organism: Lupinus albus

substrate_name: GTP

assay_conditions_summary: pH 5; 308.15 K; cofactor ADP

proof_lines:
pH 5.0, 35°C, phytase LP2
pH 5.0, 35°C, phytase LP12
pH 5.0, 35°C, phytase LP11

substrate: GTP


organism: Papiliotrema laurentii

substrate_name: myo-inositol hexakisphosphate

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.

substrate: myo-inositol hexakisphosphate

source: brenda


organism: Peniophora lycii


organism: Phaseolus vulgaris


organism: Pseudomonas sp.


organism: Pseudomonas syringae


organism: Rattus norvegicus


organism: Rhizopus microsporus var. oligosporus


organism: Rhodotorula mucilaginosa


organism: Scheffersomyces spartinae


organism: Schwanniomyces occidentalis


organism: Secale cereale

assay_conditions_summary: pH 6; 310.15 K; buffer 0.1 M sodium acetate

proof_lines: in 0.1 M sodium acetate buffer, pH 6.0, at 37°C


organism: Thermothelomyces heterothallicus


organism: Bacillus amyloliquefaciens

substrate_name: phytate

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

mutation_type: substitution

substrate: phytate


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: free, not complexed with Ca2+, competitive inhibitor

proof_lines: free, not complexed with phytate, competitive inhibitor

substrate: Unknown


organism: Bacillus sp. (in: firmicutes)

assay_conditions_summary: pH 7


organism: Bacillus subtilis


organism: Blastobotrys adeninivorans


organism: Brassica rapa subsp. oleifera

proof_lines:
phytase 1
phytase 2


organism: Brassica sp.


organism: Aspergillus ficuum

proof_lines:
pH 5.0, 58°C
pH 5.0, 58°C, native enzyme
pH 5.0, 58°C, recombinant enzyme


organism: Aspergillus fumigatus


organism: Aspergillus niger

assay_conditions_summary: pH 3.5; 310.15 K; buffer 0.2 M glycine-HCl

proof_lines: wild type enzyme, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C

proof_lines: wild type enzyme, in 0.2 M glycine-HCl, at pH 2.5

proof_lines: wild type enzyme, in 0.2 M glycine-HCl, at pH 3.2


assay_conditions_summary: pH 3.5; 310.15 K; buffer conditions

proof_lines: mutant enzyme E228K, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C

proof_lines: mutant enzyme E228K, in 0.2 M citrate buffer at pH 5.5 and 37°C


proof_lines: mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 2.5

proof_lines: mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 3.2


proof_lines: mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 3.2

proof_lines: mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 2.5


proof_lines: pH 2.5, 55°C. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate h


organism: Avena sativa

substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


enzyme_display_name: u-plasminogen activator

organism: Homo sapiens

enzyme: u-plasminogen activator


proof_lines:
pH 7.4, 37°C, pro-uPA
pH 8.8, nonphosphorylated uPA
pH 7.5, nonphosphorylated uPA


enzyme_display_name: leukocyte elastase

proof_lines: mutant enzyme F192A, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C

enzyme: leukocyte elastase


proof_lines: mutant enzyme A213V, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


proof_lines: wild type enzyme, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


proof_lines: mutant enzyme F215A, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


assay_conditions_summary: pH 9; 310.15 K; buffer 50 mM sodium phosphate


organism: Mus musculus


organism: Oryctolagus cuniculus


organism: Ovis aries


organism: Rattus norvegicus

proof_lines:
pH 8.0, 37°C
pH 7.8
2 disaccharide units, pH 8.0, 37°C


protein_accession_database: UniProt

proof_lines:
pH 7.4, 37°C, enzyme mutant H99Y
pH 7.4, 37°C, mutant H99Y


proof_lines: pH 7.4, 25°C, mutant K300H, two-chain activator

proof_lines: pH 7.4, 25°C, mutant K300H, single-chain activator


proof_lines: pH 7.4, 25°C, mutant K313A, two-chain activator

proof_lines: pH 7.4, 25°C, mutant K313A, single-chain activator


proof_lines: pH 7.4, 25°C, mutant K300A, two-chain activator

proof_lines: pH 7.4, 25°C, mutant K300A, single-chain activator


proof_lines: pH 7.4, 25°C, wild-type, single-chain activator

proof_lines: pH 7.4, 25°C, wild-type and mutant S303E, two-chain activator

proof_lines: pH 7.4, 25°C, wild-type, two-chain activator


proof_lines: pH 7.4, 25°C, mutant K300A and K313A, single-chain activator


proof_lines: pH 7.4, 25°C, mutant E301H, single-chain activator

proof_lines: pH 7.4, 25°C, mutant E301H, two-chain activator


proof_lines: pH 7.4, 25°C, mutant K300W, two-chain activator

proof_lines: pH 7.4, 25°C, mutant K300W, single-chain activator


proof_lines: pH 7.4, 25°C, mutant E301D, single-chain activator

proof_lines: pH 7.4, 25°C, mutant E301D, two-chain activator


proof_lines: pH 7.4, 25°C, mutant Y306G, two-chain activator

proof_lines: pH 7.4, 25°C, mutant Y306G, single-chain activator


proof_lines: pH 7.4, 25°C, mutant S303E, single-chain activator


proof_lines: pH 7.4, 25°C, mutant E301A, two-chain activator

proof_lines: pH 7.4, 25°C, mutant E301A, single-chain activator


enzyme_display_name: glucan 1,4-alpha-maltohydrolase

organism: Thermus sp.

substrate_name: acarbose

enzyme: glucan 1,4-alpha-maltohydrolase

substrate: acarbose


substrate_name: beta-cyclodextrin

mutation_type: deletion

proof_lines: pH 6.0, 60°C, hydrolysis, truncated mutant ThMA-DELTA124

proof_lines: pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl

substrate: beta-cyclodextrin


substrate_name: starch

substrate: starch


proof_lines: pH 6.0, 60°C, hydrolysis, variants DM and 4B74


substrate_name: maltoheptaose

substrate: maltoheptaose


substrate_name: maltohexaose

proof_lines: pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl

substrate: maltohexaose


substrate_name: maltotriose

substrate: maltotriose


enzyme_display_name: mannan endo-1,4-beta-mannosidase

organism: Aspergillus oryzae

substrate_name: konjac flour

enzyme: mannan endo-1,4-beta-mannosidase

substrate: konjac flour


organism: Bifidobacterium animalis subsp. lactis

substrate_name: Mannopentaose

substrate: Mannopentaose


organism: Cellulomonas fimi


organism: Cellvibrio japonicus

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label D283A and applied mutation signature D283A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P49424 canonical wild-type sequence, cross-checked against RCSB 1J9Y and PMID 11382747 Man26A identity

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


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label H211N and applied mutation signature H211N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label H143A and applied mutation signature H143A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label Y285A and applied mutation signature Y285A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label W217A and applied mutation signature W217A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label E212A and applied mutation signature E212A to reconstruct the assayed variant sequence.


verification_status: unverified

status: unverified


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label W156A and applied mutation signature W156A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label D283H and applied mutation signature D283H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label W162A and applied mutation signature W162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label H211A and applied mutation signature H211A to reconstruct the assayed variant sequence.


enzyme_display_name: dipeptidyl-peptidase III

proof_lines:
endomorphin-1
with Co2+
pH 7.4, 37°C

enzyme: dipeptidyl-peptidase III


organism: Pediococcus acidilactici

substrate_name: Arg-Arg-beta-naphthylamide

substrate: Arg-Arg-beta-naphthylamide


organism: Platyrrhini


proof_lines: wild-type in presence of Cu2+, pH 7.4, 25°C


substrate_name: Gly-Gly-Phe-Leu

substrate: Gly-Gly-Phe-Leu


organism: Cricetulus griseus


organism: Equus caballus

substrate_name: N-succinyl-Ala-Ala-Ala 4-nitroanilide

proof_lines:
pH 7.5, 25°C, proteinase 2B
pH 7.5, 25°C, proteinase 2A
pH 7.5, 25°C, proteinase B

substrate: N-succinyl-Ala-Ala-Ala 4-nitroanilide


organism: Gallus gallus

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


proof_lines: mutant enzyme N98T, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


proof_lines: mutant enzyme F215Y, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


proof_lines: mutant enzyme F192K, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


organism: Glycine max

substrate_name: locust bean gum

substrate: locust bean gum


organism: Hypothenemus hampei

substrate_name: guar gum

sequence_source: NCBI Protein ADF22325.1

substrate: guar gum


organism: Medicago sativa

substrate_name: soluble mannan

substrate: soluble mannan


proof_lines: pH and temperature not specified in the publication


organism: Rhizomucor miehei

sequence_source: NCBI Protein AGC24277.1


organism: Shouchella clausii

substrate_name: konjac glucomannan

substrate: konjac glucomannan


organism: Solanum lycopersicum

sequence_source: UniProt Q8L5J1


organism: Streptomyces sp. NRRL B-24484

substrate_name: galactomannan

substrate: galactomannan


organism: Blaberus craniifer

substrate_name: Proctolin

substrate: Proctolin


organism: Capra hircus

proof_lines: in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C


organism: Cavia porcellus

substrate_name: Arg-Arg-4-methylcoumarin 7-amide

substrate: Arg-Arg-4-methylcoumarin 7-amide


organism: Drosophila melanogaster

substrate_name: Arg-Tyr-Leu-Pro-Thr

sequence_source: UniProt Q9VHR8

substrate: Arg-Tyr-Leu-Pro-Thr


organism: Homo sapiens


proof_lines:
wild-type, pH 7.2, 37°C
wild-type, pH 4.75, 37°C


proof_lines:
mutant D179A, pH 4.75, 37°C
mutant D179A, pH 7.2, 37°C


proof_lines:
mutant DELTA176-181, pH 4.75, 37°C
mutant DELTA176-181, pH 7.2, 37°C


proof_lines: pH 7.4, 25°C, mutant K300A and S303E, two-chain activator


organism: Mus musculus

substrate_name: L-pyroGlu-Gly-L-Arg-p-NA

substrate: L-pyroGlu-Gly-L-Arg-p-NA


substrate_name: Unknown

substrate: Unknown


organism: Rattus norvegicus


enzyme_display_name: enteropeptidase

organism: Bos taurus

substrate_name: thiobenzyl benzyloxycarbonyl-L-lysinate

enzyme: enteropeptidase

substrate: thiobenzyl benzyloxycarbonyl-L-lysinate


assay_conditions_summary: pH 8; 310.15 K; buffer pH 8

proof_lines: 37 °C, 100 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 120 nM soybean trypsin inhibitor, 0.45 nM enteropeptidase


assay_conditions_summary: pH 8; 310.15 K; buffer conditions

proof_lines: 25°C, 28 mM sodium succinate (pH 5.6), 10 mM CaCl2

proof_lines: 0.00036 1/sec/mg, incubates 30 min at 37°C, pH 9.0, spectrophotometrically measured at 415 nm


