enzyme_display_name: ferredoxin--nitrate reductase

organism: Haloferax volcanii

substrate_name: nitrate

proof_lines: 120 mM Na2CO3 pH 9, 1 M NaCl, 4 mM methyl viologen, 35 mM KNO3, 17 mM Na2S2O4 (freshly prepared in 0.1 M NaHCO3) and 0.7 mU of enzyme preparations. The samples are incubated for 20 min at 60°C

enzyme: ferredoxin--nitrate reductase

substrate: nitrate


enzyme_display_name: L-iduronidase

organism: Homo sapiens

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

ki_unit: mM

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

proof_lines:
Aldurazyme, at pH 3.5 and 37°C
recombinant enzyme, at pH 3.5 and 37°C
at pH 2.8 and 37°C

source_databases_merged: sabio_rk brenda skid

enzyme: L-iduronidase


substrate_name: 4-methylumbelliferyl alpha-L-iduronide

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

source_license: CC BY 4.0

proof_lines: pH 4.2, 32°C, recombinant wild-type enzyme

substrate: 4-methylumbelliferyl alpha-L-iduronide

source: brenda


enzyme_display_name: rhomboid protease

organism: Escherichia coli

substrate_name: BODIPY FL casein

enzyme: rhomboid protease

substrate: BODIPY FL casein


enzyme_display_name: levanase

organism: Dyadobacter fermentans

substrate_name: low molecular weight levan

proof_lines: S0.5 value, Hill coefficient 0.98, pH 6, 37°C

enzyme: levanase

substrate: low molecular weight levan


organism: Paenarthrobacter aurescens

proof_lines: S0.5 value, Hill coefficient 1.48, pH 6, 37°C

proof_lines: S0.5 value, Hill coefficient 1.44, pH 6, 37°C


organism: Shouchella lehensis G1

substrate_name: levan

km_display: Not reported

substrate: levan


proof_lines: dialdehyde starch-tapioca/bovine serum albumine cross-linked aggregate, pH 8, 30°C

proof_lines: glutaraldehyde cross-linked aggregate, pH 8, 30°C


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

mutation_type: substitution


organism: Haemophilus influenzae

substrate_name: TatA

proof_lines: K0.5 value, Hill coefficient 1.2, pH 6.0, 3°C

substrate: TatA


organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)

source_db: uniprot

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

source: uniprot


enzyme_display_name: phosphoketolase

organism: Pseudomonas aeruginosa

substrate_name: D-Fructose 6-phosphate

source_db: oed

enzyme: phosphoketolase

substrate: D-Fructose 6-phosphate

source: oed


substrate_name: D-Xylulose 5-phosphate

substrate: D-Xylulose 5-phosphate


enzyme_display_name: hydrogenase (acceptor)

organism: Methanosarcina barkeri

substrate_name: oxidized ferredoxin

enzyme: hydrogenase (acceptor)

substrate: oxidized ferredoxin


organism: Nitratidesulfovibrio vulgaris

assay_conditions_summary: pH 7


organism: Pyrococcus furiosus

assay_conditions_summary: cofactor NAD+

proof_lines: with methyl viologen as electron acceptor

proof_lines: with methylene blue as electron acceptor


organism: Solidesulfovibrio fructosivorans


organism: Streptomyces sp.

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


organism: Trichormus variabilis

substrate_name: oxidized methyl viologen

proof_lines:
cell free extract
cell-free extract, at pH 8.0 and 30°C
purified enzyme

substrate: oxidized methyl viologen


organism: Clostridium perfringens


organism: Haloferax denitrificans


organism: Hydrogenobacter thermophilus

substrate_name: reduced ferredoxin 1

substrate: reduced ferredoxin 1


organism: Leptolyngbya boryana

substrate_name: reduced ferredoxin

substrate: reduced ferredoxin


organism: Synechococcus elongatus PCC 7942 = FACHB-805

proof_lines: mutant enzyme R46K, pH and temperature not specified in the publication


organism: Vibrio natriegens

proof_lines: S0.5 value, Hill coefficient 1.08, pH 6, 37°C

proof_lines: S0.5 value, Hill coefficient 0.77, pH 6, 37°C


organism: Bifidobacterium adolescentis

substrate_name: D-sedoheptulose 7-phosphate

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

substrate: D-sedoheptulose 7-phosphate


organism: Bifidobacterium animalis subsp. lactis

substrate_name: D-xylulose 5-phosphate

substrate: D-xylulose 5-phosphate


organism: Lactiplantibacillus plantarum

substrate_name: D-fructose 6-phosphate

proof_lines:
apparent Km value, Ca2+
apparent Km value, Mg2+
apparent Km value, Mn2+

substrate: D-fructose 6-phosphate


organism: Allochromatium vinosum

substrate_name: Abz-VAA

proof_lines: NiFe hydrogenase attached to a pyrolytic graphite electrode

substrate: Abz-VAA


organism: Azotobacter vinelandii

substrate_name: oxidized methylene blue

proof_lines:
membrane-associated enzyme
purified enzyme

substrate: oxidized methylene blue


organism: Cupriavidus necator

proof_lines:
at pH 5.5, 20°C
at pH 5.0, 30°C
at pH 6.0, 30°C


organism: Desulfomicrobium norvegicum


organism: Desulfovibrio desulfuricans

substrate_name: Unknown

substrate: Unknown


organism: Desulfovibrio multispirans


organism: Desulfovibrio vulgaris

substrate_name: Hydrogen

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

substrate: Hydrogen


organism: Escherichia coli


substrate_name: methionaquinone

substrate: methionaquinone


organism: Hydrogenophaga sp.

substrate_name: methyl viologen

substrate: methyl viologen


organism: Lamprobacter modestohalophilus


organism: Methanocaldococcus jannaschii

substrate_name: methylenetetrahydromethanopterin

substrate: methylenetetrahydromethanopterin


organism: Lactococcus lactis subsp. lactis


organism: Pseudomonas aeruginosa


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

substrate_name: levan

sequence_source: source_record and UniProtKB Q8A6W6

assay_conditions_summary: pH 8

proof_lines: kcat is 32987 min(-1) with levan as substrate (PubMed:20603004). kcat is 466 sec(-1) with levan synthesized by wild-type Lsc3 from sucrose as substrate (PubMed:28103254). kcat is 366 sec(-1) with levan synthesized by wild-type Lsc3 from raf

substrate: levan


organism: Synechococcus elongatus PCC 7942 = FACHB-805

substrate_name: nitrate

proof_lines: mutant enzyme K201R, pH and temperature not specified in the publication

substrate: nitrate


proof_lines: mutant enzyme R197Q, pH and temperature not specified in the publication


proof_lines: mutant enzyme E219QR, pH and temperature not specified in the publication


proof_lines: mutant enzyme K614R, pH and temperature not specified in the publication


proof_lines: mutant enzyme R43K, pH and temperature not specified in the publication


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


proof_lines: mutant enzyme R46Q, pH and temperature not specified in the publication


proof_lines: dithionite-reduced methyl viologen as electron donor


organism: Synechococcus sp.

proof_lines: 25°C, pH 8.0, electron donor methylviologen

proof_lines: reduced methyl viologen as electron donor, recombinant enzyme expressed in Escherichia coli


organism: Synechocystis sp. PCC 6803


organism: Rattus norvegicus

source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Pyrococcus furiosus


organism: Azotobacter chroococcum


organism: Belliella baltica

substrate_name: low molecular weight levan

proof_lines: S0.5 value, Hill coefficient 1.00, pH 6, 37°C

proof_lines: S0.5 value, Hill coefficient 1.34, pH 6, 37°C

substrate: low molecular weight levan


organism: Capnocytophaga ochracea

proof_lines: S0.5 value, Hill coefficient 2.09, pH 6, 37°C

proof_lines: S0.5 value, Hill coefficient 0.82, pH 6, 37°C


organism: Homo sapiens


enzyme_display_name: alpha-N-acetylglucosaminidase

organism: Bos taurus

substrate_name: phenyl-alpha-N-acetylglucosaminide

proof_lines:
form I 0.32, form II 0.29
form I 0.067, form II 0.043

enzyme: alpha-N-acetylglucosaminidase

substrate: phenyl-alpha-N-acetylglucosaminide


proof_lines: 0.58 in the presence of 0.025% bovine serum albumin

proof_lines: pH 4.5, 37°C, without bovine serum albumin


organism: Sus scrofa

proof_lines:
partially purified enzyme
0.08 partially purified enzyme


organism: Arthrobacter sp.


organism: Bacillus subtilis


organism: Rhodotorula sp.


proof_lines:
pH 4.5, 37°C
pH 2.8
pH 5.8, 37°C, recombinant enzyme


substrate_name: phenyl alpha-L-iduronide

substrate: phenyl alpha-L-iduronide


organism: Escherichia coli

substrate_name: FL-casein

proof_lines: K0.5 value, Hill coefficient 1.2, pH 6.0, 3°C

substrate: FL-casein


enzyme_display_name: anthrax lethal factor endopeptidase

organism: Bacillus anthracis

substrate_name: fluorescein-QRRKKVYPYPME

enzyme: anthrax lethal factor endopeptidase

substrate: fluorescein-QRRKKVYPYPME


substrate_name: reduced ferredoxin

substrate: reduced ferredoxin


enzyme_display_name: taurocyamine kinase

organism: Arenicola brasiliensis

substrate_name: Taurocyamine

enzyme: taurocyamine kinase

substrate: Taurocyamine


organism: Arenicola marina

substrate_name: N-taurocyamine

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

substrate: N-taurocyamine


organism: Phytophthora infestans

proof_lines: isoform PK1, in 100 mM Tris-HCl, at pH 8.0 and 25°C

proof_lines: isoform PK2, in 100 mM Tris-HCl, at pH 8.0 and 25°C


organism: Bitis arietans

substrate_name: methylumbelliferyl-N-acetylglucosamine

substrate: methylumbelliferyl-N-acetylglucosamine


organism: Oenococcus oeni

substrate_name: D-xylulose 5-phosphate

substrate: D-xylulose 5-phosphate


organism: Rhodotorula graminis


proof_lines:
10°C, pH 7.4
fetal and adult enzyme


organism: Rattus norvegicus


organism: Pseudomonas aeruginosa


enzyme_display_name: thymine dioxygenase

organism: Rhodotorula glutinis

substrate_name: thymine

enzyme: thymine dioxygenase

substrate: thymine


organism: Neurospora crassa

sequence_source: UniProtKB:Q7RYZ9 active accession; sequence present in UniProt but not emitted by this exact-accession verdict

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


organism: Ignavibacterium album

substrate_name: ethyl-alpha-D-glucose

proof_lines: glucosyl transferase activity, pH 5.0, 37°C

substrate: ethyl-alpha-D-glucose


organism: Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16)

substrate_name: sophorose (with pNP-alpha-glucose as an acceptor)

proof_lines: kcat is 70 sec(-1) with sophorose as substrate. kcat is 12 sec(-1) with beta-(1->2)-glucotriose as substrate. kcat is 1.0 sec(-1) with methyl-alpha-glucose as substrate. kcat is 0.55 sec(-1) with ethyl-alpha-glucose as substrate. kcat is 1.


