence

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


sequence_source: UniProt REST O13437 canonical sequence retained as accession context only

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

proof_lines: at pH 7.4, temperature not specified in the publication

proof_lines: in the absence of metal ion, at pH 7.4 and 25°C

proof_lines: in the presence of 0.003 mM W6+, at pH 7.4 and 25°C


sequence_source: UniProt REST A0A0A1EQY0 canonical sequence retained as accession context only

proof_lines: wild type enzyme R174N, at pH 7.5 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST A0A0A1EQY0 sequence plus row-specific BRENDA mutation note and applied mutation signature R174N to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme N187E/N147R, at pH 8.0 and 25°C


proof_lines: mutant enzyme N187E/Q105R, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; reconstructed from selected mutation_signature and applied mutation signature T226V to reconstruct the assayed variant sequence.


sequence_source: NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; canonical context only, variant not reconstructed

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 NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; reconstructed from selected mutation_signature and applied mutation signature T169C/T226C to reconstruct the assayed variant sequence.

proof_lines: oxidized mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8

proof_lines: reduced mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8


sequence_variant_note: Resolved canonical sequence from NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; reconstructed from selected mutation_signature and applied mutation signature D195S/Y196A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines: mutant enzyme D195S/Y196A, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; reconstructed from selected mutation_signature and applied mutation signature D195S/Q197V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195S/Q197V, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; reconstructed from selected mutation_signature and applied mutation signature D195S/Y196L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195S/Y196L, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; reconstructed from selected mutation_signature and applied mutation signature D195S/Y196S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195S/Y196S, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; reconstructed from selected mutation_signature and applied mutation signature D195S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 293.15 K; cofactor NADP+

proof_lines:
pH 8.0, 20°C, mutant enzyme D195S
mutant enzyme D195S, at pH 8.0 and 25°C
mutant enzyme D195S


sequence_variant_note: Resolved canonical sequence from NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; reconstructed from selected mutation_signature and applied mutation signature Q197V to reconstruct the assayed variant sequence.


sequence_source: NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines:
wild type enzyme, at pH 8.0 and 25°C
wild-type enzyme
pH 8.0, 20°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; reconstructed from selected mutation_signature and applied mutation signature D195S/Q197T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195S/Q197T, at pH 8.0 and 25°C


sequence_source: NCBI Protein CAA57036.1; NAD-dependent formate dehydrogenase [[Candida] methylica]; context only, not accepted as row-specific sequence

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

proof_lines: with HCO3- as cosubstrate, pH 8.0, temperature not specified in the publication

proof_lines: in the presence of 0.003 mM Fe3+, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:O13437 canonical sequence; Q00498 is a secondary accession; row-specific BRENDA mutation note N147R and applied mutation signature N147R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O13437 canonical sequence; Q00498 is a secondary accession; row-specific BRENDA mutation note Y302R and applied mutation signature Y302R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O13437 canonical sequence; Q00498 is a secondary accession; row-specific BRENDA mutation note H13E and applied mutation signature H13E to reconstruct the assayed variant sequence.


organism: Clostridium carboxidivorans

substrate_name: NADH

sequence_source: UniProtKB:E2IQB0 direct accession lookup

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

assay_conditions_summary: pH 6.8; 310.15 K; cofactor NADH

proof_lines: in 0.1 M sodium phosphate (pH 6.8), at 37°C

substrate: NADH


organism: Clostridium ljungdahlii

assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+


organism: Cupriavidus necator

sequence_source: UniProtKB:Q0KDY1 direct accession lookup

assay_conditions_summary: cofactor NAD+

proof_lines: pH and temperature not specified in the publication


organism: Gelatoporia subvermispora

sequence_source: UniProtKB:A9ZNT9 direct accession lookup


sequence_source: UniProtKB:A9ZNT8 direct accession lookup

assay_conditions_summary: pH 6.5; 298.15 K; cofactor NAD+

proof_lines: in the absence of metal ion, at pH 6.5 and 25°C

proof_lines: in the presence of 0.005 mM Mn2+, at pH 6.5 and 25°C


organism: Moraxella sp.