substrate_name: Caspase-9; Caspase-3 cleaved

substrate: Caspase-9; Caspase-3 cleaved


enzyme_display_name: macrophage elastase

enzyme: macrophage elastase


enzyme_display_name: ADAM 17 endopeptidase

enzyme: ADAM 17 endopeptidase


organism: Sus scrofa


enzyme_display_name: biotinidase

substrate_name: p-(N-biotinylamino)benzoic acid

proof_lines:
76000 Da biotinidase
human serum
human plasma

enzyme: biotinidase

substrate: p-(N-biotinylamino)benzoic acid


organism: Lacticaseibacillus casei

proof_lines: pH 7.0, 37°C, enzyme from membrane fraction

proof_lines: pH 7.0, 37°C, enzyme from supernatant fraction


organism: Lactobacillus casei

substrate_name: H2O; Biotinyl-6-aminoquinoline

substrate: H2O; Biotinyl-6-aminoquinoline


proof_lines: pH 7.0, 37°C, enzyme from membrane and supernatant fraction


substrate_name: tosyl-Arg methyl ester

substrate: tosyl-Arg methyl ester


organism: Canis lupus familiaris

substrate_name: LSDGIDE

proof_lines: pH 7.2, 37°C, recombinant enzyme, calculated by BRENDA

substrate: LSDGIDE


proof_lines:
pH 7.5
pH 7.0
pH 7.0, absence of EDTA


enzyme_display_name: cathepsin D

organism: Gallus gallus

enzyme: cathepsin D


proof_lines:
pH 4.0, 37°C
37°C, pH 4.0
human fibroblast


organism: Lamellidens corrianus

substrate_name: hemoglobin

substrate: hemoglobin


organism: Oryctolagus cuniculus

proof_lines: enzyme from animals with experimental neurofibrillary changes


proof_lines:
40°C, pH 4.0, spleen cathepsin D
enzyme from AH-130 hepatoma cells
40°C, pH 4.0, gastric cathepsin D


organism: Struthio camelus

assay_conditions_summary: pH 3.5; 318.15 K; buffer 0.05 M sodium acetate

proof_lines: in 0.05 M sodium acetate buffer, pH 3.5, at 45°C


substrate_name: EEISEVNLDAEFRG

substrate: EEISEVNLDAEFRG


organism: Todarodes pacificus


substrate_name: DQ-collagen IV

substrate: DQ-collagen IV


sequence_source: UniProt P39900 catalytic-domain context; not accepted as resolved sequence because the row remains manually blocked.

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


enzyme_display_name: cellodextrin phosphorylase

organism: Thermosipho africanus

substrate_name: cellotetraose

source_db: oed

enzyme: cellodextrin phosphorylase

substrate: cellotetraose

source: oed


substrate_name: alpha-D-glucose

substrate: alpha-D-glucose


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


substrate_name: cellotriose

substrate: cellotriose


organism: Ruminiclostridium cellulolyticum


substrate_name: cellopentaose

substrate: cellopentaose


organism: Acetivibrio thermocellus

substrate_name: phenyl beta-D-glucopyranoside

substrate: phenyl beta-D-glucopyranoside


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

proof_lines:
apparent value, at pH 7.5 and 21°C
Raw SKiD Env: Temp=21°C, pH=7.5

source_databases_merged: brenda skid


substrate_name: cellobiose

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

substrate: cellobiose


organism: Thermoclostridium stercorarium

substrate_name: 4-nitrophenyl beta-D-glucoside

substrate: 4-nitrophenyl beta-D-glucoside


substrate_name: octyl beta-D-glucoside

substrate: octyl beta-D-glucoside


sequence_source: UniProtKB:B7IED6 direct lookup; sequence exists but was not emitted in this exact-accession review lane

proof_lines:
phosphoroyltic reaction, pH 7.5, 60°C
synthetic reaction, pH 7.5, 60°C


substrate_name: alpha-D-xylose

substrate: alpha-D-xylose


enzyme_display_name: plasmepsin I

organism: Plasmodium falciparum

sequence_source: UniProtKB:P39898 direct lookup; canonical sequence exists but variant/truncated K110pN row sequence was not reconstructed

proof_lines: pH 4.5, 37°C, recombinant truncated proPfPM1 K110pN mutant

enzyme: plasmepsin I


organism: Unknown

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: semenogelase

organism: Homo sapiens

enzyme: semenogelase


substrate_name: glucose-6-phosphate (at pH 6.5)

source_db: uniprot

data_origin: experimental

substrate: glucose-6-phosphate (at pH 6.5)

source: uniprot


organism: Mus musculus

substrate_name: D-glucose 6-phosphate

proof_lines: wild-type, mixed lauryl maltose neopentyl glycol and -palmitoyl-2-oleoyl-glycero-3-phosphocholine detergent micelles, pH 6.5, 30Â°C

proof_lines: wild-type, lauryl maltose neopentyl glycol detergent micelles, pH 6.5, 30Â°C

proof_lines: wild-type, mixed lauryl maltose neopentyl glycol and cholesteryl hemisuccinate detergent micelles, pH 6.5, 30Â°C

substrate: D-glucose 6-phosphate


proof_lines: mutant N96A, lauryl maltose neopentyl glycol detergent micelles, pH 6.5, 30Â°C


organism: Rattus norvegicus

substrate_name: H2O; D-Glucose 6-phosphate

substrate: H2O; D-Glucose 6-phosphate


organism: Cavia porcellus


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

proof_lines:
pH 5.5, in disrupted vesicles
pH 6.5, in disrupted vesicles
pH 6.5, in not disrupted vesicles


substrate_name: D-Glucose 6-phosphate; H2O

substrate: D-Glucose 6-phosphate; H2O


proof_lines: 8 times less active compared to G6PC1 under the same experimental conditions.


enzyme_display_name: sedolisin

organism: Pseudomonas sp. (strain 101)

proof_lines: kcat is 59.3 sec(-1) with Lys-Pro-Ala-Leu-Phe-p-nitrophenylalanine-Arg-Leu as substrate (PubMed:10488127). kcat is 14.5 sec(-1) with Lys-Pro-Ala-Lys-Phe-(4-nitro)Phe-Arg-Leu as substrate (PubMed:1562589). kcat is 5.5 sec(-1) with Lys-Pro-Al

enzyme: sedolisin


organism: Escherichia coli (strain K12)

substrate_name: KDPG

proof_lines: kcat is 83 sec(-1) with KDPG as substrate (PubMed:17962400). kcat is 80 sec(-1) with KDPG as substrate (PubMed:17981470). kcat is 11 sec(-1) with KHPB as substrate (PubMed:17962400). kcat is 0.0063 sec(-1) with KDPGal as substrate (PubMed:1

substrate: KDPG


organism: Pseudomonas sp.


organism: Escherichia coli

substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: celloheptaose

proof_lines: degradation direction, cellulose binding module fusion protein (binding module derived from Clostridium thermocellum CbhA (UniProt: A3DCH2)), pH 7.2, 30°C

proof_lines: degradation direction, cellulose binding module fusion protein (binding module derived from Cellvibrio mixtus Cel5B (UniProt: O07653)), pH 7.2, 30°C

proof_lines: synthesis direction, cellulose binding module fusion protein (binding module derived from Clostridium thermocellum CbhA (UniProt: A3DCH2)), pH 7.2, 30°C

substrate: celloheptaose


proof_lines: synthesis direction, wild type protein, pH 7.2, 30°C

proof_lines: degradation direction, wild type protein, pH 7.2, 30°C


substrate_name: alpha-D-galactose 1-phosphate

substrate: alpha-D-galactose 1-phosphate


organism: Aspergillus oryzae

substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Bos taurus

substrate_name: Carbamoyl phosphate

proof_lines:
enzyme from testes
enzyme from brain
enzyme from pancreas

substrate: Carbamoyl phosphate


organism: Dictyostelium discoideum

proof_lines:
pH 7.5, smlA mutant enzyme
pH 7.5, coutin mutant enzyme


proof_lines: cleared lysate of countin- cells with low activity of counting factor

proof_lines: crude cytosol of cells with low counting factor

proof_lines: crude cytosol of countin- cells with low activity of counting factor


proof_lines:
crude cytosol of wild-type
pH 7.5, wild-type enzyme
cleared lysate of wild-type


organism: Gallus gallus


proof_lines:
in detergent treated microsomes
in intact microsomes


organism: Limulus sp.


organism: Mustela vison

substrate_name: H2O; Glucose 6-phosphate

substrate: H2O; Glucose 6-phosphate


substrate_name: pyruvate

proof_lines: pH 7.5, wild-type and K133Q/T161K mutant

substrate: pyruvate


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Haloferax volcanii


proof_lines:
enzyme in disrupted microsomes
pH 6.5, in disrupted vesicles
microsomal enzyme suspension


organism: Streptococcus bovis

substrate_name: Glucose 6-phosphate; H2O

substrate: Glucose 6-phosphate; H2O


organism: Sus scrofa

proof_lines:
disrupted microsomes
intact microsomes


organism: Aspergillus fumigatus

substrate_name: Phe-Pro-Ala-p-nitroanilide

substrate: Phe-Pro-Ala-p-nitroanilide


organism: Pseudomonas sp. 101


organism: Homo sapiens

assay_conditions_summary: pH 7.8; 310.15 K; buffer 50 mM Tris

proof_lines: in 50 mM Tris buffer, 0.1 M NaCl, pH 7.8

proof_lines: prostate-specific antigen without inhibitor

proof_lines: prostate-specific antigen and inhibitor 2-(2-methyl-3-nitrophenyl)-4H-3,1-benzoxazin-4-one (25 micromol)


organism: Plasmodium falciparum

proof_lines:
pH 4.4, 37°C, recombinant enzyme
pH 4.4, 37°C, naturally occuring enzyme
pH 4.4, 37°C


organism: Rattus norvegicus

proof_lines: pH 7.0, 37°C, enzyme from tigh muscle, female rat

proof_lines: pH 7.0, 37°C, enzyme from abdominal skin, female rat

proof_lines: pH 7.0, 37°C, enzyme from upper labial skin, male rat


organism: Rattus rattus

substrate_name: lipoyllysine

assay_conditions_summary: pH 6

proof_lines:
pH 6.0
crude liver extract
pH 9.5

substrate: lipoyllysine


substrate_name: epsilon-N-biotinyl-L-lysine

proof_lines:
serum
porcine liver
porcine serum

substrate: epsilon-N-biotinyl-L-lysine


enzyme_display_name: diisopropyl-fluorophosphatase

organism: Alteromonas sp.

substrate_name: diisopropyl fluorophosphate

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

enzyme: diisopropyl-fluorophosphatase

substrate: diisopropyl fluorophosphate


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: KDG (at 60 degrees Celsius and pH 6.2)

substrate: KDG (at 60 degrees Celsius and pH 6.2)


organism: Pseudomonas sp.