enzyme_display_name: ananain

organism: Ananas comosus

substrate_name: synthetic 7-amino-4-methylcoumarin (AMC) substrate Z-Phe-Val-Arg-AMC (at pH 5.0 and 37 degrees Celsius)

proof_lines: kcat is 13.9 sec(-1) for Z-Phe-Val-Arg-AMC. kcat is 1.58 sec(-1) for Z-Phe-Arg-AMC. kcat is 0.16 sec(-1) for Z-Arg-Arg-AMC. kcat is 9.80 sec(-1) for Pro-Leu-Gln. kcat is 7.13 sec(-1) for Val-Leu-Arg. kcat is 5.62 sec(-1) for Pro-Leu-Arg. kc

enzyme: ananain


enzyme_display_name: peptidyltransferase

substrate_name: N-Formylmethionyl-tRNA(fMet); Puromycin

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

proof_lines:
at 37°C and pH 7.5
when NH4Cl ribosomal wash is present
when NH4Cl ribosomal wash is absent

enzyme: peptidyltransferase

substrate: N-Formylmethionyl-tRNA(fMet); Puromycin


organism: Oryctolagus cuniculus

substrate_name: AcPhe-tRNA

proof_lines: from the competitive phase of the inhibition

substrate: AcPhe-tRNA


substrate_name: acetylphenylalanyl-tRNA

substrate: acetylphenylalanyl-tRNA


organism: Saccharomyces cerevisiae

proof_lines: strain 2A-J809 lacking the two genes encoding L24

proof_lines: strain L1729 lacking the single gene encoding L39

proof_lines: strain YKS99-2C missing the protein L41, the two genes RPL41A and RPL41B


proof_lines: triple mutant strain L1725 lacking the proteins L24 and L39


proof_lines:
wild type strain YKS99-2A
wild type strain 2D-J809


substrate_name: PLK

substrate: PLK


enzyme_display_name: dynamin GTPase

organism: Bos taurus

substrate_name: GTP

proof_lines: T65A mutant of the GTPase domain of dynamin

enzyme: dynamin GTPase

substrate: GTP


proof_lines: T141Q mutant of the GTPase domain of dynamin


organism: Ancylobacter novellus


organism: Bifidobacterium adolescentis

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


organism: Debaryomyces hansenii


organism: Leuconostoc mesenteroides


organism: Leuconostoc mesenteroides subsp. mesenteroides


enzyme_display_name: acetyl-CoA C-acetyltransferase

organism: Escherichia coli

substrate_name: acetyl-CoA

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

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines:
pH 7.8, 30°C
Raw SKiD Env: Temp=30°C, pH=7.8

source_databases_merged: brenda skid

enzyme: acetyl-CoA C-acetyltransferase

substrate: acetyl-CoA


organism: Homo sapiens

substrate_name: H2O; Oleoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: H2O; Oleoyl-CoA


assay_conditions_summary: pH 8.1; 298.15 K; cofactor CoA


substrate_name: Coenzyme A

substrate: Coenzyme A


organism: Clostridium acetobutylicum

substrate_name: Coenzyme A; Acetoacetyl-CoA

substrate: Coenzyme A; Acetoacetyl-CoA


organism: Cupriavidus necator

substrate_name: acetoacetyl-CoA

assay_conditions_summary: pH 8.3; 303.15 K; cofactor CoA

substrate: acetoacetyl-CoA


organism: Enterococcus faecalis

substrate_name: Acetyl-CoA

substrate: Acetyl-CoA


organism: Arabidopsis thaliana


organism: Aspergillus fumigatus

substrate_name: acetyl-CoA; acetoacetyl-CoA; CoA

source_db: brenda; skid

assay_conditions_summary: pH 8.1; 303.15 K; cofactor CoA

proof_lines:
pH 8.1, 30°C
Raw SKiD Env: Temp=30°C, pH=8.1

substrate: acetyl-CoA; acetoacetyl-CoA; CoA

source: brenda; skid


organism: Bacopa monnieri

substrate_name: acetoacetyl-CoA; acetyl-CoA

assay_conditions_summary: pH 8.9; 298.15 K; cofactor CoA

substrate: acetoacetyl-CoA; acetyl-CoA


organism: Candida tropicalis


organism: Zoogloea ramigera

substrate_name: Acetoacetyl-10-bis-demethylpantetheine 11-pivaloate; Coenzyme A


substrate_name: CTP

substrate: CTP


organism: Plasmodium falciparum

substrate_name: Ethanolamine phosphate

substrate: Ethanolamine phosphate


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


organism: Ricinus communis

substrate_name: CTP; Ethanolamine phosphate

substrate: CTP; Ethanolamine phosphate


organism: Trypanosoma brucei


assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


organism: Metallosphaera sedula

assay_conditions_summary: pH 7.5; 343.15 K; cofactor CoA


organism: Mus musculus

proof_lines:
isozyme Pcyt2alpha, at 37°C
isozyme Pcyt2beta, at 37°C


proof_lines: pH 8.0, 37°C, recombinant His-tagged mutant H146A enzyme


proof_lines: pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme


enzyme_display_name: phosphatidate phosphatase

substrate_name: H2O; Dioctanoyl phosphatidic acid

enzyme: phosphatidate phosphatase

substrate: H2O; Dioctanoyl phosphatidic acid


enzyme_display_name: protein-glutamine glutaminase

organism: Chryseobacterium proteolyticum

substrate_name: CBz-Gln-Gly

proof_lines: pH 6.5, 37°C, recombinant wild-type enzyme

enzyme: protein-glutamine glutaminase

substrate: CBz-Gln-Gly


proof_lines: pH 6.5, 37°C, recombinant mutant T211V/I271V enzyme


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: (S)-norcoclaurine synthase

organism: Thalictrum flavum

proof_lines: mutant E110A, 37°C, 0.1 M phosphate buffer pH 7.5

enzyme: (S)-norcoclaurine synthase


proof_lines: mutant Y108F, 37°C, 0.1 M phosphate buffer pH 7.5


proof_lines: wild-type, 37°C, 0.1 M phosphate buffer pH 7.5


organism: Pyrobaculum neutrophilum

assay_conditions_summary: pH 7.8; 358.15 K; cofactor CoA


organism: Rattus norvegicus


organism: Sus scrofa


enzyme_display_name: coenzyme-B sulfoethylthiotransferase

organism: Methanothermobacter marburgensis

substrate_name: Unknown

enzyme: coenzyme-B sulfoethylthiotransferase

substrate: Unknown


proof_lines: mutant enzyme L68T/M97V, at pH 7.5 and 30Â°C


enzyme_display_name: 3-hexulose-6-phosphate synthase

organism: Methylomonas aminofaciens

substrate_name: formaldehyde

enzyme: 3-hexulose-6-phosphate synthase

substrate: formaldehyde


organism: Mycobacterium gastri

substrate_name: D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


organism: Bos taurus

proof_lines:
isoenzyme A, thiolysis
enzyme B
isoenzyme B, thiolysis


substrate_name: acetyl-CoA

proof_lines: isoenzyme A, in the presence of 3.5 mM NH4+


organism: Unknown


organism: Methanothermobacter thermautotrophicus

substrate_name: coenzyme B

proof_lines:
isoenzyme I
isoenzyme II
below

substrate: coenzyme B


organism: Arabidopsis thaliana

substrate: acetyl-CoA


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

substrate_name: acetoacetyl-CoA (in law salt conditions)

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


organism: Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10)

substrate_name: CoA

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

substrate: CoA


organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)


substrate_name: acetoacetyl-CoA


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Methanosarcina thermophila

substrate_name: methyl-coenzyme M

sequence: AADIFAKFKTSMEVK

wild_type_sequence: AADIFAKFKTSMEVK

substrate: methyl-coenzyme M


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)


organism: Escherichia coli (strain K12)

substrate_name: undecaprenyl pyrophosphate

substrate: undecaprenyl pyrophosphate


organism: Homo sapiens


substrate_name: phosphatidate (isoform 1)

substrate: phosphatidate (isoform 1)


organism: Mus musculus

verification_status: unverified

data_origin: experimental

status: unverified


organism: Rattus norvegicus

substrate_name: 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate (at pH 6.5 and 37 degrees Celsius)


organism: Cavia cutleri

substrate_name: serotonin (for protein-glutamine serotonyltransferase activity)


organism: Thalictrum flavum subsp. glaucum


organism: Bacillus subtilis

assay_conditions_summary: pH 6; 310.15 K; cofactor CoA

substrate: acetoacetyl-CoA


organism: Bradyrhizobium japonicum


organism: Candida tropicalis

proof_lines: recombinant peroxisomal thiolase I, thiolysis

proof_lines: recombinant cytosolic thiolase I, thiolysis


organism: Clostridium acetobutylicum


organism: Enterococcus faecalis

proof_lines: synthesis thiolysis


organism: Escherichia coli


organism: Gallus gallus


organism: Helianthus annuus

substrate_name: Coenzyme A; Acetoacetyl-CoA

substrate: Coenzyme A; Acetoacetyl-CoA


mutation_type: deletion

proof_lines:
E252del mutant enzyme
mutant enzyme E252del


organism: Rhizobium sp.

proof_lines:
thiolysis
enzyme from bacteroids
synthesis


organism: Streptomyces collinus

proof_lines:
native thiolase
recombinant thiolase


proof_lines: kcat is 21 sec(-1) for the degradation of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl) (PubMed:17371050). kcat is 8 sec(-1) for the degradation of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl)


proof_lines: kcat is 14.8 sec(-1) for the degradation of acetoacetyl-CoA (3-oxoacyl-CoA thiolase) (PubMed:25478839). kcat is 1.4 sec(-1) for the synthesis of acetoacetyl-CoA (PubMed:25478839). kcat is 0.02 sec(-1) for octanoyl-CoA hydrolysis (PubMed:254


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

proof_lines: kcat is 18 sec(-1) (at 25 degrees Celsius, under conditions in which the heterodisulfide product is recycled via reduction by hydroxocobalamin). kcat is 0.96 sec(-1) (at 25 degrees Celsius, under conditions in which the heterodisulfide prod


organism: Chryseobacterium proteolyticum

substrate_name: casein

proof_lines: kcat is 323.8 min(-1) with casein as substrate. kcat is 974.5 min(-1) with oxidized insulin B chain as substrate. kcat is 525.9 min(-1) with Cbz-Gln-Gly as substrate. kcat is 342.8 min(-1) with Cbz-Gln-O-methyl as substrate. kcat is 410.8 m

substrate: casein


organism: Homo sapiens

substrate_name: benzyloxycarbonyl-Gln-Gly (for protein-glutamine deamidase activity)

proof_lines: kcat is 11.2 min(-1) with benzyloxycarbonyl-Gln-Gly substrate for protein-glutamine deamidase activity.


organism: Papaver somniferum

proof_lines: Sigmoidal saturation kinetics suggesting positive cooperativity in the binding of dopamine.


organism: Unknown


organism: Sus scrofa


organism: Thermus thermophilus

substrate_name: Acetyl-CoA

assay_conditions_summary: pH 8; 338.15 K; cofactor CoA

substrate: Acetyl-CoA


organism: Zoogloea ramigera


organism: Rattus norvegicus

substrate_name: CTP

proof_lines:
pH 7.8, 37°C
approximate value, pH 7.8, 37°C
pH 5.5

substrate: CTP


organism: Methanosarcina thermophila

substrate_name: methyl coenzyme M

substrate: methyl coenzyme M


organism: Methanothermobacter marburgensis

substrate_name: CoB

proof_lines: with SH-CoB6 as cosubstrate, pH not specified in the publication, at 25°C

proof_lines: with SH-CoB5 as cosubstrate, pH not specified in the publication, at 25°C

substrate: CoB


organism: Methanothrix soehngenii


substrate_name: H2O; Sphinganine 1-phosphate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: phosphatidate dispersed in sonicated microsomal lipid

proof_lines: phosphatidate bound to microsomal membrane

substrate: H2O; Sphinganine 1-phosphate


organism: Chryseobacterium cucumeris

substrate_name: CBz-Gln-Gly

substrate: CBz-Gln-Gly


organism: Niallia circulans

substrate_name: benzyloxycarbonyl-L-Gln-L-Pro

substrate: benzyloxycarbonyl-L-Gln-L-Pro


enzyme_display_name: maleimide hydrolase

organism: Agrobacterium tumefaciens

substrate_name: Phthalimide

enzyme: maleimide hydrolase

substrate: Phthalimide


organism: Pseudomonas putida

substrate_name: hydantoin

substrate: hydantoin


organism: Methylococcus capsulatus

substrate_name: D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


substrate_name: D-Ribulose 5-phosphate; Formaldehyde

substrate: D-Ribulose 5-phosphate; Formaldehyde


organism: Blastobacter sp.

