proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L


enzyme_display_name: ferredoxin--NADP(+) reductase

organism: Rhodobacter capsulatus

substrate_name: NADPH

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

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

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines:
diaphorase activity, pH 8.0
pH 8.0

enzyme: ferredoxin--NADP(+) reductase

substrate: NADPH

source: brenda


enzyme_display_name: pyranose oxidase

organism: Lyophyllum shimeji

substrate_name: L-sorbose

proof_lines: using D-glucose as cosubstrate, at 30°C, pH 6.5

enzyme: pyranose oxidase

substrate: L-sorbose


organism: Peniophora sp.

substrate_name: D-glucose

kcat_display: Not reported

substrate: D-glucose


organism: Phanerodontia chrysosporium

substrate_name: ferricyanide

proof_lines: substrate ferricyanide (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3-ethylbenzthiazolinesulfo

proof_lines: substrate 2-chloro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3-ethylbenzth

proof_lines: substrate 2-methyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3-ethylbenzth

substrate: ferricyanide


organism: Phlebiopsis gigantea

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

mutation_type: substitution

proof_lines: pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag


proof_lines: pH 7.3, 22°C, recombinant wild-type enzyme


substrate_name: D-allose

proof_lines: pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag

substrate: D-allose


organism: Trametes ochracea

substrate_name: ferricenium ion

proof_lines: E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

substrate: ferricenium ion


proof_lines: L537G/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 3

proof_lines: L537G/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537G/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5


assay_conditions_summary: pH 6.5; 303.15 K; buffer 50 mM phosphate

proof_lines: E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C


assay_conditions_summary: pH 6.5; 303.15 K; cofactor FAD

proof_lines: L537W/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537W/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5

proof_lines: L537W/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,


proof_lines: L537G/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537G/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,


proof_lines: L537G mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


substrate_name: D-galactose

proof_lines: L537W mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

substrate: D-galactose


proof_lines: L537W/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537W/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 3


assay_conditions_summary: pH 6.5; 323.15 K; cofactor FAD

proof_lines: T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay

proof_lines: T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay

proof_lines: T169G/E542K/V546C, mutant, 50°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay


assay_conditions_summary: cofactor FAD

proof_lines: R472L, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: R472L, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: Q448N, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: Q448N, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546P/T169G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546P/T169G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: T169S, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: T169S, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546C/T169N, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546C/T169N, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: Q448S, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: Q448S, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: T169N, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: T169N, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: H548R, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: H548R, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: H548I, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: H548I, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


assay_conditions_summary: pH 6.5; 333.15 K; buffer 50 mM phosphate; cofactor FAD

proof_lines: V546C, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: mutant enzyme V546C, pH and temperature not specified in the publication


proof_lines: R472G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: R472G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546G/T169G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546G/T169G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: Q448C, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: Q448C, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546P, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546P, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: N593R, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: N593R, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: mutant enzyme H450G/V546C, pH and temperature not specified in the publication


proof_lines: mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: mutant enzyme H450G, pH and temperature not specified in the publication


assay_conditions_summary: pH 6.5; 333.15 K; buffer 50 mM phosphate

proof_lines: mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C


assay_conditions_summary: pH 6.5; 303.15 K; buffer 50 mM KH2PO4

proof_lines: wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: wild-type, mutant, 30°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay

proof_lines: wild-type, mutant, 30°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay


proof_lines: mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


substrate_name: D-melibiose

proof_lines: mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

substrate: D-melibiose


proof_lines: mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme T196G/V546C, pH and temperature not specified in the publication


proof_lines: mutant enzyme T169G, pH and temperature not specified in the publication

proof_lines: T169G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: T169G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: mutant enzyme H167A, pH and temperature not specified in the publication


proof_lines: mutant enzyme Q448H, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme Q448H, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme Q448H, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C


organism: Anabaena sp.

substrate_name: NADH

assay_conditions_summary: cofactor NADP+

proof_lines: mutant T155G/A160T/L263P/R264P/G265P, called PP5

substrate: NADH


proof_lines: mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines: with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C


organism: Bacillus subtilis

substrate_name: oxidized [2Fe-2S]-[rubredoxin]

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

substrate: oxidized [2Fe-2S]-[rubredoxin]


organism: Chlorobaculum tepidum

proof_lines:
cosubstrate NADH, pH 7, 25°C
pH 7, 25°C
cosubstrate NADPH, pH 7, 25°C


organism: Escherichia coli

substrate_name: Fe(III)-EDTA

proof_lines: in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25°C

substrate: Fe(III)-EDTA


substrate_name: oxidized ferredoxin

mutation_type: deletion

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

substrate: oxidized ferredoxin


organism: Lathyrus oleraceus

proof_lines: mutant lacking the beta-hairpin, pH 8.0, 30°C

proof_lines: mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C


organism: Plasmodium falciparum

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q


proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A


assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor

proof_lines: using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Streptomyces clavuligerus

substrate_name: penicillin G

proof_lines: recombinant mutant S261M, pH not specified in the publication, 30°C

enzyme: deacetoxycephalosporin-C synthase

substrate: penicillin G


proof_lines: mutant I305M/T213V, pH and temperature not specified in the publication


proof_lines: mutant I305M/S261M, pH and temperature not specified in the publication


proof_lines: mutant C155Y/Y184H/V275I/C281Y, pH and temperature not specified in the publication


proof_lines: mutant I305L, pH and temperature not specified in the publication


enzyme_display_name: cathepsin B

organism: Homo sapiens

proof_lines: pH 6.0, 25°C, mutant H110A in presence of heparin

enzyme: cathepsin B


proof_lines: pH 6.0, 25°C, mutant H111A in presence of heparin


assay_conditions_summary: pH 6; 298.15 K; buffer 0.4 M sodium potassium phosphate

proof_lines: pH 6.0, 25°C, wild-type enzyme in presence of heparin

proof_lines: wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C


proof_lines: recombinant mutant S261A, pH not specified in the publication, 30°C


proof_lines: recombinant mutant Y184A, pH not specified in the publication, 30°C


proof_lines: recombinant mutant Q126M, pH not specified in the publication, 30°C


proof_lines: recombinant mutant T213V, pH not specified in the publication, 30°C


organism: Hapsidospora chrysogena


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


enzyme_display_name: isocitrate dehydrogenase (NAD(+))

organism: Xylella fastidiosa

substrate_name: NADP+

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

enzyme: isocitrate dehydrogenase (NAD(+))

substrate: NADP+


substrate_name: NAD+

proof_lines: mutant enzymeD268K/I269Y/A275V, at pH 8.0 and 25°C

substrate: NAD+


proof_lines: mutant enzyme D268K/I269Y, at pH 8.0 and 25°C


proof_lines: mutant I305M, pH and temperature not specified in the publication


proof_lines: mutant I305M/T213V/S261M, pH and temperature not specified in the publication


proof_lines: mutantI305M/T213V/M73T, pH and temperature not specified in the publication


substrate_name: Penicillin N

proof_lines: pH 6.5, 30°C, recombinant mutant V275I/I305M

proof_lines: pH 6.5, 30°C, recombinant mutants V275I and I305M

substrate: Penicillin N


proof_lines: pH 6.5, 30°C, recombinant mutants G79E and I305M


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

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

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


proof_lines: 30°C, double mutant with truncation at residue 310 and M306I


proof_lines: 30°C, triple mutant with truncation at residue 310, M306I and N305L


proof_lines: mutant R308I, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant R308L, pH not specified in the publication, temperature not specified in the publication


source_db: oed

source: oed


substrate_name: NAD+; Isocitrate

km_display: Not reported

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

substrate: NAD+; Isocitrate


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+


organism: Campylobacter curvus

assay_conditions_summary: 298.15 K; cofactor NADP+


organism: Campylobacter sp.

proof_lines: pH 75, 25°C, recombinant His6-tagged enzyme


assay_conditions_summary: 298.15 K; cofactor NAD+


proof_lines: pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R


organism: Congregibacter litoralis

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; 308.15 K; cofactor NADP+


proof_lines: mutant D487R/L488H, with Mn2+, pH 7.5, 35°C


proof_lines: wild-type enzyme, with Mg2+, pH 7.5, 35°C

proof_lines: wild-type enzyme, with Mn2+, pH 7.5, 35°C


enzyme_display_name: laccase

organism: Geobacter metallireducens

enzyme: laccase


organism: Lentinus brumalis

assay_conditions_summary: pH 4; 303.15 K; buffer McIlvaine

proof_lines:
in McIlvaine buffer (pH 4.0), at 30°C
in McIlvaine buffer (pH 5.0), at 30°C


organism: Panus rudis


enzyme_display_name: peroxidase

organism: Amycolatopsis sp.

substrate_name: H2O2; 2,4-Dichlorophenol

enzyme: peroxidase

substrate: H2O2; 2,4-Dichlorophenol


organism: Armoracia rusticana


substrate_name: 2-Chloro-4-methoxyphenol; H2O2

substrate: 2-Chloro-4-methoxyphenol; H2O2


substrate_name: L-Dopa; H2O2

substrate: L-Dopa; H2O2


organism: Bacillus altitudinis

substrate_name: H2O2; Sinapate

substrate: H2O2; Sinapate


enzyme_display_name: phenylalanine 4-monooxygenase

assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM Na-HEPES

proof_lines: mutant enzyme R155H, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C

enzyme: phenylalanine 4-monooxygenase


proof_lines: mutant enzyme D143G, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


substrate_name: L-phenylalanine

assay_conditions_summary: pH 6.8; 310.15 K; buffer 50 mM potassium phosphate

proof_lines: mutant enzyme R68S, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme R68S, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme R68S, using S-carboxymethyl-L-cysteine as cosubstrate

substrate: L-phenylalanine


proof_lines: mutant enzyme V388M, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme V388M, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme V388M, using S-carboxymethyl-L-cysteine as cosubstrate


proof_lines: mutant enzyme I65T, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme I65T, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme I65T, using S-carboxymethyl-L-cysteine as cosubstrate


proof_lines: mutant enzyme R261Q, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme R261Q, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme R261Q, using S-carboxymethyl-L-cysteine as cosubstrate


proof_lines: mutant enzyme Y414C, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme Y414C, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme Y414C, using S-carboxymethyl-L-cysteine as cosubstrate