organism: Escherichia coli

proof_lines: mutant enzyme T161A, in 20 mM HEPES, pH 7.5, at 23°C


organism: Helicobacter pylori


organism: Pseudomonas fluorescens


organism: Pseudomonas putida


organism: Thermotoga maritima


organism: Zymomonas mobilis


enzyme_display_name: xylose isomerase

organism: Actinoplanes missouriensis

substrate_name: L-arabinose

enzyme: xylose isomerase

substrate: L-arabinose


proof_lines:
wild-type
wild-type enzyme


organism: Brevundimonas diminuta


organism: Doryteuthis pealeii


organism: Loligo vulgaris

proof_lines: pH 8, 35°C, effects of pH, temperature and ionic strength on kcat are studied


organism: Pseudoalteromonas undina


organism: Azotobacter vinelandii


proof_lines:
KA2 variant, pH 7.5, 25°C
KA3 variant, pH 7.5, 25°C
KA1-1 variant, pH 7.5, 25°C


proof_lines: wild type enzyme, in 100 mM HEPES, pH 7.5


proof_lines: mutant enzyme S184D, in 100 mM HEPES, pH 7.5


proof_lines: mutant enzyme S184L, in 100 mM HEPES, pH 7.5


proof_lines: mutant enzyme S184A, in 100 mM HEPES, pH 7.5


proof_lines: mutant enzyme T161V, in 20 mM HEPES, pH 7.5, at 23°C


substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:15713782 and selected BRENDA note anchor the F26W mutation; variant sequence reconstructed in this review. and applied mutation signature F26W to reconstruct the assayed variant sequence.

substrate: D-glucose


substrate_name: D-xylose

sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the E217S mutation; variant sequence reconstructed in this review. and applied mutation signature E217S to reconstruct the assayed variant sequence.

substrate: D-xylose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the H220Q mutation; variant sequence reconstructed in this review. and applied mutation signature H220Q to reconstruct the assayed variant sequence.

proof_lines:
mutant H220Q
D-glucose, mutant H220Q
D-xylose, mutant H220Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the H220N mutation; variant sequence reconstructed in this review. and applied mutation signature H220N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the E181D mutation; variant sequence reconstructed in this review. and applied mutation signature E181D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the D255N mutation; variant sequence reconstructed in this review. and applied mutation signature D255N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the E181Q mutation; variant sequence reconstructed in this review. and applied mutation signature E181Q to reconstruct the assayed variant sequence.

proof_lines:
mutant E181Q
D-xylose, mutant E181Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the D257N mutation; variant sequence reconstructed in this review. and applied mutation signature D257N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the D257E mutation; variant sequence reconstructed in this review. and applied mutation signature D257E to reconstruct the assayed variant sequence.


organism: Arthrobacter sp.

sequence_source: UniProtKB:P12070 reviewed entry; PubMed PMID:1854338 characterizes Arthrobacter strain NRRL B3728 xylose/glucose isomerase and UniProt cites that paper for characterization.

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


organism: Bacillus sp. (in: firmicutes)

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


organism: Bacteroides stercoris

sequence_source: GenBank JF441172.1 / protein AEK21499.1; PubMed PMID:21655987 paper-linked Bacteroides stercoris strain HJ-15 xylA complete CDS.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 100 mM Tris-HCl

proof_lines: in 100 mM Tris-HCl buffer (pH 7.5), 10 mM MgCl2, at 30°C


organism: Piromyces sp.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from UniProtKB:A0ACD6B9F5 plus PMID:22685138 Table 2 and applied mutation signature E129D/V433I/E15D/E114G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E129D/V433I/E15D/E114G, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0ACD6B9F5 plus PMID:22685138 Table 2 and applied mutation signature E129D/V433I/E15D/E114G/T142S/A177T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E129D/V433I/E15D/E114G/T142S/A177T, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0ACD6B9F5 plus PMID:22685138 Table 2 and applied mutation signature E129D/V433I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E129D/V433I, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


sequence_source: UniProtKB:A0ACD6B9F5 plus PMID:22685138 Table 2

proof_lines: wild type enzyme, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


organism: Streptomyces albus


organism: Streptomyces corchorusii


organism: Streptomyces flavogriseus

proof_lines:
soluble enzyme
immobilized enzyme


organism: Streptomyces olivochromogenes


organism: Streptomyces pseudogriseolus

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, wild-type

proof_lines: native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


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

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D65A


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutants E221A and D56N


enzyme_display_name: chymotrypsin C

organism: Homo sapiens

substrate_name: succinyl-Ala-Ala-Pro-Phe 4-nitroanilide

enzyme: chymotrypsin C

substrate: succinyl-Ala-Ala-Pro-Phe 4-nitroanilide


organism: Bifidobacterium adolescentis


organism: Geobacillus stearothermophilus

substrate_name: D-xylulose

substrate: D-xylulose


organism: Heyndrickxia coagulans


organism: Lachnoclostridium phytofermentans

proof_lines:
pH 7.5, native enzyme
pH 7.5, recombinant enzyme


organism: Lactococcus lactis


organism: Lactococcus lactis subsp. lactis


organism: Levilactobacillus brevis

substrate_name: D-ribose

substrate: D-ribose


organism: Limosilactobacillus reuteri


organism: Opuntia ficus-indica

proof_lines: enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C


organism: Parabacteroides sp.

substrate_name: alpha-D-xylopyranose

substrate: alpha-D-xylopyranose


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


enzyme_display_name: acetate kinase (diphosphate)

organism: Entamoeba histolytica

substrate_name: acetate

smiles: CC(=O)O

enzyme: acetate kinase (diphosphate)

substrate: acetate


substrate_name: phosphate

proof_lines: mutant enzyme Q323A/M324A, at pH 7.0 and 37Â°C

proof_lines: mutant enzyme Q323A/M324A, at pH 5.5 and 45Â°C

substrate: phosphate


substrate_name: diphosphate

substrate: diphosphate


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


proof_lines:
wild type enzyme, at pH 5.5 and 45Â°C
wild type enzyme, at pH 7.0 and 37Â°C


substrate_name: acetyl phosphate

smiles: CC(=O)OP(=O)(O)O

substrate: acetyl phosphate


enzyme_display_name: ribonuclease H

organism: Aquifex aeolicus

substrate_name: RNA-DNA hybrid

proof_lines: wild type enzyme, in 10 mM Tris/HCl (pH 9.0) containing 10 mM MgCl2, 100 mM KCl, 1 mM beta-mercaptoethanol and 0.05 mg/ml bovine serum albumin, at 30°C

proof_lines: wild type enzyme, in 10 mM Tris/HCl (pH 9.0) containing 10 mM MnCl2, 100 mM KCl, 1 mM beta-mercaptoethanol and 0.05 mg/ml bovine serum albumin, at 30°C

enzyme: ribonuclease H

substrate: RNA-DNA hybrid


proof_lines: mutant enzyme Y45A, in 10 mM Tris/HCl (pH 9.0) containing 2 mM MnCl2, 100 mM KCl, 1 mM beta-mercaptoethanol and 0.05 mg/ml bovine serum albumin, at 30°C

proof_lines: mutant enzyme Y45A, in 10 mM Tris/HCl (pH 9.0) containing 10 mM MgCl2, 100 mM KCl, 1 mM beta-mercaptoethanol and 0.05 mg/ml bovine serum albumin, at 30°C


organism: Archaeoglobus fulgidus

substrate_name: RNA-DNA*DNA hybrid

proof_lines: recombinant mutant R46A and K143A, pH 8.0, 30°C

substrate: RNA-DNA*DNA hybrid


assay_conditions_summary: pH 7; cofactor ATP

proof_lines: mutant enzyme Q323G/M324I, at pH 7.0 and 37Â°C

proof_lines: mutant enzyme Q323G/M324I, at pH 5.5 and 45Â°C


assay_conditions_summary: pH 5.5; 355.15 K; cofactor ATP


proof_lines: mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37Â°C


assay_conditions_summary: pH 7; 355.15 K; cofactor ATP


organism: Aeropyrum pernix


assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


proof_lines:
pH 6.0, 37°C, recombinant enzyme
pH 7.0, 37°C, recombinant enzyme


organism: Shewanella sp.

substrate_name: M13 DNA-RNA hybrid

proof_lines:
pH 8.5, 15°C, recombinant enzyme
pH 8.5, 30°C, recombinant enzyme

substrate: M13 DNA-RNA hybrid


organism: Thermotoga maritima

substrate_name: M13 DNA/RNA hybrid

proof_lines: wild-type enzyme, pH 9.0, 30°C, in presence of 50 mM KCl

substrate: M13 DNA/RNA hybrid


organism: Homo sapiens


substrate_name: succinyl-Ala-Ala-Pro-Gln 4-nitroanilide

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

substrate: succinyl-Ala-Ala-Pro-Gln 4-nitroanilide


organism: Escherichia coli

proof_lines: pH 8.5, 15°C or 30°C, recombinant enzyme


organism: Geobacillus stearothermophilus

proof_lines: pH 8.5, 30°C, Mg2+, recombinant mutant K50A


proof_lines: pH 8.5, 30°C, Mg2+, recombinant wild-type enzyme


proof_lines: pH 8.5, 30°C, Mg2+, recombinant mutant V42A


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


proof_lines: mutant R291H, pH 8.0, temperature not specified in the publication


proof_lines: mutant K143I, pH 8.0, temperature not specified in the publication


substrate_name: DNA-RNA hybrid duplex RD12

proof_lines: at 28°C, pH not specified in the publication

substrate: DNA-RNA hybrid duplex RD12


organism: Pyrococcus furiosus

substrate_name: RNA-DNA heteroduplex

proof_lines: 50°C, pH 8.0, wild-type enzyme, divalent cation: Mn2+

proof_lines: 50°C, pH 8.0, wild-type enzyme, divalent cation: Mg2+

substrate: RNA-DNA heteroduplex


proof_lines: 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme A115E


proof_lines: 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme R113E


proof_lines: 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme F114E


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


organism: Xenotropic MuLV-related virus (isolate VP62)

substrate_name: RNA/DNA duplex

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

substrate: RNA/DNA duplex


sequence_source: UniProtKB:Q99895 direct lookup; canonical identity context only, variant sequence not reconstructed


proof_lines: mutant enzyme T58M, pH and temperature not specified in the publication


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: a hybrid RNA/DNA substrate

sequence_source: source_record; direct UniProt P9WLH5 FASTA match

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

substrate: a hybrid RNA/DNA substrate


enzyme_display_name: dipeptidyl-peptidase II

substrate_name: Ser-Pro-p-nitroanilide

enzyme: dipeptidyl-peptidase II

substrate: Ser-Pro-p-nitroanilide


enzyme_display_name: cystinyl aminopeptidase

substrate_name: H2O; Arginine-4-nitroanilide

enzyme: cystinyl aminopeptidase

substrate: H2O; Arginine-4-nitroanilide


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature V87G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature H172A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature H117A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature I116A to reconstruct the assayed variant sequence.


proof_lines: co-substrate: hexanoate, 45°C, pH 7.5, mutant T223P


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature V87A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature I116L to reconstruct the assayed variant sequence.