substrate_name: H2O; Succinimide

substrate: H2O; Succinimide


organism: Blastobacter sp. A17p-4

substrate_name: Maleimide

substrate: Maleimide


organism: Oreochromis niloticus


substrate_name: H2O; Phthalimide

substrate: H2O; Phthalimide


proof_lines: pH 7, 60°C, KM increases about 20-30fold when the reaction temperature increases from 25 to 60°C


organism: Corydalis chinensis

substrate_name: dopamine

substrate: dopamine


organism: Eschscholtzia tenuifolia


organism: Eschscholzia californica

proof_lines: pH 7.0, 37°C, hyperbolic saturation kinetics


organism: Nandina domestica


organism: Papaver somniferum


organism: Thalictrum flavum


organism: Thalictrum flavum ssp. glaucum

proof_lines: pH 7.5, 37°C, hyperbolic saturation kinetics


organism: Bacillus sp. (in: firmicutes)

substrate_name: D-ribulose 5-phosphate; formaldehyde

proof_lines: D-ribulose 5-phosphate generated from ribose 5-phosphate, at 50°C

proof_lines: commercial D-ribulose 5-phosphate, at 50°C

substrate: D-ribulose 5-phosphate; formaldehyde


substrate_name: D-arabino-hex-3-ulose 6-phosphate; D-ribulose 5-phosphate; formaldehyde

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM sodium potassium phosphate

proof_lines: in 50 mM sodium potassium phosphate buffer, 5 mM MgCl2, at pH 7.0, at 30°C

proof_lines: in 50 mM sodium potassium phosphate buffer, 5 mM MgCl2, at pH 7.0, at 37°C


organism: Methylomonas aminofaciens

substrate_name: formaldehyde; D-ribulose 5-phosphate

assay_conditions_summary: pH 7.4; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.4), 5 mM MgCl2

substrate: formaldehyde; D-ribulose 5-phosphate


organism: Methylomonas sp.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 300 mM Tris-HCI

proof_lines: in 300 mM Tris-HCI buffer (pH 7.5), at 30°C


organism: Methylophilus methylotrophus


organism: Methylotuvimicrobium alcaliphilum


organism: Mycobacterium gastri

assay_conditions_summary: pH 7.5; 303.15 K; buffer 500 mM potassium phosphate

proof_lines: apparent value, in 50 mM potassium phosphate, pH 7.5, with 5 mM MgCl2, at 30°C

proof_lines: in 500 mM potassium phosphate buffer, at pH 7.5, at 30°C


organism: Pseudomonas sp.


organism: Pyrococcus horikoshii

substrate_name: formaldehyde

proof_lines:
recombinant HPS, at 60°C
recombinant HPS, at 80°C

substrate: formaldehyde


enzyme_display_name: coenzyme A diphosphatase

organism: Mus musculus

substrate_name: CoA

enzyme: coenzyme A diphosphatase

substrate: CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: coenzyme A

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

substrate: coenzyme A


organism: Mycolicibacterium smegmatis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


organism: Saccharomyces cerevisiae

substrate_name: oxidized CoA disulfide

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

substrate: oxidized CoA disulfide


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 4.6 sec(-1) with CoA as substrate (PubMed:10922370). kcat is 5.0 sec(-1) with CoASSCoA as substrate (PubMed:10922370). kcat is 0.133 sec(-1) with 8-oxo-dGTP as substrate using a GST-fused enzyme (PubMed:15475388).


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature R34M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature R189A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature D53A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature R39A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature L41A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature R189M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature F40A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature E115A to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis


enzyme_display_name: D-arabinose 1-dehydrogenase (NADP(+))

organism: Saccharolobus solfataricus

substrate_name: D-arabinose

assay_conditions_summary: pH 7.5; 353.15 K; cofactor NADP+

proof_lines: pH 7.5, 70°C, determined with 10 mM D-arabinose

proof_lines: pH 7.5, 70°C, determined with 0.4 mM NADP+

enzyme: D-arabinose 1-dehydrogenase (NADP(+))

substrate: D-arabinose


enzyme_display_name: hydroquinone 1,2-dioxygenase

organism: Sphingobium chlorophenolicum

proof_lines: cosubstrate 2-chloro-6-methylhydroquinone, 1,2-cleavage, pH 7.0, 23°C

proof_lines: cosubstrate 2,6-dibromohydroquinone, pH 7.0, 23°C

enzyme: hydroquinone 1,2-dioxygenase


smiles: O=O


organism: Sphingomonas sp.

substrate_name: hydroquinone

proof_lines:
pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7

substrate: hydroquinone


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

proof_lines: kcat is 23.8 sec(-1) with D-arabinose as substrate. kcat is 26.8 sec(-1) with L-fucose as substrate. kcat is 17.7 sec(-1) with L-galactose or D-ribose as substrate.


organism: Cupriavidus necator

proof_lines: pH 7.4, temperature not specified in the publication


organism: Lactococcus lactis

sequence_source: UniProt Q9CJC0 (yaiA, Lactococcus lactis subsp. lactis strain IL1403); PMID 25430846 abstract names YaiA as the hydroquinone dioxygenase.


organism: Pseudomonas fluorescens


enzyme_display_name: pestivirus NS3 polyprotein peptidase

organism: Classical swine fever virus (strain Alfort/Tuebingen)

substrate_name: Sub-UpU

enzyme: pestivirus NS3 polyprotein peptidase

substrate: Sub-UpU


organism: Candida albicans

substrate_name: L-fucose

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines: with D-arabinose as cosubstrate, at pH 8.0 and 30°C

substrate: L-fucose


substrate_name: NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines: recombinant subunit ARA1p, at pH 8.2 and 25°C

substrate: NADPH


organism: Hepacivirus hominis

substrate_name: Unknown

proof_lines: S-isomer R-isomer SCH446211

substrate: Unknown


organism: West Nile virus

proof_lines: pH and temperature not specified in the publication

proof_lines: at pH 8.0 in Tris-HCl (10 mM), CHAPS (1 mM) and glycerol (20% v/v), at 25°C


enzyme_display_name: endopeptidase Clp

organism: Escherichia coli (strain K12)

substrate_name: N-succinyl-Leu-Tyr-AMC

enzyme: endopeptidase Clp

substrate: N-succinyl-Leu-Tyr-AMC


organism: Escherichia coli

substrate_name: fEGFP-ssrA

assay_conditions_summary: pH 7.6; 303.15 K; cofactor ATP

proof_lines: presence of adaptor protein SspB, pH 7.6, 30°C

proof_lines: absence of adaptor protein SspB, pH 7.6, 30°C

substrate: fEGFP-ssrA


organism: Plasmodium falciparum

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: 30°C, pH 7.0, PfClpP is a very weak peptidase on its own


substrate_name: Arc-ssrA

proof_lines:
AKH mutant in the presence of SspB
AKH mutant

substrate: Arc-ssrA


proof_lines: wild-type, reducing conditions, 4°C, pH not specified in the publication

proof_lines: wild-type, non-reducing conditions, 4°C, pH not specified in the publication


proof_lines: mutant A153C, reducing conditions, 4°C, pH not specified in the publication


substrate_name: glucagon

proof_lines:
value below
ClpPDELTAN
ATPase activity

substrate: glucagon


organism: Staphylococcus aureus


proof_lines: mutant L144M, pH and temperature not specified in the publication


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


enzyme_display_name: 1,4-alpha-glucan branching enzyme

organism: Parageobacillus thermoglucosidasius

substrate_name: amylose

enzyme: 1,4-alpha-glucan branching enzyme

substrate: amylose


enzyme_display_name: lipoyl-dependent peroxiredoxin

organism: Xylella fastidiosa

substrate_name: [dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine

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

enzyme: lipoyl-dependent peroxiredoxin


substrate_name: Lipoamide

substrate: Lipoamide


substrate_name: tert-butyl hydroperoxide

smiles: CC(C)(C)OO

substrate: tert-butyl hydroperoxide


organism: Mycobacterium tuberculosis


substrate_name: trans-pinocarveylhydroperoxide

substrate: trans-pinocarveylhydroperoxide


substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


smiles: OO


enzyme_display_name: aminomethyltransferase

organism: Pisum sativum

substrate_name: NAD+; Glycine; 5,6,7,8-Tetrahydrofolate

assay_conditions_summary: cofactor NAD+

enzyme: aminomethyltransferase

substrate: NAD+; Glycine; 5,6,7,8-Tetrahydrofolate


organism: Rattus norvegicus


organism: Zea mays

proof_lines: amylose AS-320, pH 7.0, 30°C, chimeric enzyme form BE II-I BspHI

proof_lines: reduced amylose of an average chain-length 405, enzyme isoenzyme BE IIa


enzyme_display_name: heterotrimeric G-protein GTPase

substrate_name: H2O; GTP

enzyme: heterotrimeric G-protein GTPase

substrate: H2O; GTP


enzyme_display_name: bacterial tyrosine kinase

organism: Gallus gallus

substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

enzyme: bacterial tyrosine kinase

substrate: ATP


organism: Myxococcus xanthus

substrate_name: L-tyrosine in poly(Glu,Tyr)

substrate: L-tyrosine in poly(Glu,Tyr)


proof_lines: cytoplasmic fragment of BtkB (Ser444-Ser710), pH 7, 37°C


organism: Burkholderia cepacia

substrate_name: L-tyrosyl-[AAVHEYLSA]

substrate: L-tyrosyl-[AAVHEYLSA]


enzyme_display_name: triphosphatase

organism: Sulfolobus acidocaldarius

substrate_name: Triphosphate

enzyme: triphosphatase

substrate: Triphosphate


substrate_name: tripolyphosphate

substrate: tripolyphosphate


organism: Bos taurus

substrate_name: GTP

proof_lines: illuminated uROS is used as source of photoexited rhodopsin required for transducin activation

proof_lines: illuminated V8-uROS is used as source of photoexited rhodopsin required for transducin activation

substrate: GTP


organism: Homo sapiens

proof_lines: G36 protein phosphorylated by protein kinase M-like kinase


organism: Mus musculus


organism: Oryza sativa

proof_lines:
30°C, pH 6, presence of CaCl2, 2 mM
30°C, pH 6, presence of MgCl2, 2 mM
30°C, pH 5, presence of CuCl2, 2 mM


organism: Saccharolobus solfataricus


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.6 sec(-1) with tert-butyl hydroperoxide as substrate and AhpD as reductant and 0.1 sec(-1) with tert-butyl hydroperoxide as substrate and TrxC as reductant.


organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)

assay_conditions_summary: cofactor ATP


substrate_name: cAMP

proof_lines: kcat is 13 sec(-1) with triphosphate as substrate and Mg(2+) as cofactor. kcat is 35 sec(-1) with triphosphate as substrate and Co(2+) as cofactor. kcat is 3.4 sec(-1) with tetraphosphate as substrate and Mg(2+) as cofactor. kcat is 7.1 sec

substrate: cAMP


organism: Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)

substrate_name: PPPi (at pH 9.7 and 37 degrees Celsius)

assay_conditions_summary: pH 9.7; cofactor ATP

proof_lines: kcat is 288 sec(-1) for hydrolysis of PPPi (at pH 9.7 and 50 degrees Celsius). kcat is 76 sec(-1) for hydrolysis of PPPi (at pH 9.7 and 37 degrees Celsius). kcat is 19 sec(-1) for hydrolysis of PPPi (at pH 7.1 and 37 degrees Celsius). kcat

substrate: PPPi (at pH 9.7 and 37 degrees Celsius)


proof_lines: pH 7.5, 30°C, reduced amylose AS-320, wild-type enzyme


proof_lines: pH 7.5, 30°C, reduced amylose AS-320, mutant enzyme R384K


enzyme_display_name: lipoamidase

substrate_name: lipoyl-4-aminobenzoate; lipoyl 4-aminobenzoate; lipoyl-4-aminobenzoic acid; biotinyl-4-aminobenzoic acid; lipoyl-6-aminoquinoline

proof_lines: enzyme from serum, at pH 6.0, temperature not specified in the publication

enzyme: lipoamidase


organism: Sus scrofa

substrate_name: lipoylmethyl ester; reduced lipoyl-4-aminobenzoate; lipoyl n-butyl ester; lipoyl isopropyl ester; L-Tyr-Arg

proof_lines: pH and temperature not specified in the publication


organism: Nitrosomonas europaea

substrate_name: tripolyphosphate; ATP

assay_conditions_summary: pH 9.7; 310.15 K; cofactor ATP

proof_lines: His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+

proof_lines: His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+

proof_lines: His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+

substrate: tripolyphosphate; ATP


proof_lines: His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+

proof_lines: His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+


proof_lines: His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+


proof_lines: His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+

proof_lines: His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+

proof_lines: His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+


proof_lines: R265H mutant, 2 mM substrate in the presence of 5 mM ATP

proof_lines: R265H mutant, 2 mM substrate in the presence of 5 mM diphosphate


organism: Enterococcus faecalis

substrate_name: octanoylated domain

substrate: octanoylated domain


organism: Arabidopsis thaliana


organism: Escherichia coli (strain K12)