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


organism: Rattus norvegicus

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


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


organism: Trametes ochracea

substrate_name: D-glucose

substrate: D-glucose


organism: Cephalosporium acremonium

substrate_name: Penicillin G; 2-Oxoglutarate; O2

substrate: Penicillin G; 2-Oxoglutarate; O2


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


proof_lines: pH 7.5, 30°C, recombinant mutant DELTA310/N305L/M306I


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Penicillin N; 2-Oxoglutarate; O2

substrate: Penicillin N; 2-Oxoglutarate; O2


proof_lines: mutant enzyme DELTAI305-310, DELTAR306-310 and mutant DELTAR307-310


organism: Bos taurus


organism: Burkholderia pseudomallei


organism: Cucumis sativus

substrate_name: H2O2; 4-Methoxy-alpha-naphthol

substrate: H2O2; 4-Methoxy-alpha-naphthol


organism: Euphorbia characias


organism: Caenorhabditis elegans


organism: Dictyostelium discoideum


organism: Homo sapiens


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

proof_lines: pH 7.0, 25°C, recombinant enzyme, versus (6R)-tetrahydrobiopterin

source_databases_merged: sabio_rk brenda skid


proof_lines: mutant enzyme R408W, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


proof_lines: mutant enzyme L348V, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


proof_lines: mutant enzyme P416Q, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


proof_lines: wild type enzyme, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37°C

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C


proof_lines: V546C/T169G/L537W mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3-ethylbenzthiazo

proof_lines: V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled ass

proof_lines: mutant enzyme V546C/T169G/L537W, at pH 6.5 and 30°C


proof_lines: V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3

proof_lines: V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay usi

proof_lines: mutant enzyme V546C/E542K, at pH 6.5 and 30°C


substrate_name: ferricenium hexafluorophosphate

proof_lines: V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay usi

proof_lines: mutant enzyme V546C/T169G, at pH 6.5 and 30°C

proof_lines: V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using

substrate: ferricenium hexafluorophosphate


organism: Saccharomyces cerevisiae

substrate_name: D-isocitrate

assay_conditions_summary: pH 7.4; 297.15 K; cofactor NAD+

proof_lines: octameric enzyme IDH1G15D/IDH2 with AMP, without DTT, pH 7.4, 24°C

proof_lines: octameric enzyme IDH1G15D/IDH2 with AMP and DTT, pH 7.4, 24°C

proof_lines: octameric enzyme IDH1G15D/IDH2 without AMP, with DTT, pH 7.4, 24°C

substrate: D-isocitrate


substrate_name: NAD+

assay_conditions_summary: pH 7.2; cofactor NAD+

proof_lines: pH 7.2, alpha-subunit mutant enzyme D181N

substrate: NAD+


proof_lines: pH 7.2, gamma-subunit mutant enzyme D190N


proof_lines: pH 7.2, beta-subunit mutant enzyme D192N


substrate_name: D-galactose

proof_lines: pH 7.0, 25°C, reductive half-reaction, mutant T169S

proof_lines: mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 4°C

substrate: D-galactose


proof_lines: pH 7.0, 25°C, reductive half-reaction, mutant T169N

proof_lines: mutant enzyme T169N, in 50 mM sodium phosphate (pH 7.0), at 4°C

proof_lines: mutant enzyme T169N, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C


proof_lines: pH 7.0, 25°C, reductive half-reaction, mutant T169G

proof_lines: mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 4°C


proof_lines: pH 7.0, 25°C, reductive half-reaction, wild-type enzyme

proof_lines: wild type enzyme F454Y, at pH 6.5 and 30°C

proof_lines: wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 4°C


organism: Ostreococcus tauri

assay_conditions_summary: pH 7.6; cofactor NADP+

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mg2+

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mn2+


substrate_name: NADP+

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R/M345H, with Mn2+

substrate: NADP+


proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R, with Mn2+


organism: Campylobacter concisus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines: mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C


substrate_name: NAD+; Isocitrate

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Isocitrate


enzyme_display_name: vanillyl-alcohol oxidase

organism: Penicillium simplicissimum

enzyme: vanillyl-alcohol oxidase


proof_lines:
pH 7.5, 25°C, mutant enzyme E502G
pH 10, 25°C, mutant enzyme E502G
pH 8, 25°C, mutant enzyme E502G


substrate_name: creosol

proof_lines:
pH 10, 25°C, mutant enzyme I237T/M437L
pH 8, 25°C, mutant enzyme I237T/M437L

substrate: creosol


substrate_name: Eugenol

substrate: Eugenol


substrate_name: O2; Vanillyl alcohol

substrate: O2; Vanillyl alcohol


substrate_name: eugenol

proof_lines:
pH 7.5, 25°C, mutant enzyme F454Y
pH 8, 25°C, mutant enzyme F454Y
pH 10, 25°C, mutant enzyme F454Y

substrate: eugenol


proof_lines:
pH 10, 25°C, mutant enzyme T505S
pH 7.5, 25°C, mutant enzyme T505S
pH 8, 25°C, mutant enzyme T505S


organism: Rhodomicrobium vannielii

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


organism: Streptococcus suis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Sus scrofa


proof_lines: mutant enzyme L545C, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L545C, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L545C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C


proof_lines: mutant enzyme T166R, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme T166R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme T166R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C


proof_lines: mutant enzyme L547R, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L547R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L547R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C


proof_lines: mutant enzyme N593C, with 1 ferrocenium ion as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme N593C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme N593C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C


assay_conditions_summary: pH 10.5; buffer the publication 100 mM ethanolamine

proof_lines: pH and temperature not specified in the publication

proof_lines: recombinant protein with a hexa-histidine tag, 0.1 M ethanolamine buffer at pH 10.5


organism: Trametes sp.


organism: Hydrogenobacter thermophilus

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NADP+


assay_conditions_summary: cofactor NADP+


organism: Micromonas commoda

assay_conditions_summary: 298.15 K; cofactor NADP+


proof_lines: pH 75, 25°C, recombinant His6-tagged enzyme


organism: Ostreococcus sp. 'lucimarinus'


proof_lines: pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H


organism: Phycomyces blakesleeanus

source_protein_accession: complex


organism: Methylovorus sp. MP688

substrate_name: Vanillyl alcohol

substrate: Vanillyl alcohol


assay_conditions_summary: pH 7.5; 298.15 K; cofactor FAD


organism: Acidithiobacillus thiooxidans

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

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines:
pH 9.0, 30°C, native enzyme
Raw SKiD Env: Temp=30°C, pH=9

source_databases_merged: brenda skid


organism: Bifidobacterium longum

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


organism: Bos taurus


organism: Campylobacter curvus


organism: Homo sapiens


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+


substrate_name: chavicol

substrate: chavicol


enzyme_display_name: phenylalanine dehydrogenase

organism: Bacillus badius

substrate_name: L-tyrosine

enzyme: phenylalanine dehydrogenase

substrate: L-tyrosine


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


substrate_name: NAD+; H2O; L-Phenylalanine

substrate: NAD+; H2O; L-Phenylalanine


organism: Lysinibacillus sphaericus

substrate_name: L-Norleucine

substrate: L-Norleucine


substrate_name: phenylpyruvate

substrate: phenylpyruvate


smiles: CCC(C)C(=O)C(=O)O


organism: Pyrococcus furiosus

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+

proof_lines: pH 8.0, 70°C, the Km-value for NADP+ is about 65fold higher than the KM-value for NAD+


organism: Rattus norvegicus

substrate_name: D-threo-Isocitrate; NAD+

substrate: D-threo-Isocitrate; NAD+


substrate_name: L-Methionine

substrate: L-Methionine


substrate_name: L-Leucine

substrate: L-Leucine


substrate_name: L-Isoleucine

substrate: L-Isoleucine


smiles: CSCCC(=O)C(=O)O


substrate_name: L-Tyrosine

substrate: L-Tyrosine


substrate_name: alpha-Ketovaline

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

substrate: alpha-Ketovaline


substrate_name: L-Norvaline

sequence_source: UniProt P23307 direct lookup: canonical sequence exists; not row-specific mutant proof.

substrate: L-Norvaline


substrate_name: L-Valine

sequence_source: UniProt P23307 direct lookup: canonical sequence exists; accession context only.

substrate: L-Valine


organism: Penicillium simplicissimum

substrate_name: creosol

proof_lines:
pH 10, 25°C, mutant enzyme I238T
pH 7.5, 25°C, mutant enzyme I238T
pH 8, 25°C, mutant enzyme I238T

substrate: creosol


proof_lines:
pH 7.5, 25°C, wild-type enzyme
pH 10, 25°C, wild-type enzyme
wild-type, pH 7.5, 25°C


proof_lines: pH 10, 25°C, mutant enzyme F93Y/P189S/I238T


substrate_name: Eugenol

substrate: Eugenol


proof_lines:
pH 8, 25°C, mutant enzyme A429V
pH 10, 25°C, mutant enzyme A429V


assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADH


assay_conditions_summary: pH 10.4; 298.15 K; cofactor NADH


smiles: CCCCC(=O)C(=O)O


proof_lines: His-tagged recombinant enzyme, pH 7.5, 25°C


organism: Rhodococcus jostii

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


substrate_name: Vanillyl alcohol

substrate: Vanillyl alcohol


substrate_name: vanillylamine

substrate: vanillylamine


assay_conditions_summary: pH 10.4; 298.15 K; cofactor NAD+


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


organism: Escherichia coli

substrate_name: But-2-enoyl-[acyl-carrier protein]

smiles: CC=CC(=O)S

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

substrate: But-2-enoyl-[acyl-carrier protein]


substrate_name: crotonoyl-CoA

substrate: crotonoyl-CoA


organism: Haemophilus influenzae

substrate_name: NADH; H+; But-2-enoyl-[acyl-carrier protein]

assay_conditions_summary: cofactor NADH


organism: Mycobacterium tuberculosis

substrate_name: NADH

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH

proof_lines:
pH 6.8, 25°C, mutant enzyme I21V
I21V mutant enoyl-ACP reductase

substrate: NADH


proof_lines:
pH 6.8, 25°C, mutant enzyme Y158F
mutant Y158F, pH 6.8, 30°C
mutant enzyme Y158F, pH 6.8, 25°C


assay_conditions_summary: pH 6.8; 298.15 K; cofactor CoA


enzyme_display_name: shikimate dehydrogenase (NADP+)

organism: Arabidopsis thaliana

substrate_name: NADP+

assay_conditions_summary: pH 8.8; 295.15 K; cofactor NADP+

enzyme: shikimate dehydrogenase (NADP+)

substrate: NADP+


substrate_name: shikimate

assay_conditions_summary: pH 8.8; 295.15 K; cofactor NADPH

substrate: shikimate


organism: Burkholderia pseudomallei


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


organism: Candidatus Liberibacter asiaticus

assay_conditions_summary: pH 7.5; 301.15 K; cofactor NADH

proof_lines: with respect to NADH, at pH 7.5 and 28°C

proof_lines: with respect to crotonyl-CoA, at pH 7.5 and 28°C


organism: Eimeria tenella

assay_conditions_summary: pH 7.2; buffer 0.1 mM Tris-HCl; cofactor NADH

proof_lines: recombinant enzyme, in the absence of enoyl-CoA as scosubstrate, in 0.1 mM Tris-HCl buffer (pH 7.2)