substrate_name: valerate

proof_lines: co-substrate: propionate, 37°C, pH 7.5, wild-type

substrate: valerate


proof_lines:
pH 6.5-7.5, 30°C, recombinant enzyme
pH 7, 30°C


organism: Bos taurus

substrate_name: poly(rAdT)

substrate: poly(rAdT)


organism: Drosophila melanogaster

substrate_name: DNA-RNA hybrid duplex

proof_lines:
at pH 8.0 and 30°C
at pH 8.0 and 37°C

substrate: DNA-RNA hybrid duplex


proof_lines: pH 8.5, 30°C, recombinant soluble non-tagged enzyme


organism: Streptomyces pseudogriseolus

substrate_name: D-glucose

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A

substrate: D-glucose


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D56N


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant E221A


substrate_name: D-xylose

proof_lines: mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

substrate: D-xylose


proof_lines: mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


enzyme_display_name: agmatine N(4)-coumaroyltransferase

organism: Hordeum vulgare

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines:
isoenzyme 1
isoenzyme 2
recombinant enzyme

enzyme: agmatine N(4)-coumaroyltransferase


substrate_name: feruloyl-CoA

proof_lines: wild type enzyme isoform ACT2, at pH 7.5 and 25°C

substrate: feruloyl-CoA


proof_lines: mutant enzyme E374A of isoform ACT1-1, at pH 7.5 and 25°C


proof_lines: wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C


enzyme_display_name: 3',5'-cyclic-AMP phosphodiesterase

organism: Dictyostelium discoideum

substrate_name: Adenosine 3',5'-phosphate; H2O

enzyme: 3',5'-cyclic-AMP phosphodiesterase

substrate: Adenosine 3',5'-phosphate; H2O


substrate_name: cAMP; H2O

substrate: cAMP; H2O


substrate_name: agmatine

proof_lines: mutant enzyme E372A of isoform ACT1-1, at pH 7.5 and 25°C

substrate: agmatine


proof_lines: mutant enzyme W376A of isoform ACT1-1, at pH 7.5 and 25°C


organism: Oryza sativa Japonica Group


organism: Triticum aestivum

substrate_name: cinnamoyl-CoA

substrate: cinnamoyl-CoA


substrate_name: ADP-L-glycero-beta-D-manno-heptose

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

substrate: ADP-L-glycero-beta-D-manno-heptose


substrate_name: alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]

proof_lines: pH 7.5, 37°C, mutant enzyme K64A/R63A/R61A


substrate: alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]


substrate_name: H2O; Adenosine 3',5'-phosphate

proof_lines: pH and temperature not specified in the publication

substrate: H2O; Adenosine 3',5'-phosphate


substrate_name: adenosine 3',5'-cyclic phosphate

substrate: adenosine 3',5'-cyclic phosphate


proof_lines: pH 7.5, 37°C, mutant enzyme K64A/R63A/R61A/R60A


proof_lines: pH and temperature not specified in the publication, in absence of detergent

proof_lines: pH and temperature not specified in the publication, with Triton X-100


proof_lines: pH 7.5, 37°C, mutant enzyme K64A/R63A/R61/R60A


proof_lines: pH 7.5, 37°C, mutant enzyme R60A/R63A/R64A


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

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

source_databases_merged: sabio_rk brenda skid


substrate_name: cAMP

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

substrate: cAMP


proof_lines: mutant enzyme T748A, in 20 mM Tris-HCl, pH 7.5, 4 mM MnCl2, at 24°C


proof_lines: wild type PDE8A1 catalytic domain, in 20 mM Tris-HCl, pH 7.5, 4 mM MnCl2, at 24°C


substrate_name: guanosine 3',5'-cyclic phosphate

substrate: guanosine 3',5'-cyclic phosphate


organism: Leishmania major


enzyme_display_name: N-methylcarbamate hydrolase

organism: Novosphingobium sp. KN65.2

substrate_name: oxamyl

smiles: CN=C(O)O/N=C(\SC)C(=O)N(C)C

enzyme: N-methylcarbamate hydrolase

substrate: oxamyl


substrate_name: carbofuran

substrate: carbofuran


organism: Pseudomonas sp. C5pp

substrate_name: Carbaryl

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

proof_lines: recombinant enzyme rCHDELTA(Tmd)a, at pH 7.5, temperature not specified in the publication

substrate: Carbaryl


organism: Pseudomonas sp. XWY-1


organism: Mus musculus


organism: Pseudomonas aeruginosa

proof_lines: the addition of FeCl2 does not significantly influence substrate affinity of CdpA increases the rate of the 5-AMP production, pH and temperature not specified in the publication


organism: Rattus norvegicus


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

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


organism: Trypanosoma cruzi


organism: Trypanosoma brucei


organism: Marchantia polymorpha


organism: Rhizobium sp. AC100

proof_lines:
at pH 7.5 and 30Â°C
at pH 7.0 and 30°C


enzyme_display_name: apyrase

organism: Aedes albopictus

substrate_name: ATP; H2O

assay_conditions_summary: cofactor ATP

enzyme: apyrase

substrate: ATP; H2O


organism: Arabidopsis thaliana


substrate_name: IDP

substrate: IDP


organism: Bacillus thuringiensis

substrate_name: H2O; ATP

substrate: H2O; ATP


organism: Sphingobium sp. CFD-1


organism: Heligmosomoides polygyrus bakeri

substrate_name: ATP

assay_conditions_summary: pH 7.5; 297.15 K; cofactor ATP

substrate: ATP


organism: Homo sapiens

substrate_name: ADP; H2O

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

proof_lines: pH 6.5, temperature not specified in the publication, NTPDase8

substrate: ADP; H2O


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


proof_lines: pH 6.5, temperature not specified in the publication, NTPDase3


proof_lines: pH 6.5, temperature not specified in the publication, NTPDase2


organism: Bos taurus


organism: Canis familiaris


organism: Gallus gallus


substrate_name: dCTP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: pH 6.5, temperature not specified in the publication, NTPDase1

substrate: dCTP


substrate_name: ADP

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ADP

proof_lines: recombinant mutant EDC DELTA MIL, pH 7.4, 25°C

substrate: ADP


substrate_name: TDP

substrate: TDP


substrate_name: GDP

substrate: GDP


proof_lines: in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25°C

proof_lines: in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25°C


substrate_name: UTP

substrate: UTP


proof_lines: recombinant mutant EDC Y314F, pH 7.4, 25°C


substrate_name: GTP

substrate: GTP


proof_lines:
at pH 7.4 and 25°C
Raw SKiD Env: Temp=25°C, pH=7.4


substrate_name: AMPCPP

substrate: AMPCPP


substrate_name: ITP

substrate: ITP


proof_lines: recombinant mutant EDC K257M, pH 7.4, 25°C


substrate_name: UDP

substrate: UDP


proof_lines: recombinant mutant EDC Y409F, pH 7.4, 25°C


substrate_name: H2O; UTP

substrate: H2O; UTP


assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP


organism: Saccharomyces cerevisiae


organism: Sus scrofa


enzyme_display_name: geranylgeranyl diphosphate synthase

organism: Plasmodium falciparum

substrate_name: isopentenyl diphosphate

proof_lines: pH 7.5, 37°C, recombinant enzyme, with dimethylallyl diphosphate

proof_lines: pH 7.5, 37°C, recombinant enzyme, with isopentenyl diphosphate

proof_lines: pH 7.5, 37°C, recombinant enzyme, with (2E,6E)-farnesyl diphosphate

enzyme: geranylgeranyl diphosphate synthase

substrate: isopentenyl diphosphate


substrate_name: Isopentenyl diphosphate

smiles: C=C(C)CCOP(=O)(O)OP(=O)(O)O

substrate: Isopentenyl diphosphate


substrate_name: trans,trans-Farnesyl diphosphate

substrate: trans,trans-Farnesyl diphosphate


organism: Haematococcus lacustris


organism: Hevea brasiliensis


substrate_name: Isopentenyl diphosphate; trans,trans-Farnesyl diphosphate


substrate: Isopentenyl diphosphate; trans,trans-Farnesyl diphosphate


organism: Lutzomyia longipalpis

proof_lines: pH 7.2, 30°C, cosubstrate: (2E,6E)-farnesyl diphosphate

proof_lines: pH 7.2, 30°C, cosubstrate: isopentenyl diphosphate


organism: Picea abies

substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Choristoneura fumiferana

substrate_name: Unknown

substrate: Unknown


organism: Eucommia ulmoides

proof_lines: fixed substrate: farnesyl diphosphate, enzyme EuFPS1, pH 7.0, 25°C

proof_lines: fixed substrate: isopentenyl diphosphate, enzyme EuFPS1, pH 7.0, 25°C

proof_lines: fixed substrate: dimethylallyl diphosphate, enzyme EuFPS1, pH 7.0, 25°C


substrate_name: geranyl diphosphate

proof_lines: fixed substrate: isopentenyl diphosphate, enzyme EuFPS2, pH 7.0, 25°C

proof_lines: fixed substrate: dimethylallyl diphosphate, enzyme EuFPS2, pH 7.0, 25°C

proof_lines: fixed substrate: farnesyl diphosphate, enzyme EuFPS2, pH 7.0, 25°C

substrate: geranyl diphosphate


organism: Geobacillus stearothermophilus

substrate_name: Isopentenyl diphosphate; Geranyl diphosphate


substrate_name: (E,E)-farnesyl diphosphate

substrate: (E,E)-farnesyl diphosphate


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


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


mutation_signature: Δ1

proof_lines:
mutant DELTA1-6, pH 7.5, 25°C
mutant DELTA1-9, pH 7.5, 25°C
mutant DELTA1-7, pH 7.5, 25°C


proof_lines:
wild-type, pH 7.5, 25°C
wild-type enzyme, pH 7.5, 25°C


organism: Taxus canadensis


organism: Thermococcus kodakarensis

substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


organism: Toxoplasma gondii


enzyme_display_name: 1-phosphatidylinositol 4-kinase

organism: Homo sapiens

substrate_name: ATP

assay_conditions_summary: 310.15 K; cofactor ATP

enzyme: 1-phosphatidylinositol 4-kinase

substrate: ATP


substrate_name: ATP; 1-Phosphatidyl-1D-myo-inositol

substrate: ATP; 1-Phosphatidyl-1D-myo-inositol


organism: Hordeum vulgare

substrate_name: agmatine

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

assay_conditions_summary: cofactor CoA

substrate: agmatine


organism: Escherichia coli O18:K1:H7 (strain RS218 / NMEC)

substrate_name: ADP-heptose

assay_conditions_summary: cofactor ADP

substrate: ADP-heptose


organism: Escherichia coli (strain K12)

substrate_name: ADP-mannose

substrate: ADP-mannose


organism: Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)

substrate_name: geranylgeranyl diphosphate (GGDP)

substrate: geranylgeranyl diphosphate (GGDP)


organism: Diaporthe amygdali

substrate_name: GPP

substrate: GPP


organism: Emericella variicolor

substrate_name: geranylgeranyl pyrophosphate

substrate: geranylgeranyl pyrophosphate


substrate_name: DMAPP

substrate: DMAPP


substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Talaromyces verruculosus

substrate_name: DMAPP (for prenyltransferase activity)

substrate: DMAPP (for prenyltransferase activity)


substrate_name: PtdIns

substrate: PtdIns


organism: Rattus norvegicus


enzyme_display_name: polynucleotide 3'-phosphatase

organism: Arabidopsis thaliana

substrate_name: single-stranded oligonucleotide

enzyme: polynucleotide 3'-phosphatase

substrate: single-stranded oligonucleotide


organism: Dictyostelium discoideum

substrate_name: cAMP (catalytic domain expressed in vegetative AX2 cells)