substrate_name: inorganic triphosphate

substrate: inorganic triphosphate


enzyme_display_name: dimethylallyltranstransferase

organism: Haematococcus lacustris

substrate_name: geranyl diphosphate

enzyme: dimethylallyltranstransferase

substrate: geranyl diphosphate


substrate_name: Isopentenyl diphosphate; Geranyl diphosphate


organism: Picea abies

substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Rattus norvegicus

substrate_name: Dimethylallyl diphosphate; Isopentenyl diphosphate


organism: Artemisia spiciformis


organism: Hevea brasiliensis

substrate_name: DMAPP

substrate: DMAPP


organism: Homo sapiens

substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


organism: Abies grandis

substrate: Dimethylallyl diphosphate; Isopentenyl diphosphate


organism: Corynebacterium glutamicum


organism: Micrococcus luteus


organism: Mycobacterium tuberculosis

proof_lines: in 50 mM sodium phosphate (pH 7.0), at 37°C


organism: Phaedon cochleariae

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

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

proof_lines: fixed substrate isopentenyl diphosphate (0.015 mM), pH and temperature not specified in the publication, metal cofactor: Co2+


organism: Vitis vinifera


organism: Escherichia coli


mutation_signature: N-terminal deletion mutant


substrate_name: reduced H-protein

substrate: reduced H-protein


substrate_name: amylose

proof_lines: amylose AS-320, pH 7.0, 30°C, wild-type enzyme

substrate: amylose


proof_lines: amylose AS-320, pH 7.0, 30°C, mutant enzyme Y300F


organism: Oryctolagus cuniculus

substrate_name: amylopectin

substrate: amylopectin


organism: Oryza sativa

proof_lines: amylose AS-1160, degree of polymerization of approximately 6,510, isoform BEI, pH 7.5, 30°C


organism: Solanum tuberosum


organism: Bos taurus

substrate_name: cholesterol

proof_lines:
in the presence of 0.45% cyclodextrin
in the presence of 4.5% cyclodextrin
by large unilamellar vesicles

substrate: cholesterol


enzyme_display_name: [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase

substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

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

substrate: ATP


substrate_name: Coenzyme A; NAD+; alpha-Ketovaline

enzyme: [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase

substrate: Coenzyme A; NAD+; alpha-Ketovaline


substrate_name: ATP; [3-Methyl-2-oxobutanoate dehydrogenase (lipoamide)]


substrate_name: phosphate

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines: 25°C, reconstituted with lipoylated recombinant E2

substrate: phosphate


substrate_name: O2; Cholesterol; Reduced adrenal ferredoxin

unit: mol/(mol*min)


substrate_name: Cholesterol; Reduced adrenal ferredoxin; O2


substrate_name: Cholest-5-ene-3beta,25-diol; Reduced ferredoxin; O2


substrate_name: BCKDH; ATP

substrate: BCKDH; ATP


enzyme_display_name: proprotein convertase 1

organism: Mus musculus

substrate_name: Unknown

enzyme: proprotein convertase 1

substrate: Unknown


proof_lines:
pH 7.0, 25°C,mixed inhibition
pH 7.0, 25°C
pH 6.5, 37°C


enzyme_display_name: steroid 15beta-monooxygenase

organism: Priestia megaterium

substrate_name: progesterone

proof_lines: pH 7.4, 30°C, for determination of Km-value the formation of the product 15beta-hydroxy-progesterone is determined

enzyme: steroid 15beta-monooxygenase

substrate: progesterone


substrate_name: deoxycorticosterone

substrate: deoxycorticosterone


enzyme_display_name: (S)-coclaurine-N-methyltransferase

organism: Coptis japonica

substrate_name: (S)-Coclaurine

enzyme: (S)-coclaurine-N-methyltransferase

substrate: (S)-Coclaurine


enzyme_display_name: sulfite dehydrogenase (cytochrome)

organism: Ancylobacter novellus

substrate_name: sulfite

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 6.0, mutant H57A

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 6.5, mutant H57A

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 7.0, mutant H57A

enzyme: sulfite dehydrogenase (cytochrome)

substrate: sulfite


proof_lines: 25°C, 20 mM Tris acetate buffer, pH 9.0, mutant Y236F

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 7.5, mutant Y236F

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236F


organism: Chlorobaculum tepidum

substrate_name: ferricytochrome c

substrate: ferricytochrome c


organism: Starkeya novella

substrate_name: H2O; Ferricytochrome c; Sulfite

substrate: H2O; Ferricytochrome c; Sulfite


substrate_name: (RS)-coclaurine

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

substrate: (RS)-coclaurine


proof_lines: mutant F332A, pH not specified in the publication, temperature not specified in the publication


substrate_name: heliamine

proof_lines: mutant Y328A, pH not specified in the publication, temperature not specified in the publication

substrate: heliamine


proof_lines: mutant W329A, pH not specified in the publication, temperature not specified in the publication


substrate_name: reduced ferredoxin

proof_lines: pH 7.4, 30°C, wild-type ferredoxin from the cyanobacterium Anabaena PCC 7119

proof_lines: pH 7.4, 30°C, wild-type flavodoxin from the cyanobacterium Anabaena PCC 7119

substrate: reduced ferredoxin


proof_lines: 25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme


proof_lines: 25°C, 20 mM Tris acetate buffer, pH 6.2, mutant R55M

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 6.6, mutant R55M

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 7.5, mutant R55M


proof_lines: 25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236Fyme


organism: Unknown

substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


enzyme_display_name: flavone 3'-O-methyltransferase

organism: Oryza sativa Japonica Group

substrate_name: S-adenosyl-L-methionine; luteolin

enzyme: flavone 3'-O-methyltransferase

substrate: S-adenosyl-L-methionine; luteolin


enzyme_display_name: clostripain

organism: Hathewaya histolytica

proof_lines: commercial enzyme preparation, in 50 mM Tris-HCl, 5 mM dithiothreitol, and 5 mM CaCl2, at pH 7.5 and 25°C

proof_lines: purified recombinant enzyme, in 50 mM Tris-HCl, 5 mM dithiothreitol, and 5 mM CaCl2, at pH 7.5 and 25°C

enzyme: clostripain


enzyme_display_name: geraniol dehydrogenase (NAD(+))

organism: Castellaniella defragrans

substrate_name: nerol

proof_lines: native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C

proof_lines: recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C

enzyme: geraniol dehydrogenase (NAD(+))

substrate: nerol


organism: Arabidopsis thaliana

proof_lines: i.e. quercetin, 30°C, pH not specified in the publication

proof_lines: i.e. mycricetin, 30°C, pH not specified in the publication


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Carpoglyphus lactis

substrate_name: geraniol

sequence_source: UniProtKB reviewed accession B2NI93, found by lit_pubmed:18422649 and fetched from UniProt FASTA.

assay_conditions_summary: pH 8.5; 295.15 K; cofactor NAD+

substrate: geraniol


organism: Acidithiobacillus ferrooxidans

substrate_name: ferricyanide

proof_lines: reaction with ferricyanide or cytochrome c

substrate: ferricyanide


organism: Acidithiobacillus thiooxidans


proof_lines:
recombinant enzyme
at pH 7.7 and 360 mV
at pH 8.0 and 264 mV


assay_conditions_summary: pH 6; buffer pH 6

proof_lines: mutant enzyme Y236F, in 20 mM bis-Tris-acetate buffer pH 6.0

proof_lines: mutant enzyme Y236F, in 20 mM Tris-acetate buffer pH 8.0


assay_conditions_summary: pH 8; buffer pH 8

proof_lines: wild type enzyme, in 20 mM Tris-acetate buffer pH 8.0

proof_lines: wild type enzyme, in 20 mM bis-Tris-acetate buffer pH 6.0


organism: Homo sapiens

proof_lines: mutant enzyme G473A, pH 8.5, using ferricyanide as the electron acceptor

proof_lines: mutant enzyme G473A, pH 7.0, using ferricyanide as the electron acceptor


proof_lines: mutant enzyme G473W, pH 8.5, using ferricyanide as the electron acceptor

proof_lines: mutant enzyme G473W, pH 7.0, using ferricyanide as the electron acceptor


assay_conditions_summary: pH 7

proof_lines: mutant enzyme G473D, pH 7.0, using ferricyanide as the electron acceptor

proof_lines: mutant enzyme G473D, pH 8.5, using ferricyanide as the electron acceptor


proof_lines: tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C


mutation_signature: tether deletion mutant enzyme DELTAKVAT

proof_lines: tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C


mutation_signature: tether deletion mutant enzyme DELTAKVA

proof_lines: tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C


proof_lines: mutant enzyme P105A/P111A, in 20 mM Tris acetate, pH 8.0, at 25°C


proof_lines: wild type enzyme, in 20 mM Tris acetate, pH 8.0, at 25°C

proof_lines: wild type enzyme, pH 8.6, using ferricyanide as the electron acceptor

proof_lines: wild type enzyme, pH 7.0, using ferricyanide as the electron acceptor


proof_lines: mutant enzyme P105A, in 20 mM Tris acetate, pH 8.0, at 25°C


proof_lines: mutant enzyme P111A, in 20 mM Tris acetate, pH 8.0, at 25°C


organism: Paracoccus pantotrophus


organism: Paracoccus versutus


organism: Rhodotorula sp.

proof_lines:
reaction with cytochrome c
reaction with ferricyanide


substrate_name: H2O; Cytochrome c; Sulfite

substrate: H2O; Cytochrome c; Sulfite


organism: Thiobacillus thioparus


organism: Coptis japonica

substrate_name: (R,S)-norreticuline

substrate: (R,S)-norreticuline


organism: Liriodendron chinense

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme


organism: Priestia megaterium

substrate_name: progesterone for the 15-beta hydroxylation

proof_lines: With deoxycorticosterone as substrate only 15-beta hydroxylation is observed.


organism: Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)

proof_lines: The values given here are for the native GeDH, the values for the recombinant protein can be found in another article (PubMed:22286981).


organism: Tanacetum cinerariifolium

substrate_name: trans-chrysanthemol

proof_lines: kcat is 0.75 sec(-1) with trans-chrysanthemol as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.64 sec(-1) with NAD(+) as substrate (in the presence of trans-chrysanthemol) (PubMed:29122986).

substrate: trans-chrysanthemol


organism: Oryza sativa subsp. japonica

substrate_name: quercetin

proof_lines: Measured at pH 7.5 and 37 degrees Celsius for all experiments.