assay_conditions_summary: pH 5.5; 298.15 K; buffer 0.1 M potassium phosphate; cofactor NAD+

proof_lines: in the presence of 0.005 mM Na+, at pH 5.5 and 25°C

proof_lines: in the absence of metal ion, at pH 5.5 and 25°C

proof_lines: in 0.1 M potassium phosphate buffer pH 7.0, at 30°C


organism: Moraxella sp. C-1

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


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

proof_lines: mutant enzyme A198G, pH and temperature not specified in the publication


organism: Paracoccus sp. 12-A

sequence_source: UniProtKB:Q93GW3 direct accession lookup

proof_lines: in the presence of 0.005 mM Mg2+, at pH 6.5 and 25°C


organism: Pseudomonas sp. 101

sequence_source: UniProtKB:P33160 canonical sequence context only

proof_lines: mutant enzyme A198G/D221S, pH and temperature not specified in the publication


assay_conditions_summary: cofactor NADP+

proof_lines: mutant enzyme D221S, pH and temperature not specified in the publication


sequence_source: UniProtKB REST direct accession check on 2026-06-19


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

proof_lines: pH 7.0, 30°C, mutant enzyme D196A/Y197R, with 0.5 M formate

proof_lines: pH 7.0, 30°C, mutant enzyme D196A/Y197R, with 0.25 M formate


proof_lines: in the presence of 0.007 mM Fe3+, at pH 6.5 and 25°C


organism: Thermochaetoides thermophila

proof_lines: C-terminally His-tagged enzyme, at pH 5.0 and 25°C

proof_lines: N-terminally His-tagged enzyme, at pH 5.0 and 25°C


organism: Thermothelomyces thermophilus

assay_conditions_summary: pH 10.5; 298.15 K; cofactor NAD+

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


organism: Thiobacillus sp. KNK65MA

proof_lines: in the presence of 0.007 mM W6+, at pH 7.0 and 25°C

proof_lines: in the absence of metal ion, at pH 7.0 and 25°C


organism: Ancylobacter aquaticus

sequence_source: UniProtKB Q845T0 direct REST lookup; live TrEMBL formate dehydrogenase entry for Ancylobacter aquaticus with EC 1.17.1.9.

assay_conditions_summary: pH 6; 298.15 K; cofactor NAD+

proof_lines: in the presence of 0.003 mM Fe3+, at pH 6.0 and 25°C

proof_lines: in the absence of metal ion, at pH 6.0 and 25°C


organism: Bacillus sp. (in: firmicutes)

proof_lines: with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.0), at 30°C

proof_lines: with NADP+ as cosubstrate, in 100 mM Tris-HCl (pH 7.0), at 30°C


organism: [Candida] boidinii

sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of K47E. and applied mutation signature K47E to reconstruct the assayed variant sequence.

assay_conditions_summary: 293.15 K; cofactor NAD+

proof_lines: mutant enzyme K47E, at 20°C, after 2 weeks of enzyme storage

proof_lines: mutant enzyme K47E, at 20°C, after 4 months of enzyme storage


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of D195A. and applied mutation signature D195A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer 0.1 M potassium phosphate; cofactor NADP+

proof_lines: mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of D195Q/Y196P. and applied mutation signature D195Q/Y196P to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of D195Q/Y196H. and applied mutation signature D195Q/Y196H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of D195Q. and applied mutation signature D195Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of D195N. and applied mutation signature D195N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of D195Q/Y196S. and applied mutation signature D195Q/Y196S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C


sequence_source: UniProtKB O13437 direct REST lookup; reviewed Swiss-Prot Candida boidinii formate dehydrogenase with EC 1.17.1.9.