substrate_name: cAMP

substrate: cAMP


organism: Drosophila melanogaster


substrate_name: cAMP (isoform 1)

substrate: cAMP (isoform 1)


substrate_name: 3',5'-cyclic AMP

substrate: 3',5'-cyclic AMP


substrate_name: ATP

assay_conditions_summary: pH 7.4; cofactor ATP

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


proof_lines: mutant enzyme R492G, at pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme R492G/E493G, at pH 7.4, temperature not specified in the publication


organism: Plasmodium falciparum


enzyme_display_name: ribonuclease Z

organism: Bacillus subtilis

substrate_name: pre-tRNA(Arg1); pre-tRNA(Arg2)

proof_lines:
pH 7.5, 37°C
presence of Co2+, pH 7.5, 37°C

enzyme: ribonuclease Z

substrate: pre-tRNA(Arg1); pre-tRNA(Arg2)


proof_lines: 25 mM Tris-HCl pH 7.0, 1 mM MgCl2, 1 mM DTT, 50 mM KCl at 28°C


organism: Methanococcus maripaludis

proof_lines:
presence of Co2+, pH 7.5, 37°C
pH 7.5, 37°C


organism: Unknown

substrate: ATP


substrate_name: adenosine 3',5'-cyclic phosphate

substrate: adenosine 3',5'-cyclic phosphate


organism: Methanolobus psychrophilus


organism: Sus scrofa

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP


substrate_name: ATP; H2O

substrate: ATP; H2O


organism: Toxoplasma gondii

proof_lines: mutant enzyme E493G, at pH 7.4, temperature not specified in the publication


organism: Taxus baccata


organism: Taxus canadensis

substrate_name: farnesyl diphosphate

proof_lines:
cosubstrate geranyl diphosphate
cosubstrate dimethylallyl diphosphate
cosubstrate farnesyl diphosphate

substrate: farnesyl diphosphate


organism: Thermococcus kodakaraensis

substrate_name: Dimethylallyl diphosphate; Isopentenyl diphosphate


organism: Bos taurus

substrate_name: phosphatidylinositol

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines:
in presence of 20 mM MgCl2
ATP in form of MgATP2-
pH 7.0, 30°C

substrate: phosphatidylinositol


organism: Daucus carota

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


organism: Dunaliella parva

assay_conditions_summary: pH 7.8; 301.15 K; cofactor ATP

proof_lines:
pH 7.8, 28°C, at 30 mM MgCl2
pH 7.8, 28°C, at 0.75 mM Triton X-100
pH 7.8, 28°C, at 1.5 mM Triton X-100


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines:
pH 7.4, 30°C, enzyme form mPIK-I
pH 7.4, 25°C
pH 7.2, 37°C


organism: Legionella micdadei

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Mus musculus

assay_conditions_summary: pH 7.1; 298.15 K; cofactor ATP


organism: Oryctolagus cuniculus

assay_conditions_summary: cofactor ATP

proof_lines:
PI kinase II
PI kinase III
PI kinase I


organism: Ovis aries


organism: Rattus norvegicus

substrate_name: ATP; 1-Phosphatidyl-D-myo-inositol

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH 7.5, 30°C, in presence of at least 20 mM MgCl2

substrate: ATP; 1-Phosphatidyl-D-myo-inositol


organism: Saccharomyces cerevisiae

substrate_name: trans,trans-farnesyl diphosphate

substrate: trans,trans-farnesyl diphosphate


proof_lines: pH 7.5, 25°C, recombinant mutant Y107A/H139A


proof_lines: pH 7.5, 25°C, recombinant mutant Y107A/F108A/H139A


proof_lines: pH 7.5, 25°C, recombinant mutant F108A/H139A


proof_lines: pH 7.5, 25°C, recombinant mutant L135A/H139A


proof_lines: pH 7.5, 25°C, recombinant mutant Y107A/F108A


proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme


proof_lines: pH 7.5, 25°C, recombinant mutant Y107A/F108A/L135A/H139A


organism: Sinapis alba

substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Sulfolobus acidocaldarius

substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


organism: Methanothermobacter thermautotrophicus


organism: Micrococcus luteus

substrate_name: isopentenyl diphosphate

proof_lines: cosubstrate dimethylallyl diphosphate at 0.175 mM

substrate: isopentenyl diphosphate


organism: Monolepta hieroglyphica

proof_lines: pH 7.4, 37°C, cosubstrate: isopentenyl diphosphate

proof_lines: pH 7.4, 37°C, cosubstrate: (2E,6E)-farnesyl diphosphate


organism: Nicotiana tabacum

proof_lines: cosubstrate farnesyl diphosphate, GGPPS2


organism: Pantoea ananatis

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


organism: Phycomyces blakesleeanus


organism: Plasmodium vivax


proof_lines: pH 7.0, 37°C, carboxy-terminal deletion mutant DELTA-12


proof_lines: pH 7.0, 37°C, carboxy-terminal deletion mutant DELTA-8


proof_lines: pH 7.0, 37°C, carboxy-terminal deletion mutant DELTA-4


organism: Ricinus communis


organism: Hordeum murinum

substrate_name: caffeoyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: caffeoyl-CoA


organism: Hordeum vulgare

substrate_name: sinapoyl-CoA

substrate: sinapoyl-CoA


organism: Escherichia coli

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

proof_lines: pH and temperature not specified in the publication


organism: Antirrhinum majus

proof_lines: heterodimer of geranyl phosphate synthase small subunit of Antirrhinum majus with Nicotiana tabacum geranylgeranyl diphosphate synthase GGPPS2

proof_lines: heterodimer of geranyl phosphate synthase small subunit of Antirrhinum majus with Nicotiana tabacum geranylgeranyl diphosphate synthase GGPPS1


organism: Bacillus subtilis


organism: Bos taurus


organism: Capsicum annuum


organism: Corynebacterium glutamicum

proof_lines: pH 7.5, 30°C, recombinant His-tagged enzyme


organism: Cucurbita pepo


organism: Homo sapiens

proof_lines: pH 7.7, 37°C, recombinant enzyme, versus trans,trans-farnesyl diphosphate


organism: Kitasatospora griseola


proof_lines:
cosubstrate farnesyl diphosphate
cosubstrate dimethylallyl diphosphate


organism: Gallus gallus


organism: Mus musculus


substrate_name: ATP (at pH 7.4)

substrate: ATP (at pH 7.4)


organism: Rattus norvegicus

substrate_name: ADP

substrate: ADP


substrate_name: ATP (with Ca2(+) as cofactor and 1900 pM enzyme)


organism: Arabidopsis thaliana

substrate_name: farnesyl diphosphate (in the presence of 500 uM of isopentenyl diphosphate)

proof_lines: kcat is 29.7 sec(-1) with farnesyl diphosphate as substrate (in the presence of 500 uM of isopentenyl diphosphate). kcat is 21.0 sec(-1) with geranylgeranyl diphosphate as substrate (in the presence of 100 uM of isopentenyl diphosphate). kc


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: IPP

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

substrate: IPP


substrate_name: bpNPP

proof_lines: kcat is 7.4 sec(-1) with bpNPP as substrate.

substrate: bpNPP


organism: Dictyostelium discoideum

substrate_name: cAMP

substrate: cAMP


proof_lines: Vmax values for isoforms 2, 3 and 4 relative to isoform 1 are 3.8, 1.6 and 2.1.


enzyme_display_name: assemblin

organism: Human cytomegalovirus (strain AD169)

proof_lines: KM is 10.7 uM according to PubMed:12549906.

enzyme: assemblin


organism: Glossina morsitans morsitans

substrate_name: ATP

proof_lines: kcat is 48.9 min(-1) with ATP as substrate. kcat is 12.7 min(-1) with ADP as substrate.

substrate: ATP


substrate_name: trnI-Thr-TCAATG-trailer

proof_lines: the first cytosine is the primary anti-determinant for RNaseZ

substrate: trnI-Thr-TCAATG-trailer


organism: Drosophila melanogaster


proof_lines: 25 mM K-MOPS, pH 6.75, 2.5 mM CaCl2, 1 mM dithiothreitol, 5% glycerol, 4 U/ml RNasin, 100 microg/ml bovine serum albumin

proof_lines: 25 mM K-MOPS, 2 mM MgCl2, at pH 6.8 and 37°C

proof_lines: 25 mM K-MOPS, pH 6.75, 1 mM MnCl2, 1 mM dithiothreitol, 5% glycerol, 4 U/ml RNasin, 100 microg/ml bovine serum albumin


organism: Sus scrofa

proof_lines:
at 37°C
at 28°C
CC is added to the 3-end of tRNA


organism: Synechocystis sp.

proof_lines: 40 mM Tris-HCl pH 7.5, 2 mM dithiothreitol


substrate_name: RNA-DNA heteroduplex

substrate: RNA-DNA heteroduplex


substrate_name: DNA/RNA hybrid

proof_lines: obtained by transcription of calf thymus DNA

substrate: DNA/RNA hybrid


organism: Methanocaldococcus jannaschii

assay_conditions_summary: pH 8

proof_lines:
pH 8.0, 50 mM NaCl, wild-type enzyme
pH 8.0, 500 mM NaCl, wild-type enzyme


substrate_name: poly(rAdT)

substrate: poly(rAdT)


organism: Pyrococcus abyssi

substrate_name: RNA-DNA/DNA hybrid

proof_lines: pH 8.0, 37°C, purified recombinant His-tagged enzyme

substrate: RNA-DNA/DNA hybrid


organism: Thermococcus kodakarensis

substrate_name: RNA*DNA hybrid

substrate: RNA*DNA hybrid


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
pH 8.0, 30°C
pH 7.5, 34°C
ATP in form of MgATP2-


organism: Spinacia oleracea

substrate_name: phosphatidylinositol

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5, enzyme form QII
pH 7.5, enzyme form QI

substrate: phosphatidylinositol


substrate_name: bis(p-nitrophenyl)phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature R252G to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-R252G, mutant, bis(p-nitrophenyl)phosphate catalysis

substrate: bis(p-nitrophenyl)phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature F51L to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-F51L, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature C40G to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-C40G, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature P178A to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-P178A, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature E208A to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-E208A, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature P64A to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-P64A, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_source: UniProtKB reviewed Q8LGU7 canonical sequence

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

proof_lines: AthTRZ1 wild-type, hydrolysis of phosphodiester bonds of bpNPP, KM value for AthTRZ1 two-fold increased relative to that of the tRNase Z of Escherichia coli


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature G62V to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-G62V, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature C25G to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-C25G, mutant, bis(p-nitrophenyl)phosphate catalysis


organism: Acetivibrio thermocellus

substrate_name: bis-p-nitrophenyl phosphate

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

proof_lines: mutant enzyme D392N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme D392N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

substrate: bis-p-nitrophenyl phosphate


proof_lines: mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 8.0),0.5 mM MnCl2

proof_lines: mutant enzyme H376N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2


substrate_name: p-nitrophenyl phosphate

proof_lines: mutant enzyme D236E, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2

proof_lines: mutant enzyme D236E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

substrate: p-nitrophenyl phosphate


proof_lines: mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2

proof_lines: mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2


proof_lines: mutant enzyme H323A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme H189A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme H189A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme H189A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2


proof_lines: mutant enzyme D392A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme H189E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme H189E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2


proof_lines: mutant enzyme R237A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme R237A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2


proof_lines: mutant enzyme D392E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2