substrate: quercetin


substrate_name: serotonin

substrate: serotonin


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


substrate_name: GlcNAc

substrate: GlcNAc


organism: Hathewaya histolytica

substrate_name: Nalpha-benzoyl-L-Lys methyl ester

sequence_source: UniProtKB reviewed P09870; BRENDA EC 3.4.22.8 organism/accession page

proof_lines:
depending on assay method
pH 7.4, 25°C

substrate: Nalpha-benzoyl-L-Lys methyl ester


organism: Tinospora cordifolia

substrate_name: (S)-norcoclaurine

proof_lines: probably allosteric enzyme, Hill coeffizient 2.6

substrate: (S)-norcoclaurine


organism: Glycine max

substrate_name: 5,7,3'-trihydroxyflavone 7-O-glucoside

substrate: 5,7,3'-trihydroxyflavone 7-O-glucoside


organism: Hordeum vulgare


organism: Oryza sativa

substrate_name: luteolin

assay_conditions_summary: pH 7.5; 310.15 K; buffer 10 mM Tris-HCl

proof_lines: OMT-15, in 10 mM Tris-HCl buffer (pH 7.5), at 37°C

proof_lines: OMT-17, in 10 mM Tris-HCl buffer (pH 7.5), at 37°C

substrate: luteolin


organism: Petroselinum crispum


organism: Zea mays


organism: Homo sapiens

substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


proof_lines:
Hep3B cell, pH 7.0, 37°C
with UDP-glucose
with UDP-N-acetylglucosamine


organism: Mesocricetus auratus

proof_lines: cosubstrate: N-acetyl-D-glucosaminyl-1,2-alpha-6-deoxy- (or-4-O-methyl-) mannosyl-1,6-beta-D-glucosyl-O-(CH2)7-CH3


organism: Rattus norvegicus


organism: Clostridium perfringens


organism: Cupriavidus pinatubonensis

substrate_name: NADH

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHCn1, via UV/VIS-NAD(P)H consumption determination, with NADPH

proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHCn1, via product determination per HPLC, with NADPH


organism: Rhodococcus opacus

substrate_name: NADPH

substrate: NADPH


organism: Sinomonas cyclohexanicum

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: Km increases as pH rises from 7.0 to 8.4


enzyme_display_name: oryzin

organism: Aspergillus heteromorphus

substrate_name: azocasein

enzyme: oryzin

substrate: azocasein


organism: Aspergillus melleus

substrate_name: Acetyl-Ala methyl ester

substrate: Acetyl-Ala methyl ester


organism: Aspergillus oryzae

substrate_name: acetyl-L-tyrosine ethyl ester

substrate: acetyl-L-tyrosine ethyl ester


organism: Aspergillus sojae

proof_lines: acetyl-(Ala)2-Phe methyl ester, Aspergillus sojae


organism: Bacillus licheniformis

substrate_name: casein

substrate: casein


proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHRo1CP, UV/VIS-NAD(P)H consumption determination

proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHRo1CP, via UV/VIS-NAD(P)H consumption determination, with NADPH


enzyme_display_name: glutathione peroxidase

substrate_name: Cumene hydroperoxide; Reduced glutathione

enzyme: glutathione peroxidase


substrate_name: glutathione

proof_lines: mutant C2S/C78S/C115S/C156S/C202S, presence of 0.03 mM H2O2, pH 7.4, 37°C

proof_lines: mutant C2S/C78S/C115S/C156S/C202S, presence of 0.10 mM H2O2, pH 7.4, 37°C

proof_lines: mutant C2S/C78S/C115S/C156S/C202S, presence of 3 mM GSH, pH 7.4, 37°C

substrate: glutathione


enzyme_display_name: glutathione oxidase

substrate_name: dithiothreitol

enzyme: glutathione oxidase

substrate: dithiothreitol


substrate_name: L-Cys

substrate: L-Cys


organism: Mus musculus


substrate_name: t-Butylhydroperoxide

substrate: t-Butylhydroperoxide


organism: Pseudoalteromonas sp. ANT506


substrate_name: H2O2; Reduced glutathione

substrate: H2O2; Reduced glutathione


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Chlamydomonas reinhardtii

proof_lines: kcat is 7.4 sec(-1) for the reduction of hydrogen peroxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) (PubMed:19690965). kcat is 7.4 sec(-1) for the reduction of tert-butyl hydroperoxide (with cytosolic thioredoxin) (at


proof_lines: kcat is 22.5 min(-1) and 30.3 min(-1) with Cu(+) and Fe(2+) as substrates, respectively.


substrate_name: bis-(2-hydroxyethyl) disulfide (HEDS)

proof_lines: kcat is 1.2 sec(-1) with bis-(2-hydroxyethyl) disulfide (HEDS) as substrate.

substrate: bis-(2-hydroxyethyl) disulfide (HEDS)


organism: Escherichia coli (strain K12)

substrate_name: phosphoadenosine 5'-phosphosulfate

substrate: phosphoadenosine 5'-phosphosulfate


organism: Aloe vera

substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


organism: Brugia pahangi

substrate_name: linolenic acid hydroperoxide

substrate: linolenic acid hydroperoxide


organism: Haemophilus influenzae


organism: Homo sapiens

substrate_name: GSH

assay_conditions_summary: pH 7; 310.15 K; buffer 50 mM PIPES

proof_lines: apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C

proof_lines: apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C

proof_lines: apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37°C

substrate: GSH


proof_lines: wild type enzyme, in the presence of 2 mM GSH, at 37°C and pH 7.0

proof_lines: wild type enzyme, in the presence of 1 mM GSH, at 37°C and pH 7.0

proof_lines: wild type enzyme, in the presence of 0.2 mM H2O2, at 37°C and pH 7.0


organism: Hyalomma dromedarii

proof_lines:
isoform Gpx2, pH 7.0, 25°C
isoform Gpx1, pH 7.0, 25°C


organism: Lateolabrax japonicus


organism: Lucilia cuprina

substrate_name: cumene peroxide

proof_lines: 27°C, pH 7.0, activity of seleno-glutathione transferase

proof_lines: 27°C, pH 7.0, reaction with H2O2, activity of seleno-glutathione transferase

proof_lines: 27°C, pH 7.0, reaction with cumene peroxide, activity of seleno-glutathione transferase

substrate: cumene peroxide


organism: Oryza sativa

substrate_name: tert-butyl hydroperoxide

substrate: tert-butyl hydroperoxide


organism: Rattus norvegicus

substrate_name: cholesterol 7beta-hydroperoxide

assay_conditions_summary: pH 7.4; 298.15 K; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.4), at 25°C

substrate: cholesterol 7beta-hydroperoxide


organism: Saccharomyces cerevisiae

proof_lines: pH 7.5, 25°C, reaction with cumene hydroperoxide


organism: Thunnus maccoyii


organism: Penicillium sp.

proof_lines: immobilized enzyme on sensor surface out of cellulose acetate


organism: Bacillus subtilis

substrate_name: 3'-phosphoadenylyl sulfate

assay_conditions_summary: pH 8

proof_lines: recombinant enzyme, pH 8.0, with thioredoxin 1

proof_lines: recombinant enzyme, pH 8.0, with substrate 3-adenylyl-sulfate

proof_lines: recombinant enzyme, pH 8.0, with glutaredoxin 1

substrate: 3'-phosphoadenylyl sulfate


organism: Escherichia coli

proof_lines: with cofactors Trx1, Trx2, or Grx1, pH 8.0


organism: Mycobacterium tuberculosis

substrate_name: adenosine 5'-phosphosulfate

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

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

substrate: adenosine 5'-phosphosulfate


proof_lines: mutant enzyme K144A, at 30°C in 100 mM bis-Tris propane buffer, pH 7.5


organism: Pseudomonas aeruginosa

substrate_name: thioredoxin I

assay_conditions_summary: pH 7.5; 293.15 K; buffer 10 mM phosphate

proof_lines: wild type enzyme, at 20°C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4

substrate: thioredoxin I


substrate_name: thioredoxin

proof_lines: with thioredoxin from E. coli as cosubstrate

proof_lines: with thioredoxin from Saccharomyces cerevisiae as cosubstrate

substrate: thioredoxin


organism: Aspergillus oryzae

substrate_name: glutathione

substrate: glutathione


substrate_name: D-Cys

substrate: D-Cys


organism: Mus musculus

substrate_name: histone octamer

substrate: histone octamer


proof_lines: All kinetic experiments are done with 10 mm Tris-HCl, 0.01% Triton X-100, and 10 mm DTT and at pH 8.5.


proof_lines: mutant enzyme S289N/S312W/S357Y, at pH 9.0 and 23°C


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: gellan tetrasaccharide unsaturated glucuronosyl hydrolase

organism: Bacillus sp. (in: firmicutes)


enzyme: gellan tetrasaccharide unsaturated glucuronosyl hydrolase


organism: Microbacterium sp. XT11

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


proof_lines:
pH 6.5, 30°C, wild-type enzyme
pH 7.5, 30°C, wild-type enzyme


substrate_name: Unknown

substrate: Unknown


organism: Bacillus sp. (strain GL1)

substrate_name: unsaturated chondroitin disaccharidee (delta0S)

mutation_signature: Δ6

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature Δ6 to reconstruct the assayed variant sequence.

proof_lines: kcat is 14.1 sec(-1) with unsaturated chondroitin (delta0S). kcat is 54.9 sec(-1) with unsaturated chondroitin disaccharide sulfated at C-6 position of GalNAc residue (delta6S).


enzyme_display_name: [isocitrate dehydrogenase (NADP(+))] kinase

substrate_name: [Isocitrate dehydrogenase (NADP+)]; ATP

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

substrate: [Isocitrate dehydrogenase (NADP+)]; ATP


substrate_name: [isocitrate dehydrogenase (NADP+)]

assay_conditions_summary: pH 7; 310.15 K; cofactor NADP+

enzyme: [isocitrate dehydrogenase (NADP(+))] kinase

substrate: [isocitrate dehydrogenase (NADP+)]


substrate_name: [isocitrate dehydrogenase (NADP+)]N15L

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

proof_lines: pH 7.5, 37°C, kinase activity at saturating ATP

substrate: [isocitrate dehydrogenase (NADP+)]N15L


substrate_name: ATP

proof_lines: pH 7.5, 37°C, mutant AceK3, kinase activity

proof_lines: pH 7.5, 37°C, mutant AceK4, kinase activity

substrate: ATP


proof_lines: pH 7.5, 37°C, wild-type and mutant AceK4, kinase activity

proof_lines: pH 7.5, 37°C, wild-type, kinase activity


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


enzyme_display_name: methyl halide transferase

organism: Arabidopsis thaliana

substrate_name: S-Adenosyl-L-methionine; Thiocyanate

enzyme: methyl halide transferase

substrate: S-Adenosyl-L-methionine; Thiocyanate


organism: Batis maritima

substrate_name: chloride

proof_lines:
pH 6.8, 22°C, recombinant enzyme
pH 6.8, 22°C, native enzyme

substrate: chloride


organism: Raphanus sativus

proof_lines: pH 7.0, 30°C, purified recombinant enzyme


organism: Brassica oleracea

proof_lines:
pH 7.5, 22°C, cosubstrate: iodide
pH 7.5, 22°C


organism: Endocladia muricata


organism: Pavlova gyrans

substrate_name: Iodide

substrate: Iodide


organism: Pavlova pinguis


organism: Phellinus pomaceus


organism: Rhizobium sp.


enzyme_display_name: cytosine deaminase

organism: Saccharomyces cerevisiae

substrate_name: cytosine

enzyme: cytosine deaminase

substrate: cytosine


enzyme_display_name: 2-methylcitrate dehydratase

organism: Escherichia coli

enzyme: 2-methylcitrate dehydratase


enzyme_display_name: poly(A)-specific ribonuclease

organism: Homo sapiens

substrate_name: Poly(A)

proof_lines: residues 1-520 with the deletion of the R3H domain, pH 7.0, temperature not specified in the publication

proof_lines: residues 1-446 with the deletion of the R3H domain, pH 7.0, temperature not specified in the publication

enzyme: poly(A)-specific ribonuclease

substrate: Poly(A)


proof_lines: N-terminal fragment residues 1-520, pH 7.0, temperature not specified in the publication

proof_lines: N-terminal fragment residues 1-446, pH 7.0, temperature not specified in the publication