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


proof_lines:
25°C, pH 8.0
pH 7.5, 22°C
Raw SKiD Env: Temp=25°C, pH=8


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 8.6; 303.15 K; cofactor NADP+

proof_lines:
with NADPH, pH 8.6, 30°C
with NADP+, pH 9.0, 30°C
pH 7.0, 30°C


substrate_name: NADP+; Shikimate

assay_conditions_summary: pH 7.5; 298.15 K; buffer notes; cofactor NADP+

proof_lines: 25°potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH

substrate: NADP+; Shikimate


assay_conditions_summary: pH 9; 293.15 K; cofactor NADP+


assay_conditions_summary: pH 9; 298.15 K; cofactor NADPH


assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

proof_lines: pH 9.0, 25°C, recombinant wild-type enzyme


substrate_name: NAD+

proof_lines: pH 9.0, 25°C, recombinant mutant S131A/L135A/N149D/V152F

substrate: NAD+


proof_lines: pH 9.0, 25°C, recombinant mutant N149D/V152F


proof_lines: pH 9.0, 25°C, recombinant mutant S131A/N149D/V152F


organism: Eucalyptus camaldulensis


assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines: pH 9.0, temperature not specified in the publication

proof_lines: pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation

proof_lines: pH 6.5, temperature not specified in the publication


substrate_name: NADPH

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: uronate dehydrogenase

organism: Chromohalobacter israelensis

substrate_name: beta-D-galacturonate

enzyme: uronate dehydrogenase

substrate: beta-D-galacturonate


substrate_name: beta-D-glucuronate

proof_lines: mutant enzyme N99K/L100H/K102V/P103K/I105V, at pH 8.0 and 25°C

substrate: beta-D-glucuronate


proof_lines: mutant enzyme T113V/M175I/D246N, at pH 8.0 and 25°C


proof_lines: mutant enzyme T113V/A172V/D246N, at pH 8.0 and 25°C


organism: Chromohalobacter salexigens

source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Pseudomonas putida KT2440

substrate_name: D-glucuronate

assay_conditions_summary: cofactor NAD+

substrate: D-glucuronate


organism: Pseudomonas syringae pv. tomato

substrate_name: D-Mannuronate

assay_conditions_summary: pH 8; 298.15 K; buffer recombinant His-tagged enzyme; cofactor NAD+

proof_lines: recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer

proof_lines: recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer

substrate: D-Mannuronate


organism: Thermobispora bispora

substrate_name: D-glucuronic acid from a beechwood xylan

assay_conditions_summary: pH 7; 333.15 K; cofactor NAD+


organism: Aquifex aeolicus

proof_lines:
25°C, pH 9.0
with shikimate, pH 9.0, 25°C
with NADP+, pH 9.0, 25°C


proof_lines:
pH 8.8, 22°C, with shikimate
pH 8.8, 22°C, with NADP+
Raw SKiD Env: Temp=-----, pH=-----


proof_lines: pH and temperature not specified in the publication, mutant S338G/T381G


substrate_name: L-quinate

proof_lines: pH and temperature not specified in the publication, mutant T381S

substrate: L-quinate


proof_lines: pH and temperature not specified in the publication, mutant T381A


proof_lines: pH and temperature not specified in the publication, mutant T381G


proof_lines: pH and temperature not specified in the publication, mutant S338G


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


organism: Agrobacterium tumefaciens

assay_conditions_summary: buffer separate potassium phosphate and Tris; cofactor NAD+


proof_lines: mutant enzyme L158A/N159C/I160V, at pH 8.0 and 25°C


proof_lines: mutant enzyme T113V/A172V/M175I, at pH 8.0 and 25°C


proof_lines: mutant enzyme T113V/A172V/M175I/D236N, at pH 8.0 and 25°C


organism: Pseudomonas putida

assay_conditions_summary: pH 8.8; cofactor NADP+

proof_lines:
pH 8.8, presence of 2 mM quinate
pH 8.8, presence of 2 mM NAD+
pH 8.8, presence of 2 mM shikimate


proof_lines:
pH 8.8, presence of 2 mM NAD+
pH 8.8, presence of 2 mM shikimate
pH 8.8, presence of 2 mM NADP+


assay_conditions_summary: pH 8.8; 298.15 K; cofactor NADP+

proof_lines:
pH 8.8, 25°C, with shikimate
pH 8.8, 25°C, with NADP+
pH 8.8, presence of 2 mM NADP+


assay_conditions_summary: cofactor NADP+

proof_lines:
in the presence of 2 mM NAD+
in the presence of shikimate
in the presence of 2 mM NADP+


proof_lines:
in the presence of 2 mM NADP+
in the presence of shikimate
in the presence of 2 mM NAD+


organism: Staphylococcus epidermidis

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines:
pH 7.0, 25°C, with NADP+
pH 7.0, 25°C, with shikimate


organism: Staphylococcus epidermidis RP62A


organism: Toxoplasma gondii

proof_lines:
pH 8.8, 25°C, with NADP+
pH 8.8, 25°C, with shikimate


organism: Vitis vinifera


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 7.3; 360.15 K; cofactor NADP+

proof_lines:
with shikimate, pH 7.3, 87°C
with NADP+, pH 7.3, 87°C


organism: Aspergillus nidulans

substrate_name: NADPH; 3-Dehydroshikimate; H+

proof_lines:
with NADP+, pH 7.0, 25°C
with shikimate, pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7

substrate: NADPH; 3-Dehydroshikimate; H+


organism: Camellia sinensis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 10; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+


proof_lines: pH 7.0, 30°C, recombinant isozyme VvSDH3

proof_lines: pH 9.0, 30°C, recombinant isozyme VvSDH3


proof_lines: pH 9.0, 30°C, recombinant isozyme VvSDH4

proof_lines: pH 7.0, 30°C, recombinant isozyme VvSDH4


proof_lines: pH 7.0, 30°C, recombinant isozyme VvSDH1

proof_lines: pH 9.0, 30°C, recombinant isozyme VvSDH1


organism: Alistipes finegoldii

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

proof_lines: K0.5 value, Hill coefficient 2.4, pH 8, 30°C

proof_lines: K0.5 value, Hill coefficient 1.5, pH 8, 30°C


organism: Arabidopsis thaliana

substrate_name: NADH; H+; Crotonoyl-CoA

substrate: NADH; H+; Crotonoyl-CoA


organism: Bacillus subtilis

assay_conditions_summary: cofactor NADPH


organism: Burkholderia mallei

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADH


organism: Eucalyptus camaldulensis

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines: pH 9.0, temperature not specified in the publication

proof_lines: pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

proof_lines: pH 8.5, temperature not specified in the publication


organism: Haemophilus influenzae

assay_conditions_summary: pH 7.5; cofactor NADP+


assay_conditions_summary: pH 8.8; 303.15 K; cofactor NADP+


organism: Helicobacter pylori

assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+


organism: Mycobacterium tuberculosis

proof_lines:
pH 7.0, 25°C, recombinant AroE
25°C, pH 7.3


assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH


assay_conditions_summary: pH 6.8; 303.15 K; cofactor NADH

proof_lines:
wild-type, pH 6.8, 30°C
pH 7.5, 25°C, wild-type enzyme
pH 6.8, 25°C, wild-type enzyme


organism: Mycolicibacterium smegmatis

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH


proof_lines:
pH 6.8, 25°C, mutant enzyme M161V
mutant enzyme M161V, pH 6.8, 25°C


organism: Plasmodium falciparum

substrate_name: H+; NADH; Crotonoyl-CoA

substrate: H+; NADH; Crotonoyl-CoA


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

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


substrate_name: 2-trans-Dodecenoyl-CoA; NADH; H+

assay_conditions_summary: cofactor NADH

substrate: 2-trans-Dodecenoyl-CoA; NADH; H+


substrate_name: NADH

proof_lines: I16T mutantwild type enoyl-ACP reductase

substrate: NADH


assay_conditions_summary: pH 6.8; cofactor NADH

proof_lines: pH 6.8, temperature not specified in the publication


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


substrate_name: octenoyl-CoA

substrate: octenoyl-CoA


substrate_name: crotonoyl-CoA

substrate: crotonoyl-CoA


organism: Lysinibacillus sphaericus

substrate_name: L-Isoleucine

substrate: L-Isoleucine


substrate_name: L-Methionine

substrate: L-Methionine


substrate_name: L-Norleucine

substrate: L-Norleucine


substrate_name: NAD+; H2O; L-Phenylalanine

assay_conditions_summary: cofactor NAD+

substrate: NAD+; H2O; L-Phenylalanine


substrate_name: L-Norvaline

substrate: L-Norvaline


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


substrate_name: phenylpyruvate

substrate: phenylpyruvate


organism: Pseudobacillus badius

substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Rhodococcus sp.