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

proof_lines: wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2


proof_lines: mutant enzyme D233E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


substrate_name: 3',5'-cyclic AMP

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

substrate: 3',5'-cyclic AMP


organism: Pseudomonas aeruginosa


substrate_name: cAMP (isoform 1)

substrate: cAMP (isoform 1)


substrate_name: Unknown

substrate: Unknown


organism: Aedes aegypti

substrate_name: ADP

substrate: ADP


organism: Aedes albopictus


organism: Arabidopsis thaliana


organism: Thermus thermophilus

substrate_name: DNA-RNA-DNA hybrid

substrate: DNA-RNA-DNA hybrid


proof_lines: mutant A12S/K75M and A12S/K75M/A77P, pH 8.0, 30°C


substrate_name: M13 DNA/RNA

proof_lines:
at 37°C
at 70°C

substrate: M13 DNA/RNA


proof_lines: mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2

proof_lines: mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2


proof_lines: mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2


proof_lines: mutant enzyme H189D, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme H189D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2

proof_lines: mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2

proof_lines: mutant enzyme D236N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme H189Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2


proof_lines: mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2

proof_lines: mutant enzyme D236A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2


mutation_signature: truncated mutant RNase HII-217

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

mutation_type: truncation

proof_lines: truncated mutant RNase HII-217, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_paper_variant_reconstruction and applied mutation signature D135A to reconstruct the assayed variant sequence.


mutation_signature: truncated mutant RNase HII-213

proof_lines: truncated mutant RNase HII-213, pH 8.0, 30°C


mutation_signature: truncated mutant RNase HII-203

proof_lines: truncated mutant RNase HII-203, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_paper_variant_reconstruction and applied mutation signature H132A to reconstruct the assayed variant sequence.


mutation_signature: truncated mutant RNase HII-207

proof_lines: truncated mutant RNase HII-207, pH 8.0, 30°C


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


enzyme_display_name: sortase A

organism: Unknown

enzyme: sortase A


enzyme_display_name: xanthomonalisin

organism: Xanthomonas sp.

enzyme: xanthomonalisin


organism: Lactococcus lactis subsp. lactis

substrate_name: Dabsyl-LPFAGGAG-Edans

substrate: Dabsyl-LPFAGGAG-Edans


organism: Staphylococcus aureus


organism: Xanthomonas sp. (strain T-22)

assay_conditions_summary: pH 3.5; buffer 0.1 M sodium formate

proof_lines: kcat is 30.4 sec(-1) with Lys-Pro-Ala-Asp-Phe-p-nitrophenylalanine-Arg-Leu as substrate (PubMed:8902622). kcat is 49.1 sec(-1) with Lys-Pro-Ala-Lys-Phe-p-nitrophenylalanine-Arg-Leu as substrate (PubMed:8902622).


proof_lines: mutant enzyme H376D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme H376D, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2


proof_lines: mutant enzyme H323Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme R237Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme R237Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2


proof_lines: mutant enzyme R237K, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2

proof_lines: mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2


organism: Homo sapiens


organism: Kostyavirus CJW1

substrate_name: dTMP

substrate: dTMP


organism: Omegavirus omega


organism: Rattus norvegicus

substrate_name: DNA with 5'-hydroxyl ends

substrate: DNA with 5'-hydroxyl ends


organism: Rhodothermus phage RM378

substrate_name: cAMP

substrate: cAMP


organism: Bos taurus


organism: Dictyostelium discoideum


substrate_name: adenosine 3',5'-cyclic phosphate

substrate: adenosine 3',5'-cyclic phosphate


organism: Mus musculus

proof_lines: isoform PDE4D3, pH and temperature not specified in the publication


organism: Myxococcus xanthus

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

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


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

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


proof_lines:
pH 7.5, 37°C
CAP-II
pH 7.4


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


proof_lines:
mutant A429G, 37°C
pH 7.4, 37°C, mutant enzyme A429G


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature W375Y to reconstruct the assayed variant sequence.


sequence_source: NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature F484Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature V501A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature L391A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature W375F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature A590C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature P595I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature D440A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature D440N to reconstruct the assayed variant sequence.


proof_lines: PDE7B expressed in transfected COS-7 cells


organism: Leishmania mexicana


enzyme_display_name: D-xylose reductase (NADH)

organism: Candida parapsilosis

substrate_name: NADH

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines:
pH 6.0
pH 6.0, coenzyme: NADH
pH 6.0, coenzyme: NADPH

enzyme: D-xylose reductase (NADH)

substrate: NADH


organism: Yamadazyma tenuis

substrate_name: D-xylose

substrate: D-xylose


assay_conditions_summary: pH 6.5; 315.15 K; cofactor NADH

proof_lines: pH 6.5, 42°C, recombinant His-tagged enzyme


substrate_name: D-Xylose

substrate: D-Xylose


organism: Sus scrofa


organism: Pseudomonas sp.

proof_lines:
autentic and recombinant PCP
recombinant PCP
autentic PCP


organism: Xanthomonas sp.


enzyme_display_name: chymotrypsin C

organism: Conogethes punctiferalis

proof_lines: in 50 mM Tris-HCl (pH 8.0), with 20 mM CaCl2, at 37°C

enzyme: chymotrypsin C


substrate_name: benzoyl-L-Leu methyl ester

substrate: benzoyl-L-Leu methyl ester


organism: Human alphaherpesvirus 1


organism: Human betaherpesvirus 5


proof_lines: pH 7.2, 30°C, wild-typelike mutant enzyme A143Q


organism: Staphylococcus aureus

substrate_name: Gly-Gly-Gly

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

substrate: Gly-Gly-Gly


proof_lines:
mutant enzyme
37°C, pH 7.5, mutant enzyme R197Cit


proof_lines:
37°C, pH 7.5, mutant enzyme E171A
mutant enzyme E171A


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


proof_lines:
37°C, pH 7.5, mutant enzyme D170A
mutant enzyme D170A


substrate_name: Dabcyl-QALPETGEE-Edans

proof_lines: pH 7.5, 37°C, recombinant circular truncated mutant CSrtADELTAN59 enzyme

proof_lines: pH 7.5, 37°C, recombinant linear truncated mutant LSrtADELTAN59 enzyme

substrate: Dabcyl-QALPETGEE-Edans


organism: Achromobacter sp. WM111

substrate_name: Carbaryl

proof_lines:
at pH 6.8 and 37°C
at pH 8.5 and 37Â°C
at pH 8.3 and 25°C

substrate: Carbaryl


proof_lines: pH 7.2, 30°C, mutant enzyme S134A/A143Q/H157A


proof_lines: pH 7.2, 30°C, mutant enzyme A143Q/S225Y/L229R


proof_lines: presence of 25% glycerol, enzyme HCMV A134Q

proof_lines: presence of 50% glycerol, enzyme HCMV A134Q


proof_lines:
soluble enzyme
pH 7.4, enzyme in solution
inclusion bodies


organism: Scheffersomyces stipitis

substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from PMID 18028553 article text plus GenBank X59465/UniProt P31867; row-specific PsXR 2-2C12 sequence reconstructed from K270S/S271G/N272P/R276F. and applied mutation signature K270S/N272P/S271G/R276F to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, temperature not specified in the publication, mutant enzyme K270S/N272P/S271G/R276F

proof_lines: pH 6.0, temperature not specified in the publication, cofactor: NADPH, mutant enzyme K270S/N272P/S271G/R276F

proof_lines: pH 6.0, temperature not specified in the publication, cofactor: NADH, mutant enzyme K270S/N272P/S271G/R276F

substrate: NADPH


sequence_source: PMID 18028553 article text plus GenBank X59465/UniProt P31867 canonical Scheffersomyces/Pichia stipitis XYL1 sequence.

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

proof_lines: pH 6.0, temperature not specified in the publication, wild-type enzyme, wild-type enzyme

proof_lines: pH 6.0, temperature not specified in the publication, cofactor: NADH, wild-type enzyme

proof_lines: pH 6.0, temperature not specified in the publication, cofactor: NADPH, wild-type enzyme


organism: Sungouiella intermedia

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 NADH

proof_lines: pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH

proof_lines: pH 7.0, 25°C, dual specific xylose reductase (dsXR)


substrate_name: NAD+

sequence_source: PMID 11513616 title plus UniProt O74237/XYL1_CANTE canonical Candida tenuis xylose reductase sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

substrate: NAD+


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from PMID 17391061 title plus UniProt Q9UIQ6/LNPEP canonical human IRAP sequence; G428D reconstructed directly from the canonical Gly428 residue. and applied mutation signature G428D to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

substrate_name: Vasopressin

substrate: Vasopressin


organism: Saccharomyces cerevisiae

substrate_name: L-cysteine-nitroanilide

substrate: L-cysteine-nitroanilide


organism: Streptococcus thermophilus

substrate_name: L-Lysine-p-nitroanilide

substrate: L-Lysine-p-nitroanilide


substrate_name: S-benzyl-L-cysteine-p-nitroanilide

substrate: S-benzyl-L-cysteine-p-nitroanilide


organism: Bos taurus

assay_conditions_summary: pH 5.5; 310.15 K; buffer acetate

proof_lines: enzyme from lung, in acetic buffer (pH 5.5), at 37°C

proof_lines: enzyme from renal cortex, in acetic buffer (pH 5.5), at 37°C


substrate_name: Lys-Pro-p-nitroanilide

substrate: Lys-Pro-p-nitroanilide


substrate_name: Gly-Pro-Ala

proof_lines:
enzyme form DPP II-M
enzyme form DPP II-S

substrate: Gly-Pro-Ala


enzyme_display_name: pancreatic elastase

organism: Salmo salar

substrate_name: Suc-AAA-pNA (at 22 degrees Celsius)

enzyme: pancreatic elastase

substrate: Suc-AAA-pNA (at 22 degrees Celsius)


enzyme_display_name: [pyruvate dehydrogenase (acetyl-transferring)] kinase

organism: Arabidopsis thaliana

substrate_name: pyruvate dehydrogenase

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

proof_lines: pH 7.5, 37°C, recombinant PDK mutant L234A

substrate: pyruvate dehydrogenase


proof_lines: pH 7.5, 37°C, recombinant PDK mutant H233A

enzyme: [pyruvate dehydrogenase (acetyl-transferring)] kinase


proof_lines: pH 7.5, 37°C, recombinant PDK mutant E238A


substrate_name: ATP

assay_conditions_summary: 310.15 K; cofactor ATP

proof_lines: 37°C, recombinant mutant G319A of isozyme PDK2

substrate: ATP


proof_lines:
kidney enzyme
pH 7.5, 30°C
pH 7.0, 30°C


organism: Lathyrus oleraceus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Sus scrofa

assay_conditions_summary: pH 7.8; 303.15 K; buffer and pH notes; cofactor ATP

proof_lines:
at 0.2 M buffer concentration
at 0.04 M buffer concentration
pH 7.8, 30°C