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


proof_lines: subunit Bb, mutant with Cys-residues at positions 428, 435


enzyme_display_name: naringenin 7-O-methyltransferase

organism: Oryza sativa Japonica Group

proof_lines:
cultivar Nipponbare, pH 9.4, 30°C
cultivar Kasalath, pH 9.4, 30°C

enzyme: naringenin 7-O-methyltransferase


organism: Perilla frutescens

substrate_name: kaempferol

substrate: kaempferol


enzyme_display_name: cytokinin 7-beta-glucosyltransferase

substrate_name: UDPglucose; trans-Zeatin

enzyme: cytokinin 7-beta-glucosyltransferase

substrate: UDPglucose; trans-Zeatin


substrate_name: 3'-phosphoadenylyl sulfate

proof_lines: pH 9.0, 37°C, isozyme SOT18, ecotype C24

proof_lines: pH 9.0, 37°C, isozyme SOT18, ecotype Columbia-0

substrate: 3'-phosphoadenylyl sulfate


organism: Brassica napus


organism: Lachnoclostridium phytofermentans


enzyme_display_name: dual-specificity kinase

assay_conditions_summary: pH 6.8; 295.15 K; cofactor ATP

enzyme: dual-specificity kinase


substrate_name: desulfobenzylglucosinolate

proof_lines:
pH 9.0, 30°C
pH 9.0, 37°C, isozyme SOT17

substrate: desulfobenzylglucosinolate


enzyme_display_name: procollagen-proline 3-dioxygenase

enzyme: procollagen-proline 3-dioxygenase


organism: Oryza sativa

proof_lines: pH 8.5, 30°C, purified recombinant GST-tagged NOMT


enzyme_display_name: endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase


enzyme: endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase


proof_lines: 37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, wild-type enzyme


organism: Candida albicans


proof_lines: 37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q/E599Q


proof_lines: 37°C, pH 6.8, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N


proof_lines: 37°C, pH 6.7, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E599Q


organism: Mus musculus

substrate_name: CMP-N-acetyl-beta-neuraminate

proof_lines: pH and temperature not specified in the publication

substrate: CMP-N-acetyl-beta-neuraminate


proof_lines: 37°C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N/E599Q


proof_lines: 37°C, pH 6.9, pyridylamine-tagged Man9GlcNAc2, mutant enzyme H524A


proof_lines: 37°C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q

proof_lines: 37°C, pH 5.3, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q


proof_lines: truncated enzyme protein consisting of amino acids 26-340, hST3-DELTA25, pH and temperature not specified in the publication


proof_lines: truncated enzyme protein consisting of amino acids 57-340, hST3-DELTA56, pH and temperature not specified in the publication


substrate_name: ganglioside GM1a

substrate: ganglioside GM1a


enzyme_display_name: 4-hydroxybenzoate 1-hydroxylase

organism: Unknown

enzyme: 4-hydroxybenzoate 1-hydroxylase


substrate_name: complement component C3

substrate: complement component C3


substrate_name: cis-aconitate

substrate: cis-aconitate


organism: Gallus gallus

proof_lines: above, competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate


organism: Rattus norvegicus

substrate_name: Procollagen

substrate: Procollagen


organism: Candida parapsilosis

proof_lines:
recombinant enzyme, pH 7.6, 25°C
pH 7.6, 30°C
3-chloro-4-hydroxybenzoate


organism: Eucalyptus nitida

substrate_name: pinocembrin

substrate: pinocembrin


substrate_name: S-adenosyl-L-methionine

proof_lines:
cultivar Nipponbare, pH 9.5, 30°C
cultivar Kassalath, pH 9.5, 30°C
cultivar Nipponbare, pH 9.5, 30°c

substrate: S-adenosyl-L-methionine


enzyme_display_name: gentamicin 3-N-acetyltransferase

substrate_name: Acetyl-CoA; Gentamicin C1a

assay_conditions_summary: cofactor CoA

enzyme: gentamicin 3-N-acetyltransferase

substrate: Acetyl-CoA; Gentamicin C1a


organism: Raphanus sativus

substrate_name: UDPglucose

substrate: UDPglucose


organism: Opitutus terrae

proof_lines: recombinant enzyme, pH 7.0, 37°C, reverse reaction

proof_lines: recombinant enzyme, pH 7.0, 37°C, forward reaction


substrate_name: gangloside asialo-GM1

proof_lines: pH 6.4, 37°C, reaction with ganglioside GM1

substrate: gangloside asialo-GM1


organism: Campylobacter jejuni


substrate_name: Ala-Leu-Gln-Asn-Ala-Thr-Arg

proof_lines:
solublilized enzyme
solubilized enzyme
membrane-bound enzyme

substrate: Ala-Leu-Gln-Asn-Ala-Thr-Arg


substrate_name: Tyr-Asn-Leu-Thr-Ser-Val

substrate: Tyr-Asn-Leu-Thr-Ser-Val


organism: Pseudomonas chlororaphis subsp. aureofaciens

substrate_name: cytosine

substrate: cytosine


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.5; 298.15 K; buffer PBS

proof_lines:
pH 7.5, 25°C, transient kinetics
pH 7.5, 25°C, steady-state kinetics
at pH 5,7 and 8


proof_lines: mutant E64D, pH 7.5, temperature not specified in the publication


proof_lines: mutant E64A, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, pH 7.5, temperature not specified in the publication


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Serratia marcescens


organism: Yarrowia lipolytica


organism: Homo sapiens

substrate_name: poly(A) RNA

proof_lines:
mutant p74deltaR3H
mutant p54deltaR3H

substrate: poly(A) RNA


enzyme_display_name: (S)-methylmalonyl-CoA hydrolase

substrate_name: Malonyl-CoA; H2O

assay_conditions_summary: pH 6; 303.15 K; cofactor CoA

enzyme: (S)-methylmalonyl-CoA hydrolase

substrate: Malonyl-CoA; H2O


proof_lines: hydrolysis of the fluorogenic substrate follows hyperbolic kinetics

proof_lines: MUaMan, fluorogenic substrate. Vmax 36.2 nmol of 4-methylumbelliferone min-1 mg-1 of protein


organism: Sporothrix schenckii

assay_conditions_summary: pH 7; 310.15 K; buffer 50 mM MES-Tris

proof_lines: at pH 7.0 in 50 mM MES-Tris buffer and at 37°C


substrate_name: complement component C5

proof_lines: high-affinity C5 convertase (EMan,C3bC4b,C2a)

substrate: complement component C5


organism: Aspergillus fumigatus


organism: Aspergillus niger


organism: Chromobacterium violaceum


organism: Escherichia coli

proof_lines:
pH 7.5, 25°C, Zn2+CDase
pH 7.5, 25°C, CDase
pH 7.3, 37°C


organism: Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)

substrate_name: L-rhamnose

substrate: L-rhamnose


substrate_name: CMP-N-acetyl-beta-neuraminate

substrate: CMP-N-acetyl-beta-neuraminate


substrate_name: ganglioside GA1

substrate: ganglioside GA1


organism: Arabidopsis thaliana

substrate_name: desulfobenzyl glucosinolate (in cv. Columbia)


substrate_name: desulfo-benzyl glucosinolate

substrate: desulfo-benzyl glucosinolate


organism: Escherichia coli (strain K12)


organism: Yarrowia lipolytica (strain CLIB 122 / E 150)


proof_lines:
mutant D314A, pH 7.5, 37°C
pH 7.5, 37°C, mutant D314A


proof_lines: mutant enzyme D314E/F316L/D317G, pH and temperature not specified in the publication


proof_lines: mutant enzyme V152A/F316C/D317G, pH and temperature not specified in the publication


proof_lines: mutant enzyme V315L/F316V/D317G, pH and temperature not specified in the publication


proof_lines:
wild-type, pH 8.5, 30°C
pH 7.5, 25°C, wild-type enzyme
wild-type, pH 7.5, 37°C


proof_lines: reaction with dolichyl diphosphochitobiose-Man9Glc3


organism: Sus scrofa


organism: Arachis hypogaea

substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: versus ATP, pH 7.5, 30°C, recombinant mutant Y148F

proof_lines: versus histone H1, pH 7.5, 30°C, recombinant mutant Y148F

substrate: ATP


substrate_name: histone H1

proof_lines: versus ATP, pH 7.5, 30°C, recombinant mutant Y297F

substrate: histone H1


proof_lines: versus ATP, pH 7.5, 30°C, recombinant mutant Y317F

proof_lines: versus histone H1, pH 7.5, 30°C, recombinant mutant Y317F


proof_lines: versus ATP, pH 7.5, 30°C, recombinant mutant Y213F


proof_lines: versus ATP, pH 7.5, 30°C, recombinant wild-type enzyme

proof_lines: versus histone H1, pH 7.5, 30°C, recombinant wild-type enzyme


substrate_name: glucoerucin

assay_conditions_summary: pH 9; 310.15 K; buffer conditions and substrate names

proof_lines: in 80 mM Tris/HCl, pH 9.0, 9.2 mM MgCl2, at 37°C

substrate: glucoerucin


organism: Bos taurus

substrate_name: Poly(A)

assay_conditions_summary: pH 7

substrate: Poly(A)


mutation_signature: C-terminal truncated form C-terminal truncated form

mutation_type: truncation


proof_lines:
full-length 74 kDa PARN
54 kDa form
46 kDa form


enzyme_display_name: phosphomevalonate kinase

organism: Enterococcus faecalis

substrate_name: ATP; (R)-5-Phosphomevalonate

assay_conditions_summary: cofactor ATP

enzyme: phosphomevalonate kinase

substrate: ATP; (R)-5-Phosphomevalonate


substrate_name: (R)-mevalonate 5-phosphate

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

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

substrate: (R)-mevalonate 5-phosphate


substrate_name: ADP

substrate: ADP


substrate_name: (R)-mevalonate 5-diphosphate

substrate: (R)-mevalonate 5-diphosphate


enzyme_display_name: phosphonoacetaldehyde hydrolase

organism: Bacillus cereus

substrate_name: phosphonoacetaldehyde

enzyme: phosphonoacetaldehyde hydrolase

substrate: phosphonoacetaldehyde


proof_lines: triple mutant K121R/K146R/K192R, pH 7.5, 25°C


proof_lines: wild-type enzyme and mutant M49L, pH 7.5, 25°C

proof_lines: wild-type enzyme, mutant C22S, and mutant Y128F/C22S, pH 7.5, 25°C


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines:
at pH 7.2 and 37°C
at pH 7.2 and 30°C


organism: Sulfolobus solfataricus

substrate_name: (R)-5-Phosphomevalonate; ATP

substrate: (R)-5-Phosphomevalonate; ATP


smiles: O=CCP(=O)(O)O


enzyme_display_name: nigerose phosphorylase

organism: Lachnoclostridium phytofermentans

substrate_name: methyl alpha-D-glucopyranoside

enzyme: nigerose phosphorylase

substrate: methyl alpha-D-glucopyranoside


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-galactose

proof_lines: pH 7.0, 30°C, reverse phosphorolysis, donor beta-D-glucopyranose 1-phosphate

proof_lines: pH 7.0, 30°C, reverse phosphorolysis, acceptor D-glucose

substrate: D-galactose


substrate_name: H2O; Phosphonoacetaldehyde

substrate: H2O; Phosphonoacetaldehyde


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


substrate_name: D-Xylose

substrate: D-Xylose


enzyme_display_name: ketosteroid monooxygenase

organism: Rhodococcus rhodochrous

substrate_name: phenylacetone

proof_lines: mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication

enzyme: ketosteroid monooxygenase

substrate: phenylacetone


proof_lines: kcat_Km less than 0.1 1/sec*min, mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication


proof_lines: wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication


proof_lines: pH 7.0, 30°C, reverse phosphorolysis reaction, cosubstrate beta-D-glucose 1-phosphate

proof_lines: pH 7.0, 30°C, cosubstrate 3-O-alpha-D-glucopyranosyl-D-glucopyranose


substrate_name: beta-D-glucopyranose 1-phosphate

substrate: beta-D-glucopyranose 1-phosphate


proof_lines: mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication


substrate_name: NAD+; Coenzyme A; alpha-Ketoisovalerate

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Coenzyme A; alpha-Ketoisovalerate


substrate_name: Dihydrolipoamide; 3-Methylbutanoyl-CoA

substrate: Dihydrolipoamide; 3-Methylbutanoyl-CoA


organism: Paenarthrobacter nicotinovorans

proof_lines:
wild-type, PBS, pH 6.4, 30°C
wild-type, Tris/HCl, pH 8.5, 30°C
wild-type, Tris/HCl, pH 8.0, 30°C


enzyme_display_name: leishmanolysin

organism: Leishmania donovani donovani

substrate_name: casein

enzyme: leishmanolysin

substrate: casein


proof_lines: fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA484


proof_lines: fluorogenic substrate, pH 7.2, 37°C, mutant F448Y


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


organism: Leishmania mexicana

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


enzyme_display_name: 2-hydroxyacyl-CoA lyase

organism: Actinomycetospora chiangmaiensis

assay_conditions_summary: pH 7.2; 310.15 K; cofactor CoA

enzyme: 2-hydroxyacyl-CoA lyase


organism: Rattus norvegicus

substrate_name: NAD+; Coenzyme A; 2-Oxoisocaproate

substrate: NAD+; Coenzyme A; 2-Oxoisocaproate


enzyme_display_name: staphopain

organism: Staphylococcus aureus

substrate_name: cystatin C

mutation_signature: N-terminal truncation shown to impair inhibition of additional targets / N-terminal truncation shown to impair inhibition of additional targets

proof_lines: Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair inhibition of additional targets, disturbance of the host protease-inhibitor balance