substrate_name: phenylacetone

substrate: phenylacetone


organism: Yersinia pestis


substrate_name: L-Valine

assay_conditions_summary: pH 10.4; 298.15 K; cofactor NADH

substrate: L-Valine


substrate_name: alpha-Ketovaline

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADH

substrate: alpha-Ketovaline


substrate_name: Unknown

substrate: Unknown


assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA


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


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

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


organism: Pseudomonas aeruginosa

substrate_name: NADH; H+; trans-Dodec-2-enoyl-[acp]

substrate: NADH; H+; trans-Dodec-2-enoyl-[acp]


substrate_name: NADH; H+; Crotonoyl-CoA

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

assay_conditions_summary: pH 7; cofactor NADH

proof_lines: pH 7.0, temperature not specified in the publication

substrate: NADH; H+; Crotonoyl-CoA


organism: Staphylococcus aureus

substrate_name: NADH; H+; Crotonyl-CoA

assay_conditions_summary: cofactor NADPH

substrate: NADH; H+; Crotonyl-CoA


organism: Streptococcus pneumoniae

substrate_name: NADH; H+; But-2-enoyl-[acyl-carrier protein]


assay_conditions_summary: cofactor CoA


organism: uncultured bacterium

substrate_name: NADH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


organism: Thermoactinomyces intermedius


substrate_name: L-Isoleucine

substrate: L-Isoleucine


substrate_name: L-Norleucine


substrate_name: L-Leucine

substrate: L-Leucine


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

proof_lines: mutant enzyme K66Q/S149G/N262C, at pH 9.6 and 30°C


substrate: L-Norleucine


substrate_name: L-Ethionine

substrate: L-Ethionine


substrate_name: L-Methionine

substrate: L-Methionine


substrate_name: L-Norvaline

substrate: L-Norvaline


assay_conditions_summary: pH 5.5; 303.15 K; cofactor NADH

proof_lines:
pH 5.5, 30°C
Raw SKiD Env: Temp=30°C, pH=5.5


organism: Vibrio cholerae

substrate: NADH; H+; But-2-enoyl-[acyl-carrier protein]


organism: Xanthomonas oryzae

substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


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


assay_conditions_summary: pH 8; 303.15 K; cofactor NADH


assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


proof_lines: IC50 above 0.05 mM, wild type enzyme, at pH 8.0 and 30°C


enzyme_display_name: pyruvate kinase

organism: Chlamydia trachomatis

substrate_name: Phosphoenolpyruvate; ADP

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Corynebacterium glutamicum


organism: Escherichia coli


organism: Homo sapiens

substrate_name: ADP; Phosphoenolpyruvate

substrate: ADP; Phosphoenolpyruvate


organism: Lactococcus lactis subsp. cremoris


organism: Lactococcus lactis subsp. lactis


organism: Mus musculus


organism: Oryctolagus cuniculus

substrate_name: Phosphoenolpyruvate; dADP

assay_conditions_summary: cofactor ADP

substrate: Phosphoenolpyruvate; dADP


organism: Rattus norvegicus


enzyme_display_name: phenylalanine ammonia-lyase

organism: Arabidopsis thaliana

substrate_name: L-Phenylalanine

enzyme: phenylalanine ammonia-lyase

substrate: L-Phenylalanine


substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


enzyme_display_name: beta-lactamase

organism: Serratia marcescens

substrate_name: H2O; Cephaloridine

enzyme: beta-lactamase

substrate: H2O; Cephaloridine


substrate_name: H2O; Ampicillin

substrate: H2O; Ampicillin


proof_lines:
pH 7.5, 25°C
at 30°C
Raw SKiD Env: Temp=25°C, pH=7.5


organism: Staphylococcus aureus


organism: Stenotrophomonas maltophilia

substrate_name: Nitrocefin; H2O

substrate: Nitrocefin; H2O


organism: Treponema pallidum

substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


organism: Anthoceros agrestis


organism: Mycobacterium tuberculosis

substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


organism: Nocardia asteroides


organism: Nocardia farcinica

unit: uM/s


organism: Ochrobactrum anthropi


organism: Proteus mirabilis


organism: Providencia stuartii


organism: Pseudomonas aeruginosa

substrate_name: H2O; Cefotaxime

substrate: H2O; Cefotaxime


organism: Serratia fonticola

substrate_name: H2O; Benzylpenicillin

substrate: H2O; Benzylpenicillin


organism: Aeromonas hydrophila


organism: Bacillus cereus


substrate_name: 6-Aminopenicillanate; H2O

substrate: 6-Aminopenicillanate; H2O


organism: Bacillus licheniformis

substrate_name: H2O; Phenoxymethylpenicillin

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----

substrate: H2O; Phenoxymethylpenicillin


organism: Bacteroides fragilis

proof_lines: pH and temperature not specified in the publication


organism: Burkholderia pseudomallei


organism: Citrobacter diversus


organism: Citrobacter freundii


organism: Enterobacter cloacae


organism: Escherichia coli


substrate_name: Benzylpenicillin; H2O

substrate: Benzylpenicillin; H2O


organism: Thermoactinomyces intermedius

substrate_name: L-Methionine

substrate: L-Methionine


substrate_name: L-Leucine

substrate: L-Leucine


substrate_name: L-Ethionine

substrate: L-Ethionine


substrate_name: L-Norvaline

substrate: L-Norvaline


substrate_name: NAD+; H2O; L-Phenylalanine

substrate: NAD+; H2O; L-Phenylalanine


enzyme_display_name: arylamine N-acetyltransferase

organism: Mycobacterium smegmatis

substrate_name: Acetyl-CoA; Isoniazid

enzyme: arylamine N-acetyltransferase

substrate: Acetyl-CoA; Isoniazid


enzyme_display_name: anthranilate phosphoribosyltransferase

organism: Saccharomyces cerevisiae

enzyme: anthranilate phosphoribosyltransferase


organism: Sulfolobus solfataricus


organism: Amycolatopsis methanolica

substrate_name: Phosphoenolpyruvate; ADP

substrate: Phosphoenolpyruvate; ADP


organism: Bos taurus


organism: Saccharolobus solfataricus

substrate_name: anthranilate

substrate: anthranilate


organism: Homo sapiens


organism: Larimichthys crocea

substrate_name: Z-L-Phe-L-Arg 7-amido-4-methylcoumarin

substrate: Z-L-Phe-L-Arg 7-amido-4-methylcoumarin


organism: Meretrix meretrix


organism: Mus musculus


organism: Naegleria fowleri


organism: Nicotiana benthamiana

substrate_name: Abz-GIVRAK-Dnp

substrate: Abz-GIVRAK-Dnp


organism: Rattus norvegicus


assay_conditions_summary: cofactor ATP


organism: Ricinus communis


assay_conditions_summary: pH 4.5; cofactor ADP


organism: Klebsiella pneumoniae

substrate_name: H2O; Cephalothin

substrate: H2O; Cephalothin


substrate_name: H2O; Imipenem

substrate: H2O; Imipenem


substrate_name: Nitrocefin; H2O

proof_lines:
pH 7.2, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=7.2

substrate: Nitrocefin; H2O


substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


organism: Klebsiella pneumoniae subsp. ozaenae


organism: Kluyvera ascorbata


organism: Moraxella catarrhalis

substrate_name: Amoxicillin; H2O

substrate: Amoxicillin; H2O


organism: Morganella morganii

substrate_name: H2O; Ampicillin

substrate: H2O; Ampicillin


substrate_name: Benzylpenicillin; H2O

substrate: Benzylpenicillin; H2O


organism: Trichomonas vaginalis


organism: Trypanosoma brucei


organism: Ustilago maydis


organism: Zymomonas mobilis


enzyme_display_name: arginine kinase

organism: Cissites cephalotes

substrate_name: L-Arg

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines: in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25°C

enzyme: arginine kinase

substrate: L-Arg


organism: Daphnia magna

substrate_name: ATP

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

substrate: ATP


proof_lines: mutant enzyme H284A, pH and temperature not specified in the publication


organism: Euphausia superba

substrate_name: L-arginine

assay_conditions_summary: pH 8; 293.15 K; cofactor ATP

substrate: L-arginine


organism: Fenneropenaeus chinensis

substrate_name: L-Arginine; ATP

substrate: L-Arginine; ATP


organism: Frankliniella occidentalis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Haemonchus contortus

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


organism: Nicotiana benthamiana


organism: Rattus norvegicus

substrate_name: Z-Arg-Arg-p-nitroanilide

substrate: Z-Arg-Arg-p-nitroanilide


substrate_name: H2O; Z-Arg-Arg-p-nitroanilide

substrate: H2O; Z-Arg-Arg-p-nitroanilide


organism: Schistosoma mansoni


substrate_name: Z-Arg-Arg-p-nitroanilide; H2O

substrate: Z-Arg-Arg-p-nitroanilide; H2O


organism: Aeromonas hydrophila

proof_lines:
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=-----, pH=9
Raw SKiD Env: Temp=30°C, pH=6.5


organism: Arabidopsis thaliana

substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: trans-cinnamate

substrate: trans-cinnamate


organism: Bambusa oldhamii

substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


substrate_name: L-Phe

proof_lines: recombinant protein from Escherichia coli, pH 8.5, 37°C

proof_lines: recombinant protein from Pichia pastoris, pH 8.5, 37°C

proof_lines: recombinant enzyme expressed in Escherichia coli

substrate: L-Phe


proof_lines: recombinant enzyme, in 50 mM Tris-HCl, pH 8.5, at 37°C


substrate_name: L-Tyr

substrate: L-Tyr


organism: Jatropha curcas


organism: Kitagawia praeruptora


organism: Lycoris radiata


organism: Nicotiana tabacum


proof_lines: isoform PAL1, at 30°C in 50 mM Tris/HCl, pH 8.5


organism: Limulus polyphemus

substrate_name: L-Arginine phosphate; ADP

substrate: L-Arginine phosphate; ADP


organism: Litopenaeus vannamei

substrate_name: ATP; dTDP

substrate: ATP; dTDP


organism: Myxococcus xanthus

substrate_name: Nomega-phospho-L-Arg

substrate: Nomega-phospho-L-Arg


organism: Toxocara canis

assay_conditions_summary: pH 8; 298.15 K; buffer and temperature description (Tris-HCl; cofactor NADH

proof_lines: in 100 mM Tris-HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, 5 mM NADH, at 25°C


enzyme_display_name: prolyl oligopeptidase

organism: Bos taurus

substrate_name: H2O; Z-Gly-Pro-AMC

enzyme: prolyl oligopeptidase

substrate: H2O; Z-Gly-Pro-AMC


organism: Homo sapiens


enzyme_display_name: oligopeptidase B

organism: Serratia proteamaculans

proof_lines: pH 8.0, 25°C, recombinant protein with a modified hinge region (PSPmod)

proof_lines: pH 8.0, 25°C, bacterial oligopeptidase B from Serratia proteomaculans (PSP)

proof_lines: substrate Nalpha-benzoyl-DL-Arg-4-nitroanilide, pH 8.0, 25°C

enzyme: oligopeptidase B


enzyme_display_name: cathepsin B

assay_conditions_summary: pH 5

enzyme: cathepsin B


organism: Capra hircus

substrate_name: Unknown

proof_lines:
pH 6, 37°C
pH 5, 37°C

substrate: Unknown


organism: Fasciola gigantica


proof_lines:
pH 6.0, 37°C, recombinant enzyme
pH 6.2, 25°C
200 mM NaCl, 2.5 mM DTT, pH 4.5, 37°C


organism: Escherichia coli

substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


substrate_name: H2O; Benzylpenicillin

substrate: H2O; Benzylpenicillin


substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


substrate_name: H2O; Nitrocefin

proof_lines: pH 7.2, temperature not specified in the publication, recombinant enzyme