enzyme_display_name: rRNA N-glycosylase

organism: Cinnamomum camphora

substrate_name: rRNA

proof_lines:
pH 7.6, 35°C, 80S ribosome, cinnamomin
pH 7.6, 35°C, naked RNA, cinnamomin

enzyme: rRNA N-glycosylase

substrate: rRNA


organism: Escherichia coli

proof_lines: pH 7.4, 28°C, Artemia salina ribosomes, untreated holotoxin

proof_lines: pH 7.4, 28°C, Artemia salina ribosomes, A subunit treated with trypsin, urea and dithiothreitol

proof_lines: pH 7.4, 28°C, Artemia salina ribosomes, A subunit treated with urea and dithiothreitol


organism: Ricinus communis


organism: Saponaria officinalis

proof_lines:
37°C, presence of 50 mM KCl, 1 mM MgCl2
saporin-L1, pH 7.7, 20°C
pH 7.8, 25°C


proof_lines:
isoform CELA3A, at pH 8.0 and 22°C
isoform CELA3B, at pH 8.0 and 22°C
pancreatic elastase


organism: Ovis aries

substrate_name: succinyl-Ala-Ala-Ala-p-nitroanilide

substrate: succinyl-Ala-Ala-Ala-p-nitroanilide


substrate_name: succinyl-Ala-Ala-Pro-Ile-p-nitroanilide

substrate: succinyl-Ala-Ala-Pro-Ile-p-nitroanilide


assay_conditions_summary: pH 8; 295.15 K; buffer 0.1 M phosphate

proof_lines: in the presence of 0.2 mM spermidine, at pH 8.5 and 37°C

proof_lines: in the presence of 0.5 mM spermidine, at pH 8.5 and 37°C


proof_lines: 37°C, recombinant mutant G284A of isozyme PDK2


proof_lines: 37°C, recombinant isozyme PDK2 wild-type


assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

proof_lines: recombinant His-tagged isozyme PDK1, 37°C, pH 7.8


substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


assay_conditions_summary: pH 7.4; 303.15 K; buffer composition, overview; cofactor ATP

proof_lines: pH 7.4, 30°C, with oxidized E2, in presence of 2 mM DTT

proof_lines: pH 7.4, 30°C, with reduced E2, in presence of NADH/NAD+

proof_lines: pH 7.4, 30°C, with oxidized E2, in presence of NADH/NAD+


substrate_name: [Pyruvate dehydrogenase (lipoamide)]

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: phosphorylation site 1 of subunit E1, isozyme PDK1, pH 7.0, 30°C

proof_lines: phosphorylation site 3 of subunit E1, isozyme PDK1, pH 7.0, 30°C

proof_lines: phosphorylation site 2 of subunit E1, isozyme PDK4, pH 7.0, 30°C

substrate: [Pyruvate dehydrogenase (lipoamide)]


organism: Unknown


proof_lines: about, pH 7.5, 37°C, recombinant PDK mutant E238H


proof_lines: pH 7.5, 37°C, recombinant PDK mutant L234H


proof_lines: pH 7.5, 37°C, recombinant PDK mutant E238Q


substrate_name: 28S rRNA within the native ribosome

substrate: 28S rRNA within the native ribosome


organism: Mimosa pudica

substrate_name: ADP

substrate: ADP


organism: Ornithodoros savignyi

assay_conditions_summary: cofactor ATP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C, presence of Mg2+
free ATP
pH 7.5, 37°C, presence of Ca2+


organism: Rhodnius prolixus


organism: Solanum tuberosum

assay_conditions_summary: pH 6; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 6.0, presence of Ca2+
pH 6.0, 22°C
variety Desiree, 20°C


substrate_name: ATP; H2O

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines:
pH 7.6, 37°C
pH 7.6, 37°C, substrate ADP
pH 7.6, 37°C, substrate ATP

substrate: ATP; H2O


organism: Taenia crassiceps


organism: Trichomonas vaginalis

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Triticum aestivum

assay_conditions_summary: pH 5.5; 310.15 K; cofactor ATP


organism: Trypanosoma brucei brucei

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP


organism: Trypanosoma cruzi

substrate_name: UDP

substrate: UDP


enzyme_display_name: xylose isomerase

organism: Streptomyces sp.

substrate_name: D-Xylose

enzyme: xylose isomerase

substrate: D-Xylose


organism: Arabidopsis thaliana

substrate_name: ATP (at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: kcat is 0.55 sec(-1) with ATP as substrate (at pH 7.5, in PubMed:15629119).

substrate: ATP (at pH 7.5)


organism: Aedes aegypti


organism: Bacillus subtilis

substrate_name: dATP

substrate: dATP


organism: Bos taurus


organism: Candida parapsilosis


organism: Cicer arietinum


organism: Ctenocephalides felis

assay_conditions_summary: cofactor ADP


organism: Daboia russelii

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


organism: Gallus gallus


organism: Glycine max


organism: Homo sapiens

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


organism: Legionella pneumophila


organism: Lupinus luteus


organism: Agrobacterium sp. XWY-2

substrate_name: Carbaryl

substrate: Carbaryl


organism: Aminobacter aminovorans

substrate_name: methomyl

substrate: methomyl


organism: Aspergillus niger

substrate_name: isoprocarb

assay_conditions_summary: pH 7

substrate: isoprocarb


organism: Blastobacter sp. M501

substrate_name: xylylcarb

substrate: xylylcarb


organism: Novosphingobium sp. KN65.2

substrate_name: carbofuran

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

substrate: carbofuran


organism: Pseudomonas aeruginosa


organism: Pseudomonas sp. 50432


organism: Pseudomonas sp. C7

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


organism: Pseudomonas sp. CRL-OK

proof_lines: at pH 7.0, temperature not specified in the publication


organism: Pseudomonas sp. OXA20


organism: Sphingobium sp. CFD-1


organism: Sphingomonas sp. CDS-1

substrate_name: oxamyl

substrate: oxamyl


organism: Unknown

substrate_name: rRNA

substrate: rRNA


enzyme_display_name: strictosidine synthase

organism: Rauvolfia serpentina

substrate_name: tryptamine

enzyme: strictosidine synthase

substrate: tryptamine


substrate_name: serotonin

proof_lines:
wild-type enzyme
wild type, pH 7.0, 35°C, 15 min

substrate: serotonin


proof_lines: kcat is 78.2 min(-1) with tryptamine and secologanin as substrates (PubMed:16531499). kcat is 10.65 sec(-1) with tryptamine and secologanin as substrates (PubMed:17884630). kcat is 2.32 sec(-1) with 6-methyl-tryptamine and secologanin as su


organism: Streptomyces sp. 1

substrate_name: D-glucose

substrate: D-glucose


organism: Streptomyces sp. 32

substrate_name: D-xylose

substrate: D-xylose


organism: Streptomyces violaceoruber

proof_lines:
with 1 mM Co2+
with 10 mM Mg2+


organism: Streptomyces viridobrunneus

substrate_name: xylose

substrate: xylose


organism: Thermoanaerobacterium saccharolyticum

substrate_name: D-fructose

substrate: D-fructose


organism: Catharanthus roseus


substrate_name: secologanin

substrate: secologanin


proof_lines: wild-type strictosidine synthase expressed in yeast


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


organism: Cinchona robusta

proof_lines:
isoform II b
isoform I a
isoform I b


organism: Escherichia coli

proof_lines: HPLC, neutral pH, micromolar to low millimolar substrate concentrations


organism: Ophiorrhiza pumila

proof_lines: pH and temperature not specified in the publication


proof_lines:
in reaction with tryptamine
at pH 6.5 and 45°C


organism: Rauvolfia vomitoria


enzyme_display_name: plasma kallikrein

organism: Homo sapiens

proof_lines: catalytic domain expressed after mutagenizing three asparagines to glutamate in a baculovirus/Sf9 system

proof_lines: protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase

enzyme: plasma kallikrein


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


organism: Rattus norvegicus

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: carboxypeptidase U

organism: Bos taurus

substrate_name: hippuryl-Arg

proof_lines:
Vmax: 46.05 micromol/l/min
Raw SKiD Env: Temp=-----, pH=-----

enzyme: carboxypeptidase U

substrate: hippuryl-Arg


enzyme_display_name: peptidyl-glutamate 4-carboxylase

substrate_name: vitamin KH2

proof_lines: R406A/H408A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM

enzyme: peptidyl-glutamate 4-carboxylase

substrate: vitamin KH2


substrate_name: FLEEL

proof_lines: R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM

substrate: FLEEL


proof_lines:
R359A/H360A/K361A mutant
FLEEL, R359A/H360A/K361A mutant


organism: Conus textile

substrate_name: 28-residue peptides based on residues -18 to +10 of human proprothrombin


substrate_name: reduced vitamin K

proof_lines: cosubstrate chimeric coagulation factor, pH not specified in the publication, temperature not specified in the publication

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

proof_lines: cosubstrate matrix Gla protein, pH not specified in the publication, temperature not specified in the publication

substrate: reduced vitamin K


substrate_name: anisylazoformyl-Lys

proof_lines:
24°C
room temperature
recombinant enzyme

substrate: anisylazoformyl-Lys


substrate_name: hippuryl-arginine

proof_lines: mutant P91S, activation of TAFI by plasmin

substrate: hippuryl-arginine


proof_lines: mutant S90D/S94V/S90D, activation of TAFI by plasmin


substrate_name: p-anisylazoformyl-L-arginine

proof_lines: mutant R92K, activation of TAFI by thrombin in the presence of thrombomodulin

proof_lines: mutant R92K, activation of TAFI by plasmin

substrate: p-anisylazoformyl-L-arginine


proof_lines: mutant S94V, activation of TAFI by plasmin

proof_lines: mutant S94V, activation of TAFI by thrombin in the presence of thrombomodulin


proof_lines: mutant A93V, activation of TAFI by thrombin in the presence of thrombomodulin

proof_lines: mutant A93V, activation of TAFI by plasmin


proof_lines: wild-type, activation of TAFI by thrombin in the presence of thrombomodulin

proof_lines: wild-type, activation of TAFI by plasmin


proof_lines: mutant S90P, activation of TAFI by plasmin

proof_lines: mutant S90P, activation of TAFI by thrombin in the presence of thrombomodulin


substrate_name: kininogen

proof_lines:
pH 8.0, 37°C
at pH 7.4 and 37°C
at 37°C

substrate: kininogen


proof_lines: ecotin with mutation H53P in the 50s loop, at room temperature


proof_lines: ecotin with mutations S82W/T83N/M84R/M85R/A86S in the 80s loop, at room temperature


proof_lines: ecotin with mutations S82W/T83N/M84R/M85R/A86S in the 80s loop and mutations R108S/N110S in the 100s loop, at room temperature


proof_lines: ecotin with mutation H53P in the 50s loop and mutations S82W/T83N/M84R/M85R/A86S in the 80s loop, at room temperature


proof_lines: ecotin with mutation H53P in the 50s loop, mutations S82W/T83N/M84R/M85R/A86S in the 80s loop and mutations R108S/N110S in the 100s loop, at room temperature