enzyme: staphopain

substrate: cystatin C


substrate_name: cystatin D

mutation_signature: truncation of cystatin D shown to cause alleviated inhibition of endogenous target enzymes investigated / truncation of cystatin D shown to cause alleviated inh

proof_lines: Ala10 bond hydrolyzed by staphopain A, truncation of cystatin D shown to cause alleviated inhibition of endogenous target enzymes investigated, disturbance of the host protease-inhibitor balance

substrate: cystatin D


organism: Leishmania amazonensis

assay_conditions_summary: pH 10

proof_lines:
pH 10.0, 37Â°C
pH 10.0, 37Â°C, with secreted gp63


proof_lines: fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA389


proof_lines: fluorogenic substrate, pH 7.2, 37°C, mutant F448V


proof_lines: fluorogenic substrate, pH 7.2, 37°C, mutant S446T


proof_lines: fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA542


proof_lines: fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA420


proof_lines: fluorogenic substrate, pH 7.2, 37°C, mutant S446A


organism: Homo sapiens

substrate_name: NAD+; Coenzyme A; alpha-Ketovaline

substrate: NAD+; Coenzyme A; alpha-Ketovaline


organism: Rhodospirillales bacterium

substrate_name: formaldehyde

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

substrate: formaldehyde


proof_lines:
pH 7.4, 37°C
at pH 7.5 and 37°C


enzyme_display_name: methyltransferase cap1

organism: Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969)

substrate_name: N-acetyl-Gly-Arg-Arg-AMC

enzyme: methyltransferase cap1

substrate: N-acetyl-Gly-Arg-Arg-AMC


organism: Kokobera virus

substrate_name: ATPase of serine protease NS3

substrate: ATPase of serine protease NS3


organism: Tick-borne encephalitis virus European subtype (strain Neudoerfl)

substrate_name: ATP

substrate: ATP


organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: 1,3-beta-glucan synthase

organism: Cryptococcus neoformans (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)

substrate_name: UDP-glucose (at pH 7.75)

enzyme: 1,3-beta-glucan synthase

substrate: UDP-glucose (at pH 7.75)


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

substrate_name: (R,S)-5-phosphomevalonate (at 37 degrees Celsius)


organism: Sus scrofa

substrate_name: phosphomevalonate

substrate: phosphomevalonate


organism: Bacillus cereus

substrate_name: phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius)


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


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

substrate: phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius)


substrate_name: CBZ-Phe-Leu-Glu-pNA

substrate: CBZ-Phe-Leu-Glu-pNA


enzyme_display_name: naringenin 7-O-methyltransferase

organism: Ocimum basilicum

substrate_name: apigenin (in the presence of S-adenosyl-L-methionine)

proof_lines: kcat is 43x10(-3) sec(-1) with apigenin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 49x10(-3) sec(-1) with luteolin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat i

enzyme: naringenin 7-O-methyltransferase


proof_lines: kcat is 91x10(-3) sec(-1) with apigenin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat is 100x10(-3) sec(-1) with luteolin as substrate (in the presence of S-adenosyl-L-methionine) (PubMed:22923679). kcat

substrate: apigenin (in the presence of S-adenosyl-L-methionine)


organism: Oryza sativa subsp. japonica

substrate_name: naringenin

proof_lines: kcat is 25 sec(-1) with naringenin as substrate.

substrate: naringenin


organism: Dengue virus type 2 (strain Thailand/NGS-C/1944)

substrate_name: triphosphorylated RNA

proof_lines: Vmax with 0.65 nmol/s/ug enzyme for RTPase activity with triphosphorylated RNA as substrate.

substrate: triphosphorylated RNA


organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

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

substrate: peptide TSAVLQSGFRK-NH(2)


organism: Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)

substrate_name: nigerose

proof_lines: kcat is 67 sec(-1) for nigerose. kcat is 110 sec(-1) for D-glucose.

substrate: nigerose


organism: Cordyceps militaris (strain CM01)

proof_lines: kcat is 1.42 min(-1) for UDP-glucose (at 37 degrees Celsius and pH 7).


organism: Mus musculus

proof_lines: Vmax is 10 fold higher with Gal-beta-1,3-GalNAc than with Gal-beta-1,3-GlcNAc as substrate.


proof_lines: Vmax is 4 fold higher with Gal-beta-1,3-GalNAc than with Gal-beta-1,3-GlcNAc as substrate.


proof_lines: Relative Vmax is 2:5:1 for Gal-beta-1,3-GlcNAc, Gal-beta-1,4-GlcNAc and Gal-beta-1,3-GalNAc as substrate, respectively.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: an Asn-Tyr-Thr tripeptide

proof_lines: Glycosylates at a rate of 3.5 peptides per minute per OST.

substrate: an Asn-Tyr-Thr tripeptide


organism: Caenorhabditis elegans

substrate_name: mei-1 (Isoform a)

proof_lines: The presence of egg-4 in the assay increases the KM of mbk-2 for mei-1.

substrate: mei-1 (Isoform a)


organism: Rattus norvegicus


organism: Arabidopsis thaliana

verification_status: corrected

proof_lines: kcat is 20.9 sec(-1) with (R)-5-phosphomevalonate.

status: corrected


organism: Homo sapiens

substrate_name: complement C3

proof_lines: kcat is 1.78 sec(-1) with complement C3 as substrate.

substrate: complement C3


enzyme_display_name: cytosine deaminase

organism: Escherichia coli (strain K12)

substrate_name: cytosine

proof_lines: kcat is 185 sec(-1) for the deamination of cytosine using Fe(2+) as cofactor, kcat is 92 sec(-1) using Mn(2+) as cofactor, kcat is 52 sec(-1) using Co(2+) as cofactor, and kcat is 32 sec(-1) using Zn(2+) as cofactor (PubMed:8226944). kcat i

enzyme: cytosine deaminase

substrate: cytosine


proof_lines: kcat is 91 sec(-1) with cytosine as substrate and 17 sec(-1) with 5-fluorocytosine as substrate.


organism: Aspergillus fumigatus

substrate_name: UDPglucose

substrate: UDPglucose


organism: Cryptococcus neoformans

substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Euglena gracilis


organism: Exophiala dermatitidis


organism: Gossypium hirsutum


organism: Nakaseomyces glabratus

proof_lines:
enzyme from wild-type strain 3168
enzyme from wild-type strain 218
enzyme from wild-type strain 90030


organism: Neurospora crassa


organism: Papiliotrema laurentii


organism: Saccharomyces cerevisiae


organism: Saprolegnia monoica

proof_lines:
1,3-beta-glucan synthase 2
1,3-beta-glucan synthase 1


organism: Schizophyllum commune


organism: Staphylococcus aureus


organism: Mus musculus


organism: Rattus norvegicus

substrate_name: N-palmitoylphosphatidylethanolamine

proof_lines: 37°C, pH not specified in the publication, Triton X-100 stimulated enzyme

substrate: N-palmitoylphosphatidylethanolamine


organism: Ilyonectria destructans

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: with androstenedione and O2 as cosubstrates

proof_lines: with progesterone and NADPH as cosubstrates

proof_lines: with progesterone and O2 as cosubstrates

substrate: NADPH


organism: Neonectria radicicola

substrate_name: H+; NADPH; O2; Progesterone

assay_conditions_summary: cofactor NADP+

substrate: H+; NADPH; O2; Progesterone


organism: Rhodococcus rhodochrous

assay_conditions_summary: pH 8.3; 310.15 K; cofactor NADPH


organism: Dengue virus

substrate_name: S-adenosyl-L-methionine

assay_conditions_summary: pH 10; 295.15 K; buffer glycine

proof_lines: apparent value, in glycine buffer (pH 10.0), at 22°C

substrate: S-adenosyl-L-methionine


organism: Usutu virus

proof_lines: methyltransferase domain of NS5, at pH 7.4 and 30°C


organism: Bos taurus

substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


organism: Oryctolagus cuniculus

substrate_name: NAD+; Coenzyme A; 3-Methyl-2-oxopentanoate


organism: Achlya ambisexualis


organism: Arabidopsis thaliana


organism: Arachis hypogaea


enzyme_display_name: corrinoid adenosyltransferase EutT

organism: Listeria monocytogenes serotype 1/2a

substrate_name: cob(II)alamin

proof_lines: mutant D110N, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant D110N, Khalf value, Hill coefficient 1.2, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant D110N, Khalf value, Hill coefficient 2.5, pH not specified in the publication, temperature not specified in the publication

enzyme: corrinoid adenosyltransferase EutT

substrate: cob(II)alamin


substrate_name: ATP

proof_lines: mutant E207Q, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant E207Q, Khalf value, Hill coefficient 2.4, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant E207Q, Khalf value, Hill coefficient 1.7, pH not specified in the publication, temperature not specified in the publication

substrate: ATP


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

proof_lines: wild-type, Khalf value, Hill coefficient 1.9, pH not specified in the publication, temperature not specified in the publication

proof_lines: wild-type, Khalf value, Hill coefficient 2.3, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant T88V, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant T88V, Khalf value, Hill coefficient 1.8, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant T88V, Khalf value, Hill coefficient 1.2, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant K98Q, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant K98Q, Khalf value, Hill coefficient 1.7, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant K98Q, Khalf value, Hill coefficient 0.9, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant R200K, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant R200K, Khalf value, Hill coefficient 1.3, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant R200K, Khalf value, Hill coefficient 1.9, pH not specified in the publication, temperature not specified in the publication


substrate_name: ATP; (R)-5-Phosphomevalonate

substrate: ATP; (R)-5-Phosphomevalonate


organism: Catharanthus roseus


organism: Enterococcus faecalis


organism: Hevea brasiliensis

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP


organism: Homo sapiens


proof_lines:
wild-type, 30°C, pH 7.0
wild-type, 30°C, pH 8.0


enzyme_display_name: arsenate reductase (donor)

organism: Oryza sativa

substrate_name: reduced glutaredoxin

enzyme: arsenate reductase (donor)

substrate: reduced glutaredoxin


substrate_name: arsenate

substrate: arsenate


enzyme_display_name: urethanase

organism: Candida parapsilosis

substrate_name: ethyl carbamate

proof_lines: mutant N194V, 40°C, pH not specified in the publication

enzyme: urethanase

substrate: ethyl carbamate


substrate_name: 2-aminomuconate semialdehyde

proof_lines: Cu-substituted enzyme, pH 7.0, temperature not specified in the publication

proof_lines: enzyme with 64.4% zinc ion occupancy, pH 7.0, temperature not specified in the publication

substrate: 2-aminomuconate semialdehyde


organism: Rattus norvegicus

proof_lines:
pH 6.0, 25°C, kidney enzyme
pH 6.0, 25°C, liver enzyme


enzyme_display_name: streptomycin 3''-adenylyltransferase

organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 7.5; 296.15 K; cofactor ATP

enzyme: streptomycin 3''-adenylyltransferase


mutation_signature: C-terminal deletion mutant

proof_lines: C-terminal deletion mutant, pH 7.5, 23°C


substrate_name: spectinomycin

substrate: spectinomycin


substrate_name: streptomycin

substrate: streptomycin


enzyme_display_name: 2-phosphinomethylmalate synthase

organism: Streptomyces hygroscopicus

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.8; 298.15 K; cofactor CoA

proof_lines: pH 7.8, 25°C, mutant enzyme W112A, apparent KM value from Michaelis-Menten plots due to inability to accurately measure activity at substrate concentrations less than 0.0025 mM

enzyme: 2-phosphinomethylmalate synthase

substrate: acetyl-CoA


proof_lines: pH 7.8, 25°C, mutant enzyme E82A, apparent KM value from Michaelis-Menten plots due to inability to accurately measure activity at substrate concentrations less than 0.0025 mM


organism: Bifidobacterium bifidum

substrate_name: H2O; 2'-Fucosyllactose

substrate: H2O; 2'-Fucosyllactose


organism: Streptosporangium roseum

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


organism: Thermotoga maritima

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


enzyme_display_name: glutamin-(asparagin-)ase

organism: Acinetobacter glutaminasificans

substrate_name: H2O; L-Glutamine

enzyme: glutamin-(asparagin-)ase

substrate: H2O; L-Glutamine


substrate_name: oxaloacetic acid

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: oxaloacetic acid


proof_lines: pH 7.8, 25°C, mutant enzyme E82Q, apparent KM value from Michaelis-Menten plots due to inability to accurately measure activity at substrate concentrations less than 0.0025 mM