substrate: H2O; Nitrocefin


substrate_name: CENTA; H2O

substrate: CENTA; H2O


substrate_name: H2O; Cephaloridine

proof_lines:
pH 6.5, 22°C
Raw SKiD Env: Temp=-----, pH=-----

substrate: H2O; Cephaloridine


substrate_name: H2O; Cefuroxime

substrate: H2O; Cefuroxime


substrate_name: H2O; Ampicillin

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

substrate: H2O; Ampicillin


organism: Fluoribacter gormanii


substrate_name: H2O; Cefotaxime

substrate: H2O; Cefotaxime


substrate_name: H2O; Imipenem

substrate: H2O; Imipenem


organism: Klebsiella oxytoca


organism: Bambusa oldhamii

substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-Tyr

substrate: L-Tyr


organism: Cistanche deserticola


organism: Ephedra sinica

substrate_name: L-phenylalanine

proof_lines:
pH 8.5, 37°C, isozyme PAL2
pH 8.5, 37°C, isozyme PAL1
pH 8.5, 37°C, isozyme PAL3

substrate: L-phenylalanine


organism: Glycine max

substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


organism: Gossypium hirsutum


organism: Nicotiana tabacum


organism: Nostoc punctiforme


assay_conditions_summary: pH 8.5; 303.15 K; buffer a stated assay temperature and Tris/HCl

proof_lines: isoform PAL2, at 30°C in 50 mM Tris/HCl, pH 8.5


proof_lines: isoform PAL4, at 30°C in 50 mM Tris/HCl, pH 8.5


assay_conditions_summary: pH 8.5; 303.15 K; buffer Tris/HCl

proof_lines: isoform PAL3, at 30°C in 50 mM Tris/HCl, pH 8.5


organism: Petroselinum crispum


substrate_name: trans-cinnamate

assay_conditions_summary: pH 10; 303.15 K; buffer E. coli cells as whole cell biocatalysts in ammonium carbonate

substrate: trans-cinnamate


proof_lines:
pH 8.8, 30°C
pH 10, 30°C
Raw SKiD Env: Temp=30°C, pH=8.8


proof_lines: pH and temperature not specified in the publication, mutant enzyme I460V


proof_lines: pH and temperature not specified in the publication, mutant enzyme I460T


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


organism: Rhodobacter sphaeroides


enzyme_display_name: glutamine synthetase

organism: Anabaena azollae

substrate_name: ATP

enzyme: glutamine synthetase

substrate: ATP


substrate_name: L-Glutamate

substrate: L-Glutamate


organism: Arabidopsis thaliana

substrate_name: L-glutamate

assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP

proof_lines:
pH 7.8, 30°C, isoenzyme GLN1,4
pH 7.8, 30°C, below, isoenzyme GLN1,4

substrate: L-glutamate


proof_lines:
pH 7.8, 30°C, below, isoenzyme GLN1,1
pH 7.8, 30°C, isoenzyme GLN1,1


substrate_name: ATP; L-Glutamate; NH3

substrate: ATP; L-Glutamate; NH3


organism: Exiguobacterium sp.

substrate_name: L-glutamine

proof_lines:
pH 6.0, 35°C, recombinant mutant E60A
pH 6.0, 35°C, recombinant E60A

substrate: L-glutamine


proof_lines:
pH 6.0, 35°C, recombinant mutant R64G
pH 6.0, 35°C, recombinant R64G


substrate_name: ADP

substrate: ADP


proof_lines: pH 6.0, 35°C, recombinant wild-type enzyme


organism: Homo sapiens

substrate_name: L-Glutamine; ADP; Phosphate

substrate: L-Glutamine; ADP; Phosphate


organism: Hordeum vulgare

substrate_name: Unknown

substrate: Unknown


organism: Drosophila melanogaster


organism: Escherichia coli

substrate_name: L-Glutamate; NH3; ATP

substrate: L-Glutamate; NH3; ATP


smiles: N


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


assay_conditions_summary: pH 6; 308.15 K; cofactor ADP


proof_lines: pH 6.0, 35°C, recombinant mutant E60A/R64G


substrate_name: L-Glu

substrate: L-Glu


proof_lines:
isoenzyme GLN1,3
pH 7.8, 30°C, isoenzyme GLN1,3
pH 7.8, 30°C, below, isoenzyme GLN1,3


organism: Rhodotorula glutinis


organism: Rhodotorula graminis

substrate_name: (2E)-3-nitro-cinnamic acid

substrate: (2E)-3-nitro-cinnamic acid


substrate_name: (2E)-3-bromo-cinnamic acid

substrate: (2E)-3-bromo-cinnamic acid


organism: Sorghum bicolor


organism: Trichormus variabilis

proof_lines: mutant Q292C/C565S, pH and temperature not specified in the publication


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


substrate_name: (2S)-2-amino-3-phenylpropanoic acid

substrate: (2S)-2-amino-3-phenylpropanoic acid


proof_lines:
pH 8.3, 30°C
Raw SKiD Env: Temp=30°C, pH=8.3
Raw SKiD Env: Temp=-----, pH=-----


organism: Zea mays


organism: Trichormus azollae

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: D51E mutant enzyme, biosynthetic reaction, pH 7.0, 30°C


organism: Trypanosoma cruzi

proof_lines: recombinant enzyme, coupled reactions assay, pH and temperature not specified in the publication

proof_lines: recombinant enzyme, Malachite green assay, pH and temperature not specified in the publication

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


organism: Tuber borchii

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Bacillus subtilis

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

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


assay_conditions_summary: pH 7; cofactor ATP

proof_lines: pH 7.0, temperature not specified in the publication, wild-type enzyme


proof_lines: pH 7.0, temperature not specified in the publication, mutant E304A


substrate_name: hydroxylamine

proof_lines: pH 7.0, temperature not specified in the publication, mutant R62A

substrate: hydroxylamine


assay_conditions_summary: cofactor ADP


organism: Camellia sinensis

assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines:
pH 7.8
substrate NH4+, pH 7.8
substrate L-glutamate, pH 7.8


organism: Canis familiaris

assay_conditions_summary: cofactor ATP


organism: Pseudomonas taetrolens


organism: Pyrococcus sp.


assay_conditions_summary: pH 7.8; 333.15 K; cofactor ATP


organism: Rattus norvegicus


organism: Ruminococcus albus

assay_conditions_summary: pH 6.4; 310.15 K; cofactor ATP


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Sulfolobus acidocaldarius

assay_conditions_summary: 353.15 K; cofactor ADP


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


organism: Leishmania donovani


organism: Medicago truncatula


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


proof_lines: pH not specified in the publication, 30°C, mutant mature enzyme lacking the C-terminal peptide


organism: Methanocaldococcus jannaschii


organism: Mus musculus


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5
Raw SKiD Env: Temp=-----, pH=7.5


organism: Oryza sativa


organism: Oryza sativa Japonica Group

assay_conditions_summary: 303.15 K; cofactor ATP


organism: Phaseolus vulgaris


organism: Lysinibacillus sphaericus

substrate_name: DL-propargylglycine

substrate: DL-propargylglycine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Arabidopsis thaliana

substrate_name: NADP+

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADP+

substrate: NADP+


substrate_name: shikimate

substrate: shikimate


proof_lines: pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant


proof_lines:
isoenzyme GLN1,4
pH 7.8, 30°C, isoenzyme GLN1,2
pH 7.8, 30°C, below, isoenzyme GLN1,2


organism: Auricularia auricula-judae

substrate_name: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) (Dye-decolorizing peroxidase AauDyP1, at pH 4.5)

source_db: uniprot

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

source: uniprot


organism: Bubalus bubalis

substrate_name: 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (at pH 6.0 and 60 degrees Celsius)


organism: Equus caballus

substrate_name: bromide

substrate: bromide


organism: Metapenaeus ensis

substrate_name: ATP (at pH 8.5 and 30 degrees Celsius)

substrate: ATP (at pH 8.5 and 30 degrees Celsius)


organism: Penaeus vannamei

substrate_name: ATP (at pH 8.6 and 30 degrees Celsius)

substrate: ATP (at pH 8.6 and 30 degrees Celsius)


organism: Populus trichocarpa

assay_conditions_summary: pH 8.5; 295.15 K; cofactor NADP+

proof_lines: with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1

proof_lines: pH 8.5, 22°C, with NADP+, isozyme Poptr5

proof_lines: with NAD+, pH 8.5, 22°C, recombinant His-tagged Poptr1


organism: Homo sapiens

substrate_name: Acetyl-CoA; 2-Aminofluorene

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

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

substrate: Acetyl-CoA; 2-Aminofluorene


organism: Bos taurus

substrate_name: Phosphoenolpyruvate; ADP

proof_lines:
M-type isozyme, 25°C, pH 7.0
L-type isozyme, 25°C, pH 7.0

substrate: Phosphoenolpyruvate; ADP


organism: Monoraphidium minutum

substrate_name: IDP

proof_lines:
isozyme PKc
PKc-isozyme
isozyme PKp

substrate: IDP


organism: Rattus norvegicus

assay_conditions_summary: pH 7.1; 310.15 K; cofactor ATP

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


organism: Ricinus communis

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ADP

proof_lines: 2 isozymes with different kinetic mechanisms


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: ADP

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ADP

proof_lines:
enzyme form I
30°C, pH 6.8
isozyme II, 30°C, pH 6.8

substrate: ADP


organism: Spinacia oleracea

proof_lines:
isozyme PKII, pH 7.1, 25°C
isozyme PKI, pH 7.1, 25°C
pH 7.1, 25°C


organism: Sus scrofa

proof_lines:
isoenzyme I
isoenzyme II
isoenzyme I and isoenzyme II


organism: Petroselinum crispum

substrate_name: L-Phenylalanine

proof_lines:
30°C
pH 8.8, 30°C
isoenzyme PAL-4

substrate: L-Phenylalanine


organism: Unknown

substrate_name: L-Phe

substrate: L-Phe


organism: Beta vulgaris

substrate_name: Unknown

substrate: Unknown


organism: Bradyrhizobium japonicum

substrate_name: hydroxylamine

proof_lines:
second value 8.9 mM, biphasic plot
glutamyl transferase reaction
biosynthetic reaction


organism: Hordeum vulgare


organism: Senna obtusifolia


substrate_name: Glu

proof_lines:
synthetase assay
transferase assay
plastidic isozyme

substrate: Glu


organism: Triticum aestivum

proof_lines: in the presence of 3.5 mM L-glutamate, pH and temperature not specified in the publication

proof_lines: in the presence of 1 mM L-glutamate, pH and temperature not specified in the publication


organism: Xylanibacter ruminicola

substrate_name: ATP

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP

proof_lines: isozyme GSIII-1, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity

proof_lines: isozyme GSIII-2, pH 7.5, 37°C, glutamine synthetase activity

proof_lines: isozyme GSIII-2, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity

substrate: ATP


organism: Zea mays


organism: Arabidopsis thaliana

assay_conditions_summary: 295.15 K; cofactor NADP+


substrate_name: NADP+


substrate_name: shikimate


organism: Lysinibacillus sphaericus

substrate_name: DL-propargylglycine


substrate_name: L-phenylalanine


organism: Agrobacterium tumefaciens

substrate_name: D-glucuronic acid

proof_lines: mutant enzyme H99Y/H234K, at pH 8.0 and 30°C

substrate: D-glucuronic acid


proof_lines: mutant enzyme A39P/H99Y, at pH 8.0 and 30°C


proof_lines: mutant enzyme A39P/H234K, at pH 8.0 and 30°C


proof_lines: mutant enzyme A39P/H99Y/H234K, at pH 8.0 and 30°C


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Streptomyces clavuligerus

substrate_name: Penicillin N

enzyme: deacetoxycephalosporin-C synthase

substrate: Penicillin N


proof_lines: pH 6.5, 30°C, recombinant mutants C281Y and I305L


substrate_name: penicillin G

substrate: penicillin G


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Homo sapiens

substrate_name: NAD+

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

enzyme: dihydrolipoyl dehydrogenase

substrate: NAD+


substrate_name: dihydrolipoamide

substrate: dihydrolipoamide


smiles: N=C(O)CCCCC(S)CCS


substrate_name: Pyruvate; NAD+; Coenzyme A

assay_conditions_summary: cofactor NAD+

substrate: Pyruvate; NAD+; Coenzyme A


substrate_name: NAD+; 2-Oxoglutarate; Coenzyme A

substrate: NAD+; 2-Oxoglutarate; Coenzyme A


substrate_name: NAD+; Coenzyme A; alpha-Ketovaline

substrate: NAD+; Coenzyme A; alpha-Ketovaline


substrate_name: NAD+; Coenzyme A; 2-Oxoglutarate

substrate: NAD+; Coenzyme A; 2-Oxoglutarate


substrate_name: Lipoamide

substrate: Lipoamide


proof_lines:
mutant enzyme N286Q
mutant N286Q


proof_lines:
mutant enzyme N286D
mutant N286D


proof_lines:
mutant enzyme D320N
mutant D320N


proof_lines:
wild-type enzyme, pH 8.0, 37°C
wild type enzyme, at pH 8.0 and 37°C
wild-type


substrate_name: NADH

assay_conditions_summary: pH 8; 310.15 K; cofactor NADH

substrate: NADH


substrate_name: Dihydrolipoamide; NAD+

substrate: Dihydrolipoamide; NAD+


organism: Solanum tuberosum


substrate_name: 2-Oxoglutarate; NAD+; Coenzyme A

substrate: 2-Oxoglutarate; NAD+; Coenzyme A


substrate_name: 2-Oxopentanoate; NAD+; Coenzyme A

substrate: 2-Oxopentanoate; NAD+; Coenzyme A


substrate_name: NADH; H+; (R)-Lipoate

assay_conditions_summary: cofactor NADH

substrate: NADH; H+; (R)-Lipoate


organism: Thermus scotoductus

substrate_name: Cr(VI)

substrate: Cr(VI)


organism: Xenopus laevis


enzyme_display_name: sulfite oxidase

substrate_name: sulfite

enzyme: sulfite oxidase

substrate: sulfite


organism: Gallus gallus

proof_lines:
wild-type, 25°C, pH 8.5
wild-type, 25°C, pH 7.0


proof_lines:
mutant Y322N/R450M, 25°C, pH 8.5
mutant Y322N/R450M, 25°C, pH 7.0


proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.5
Raw SKiD Env: Temp=25°C, pH=7


substrate_name: Sulfite; Cytochrome c; H2O

substrate: Sulfite; Cytochrome c; H2O


proof_lines: with ferricanide, pH 6.0, 25°C, recombinant wild-type enzyme

proof_lines: with ferricanide, pH 8.9, 25°C, recombinant wild-type enzyme

proof_lines: with ferricanide, pH 7.1, 25°C, recombinant wild-type enzyme


proof_lines: with ferricanide, pH 6.0, 25°C, recombinant mutant C242S/C253S/C260S/C451S

proof_lines: with ferricanide, pH 7.1, 25°C, recombinant mutant C242S/C253S/C260S/C451S

proof_lines: with ferricanide, pH 8.4, 25°C, recombinant mutant C242S/C253S/C260S/C451S


organism: Microbacterium luteolum

assay_conditions_summary: pH 6; 298.15 K; buffer 50 mM potassium phosphate; cofactor NAD+

proof_lines: in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25°C


organism: Mycobacterium tuberculosis


substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Pisum sativum


substrate_name: Dihydrolipoylprotein

smiles: NC(=O)CCCCC(S)CCS

substrate: Dihydrolipoylprotein


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

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


organism: Rattus norvegicus


organism: Escherichia coli


organism: Glycine max

substrate_name: ferrileghemoglobin

substrate: ferrileghemoglobin


organism: Halobacterium volcanii

substrate_name: NAD+; Dihydrolipoamide

substrate: NAD+; Dihydrolipoamide


organism: Haloferax volcanii

substrate_name: NAD+

substrate: NAD+


substrate_name: dihydrolipoamide

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+

proof_lines: pH 7.0, 30°C, mutant enzyme E423S, assay in the absence of KCI

substrate: dihydrolipoamide


proof_lines: pH 7.0, 30°C, mutant enzyme E423D, assay in the absence of KCI


proof_lines: pH 7.0, 30°C, mutant enzyme E423A, assay in the absence of KCI


proof_lines: pH 7.0, 30°C, wild-type enzyme, assay in the absence of KCI


proof_lines: pH 7.0, 30°C, mutant enzyme E423Q, assay in the absence of KCI


substrate_name: (S)-Lipoic acid

substrate: (S)-Lipoic acid


substrate_name: (R)-Lipoic acid

substrate: (R)-Lipoic acid


substrate_name: 1,2-Diselenolane-3-pentanoic acid

substrate: 1,2-Diselenolane-3-pentanoic acid


organism: Acidianus ambivalens


organism: Azotobacter vinelandii

substrate_name: Coenzyme A; NAD+; 2-Oxoglutarate

substrate: Coenzyme A; NAD+; 2-Oxoglutarate


organism: Bos taurus

substrate_name: NAD+; Coenzyme A; Pyruvate

substrate: NAD+; Coenzyme A; Pyruvate


organism: Clostridium kluyveri


organism: Corynebacterium glutamicum

substrate_name: NAD+; Coenzyme A; 2-Oxoglutarate

substrate: NAD+; Coenzyme A; 2-Oxoglutarate


substrate_name: Pyruvate; NAD+; Coenzyme A

substrate: Pyruvate; NAD+; Coenzyme A


assay_conditions_summary: pH 7.98; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7.98; 298.15 K; cofactor NADP+


substrate_name: NADP+

substrate: NADP+


organism: Zea mays

substrate_name: sulfite

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

substrate: sulfite


enzyme_display_name: thymidylate synthase

organism: Bacillus subtilis

substrate_name: 5,10-Methylenetetrahydrofolate; dUMP

enzyme: thymidylate synthase

substrate: 5,10-Methylenetetrahydrofolate; dUMP


organism: Bacteriophage T4


organism: Crithidia fasciculata


substrate_name: dUMP

substrate: dUMP


organism: Homo sapiens


proof_lines:
presence of Mg2+, pH 7.5, 22°C
pH 7.5, 22°C
pH 7.2, 22°C


organism: Lactobacillus casei


organism: Leishmania major


assay_conditions_summary: cofactor NADPH


organism: Rattus norvegicus


organism: Toxoplasma gondii

substrate_name: H+; NADPH; 5,10-Methylenetetrahydrofolate; dUMP


organism: Trypanosoma cruzi


enzyme_display_name: glycine hydroxymethyltransferase

organism: Alloalcanivorax dieselolei

substrate_name: L-serine

proof_lines: pH 7.4, 40°C, recombinant wild-type enzyme

enzyme: glycine hydroxymethyltransferase

substrate: L-serine


proof_lines: pH 7.4, 40°C, recombinant mutant E160L/E193Q


organism: Aphanothece halophytica

substrate_name: glycine

proof_lines: pH 7.2, 30°C, recombinant enzyme, in presence of 0.375 M NaCl

substrate: glycine


organism: Arabidopsis thaliana

substrate_name: tetrahydrofolate

proof_lines: pH 8.5, temperature not specified in the publication, recombinant AtSHMT3

substrate: tetrahydrofolate


substrate_name: Tetrahydropteroyl di-L-glutamate

substrate: Tetrahydropteroyl di-L-glutamate


substrate_name: L-Serine; 5,6,7,8-Tetrahydrofolate

substrate: L-Serine; 5,6,7,8-Tetrahydrofolate


substrate_name: Tetrahydropteroyl penta-L-glutamate

substrate: Tetrahydropteroyl penta-L-glutamate


substrate_name: Tetrahydropteroyl tri-L-glutamate

substrate: Tetrahydropteroyl tri-L-glutamate


substrate_name: Tetrahydropteroyl tetra-L-glutamate

substrate: Tetrahydropteroyl tetra-L-glutamate


organism: Bombyx mori


organism: Danio rerio


substrate_name: serine

substrate: serine


organism: Escherichia coli


proof_lines: apparent value, mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA


proof_lines: pH 7.2, 30°C, recombinant enzyme, in presence of 0.75 M NaCl

proof_lines: pH 7.2, 30°C, recombinant enzyme, in presence of 0.125 M NaCl

proof_lines: pH 7.2, 30°C, recombinant enzyme, in presence of 0.50 M NaCl


proof_lines: apparent value, mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA


proof_lines: apparent value, wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA


proof_lines: apparent value, mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA


substrate_name: L-Serine

substrate: L-Serine


organism: Geobacillus stearothermophilus


substrate_name: L-allo-Threonine

substrate: L-allo-Threonine


organism: Glutamicibacter nicotianae


organism: Glycine max

proof_lines: pH 7.5, temperature not specified in the publication, enzyme SHMT8 from Glycine max cv. Essex


substrate_name: D-Serine

substrate: D-Serine


assay_conditions_summary: pH 7; 298.15 K; buffer HEPES

proof_lines: pH 7.0, 25°C, recombinant enzyme, in HEPES buffer

proof_lines: pH 7.0, 25°C, recombinant enzyme, in phosphate buffer


proof_lines:
isoform SHMT2, at pH 7.2 and 20°C
isoform SHMT2, at pH 7.2 and 30°C
isoform SHMT2, at pH 7.8 and 30°C


proof_lines: mutant H135N/R137A/E168N, at pH 7.2 and 20°C


proof_lines: wild type enzyme SHMT1, at pH 7.2 and 20°C


organism: Idiomarina loihiensis

substrate_name: DL-beta-Phenylserine

substrate: DL-beta-Phenylserine


organism: Leishmania donovani


organism: Methanosarcina barkeri

proof_lines: pH and temperature not specified in the publication


organism: Oryctolagus cuniculus

substrate_name: L-Ser

proof_lines: wild-type, in the presence of pyridoxal phosphate

substrate: L-Ser


proof_lines: mutant L474F, in the presence of pyridoxal phosphate


proof_lines: mutant S394N, in the presence of pyridoxal phosphate


organism: Plasmodium vivax


organism: Psychromonas ingrahamii

proof_lines:
pH 7.2, 20°C
Raw SKiD Env: Temp=20°C, pH=7.2


organism: Rattus norvegicus


organism: Ovis aries


organism: Plasmodium falciparum


enzyme_display_name: hypoxanthine phosphoribosyltransferase

organism: Trypanosoma cruzi

substrate_name: IMP

enzyme: hypoxanthine phosphoribosyltransferase

substrate: IMP


substrate_name: diphosphate

substrate: diphosphate


substrate_name: Hypoxanthine

substrate: Hypoxanthine


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

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


organism: Saccharomyces cerevisiae


organism: Thermoanaerobacter tengcongensis


substrate_name: Guanine

substrate: Guanine


organism: Thermus thermophilus

substrate_name: guanine

substrate: guanine


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

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


substrate_name: hypoxanthine

substrate: hypoxanthine


organism: Trypanosoma brucei brucei


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


organism: Legionella pneumophila


organism: Leishmania tarentolae

proof_lines: recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate


organism: Mycobacterium tuberculosis


assay_conditions_summary: pH 7.4; 296.15 K; buffer two

proof_lines: activated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C

proof_lines: activated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C

proof_lines: activated enzyme, with hypoxanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C


substrate_name: xanthine

substrate: xanthine


organism: Thermoplasma acidophilum

substrate_name: L-serine

substrate: L-serine


substrate_name: L-Serine; 5,6,7,8-Tetrahydrofolate

substrate: L-Serine; 5,6,7,8-Tetrahydrofolate


enzyme_display_name: glycogen phosphorylase

organism: Corynebacterium callunae

substrate_name: D-Glucose 1-phosphate

enzyme: glycogen phosphorylase

substrate: D-Glucose 1-phosphate


substrate_name: starch

substrate: starch


substrate_name: Starch; Phosphate

assay_conditions_summary: pH 7

substrate: Starch; Phosphate


organism: Escherichia coli

substrate_name: Maltoheptaose; Phosphate

substrate: Maltoheptaose; Phosphate


substrate_name: GMP

substrate: GMP


organism: Agrobacterium sp.

substrate_name: Unknown

substrate: Unknown


organism: Bacillus cereus

substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


organism: Bacillus subtilis


organism: Brucella anthropi

proof_lines: mutant E145G/N163H/N267S/P318R/M377V/M425T/P438L, pH 7.0, temperature not specified in the publication


proof_lines: mutant M425T, pH 7.0, temperature not specified in the publication


proof_lines: mutant N267S/P318R/M425T, pH 7.0, temperature not specified in the publication


proof_lines: mutant N267S, pH 7.0, temperature not specified in the publication


proof_lines: mutant P318R, pH 7.0, temperature not specified in the publication


organism: Oryctolagus cuniculus

substrate_name: Glycogen; D-Glucose 1-phosphate

substrate: Glycogen; D-Glucose 1-phosphate


organism: Solanum tuberosum


organism: Zea mays


organism: Homo sapiens


substrate_name: Hypoxanthine

substrate: Hypoxanthine


substrate_name: IMP

substrate: IMP


substrate_name: diphosphate

substrate: diphosphate


substrate_name: Guanine

substrate: Guanine


substrate_name: guanine

proof_lines:
at pH 7.4 and 37°C
at pH 7.4 and 25°C
above, pH 7.4, 25°C

substrate: guanine


proof_lines: 50 mM KCl, mutant E341Q, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant E341Q, cosubstrate: phosphoenolpyruvate


substrate_name: shikimate 3-phosphate

substrate: shikimate 3-phosphate


substrate_name: Phosphoenolpyruvate

substrate: Phosphoenolpyruvate


proof_lines: 50 mM KCl, mutant D313A, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant D313A, cosubstrate: phosphoenolpyruvate


proof_lines: 50 mM KCl, mutant K22A value above 0.3, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant K22A value above 0.3, cosubstrate: phosphoenolpyruvate


proof_lines: 50 mM KCl, mutant K22R value above 0.3, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant K22R value above 0.3, cosubstrate: phosphoenolpyruvate


proof_lines: wild-type, pH 7.0, temperature not specified in the publication


proof_lines:
+/-0.005 mM, mutant P101S
+/-0.006 mM, mutant P101S
mutant P101S


proof_lines: mutant G96A, in presence of 1 mM shikimate 3-phosphate


proof_lines: mutant G96A/A183T, in presence of 1 mM shikimate 3-phosphate


proof_lines: mutant A183T, in presence of 1 mM shikimate 3-phosphate


proof_lines: 50 mM KCl, mutant D313L, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant D313L, cosubstrate: phosphoenolpyruvate


proof_lines: 50 mM KCl, mutant E341M, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant E341M, cosubstrate: phosphoenolpyruvate


proof_lines: wild-type AroA, 100 mM KCl, cosubstrate: 3-phosphoshikimate

proof_lines: wild-type AroA, 100 mM KCl, cosubstrate: phosphoenolpyruvate


proof_lines: 50 mM KCl, mutant E341C, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant E341C, cosubstrate: phosphoenolpyruvate


proof_lines: 50 mM KCl, mutant D313N, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant D313N, cosubstrate: phosphoenolpyruvate


proof_lines: 50 mM KCl, mutant D313C, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant D313C, cosubstrate: phosphoenolpyruvate


organism: Stutzerimonas stutzeri


substrate_name: Isopentenyl diphosphate; cis,trans,trans-Geranylgeranyl diphosphate


substrate_name: Isopentenyl diphosphate

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

substrate: Isopentenyl diphosphate


substrate_name: trans,trans-Farnesyl diphosphate

substrate: trans,trans-Farnesyl diphosphate


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

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


proof_lines: 50 mM KCl, mutant E341A, cosubstrate: phosphoenolpyruvate

proof_lines: 50 mM KCl, mutant E341A, cosubstrate: 3-phosphoshikimate


proof_lines: 50 mM KCl, mutant H385A, cosubstrate: 3-phosphoshikimate

proof_lines: 50 mM KCl, mutant H385A, cosubstrate: phosphoenolpyruvate


proof_lines: C-terminal His6-tagged AroA, 100 mM KCl, cosubstrate: 3-phosphoshikimate

proof_lines: C-terminal His6-tagged AroA, 100 mM KCl, cosubstrate: phosphoenolpyruvate

proof_lines: C-terminal His6-tagged AroA, 50 mM KCl, cosubstrate: 3-phosphoshikimate


organism: Halothermothrix orenii


organism: Janibacter sp.


organism: Oryza sativa


organism: Pseudomonas fluorescens

proof_lines: +/-0.00573 mM, full-length G2 EPSPS, crude lysate from overexpressing Escherichia coli ER2799, malachite green dye assay

proof_lines: +/-0.01101 mM, reconstituted G2-EPSPS (by intein-mediated protein complementation), crude lysate from transformed Escherichia coli ER2799, malachite green dye assay

proof_lines: +/-0.00578 mM, reconstituted G2-EPSPS (by intein-mediated protein complementation), crude lysate from transformed Escherichia coli ER2799, malachite green dye assay


organism: Rahnella aquatilis


organism: Streptococcus pneumoniae


substrate_name: Phosphate

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

substrate: Phosphate


proof_lines: in the presence of 1 mM NH4Cl and 10 mM KCl


organism: Micrococcus luteus

substrate_name: (2Z,6E,10E)-geranylgeranyl diphosphate

substrate: (2Z,6E,10E)-geranylgeranyl diphosphate


enzyme_display_name: cysteine synthase

organism: Arabidopsis thaliana

substrate_name: O-Acetyl-L-serine

enzyme: cysteine synthase

substrate: O-Acetyl-L-serine


substrate_name: O-Acetyl-L-serine; Sulfide

substrate: O-Acetyl-L-serine; Sulfide


organism: Salmonella typhimurium

substrate_name: Hydrogen sulfide

smiles: S

substrate: Hydrogen sulfide


organism: Schizosaccharomyces pombe

substrate_name: O-Acetyl-L-serine; Hydrogen sulfide

substrate: O-Acetyl-L-serine; Hydrogen sulfide


substrate_name: Hydrogen sulfide; O-Acetyl-L-serine

substrate: Hydrogen sulfide; O-Acetyl-L-serine


organism: Bacillus anthracis

substrate_name: O-acetyl-L-serine

substrate: O-acetyl-L-serine


organism: Bacillus subtilis


organism: Caenorhabditis elegans

substrate_name: Cyanide

smiles: C#N

substrate: Cyanide


substrate_name: S-Sulfo-L-cysteine

substrate: S-Sulfo-L-cysteine


substrate_name: L-Cysteine

substrate: L-Cysteine


organism: Escherichia coli


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


substrate_name: Isopentenyl diphosphate; trans,trans-Farnesyl diphosphate


organism: Helicobacter pylori


organism: Lactobacillus plantarum

substrate_name: trans,trans-Farnesyl diphosphate; Isopentenyl diphosphate


substrate_name: Sulfide

substrate: Sulfide


organism: Leucaena leucocephala

proof_lines: pH 7.5, 22°C, recombinant enzymem, Michaelis-Menten model

proof_lines: pH 7.5, 22°C, recombinant enzyme, Lineweaver-Burke model


organism: Microcystis aeruginosa


organism: Mimosa pudica


substrate_name: hydrogen sulfide

substrate: hydrogen sulfide


substrate_name: Sulfide; O-Acetyl-L-serine

substrate: Sulfide; O-Acetyl-L-serine


substrate_name: O-acetyl-L-Ser

substrate: O-acetyl-L-Ser


substrate_name: L-Serine; Acetyl-CoA

assay_conditions_summary: cofactor CoA

substrate: L-Serine; Acetyl-CoA


substrate_name: O-Acetyl-L-serine; Thiosulfate

substrate: O-Acetyl-L-serine; Thiosulfate


substrate_name: (2Z,6E,10E)-geranylgeranyl diphosphate


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

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


substrate: (2Z,6E,10E)-geranylgeranyl diphosphate


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.3
Raw SKiD Env: Temp=30°C, pH=7.5


organism: Aeropyrum pernix

substrate_name: O-Acetyl-L-serine

substrate: O-Acetyl-L-serine


substrate_name: O-Phospho-L-serine

substrate: O-Phospho-L-serine


substrate_name: Hydrogen sulfide

substrate: Hydrogen sulfide


substrate_name: Hydrogen sulfide; O-Acetyl-L-serine


substrate_name: O-Acetyl-L-serine; Sulfide

substrate: O-Acetyl-L-serine; Sulfide


organism: Streptomyces lavendulae

substrate_name: thiosulfate

substrate: thiosulfate


organism: Thermus thermophilus

substrate: Hydrogen sulfide; O-Acetyl-L-serine


enzyme_display_name: protein farnesyltransferase

organism: Rattus norvegicus

enzyme: protein farnesyltransferase


substrate_name: Farnesyl diphosphate; Protein cysteine

substrate: Farnesyl diphosphate; Protein cysteine


enzyme_display_name: aspartate transaminase

organism: Advenella mimigardefordensis

substrate_name: L-aspartate

enzyme: aspartate transaminase

substrate: L-aspartate


substrate_name: L-Aspartate

substrate: L-Aspartate


organism: Solanum tuberosum


organism: Spinacia oleracea


substrate_name: Sulfide

substrate: Sulfide


substrate_name: hydrogen sulfide

proof_lines: 30°C, pH 8.0, cosubstrate: hydrogen sulfide

substrate: hydrogen sulfide


substrate_name: L-Cysteine

substrate: L-Cysteine


organism: Arabidopsis thaliana

substrate_name: L-Aspartate; 2-Oxoglutarate

substrate: L-Aspartate; 2-Oxoglutarate


smiles: O=C(O)CCC(=O)C(=O)O


substrate_name: Prephenate

substrate: Prephenate


substrate_name: L-Aspartate; Prephenate

substrate: L-Aspartate; Prephenate


substrate_name: L-Glutamate

substrate: L-Glutamate


substrate_name: oxaloacetate

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

substrate: oxaloacetate


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


substrate_name: L-Tyrosine

substrate: L-Tyrosine


substrate_name: L-Phe

assay_conditions_summary: pH 8

proof_lines: pH 8, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S

proof_lines: pH 8, cosubstrate: L-Asp, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S

proof_lines: pH 8, cosubstrate: L-Phe, mutant enzyme A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S

substrate: L-Phe


substrate_name: L-glutamate

substrate: L-glutamate


proof_lines:
at pH 7.4 and 30°C
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.4


organism: Geobacillus thermopakistaniensis

proof_lines: using L-aspartate as a cosubstrate, at pH 8.0 and 60°C


organism: Homo sapiens


organism: Mycobacterium tuberculosis


substrate_name: kynurenine

substrate: kynurenine


organism: Panicum miliaceum


organism: Petunia hybrida


substrate_name: L-Arogenate

substrate: L-Arogenate


organism: Bacillus sp.


organism: Bacillus subtilis


organism: Escherichia coli


enzyme_display_name: branched-chain-amino-acid transaminase

organism: Thermococcus sp.

enzyme: branched-chain-amino-acid transaminase


substrate_name: L-norleucine

substrate: L-norleucine


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


substrate_name: L-Isoleucine

substrate: L-Isoleucine


proof_lines: half transamination reaction, pH 8.0, 90°C


substrate_name: L-norvaline

substrate: L-norvaline


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: L-Valine

substrate: L-Valine


organism: Burkholderia mallei

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADH


substrate_name: crotonyl-[acyl-carrier protein]

proof_lines: substrate 2-dodecenoyl-CoA, pH 7.9, 25°C

substrate: crotonyl-[acyl-carrier protein]


organism: Burkholderia pseudomallei

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH

proof_lines:
pH 6.8, 25°C
Raw SKiD Env: Temp=25°C, pH=6.8


substrate_name: L-Leucine

substrate: L-Leucine


organism: Pinus pinaster

substrate_name: L-Aspartate; 2-Oxoglutarate

substrate: L-Aspartate; 2-Oxoglutarate


organism: Rattus norvegicus


organism: Rattus rattus


organism: Rhizobium meliloti


organism: Saccharolobus solfataricus

substrate_name: L-aspartate

substrate: L-aspartate


organism: Sinorhizobium meliloti

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


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


proof_lines: cosubstrate 4,4-dimethyl-2-oxopentanoate, pH 8.0, 37°C


organism: Gluconobacter oxydans


organism: Haliangium ochraceum


proof_lines:
pH 10.0, 40°C
Raw SKiD Env: Temp=40°C, pH=10


substrate_name: L-leucine

substrate: L-leucine


organism: Helicobacter pylori

substrate_name: L-isoleucine

substrate: L-isoleucine


organism: Homo sapiens

substrate_name: L-Leucine; 2-Oxoglutarate

substrate: L-Leucine; 2-Oxoglutarate


substrate_name: L-Glutamate

substrate: L-Glutamate


substrate_name: L-Isoleucine; alpha-Ketovaline

substrate: L-Isoleucine; alpha-Ketovaline


proof_lines:
cytosolic isoform, oxidized
cytosolic isoform, reduced
mitochondrial isoform, reduced


organism: Sus scrofa


organism: Thermus thermophilus


organism: Triticum aestivum

proof_lines:
allozyme AAT-2a, pH 7.5, 25°C
allozyme AAT-2b, pH 7.5, 25°C
allozyme AAT-2c, pH 7.5, 25°C


proof_lines:
allozyme AAT-3b, pH 7.5, 25°C
allozyme AAT-3c, pH 7.5, 25°C
allozyme AAT-3a, pH 7.5, 25°C


substrate_name: L-Aspartate

substrate: L-Aspartate


organism: Trypanosoma brucei


organism: Trypanosoma cruzi


substrate_name: L-tyrosine

proof_lines:
pH 7.5, 37°C
Raw SKiD Env: Temp=37°C, pH=7.5

substrate: L-tyrosine


substrate_name: L-valine

substrate: L-valine


organism: Methanococcus aeolicus

substrate_name: L-Isoleucine; 2-Ketoglutaric acid

substrate: L-Isoleucine; 2-Ketoglutaric acid


organism: Mycobacterium tuberculosis

substrate_name: L-glutamate

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

substrate: L-glutamate


organism: Pseudomonas aeruginosa

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


organism: Rattus norvegicus


organism: Synechocystis sp.


organism: Thermobaculum terrenum

proof_lines: pH 9.0, 50°C, recombinant enzyme, with 2-oxogluarate


organism: Thermococcus sp.

smiles: CCCCC(=O)C(=O)[O-]


organism: Arabidopsis thaliana

substrate_name: L-Glutamate; 3-Methyl-2-oxobutanoate

substrate: L-Glutamate; 3-Methyl-2-oxobutanoate


organism: Bacillus anthracis


organism: Bacillus cereus


organism: Bacillus subtilis


organism: Brevibacillus brevis


organism: Escherichia coli

smiles: CCC(C)C(=O)C(=O)O


smiles: CCCCCC(N)C(=O)O


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


smiles: CCCCCCC(N)C(=O)O


organism: Thermoproteus uzoniensis


substrate_name: pyruvate

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

substrate: pyruvate


substrate_name: L-alanine

substrate: L-alanine


organism: Vulcanisaeta moutnovskia

substrate_name: L-Ornithine

substrate: L-Ornithine


proof_lines:
pH 8.0, 65°C
Raw SKiD Env: Temp=65°C, pH=8


enzyme_display_name: acetate kinase

organism: Methanosarcina thermophila

substrate_name: Acetate

smiles: CC(=O)O

enzyme: acetate kinase

substrate: Acetate


substrate_name: ATP

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: ADP

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: mutant R91A, pH 7.0, presence of 200 mM guanidine/HCl

substrate: ADP


assay_conditions_summary: pH 7; cofactor ATP

proof_lines:
mutant R91K, pH 7.0
mutant R91K, pH 7.4


substrate_name: ATP; D-Fructose 6-phosphate

assay_conditions_summary: cofactor ATP

substrate: ATP; D-Fructose 6-phosphate


substrate_name: beta-D-Fructose 6-phosphate; ATP

substrate: beta-D-Fructose 6-phosphate; ATP


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


assay_conditions_summary: pH 6.5; cofactor ATP


organism: Spinacia oleracea

substrate_name: beta-D-fructose 6-phosphate

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP

proof_lines:
pH 7.8, 25°C, effect of phosphate on Km
pH 7.8, 25°C

substrate: beta-D-fructose 6-phosphate


substrate_name: L-Valine

substrate: L-Valine


substrate_name: L-norvaline

substrate: L-norvaline


substrate_name: L-valine

substrate: L-valine


assay_conditions_summary: pH 6; 298.15 K; cofactor ATP


organism: Bos taurus


organism: Gallus gallus


organism: Homo sapiens

substrate_name: D-Fructose 6-phosphate; ATP

substrate: D-Fructose 6-phosphate; ATP


proof_lines: pH 7.5, 30°C, recombinant His-tagged HBP1 deletion mutant


mutation_signature: is-tagged HBP1 deletion mutant

proof_lines: pH 7.5, 30°C, recombinant Hnon-phosphorylated, is-tagged HBP1 deletion mutant


proof_lines: pH 7.5, 30°C, recombinant His-tagged HBP1 mutant S302R

proof_lines: pH 7.5, 30°C, recombinant non-phosphorylated, His-tagged HBP1 mutant S302R


proof_lines: pH 7.5, 30°C, recombinant HBP1 mutant S460D

proof_lines: pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant S460D


proof_lines: pH 7.5, 30°C, recombinant HBP1 mutant H253A

proof_lines: pH 7.5, 30°C, recombinant non-phosphorylated, HBP1 mutant H253A


substrate_name: ADP; Acetyl phosphate

substrate: ADP; Acetyl phosphate


organism: Fructilactobacillus sanfranciscensis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Lactococcus lactis

substrate_name: acetate

proof_lines: pH 7.5, 30°C, recombinant His-tagged isozyme AckA1

substrate: acetate


proof_lines: pH 7.5, 30°C, recombinant His-tagged isozyme AckA2


organism: Methanosarcina mazei

proof_lines: pH 7.0, temperature not specified in the publication