proof_lines: ecotin with mutations R108S/N110S in the 100s loop, at room temperature


proof_lines: ecotin with mutation H53P in the 50s loop and mutations R108S/N110S in the 100s loop, at room temperature


organism: Lachesis muta


organism: Macaca fascicularis


organism: Mus musculus


organism: Human betaherpesvirus 5

substrate_name: GVVNASCRLA

substrate: GVVNASCRLA


proof_lines:
mutant V141G/V207G, soluble
mutant V141G/V207G, refolded


organism: Human betaherpesvirus 6


organism: Bacillus anthracis

proof_lines: sortase A DELTA64 (residues Asp65–Lys210), in 20 mM HEPES, pH 7.5


proof_lines: sortase A DELTA56 (residues Asp-57-Lys210), in 20 mM HEPES, pH 7.5


organism: Staphylococcus aureus

substrate_name: Abz-LPETG-Dap(Dnp)

substrate: Abz-LPETG-Dap(Dnp)


organism: Thermotoga neapolitana

substrate_name: D-glucose

proof_lines: soluble wild type enzyme, at 90°C, pH 7.0

proof_lines: soluble wild type enzyme, at 80°C, pH 7.0


proof_lines: unbound CBD-TNX fusion protein, at 80°C, pH 7.0

proof_lines: immobilized CBD-TNX fusion protein, at 90°C, pH 7.0

proof_lines: unbound CBD-TNX fusion protein, at 90°C, pH 7.0


proof_lines:
FLEEL, R513A/K515A mutant
R513A/K515A mutant
proPT28, R513A/K515A mutant


enzyme_display_name: NAD(+) glycohydrolase

organism: Aspergillus fumigatus

substrate_name: NADP+

assay_conditions_summary: pH 7.5; 293.15 K; cofactor NADP+

enzyme: NAD(+) glycohydrolase

substrate: NADP+


substrate_name: etheno-NAD+

assay_conditions_summary: pH 5.5; 298.15 K; cofactor NAD+

substrate: etheno-NAD+


substrate_name: NAD+; H2O

assay_conditions_summary: cofactor NAD+

substrate: NAD+; H2O


substrate_name: NADP+; Nicotinic acid

substrate: NADP+; Nicotinic acid


substrate_name: Nicotinamide guanine dinucleotide

substrate: Nicotinamide guanine dinucleotide


organism: Sphingobacterium faecium


organism: Streptococcus equisimilis

substrate_name: H2O; NAD+

substrate: H2O; NAD+


organism: Streptococcus pyogenes


proof_lines: wild-type carboxylase in bovine liver microsomes

proof_lines: for wild type FLAG-vitamin K-dependent gamma-glutamyl carboxylase


proof_lines: FLAG-vitamin K-dependent gamma-glutamyl carboxylase

proof_lines: recombinant His6-carboxylase present in Sf9 cell microsomes


organism: Unknown

substrate_name: NAD+

assay_conditions_summary: cofactor NADP+

substrate: NAD+


enzyme_display_name: flavodoxin--NADP(+) reductase

organism: Escherichia coli

substrate_name: reduced flavodoxin II

enzyme: flavodoxin--NADP(+) reductase

substrate: reduced flavodoxin II


organism: Lathyrus oleraceus

substrate_name: reduced flavodoxin

substrate: reduced flavodoxin


enzyme_display_name: steryl-sulfatase

organism: Pseudomonas aeruginosa

substrate_name: testosterone 3-sulfate

enzyme: steryl-sulfatase

substrate: testosterone 3-sulfate


organism: Nostoc sp.


organism: Rhodobacter capsulatus

substrate_name: NADPH

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: substrate ferricyanide, pH 8.0, temperature not specified in the publication

proof_lines: presence of flavodoxin, pH 8.0, temperature not specified in the publication

substrate: NADPH


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH

proof_lines: wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C

proof_lines: wild-type, substrate ferricyanide, pH 7.2, 25°C


proof_lines: mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C

proof_lines: mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C


proof_lines: mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C

proof_lines: mutant A266Y, substrate ferricyanide, pH 7.2, 25°C

proof_lines: mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C


organism: Danio rerio

substrate_name: pregnenolone 3-sulfate

substrate: pregnenolone 3-sulfate


organism: Homo sapiens

proof_lines: pH 7.4, 37°C, enzyme from human placenta


substrate_name: testosterone 17-sulfate

substrate: testosterone 17-sulfate


organism: Sus scrofa

substrate_name: Estrone sulfate

proof_lines: 37°C, 10 min reaction time, Ringer-HEPES buffer, Vmax=24.05 fmol/s/microgram protein

substrate: Estrone sulfate


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

substrate_name: NAD(+)

substrate: NAD(+)


organism: Mus musculus

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


enzyme_display_name: chloride peroxidase

organism: Curvularia inaequalis

substrate_name: Br-; Monochlorodimedone; H2O2

enzyme: chloride peroxidase

substrate: Br-; Monochlorodimedone; H2O2


organism: Leptoxyphium fumago

substrate_name: estrone

assay_conditions_summary: pH 3

proof_lines: with Cl-, pH 3.0, temperature not specified in the publication

proof_lines: with Br-, pH 3.0, temperature not specified in the publication

substrate: estrone


enzyme_display_name: 6-aminohexanoate aminotransferase

organism: Vibrio fluvialis

enzyme: 6-aminohexanoate aminotransferase


substrate_name: benzylamine

substrate: benzylamine


substrate_name: Styrene

assay_conditions_summary: pH 3; 293.15 K; buffer pH 5

proof_lines:
enzyme in ternary system P1
from the dimer model
pH 3, without Cl-

substrate: Styrene


organism: Musa x paradisiaca

substrate_name: monochlorodimedone

proof_lines: in 50 mM phosphate buffer pH 2.75 at 30°C, with 20 mM KCl

substrate: monochlorodimedone


organism: Streptomyces toyocaensis

substrate_name: Cl-

substrate: Cl-


organism: Bacillus cereus

substrate_name: reduced flavodoxin 2

proof_lines: pH 7.5, temperature not specified in the publication, recombinant FNR1

proof_lines: pH 7.5, temperature not specified in the publication, recombinant FNR2

substrate: reduced flavodoxin 2


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


substrate_name: NADH

substrate: NADH


substrate_name: ferricytochrome c2

substrate: ferricytochrome c2


organism: Chromobacterium violaceum


organism: Pseudomonas jessenii


organism: Bos taurus

substrate_name: dehydroepiandrosterone 3-sulfate

substrate: dehydroepiandrosterone 3-sulfate


organism: Chlamydomonas reinhardtii

substrate_name: p-Nitrophenyl sulfate

substrate: p-Nitrophenyl sulfate


organism: Haliotis sp.

substrate_name: 4-nitrophenyl sulfate

substrate: 4-nitrophenyl sulfate


organism: Helix pomatia


substrate_name: dehydroepiandrosterone sulfate

proof_lines:
pH 8, 37°C
esterone 3-sulfate
37°C, mammary myoepithelial cells

substrate: dehydroepiandrosterone sulfate


organism: Macaca mulatta


substrate_name: methylumbelliferyl sulfate

proof_lines:
hydropobic form
hydrophilic form

substrate: methylumbelliferyl sulfate


organism: Patella vulgata


organism: Rattus norvegicus


organism: Aplysia californica

substrate_name: NAD+

assay_conditions_summary: pH 7.4; cofactor NAD+

substrate: NAD+


organism: Bacillus subtilis

substrate_name: NAD+; H2O

substrate: NAD+; H2O


substrate_name: 1,N6-etheno-NAD+; H2O

assay_conditions_summary: 298.15 K; cofactor NAD+

proof_lines:
spleen
25°C , seminal fluid
erythrocytes

substrate: 1,N6-etheno-NAD+; H2O


organism: Bungarus fasciatus

substrate_name: NADP+

substrate: NADP+


organism: Escherichia coli (strain K12)

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 338.9 min(-1) with NADPH as the donor. kcat is 33 min(-1) with NADP as the donor (PubMed:11085917). kcat is 0.15 sec(-1) with ferredoxin as substrate. kcat is 0.0042 sec(-1) with flavodoxin 1 as substrate. kcat is 0.0039 sec(-1) wit

substrate: NADPH


organism: Rhodobacter capsulatus

substrate_name: NADPH (in the presence of K(3)Fe(CN)(6))

proof_lines: kcat is 222 sec(-1) with K(3)Fe(CN)(6) as substrate. kcat is 20 sec(-1) with 2,6-dichlorophenolindophenol as substrate.


organism: Bacillus cereus (strain MSX-D12)

substrate_name: NAD(+)

substrate: NAD(+)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Sphingobacterium faecium (strain DSM 11690 / JCM 21820 / NBRC 15299 / NCIMB 13408 / KS 0470)


organism: Vibrio fluvialis

smiles: CCCCCN


smiles: NCCCCCC(=O)O


smiles: O=CCCCCC(=O)O


smiles: NCCCC(=O)O


proof_lines:
pH 8.0, 30°C
Raw SKiD Env: Temp=30°C, pH=8


smiles: NCCCCC(=O)O


enzyme_display_name: anthrax lethal factor endopeptidase

organism: Bacillus anthracis

enzyme: anthrax lethal factor endopeptidase


proof_lines: copper-substituted enzyme, at pH 6.5 and 20°C

proof_lines: pH 7.4, 22°C, apoprotein reconstituted in presence of Cu2+

proof_lines: pH 7.4, 22°C, apoprotein reconstituted in presence of Zn2+


organism: Thermus thermophilus

substrate_name: D-xylose

substrate: D-xylose


substrate_name: D-glucose

substrate: D-glucose


enzyme_display_name: deacetoxycephalosporin-C hydroxylase

organism: Streptomyces clavuligerus

substrate_name: cephalosporin G

enzyme: deacetoxycephalosporin-C hydroxylase

substrate: cephalosporin G


proof_lines: pH 7.5, 25°C, recombinant mutant T90A/P72L/A311V


organism: Deinagkistrodon acutus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+


organism: Homo sapiens

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

proof_lines:
membrane fraction, pH 7.0, 37°C
pH 7.2, 37°C, purified enzyme


organism: Microdochium nivale


organism: Mus musculus

substrate_name: Unknown

substrate: Unknown


organism: Mycobacterium tuberculosis


organism: Neurospora crassa


organism: Oryctolagus cuniculus


organism: Pseudomonas putida


organism: Rattus norvegicus

proof_lines:
microsomal
chromatin
plasma membrane


organism: Streptococcus pyogenes

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

proof_lines:
pH 7.4, 37°C, recombinant mutant enzyme
enzyme variant SPNJ4, pH 7.4, 37°C


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


proof_lines: enzyme variant SPNJ4 mutant R289N, pH 7.4, 37°C


organism: Actinomyces sp.

substrate_name: Fe2+; 2-oxoglutarate; deacetoxycephalosporin C


substrate_name: Penicillin N; penicillin G

substrate: Penicillin N; penicillin G


substrate_name: penicillin G; Penicillin N

substrate: penicillin G; Penicillin N


proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme


proof_lines: pH 7.5, 25°C, recombinant mutant T90A/P72L/A311V/A40V/M229I/T273A