proof_lines: pH 7.8, 25°C, mutant enzyme R173A, apparent KM value from Michaelis-Menten plots due to inability to accurately measure activity at substrate concentrations less than 0.0025 mM


enzyme_display_name: acetylputrescine deacetylase

substrate_name: Boc-Lys-(Ac)-AMC

enzyme: acetylputrescine deacetylase

substrate: Boc-Lys-(Ac)-AMC


proof_lines: mutant T111L, 40°C, pH not specified in the publication


proof_lines: wild-type, 40°C, pH not specified in the publication


proof_lines: mutant Y133A, 40°C, pH not specified in the publication


enzyme_display_name: reticuline oxidase

organism: Eschscholzia californica

substrate_name: (S)-scoulerine

enzyme: reticuline oxidase

substrate: (S)-scoulerine


organism: Shewanella sediminis

substrate_name: tetrachloroethene

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

substrate: tetrachloroethene


organism: Vitis vinifera

substrate_name: coumaroyl-CoA

assay_conditions_summary: pH 6.5; 303.15 K; cofactor CoA

substrate: coumaroyl-CoA


substrate_name: cyanidin 3-O-beta-D-glucoside

substrate: cyanidin 3-O-beta-D-glucoside


substrate_name: delphinidin 3-O-beta-D-glucoside

substrate: delphinidin 3-O-beta-D-glucoside


substrate_name: cyanidin 3-O,5-O-beta-D-diglucoside

substrate: cyanidin 3-O,5-O-beta-D-diglucoside


substrate_name: arsenate

substrate: arsenate


substrate_name: (S)-reticuline

substrate: (S)-reticuline


assay_conditions_summary: cofactor FAD


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: malvidin 3-O-beta-D-glucoside

substrate: malvidin 3-O-beta-D-glucoside


enzyme_display_name: flavonoid 4'-O-methyltransferase

organism: Streptomyces sp. KCTC 0041BP

substrate_name: S-adenosyl-L-methionine

enzyme: flavonoid 4'-O-methyltransferase

substrate: S-adenosyl-L-methionine


substrate_name: quercetin

substrate: quercetin


substrate_name: peonidin 3-O-beta-D-glucoside

substrate: peonidin 3-O-beta-D-glucoside


enzyme_display_name: meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I

organism: Mycobacterium tuberculosis

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 1-deoxy-D-xylulose-5-phosphate synthase

organism: Escherichia coli

substrate_name: D-Glyceraldehyde 3-phosphate; Pyruvate

enzyme: 1-deoxy-D-xylulose-5-phosphate synthase

substrate: D-Glyceraldehyde 3-phosphate; Pyruvate


substrate_name: D-glyceraldehyde 3-phosphate

proof_lines: pH 8, temperature not specified in the publication

substrate: D-glyceraldehyde 3-phosphate


substrate_name: pyruvate

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

substrate: pyruvate


proof_lines: mutant lacking loop 190-234, pH 8.0, temperature not specified in the publication


substrate_name: guanine9 in tRNAValUAC

substrate: guanine9 in tRNAValUAC


organism: Saccharomyces cerevisiae

substrate_name: guanine9 in tRNAGlyGCC

proof_lines: tRNA from Schizosaccharomyces pombe, recombinant enzyme, pH and temperature not specified in the publication

substrate: guanine9 in tRNAGlyGCC


organism: Schizosaccharomyces pombe

substrate_name: guanine9 in tRNAGly

substrate: guanine9 in tRNAGly


organism: Thermococcus kodakarensis

proof_lines: pH 8.0, 40°C, recombinant enzyme, tRNA substrate from Saccharomyces cerevisiae

proof_lines: pH 8.0, 50°C, recombinant enzyme, tRNA substrate from Thermococcus kodakarensis


organism: EDTA-degrading bacterium BNC1

substrate_name: ethylenediaminetetraacetate

proof_lines: mutant P291A, presence of Mg2+, pH 7.6, temperature not specified in the publication

substrate: ethylenediaminetetraacetate


proof_lines: mutant Q58A, presence of Mg2+, pH 7.6, temperature not specified in the publication


proof_lines: mutant R68A, presence of Mg2+, pH 7.6, temperature not specified in the publication


proof_lines: mutant W11A, presence of Mg2+, pH 7.6, temperature not specified in the publication


enzyme_display_name: dibenzothiophene monooxygenase

organism: Paenibacillus sp.

substrate_name: benzothiophene

enzyme: dibenzothiophene monooxygenase

substrate: benzothiophene


organism: Rhodococcus erythropolis

substrate_name: dibenzothiophene

proof_lines: mutant enzyme A101K/W327C, calculated, pH and temperature not specified in the publication

substrate: dibenzothiophene


proof_lines: mutant enzyme A101K, calculated, pH and temperature not specified in the publication


organism: Plasmodium vivax

proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas aeruginosa


enzyme_display_name: mannosyl-3-phosphoglycerate synthase

organism: Pyrococcus horikoshii

substrate_name: Glycerate 3-phosphate; GDPmannose

enzyme: mannosyl-3-phosphoglycerate synthase

substrate: Glycerate 3-phosphate; GDPmannose


organism: Rubrobacter xylanophilus

substrate_name: GDP-mannose

proof_lines: A164S/A208S/F211Y mutant, with GDP-mannose

substrate: GDP-mannose


proof_lines: mutant enzyme W327C, calculated, pH and temperature not specified in the publication


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


proof_lines: mutant enzyme A101K/W327C/P413A, calculated, pH and temperature not specified in the publication


proof_lines: mutant Q294A, presence of Mg2+, pH 7.6, temperature not specified in the publication


proof_lines: wild-type, presence of Mg2+ and flavin reductase from Escherichia coli, pH 7.6, temperature not specified in the publication

proof_lines: wild-type, presence of Mg2+ and oxidoreductase EmoB, pH 7.6, temperature not specified in the publication

proof_lines: wild-type, presence of Mg2+, pH 7.6, temperature not specified in the publication


smiles: O=C(O)CN(CCN(CC(=O)O)CC(=O)O)CC(=O)O


proof_lines: no addition of divalent ions, pH 7.8, 35°C


enzyme_display_name: aliphatic sulfonate oxidoreductase

organism: Pyrococcus furiosus

substrate_name: hexanal

proof_lines:
at pH 8.0 and 80Â°C
at pH 8.4 and 60Â°C

enzyme: aliphatic sulfonate oxidoreductase

substrate: hexanal


enzyme_display_name: fatty acid kinase

organism: Cereibacter sphaeroides

substrate_name: valerate

sequence_source: UniProtKB Q3IYF1 direct accession check; sequence exists but is not emitted in this exact-accession lane

smiles: CCCCC(=O)O

enzyme: fatty acid kinase

substrate: valerate


substrate_name: acetate

smiles: CC(=O)O

substrate: acetate


substrate_name: ATP

assay_conditions_summary: pH 5.7; 310.15 K; cofactor ATP

proof_lines: with acetate as cosubstrate, at pH 5.7 and 37°C

substrate: ATP


proof_lines:
wild-type
wild-type, with GDP-mannose


organism: Thermus thermophilus


enzyme_display_name: oleanolate 3-O-glucosyltransferase

organism: Barbarea vulgaris

substrate_name: UDP-alpha-D-glucose

enzyme: oleanolate 3-O-glucosyltransferase

substrate: UDP-alpha-D-glucose


substrate_name: Isobutyrate

smiles: CC(C)C(=O)O

substrate: Isobutyrate


substrate_name: propionate

substrate: propionate


substrate_name: Butyrate

smiles: CCCC(=O)O

substrate: Butyrate


enzyme_display_name: amine sulfotransferase

organism: Homo sapiens

enzyme: amine sulfotransferase


organism: Arabidopsis thaliana


substrate_name: Inositol 1,3,4,5-tetrakisphosphate

proof_lines: mutant enzyme F593D/L597D, at pH 7.0 and 23°C

substrate: Inositol 1,3,4,5-tetrakisphosphate


organism: Mus musculus


organism: Oryctolagus cuniculus


organism: Oryza sativa

substrate_name: H2O; 4-Nitrophenyl phosphate

substrate: H2O; 4-Nitrophenyl phosphate


organism: Rattus norvegicus


enzyme_display_name: (R)-specific secondary-alkylsulfatase (type III)

organism: Pseudomonas sp. DSM 6611

substrate_name: (2R)-octan-2-yl hydrogen sulfate

proof_lines: mutant H317A, pH not specified in the publication, temperature not specified in the publication

substrate: (2R)-octan-2-yl hydrogen sulfate


proof_lines: mutant S233Y, pH not specified in the publication, temperature not specified in the publication

enzyme: (R)-specific secondary-alkylsulfatase (type III)


proof_lines: mutant F250G, pH not specified in the publication, temperature not specified in the publication


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


proof_lines: mutant S233F/F250S, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant S233F/F250G, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant S233Y/F250G, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant Y417F, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: sialate O-acetylesterase

organism: Danio rerio

substrate_name: 4-nitrophenyl acetate

enzyme: sialate O-acetylesterase

substrate: 4-nitrophenyl acetate


organism: Tannerella forsythia


proof_lines: mutant Y417H, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: isoamylase

substrate_name: amylopectin

enzyme: isoamylase

substrate: amylopectin


enzyme_display_name: inosine nucleosidase

organism: Bacillus thuringiensis

substrate_name: Inosine

enzyme: inosine nucleosidase

substrate: Inosine


enzyme_display_name: gingipain R

organism: Porphyromonas gingivalis

substrate_name: Unknown

proof_lines: pH 7.6, HRgpA and RgpB, in absence of Zn2+

enzyme: gingipain R

substrate: Unknown


enzyme_display_name: asclepain

organism: Asclepias curassavica

enzyme: asclepain


substrate_name: Nalpha-CBZ-L-Gln-4-nitrophenyl ester

substrate: Nalpha-CBZ-L-Gln-4-nitrophenyl ester


enzyme_display_name: phytepsin

organism: Cynara cardunculus

proof_lines: native mature enzyme, at pH 4.0 and 37°C

proof_lines: recombinant proenzyme with plant-specific insert domain, at pH 4.0 and 37°C

proof_lines: recombinant proenzyme without plant-specific insert domain, at pH 4.0 and 37°C

enzyme: phytepsin


enzyme_display_name: intramembrane prenyl-peptidase Rce1

enzyme: intramembrane prenyl-peptidase Rce1


substrate_name: acetyl-L-Cys(farnesyl)VIS

substrate: acetyl-L-Cys(farnesyl)VIS


enzyme_display_name: phosphonopyruvate decarboxylase

organism: Streptomyces viridochromogenes

proof_lines: mutant enzyme S25D, at pH 8.0 (HEPES buffer) and at 30°C

enzyme: phosphonopyruvate decarboxylase


proof_lines: mutant enzyme D297N, at pH 8.0 (HEPES buffer) and at 30°C


organism: Saccharomyces cerevisiae

proof_lines:
at pH 7.5 and 30°C
at pH 7.5 and 35°C


substrate_name: N-palmitoylethanolamine

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

proof_lines: pH 4.6, temperature not specified in the publication

substrate: N-palmitoylethanolamine


proof_lines: pH 4.5, 37°C, recombinant His6-tagged enzyme


enzyme_display_name: acetylputrescine deacetylase

organism: Marinobacter subterrani

proof_lines: pH 7.75, 25°C, in presence of 10 mM KCl, recombinant enzyme

proof_lines: pH 7.75, 25°C, in absence of KCl, recombinant enzyme

enzyme: acetylputrescine deacetylase


enzyme_display_name: reticuline oxidase

organism: Unknown

substrate_name: (S)-reticuline

enzyme: reticuline oxidase

substrate: (S)-reticuline


substrate_name: tetrachloroethene

substrate: tetrachloroethene


enzyme_display_name: gastricsin

substrate_name: acetyl-Tyr-Leu-Val-His methyl ester

enzyme: gastricsin

substrate: acetyl-Tyr-Leu-Val-His methyl ester