proof_lines: wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of D195S. and applied mutation signature D195S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of N187S/T321S. and applied mutation signature N187S/T321S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N187S/T321S, at pH 7.2 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of T321S. and applied mutation signature T321S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of N187S. and applied mutation signature N187S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of K328V. and applied mutation signature K328V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines: mutant enzyme K328V, at 20°C, after 2 weeks of enzyme storage

proof_lines: mutant enzyme K328V, at 20°C, after 4 months of enzyme storage


sequence_variant_note: Resolved canonical sequence from UniProtKB O13437 canonical sequence with row-specific reconstruction of N187D. and applied mutation signature N187D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


organism: Gossypium hirsutum

proof_lines:
at pH 7.0 and 30°C
native enzyme, at pH 7.0 and 25°C


proof_lines: mutant enzyme M225L/M234L/M243L, at pH 7.0 and 25°C


proof_lines: mutant enzyme M225L/M243L, at pH 7.0 and 25°C


organism: Gottschalkia acidurici

substrate_name: benzyl viologen

substrate: benzyl viologen


organism: Kloeckera sp.


organism: Komagataella pastoris


organism: Lathyrus oleraceus

substrate_name: S-formylglutathione

proof_lines: and 1.67 mM at the second catalytic site

proof_lines: and 6.25 mM at the second catalytic site

substrate: S-formylglutathione


organism: Methylobacterium sp.


organism: Mycolicibacterium vaccae

assay_conditions_summary: pH 7; 295.15 K; buffer 0.1 M sodium phosphate; cofactor NADP+

proof_lines: mutant enzyme D221G, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C


proof_lines: mutant enzyme C145S/D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C


organism: Ogataea parapolymorpha

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

proof_lines: pH and temperature not specified in the publication


organism: Paracoccus sp. 12-A

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+


organism: Paracoccus sp. (in: a-proteobacteria)

substrate_name: glyoxylate

substrate: glyoxylate


organism: Pseudomonas sp.


assay_conditions_summary: pH 7; 310.15 K; buffer 0.1 M sodium phosphate; cofactor NAD+

proof_lines: wild type enzyme, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


assay_conditions_summary: pH 7; buffer 0.1 M sodium phosphate; cofactor NAD+

proof_lines: mutant enzyme F311S, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


proof_lines: mutant enzyme F311Y, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


organism: [Candida] methylica

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


organism: Citrobacter sp.


organism: Cupriavidus necator


organism: Cupriavidus oxalaticus

proof_lines: with HCO3- as cosubstrate, pH and temperature not specified in the publication

proof_lines: formate dehydrogenase II, reaction with formate


organism: Desulfovibrio desulfuricans

proof_lines:
at pH 7.0 and 22°C
at pH 8.0 and 22°C


organism: Gelatoporia subvermispora

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NAD+

proof_lines:
pH 6.5, 30°C
substrate NAD+, pH 6.5, 30°C
substrate formate, pH 6.5, 30°C


organism: Glycine max

assay_conditions_summary: pH 7; 303.15 K; buffer 0.1 M sodium phosphate; cofactor NAD+

proof_lines: mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C

proof_lines: mutant enzyme F290N, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


proof_lines: mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C

proof_lines: mutant enzyme F290D, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


proof_lines: mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C

proof_lines: mutant enzyme F290S, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


proof_lines: wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+


proof_lines: mutant enzyme A267M/I272V/F290S, at pH 8.0 and 37°C


proof_lines: mutant enzyme A267M/I272V/F290N, at pH 8.0 and 37°C


proof_lines: mutant enzyme A267M/I272V/F290D, at pH 8.0 and 37°C


proof_lines: mutant enzyme A267M/I272V, at pH 8.0 and 37°C


assay_conditions_summary: pH 7; buffer 0.1 M sodium phosphate

proof_lines: mutant enzyme F290Y, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


proof_lines: mutant enzyme F290T, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


proof_lines: mutant enzyme F290Q, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


proof_lines: mutant enzyme F290E, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication


proof_lines: mutant enzyme F290A, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication