organism: Homo sapiens

substrate_name: benzyl alcohol

substrate: benzyl alcohol


enzyme_display_name: alcohol sulfotransferase

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06520 direct FASTA; variant reconstructed by applying L246P. and applied mutation signature L246P to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: alcohol sulfotransferase(Enzyme) mutant L246P

enzyme: alcohol sulfotransferase


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06520 direct FASTA; variant reconstructed by applying E147K. and applied mutation signature E147K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: alcohol sulfotransferase(Enzyme) mutant E147K


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06520 direct FASTA; variant reconstructed by applying P76T. and applied mutation signature P76T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: alcohol sulfotransferase(Enzyme) mutant P76T


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06520 direct FASTA; variant reconstructed by applying E148K. and applied mutation signature E148K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: alcohol sulfotransferase(Enzyme) mutant E148K


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06520 direct FASTA; variant reconstructed by applying F258L. and applied mutation signature F258L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: alcohol sulfotransferase(Enzyme) mutant F258L


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06520 direct FASTA; variant reconstructed by applying Q262E. and applied mutation signature Q262E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: alcohol sulfotransferase(Enzyme) mutant Q262E


organism: Mus musculus

km_display: Not reported

mutation_signature: Unknown

sequence_source: UniProtKB reviewed accession P52843 direct FASTA.

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


enzyme_display_name: Sulfotransferase 2B1

sequence_source: UniProtKB FASTA O35400

enzyme: Sulfotransferase 2B1


enzyme_display_name: Sulfotransferase 2A6

organism: Rattus norvegicus

source_db: brenda

source_license: CC BY 4.0

sequence_source: UniProtKB FASTA P22789

enzyme: Sulfotransferase 2A6

source: brenda


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

sequence_source: UniProtKB FASTA Q29YR5

proof_lines: pH 7.5, 37°C, recombinant isozyme SULT2B1b

proof_lines: pH 7.5, 37°C, recombinant isozyme SULT2B1a


organism: Escherichia coli

source_db: oed

verification_status: unverified

sequence_source: UniProtKB FASTA P0AF12

data_origin: experimental

status: unverified

source: oed


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


enzyme_display_name: Aminodeoxyfutalosine nucleosidase / MTAN-family source context

organism: Helicobacter pylori

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA Q9ZMY2 with H109A reconstruction and applied mutation signature H109A to reconstruct the assayed variant sequence.


substrate_name: S-adenosyl-L-homocysteine

sequence_source: UniProtKB FASTA Q9ZMY2 with H109A reconstruction

enzyme: Aminodeoxyfutalosine nucleosidase / MTAN-family source context

substrate: S-adenosyl-L-homocysteine


organism: Arabidopsis thaliana

substrate_name: m-cresol

sequence_source: UniProtKB reviewed entry P52839 REST lookup on 2026-06-05

substrate: m-cresol


substrate_name: o-Cresol

substrate: o-Cresol


substrate_name: dehydroepiandrosterone

mutation_signature: recombinant truncated mutant SULT2B1

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

mutation_type: truncation

proof_lines: pH 7.5, 37°C, recombinant truncated mutant SULT2B1

substrate: dehydroepiandrosterone


sequence_source: UniProtKB reviewed entry O00204 REST lookup on 2026-06-05

proof_lines: pH 7.5, 37°C, recombinant wild-type, full-length SULT2B1


substrate_name: androsterone

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q06520 REST lookup on 2026-06-05 with Y238A residue substitution reconstruction and applied mutation signature Y238A to reconstruct the assayed variant sequence.

substrate: androsterone


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q06520 REST lookup on 2026-06-05 with M137I residue substitution reconstruction and applied mutation signature M137I to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed entry Q06520 REST lookup on 2026-06-05

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q06520 REST lookup on 2026-06-05 with M137I and Y238A residue substitution reconstruction and applied mutation signature M137I/Y238A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 25°C, recombinant mutant M137I/Y238A


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature Y238F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature M137W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature M137V/Y238A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 25°C, recombinant mutant M137V/Y238A


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature M137V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature M137W/Y238A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 25°C, recombinant mutant M137W/Y238A


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature Y238W to reconstruct the assayed variant sequence.


substrate_name: (24S)-Hydroxycholesterol 24-sulfate

substrate: (24S)-Hydroxycholesterol 24-sulfate


organism: Unknown

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


source_db: uniprot

source: uniprot


substrate_name: DHEA

substrate: DHEA


substrate_name: cholesterol (isoform 2)

substrate: cholesterol (isoform 2)


substrate_name: pregnenolone (isoform 2)

substrate: pregnenolone (isoform 2)


substrate_name: 3'-phosphoadenylyl sulfate

substrate: 3'-phosphoadenylyl sulfate


substrate_name: (24S)-Hydroxycholesterol 3-sulfate

sequence_source: UniProtKB reviewed direct accession lookup Q06520; REST/FASTA checked 2026-06-05

substrate: (24S)-Hydroxycholesterol 3-sulfate


sequence_source: UniProtKB reviewed direct accession lookup O00204; REST/FASTA checked 2026-06-05


proof_lines: SULT2A1, pH and temperature not specified in the publication


sequence_source: UniProtKB reviewed direct accession lookup P49888; sequence withheld from accepted row because EC annotation contradicts selected EC 2.8.2.2


proof_lines: SULT2B1a, pH and temperature not specified in the publication

proof_lines: SULT2B1b, pH and temperature not specified in the publication


sequence_source: UniProtKB reviewed direct accession lookup P50226; sequence withheld from accepted row because EC annotation contradicts selected EC 2.8.2.2


sequence_source: UniProtKB reviewed direct accession lookup P50225; sequence withheld from accepted row because EC annotation contradicts selected EC 2.8.2.2


enzyme_display_name: adenosylhomocysteine nucleosidase

verification_status: corrected

sequence_source: UniProtKB reviewed accession Q9ZMY2 FASTA

enzyme: adenosylhomocysteine nucleosidase

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9ZMY2 FASTA with direct H109A reconstruction and applied mutation signature H109A to reconstruct the assayed variant sequence.


organism: Aquarana catesbeiana

proof_lines: in 0.1 M sodium phosphate, pH 7.2, and 2 mM EDTA for 30 min at 16°C


organism: Cavia porcellus


substrate_name: triiodothyronine

proof_lines:
pH 6.0, 37°C, isoform SULT2A1
pH 7.4, 37°C
pH 7.5, 37°C

substrate: triiodothyronine


organism: Mesocricetus auratus


organism: Petromyzon marinus


proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C cosubstrate ethanol
pH 5.5, 37°C


organism: Secale cereale

substrate_name: DIBOA-glucoside

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

substrate: DIBOA-glucoside


substrate_name: DIMBOA-glucoside

substrate: DIMBOA-glucoside


substrate_name: 4-nitrophenyl beta-D-glucoside

substrate: 4-nitrophenyl beta-D-glucoside


organism: Triticum aestivum

substrate_name: 4-nitrophenyl beta-D-fucoside

proof_lines: pH and temperature not specified in the publication

substrate: 4-nitrophenyl beta-D-fucoside


enzyme_display_name: xanthine dehydrogenase

organism: Blastobotrys adeninivorans

substrate_name: xanthine in pH 8.5 and at 43 degrees Celsius

enzyme: xanthine dehydrogenase


organism: Bos taurus

substrate_name: molecular oxygen in dehydrogenase form

substrate: molecular oxygen in dehydrogenase form


organism: Rhodobacter capsulatus

substrate_name: xanthine

substrate: xanthine


substrate_name: NAD+

sequence_source: UniProtKB O54050 direct REST lookup

assay_conditions_summary: pH 8.5; 313.15 K; cofactor NAD+

substrate: NAD+


proof_lines:
pH 8.5, 40°C, Split166 mutant
pH 8.5, 40°C, Split178 mutant


organism: Drosophila melanogaster

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines: activation of mutant G1011E activity after preincubation with ferricyanide, electron acceptor: methylene blue

proof_lines: activation of mutant G1011E activity after preincubation with phenazine methosulfate and cytochrome c, electron acceptor: methylene blue

substrate: NADH


assay_conditions_summary: cofactor NAD+

proof_lines: increased Km for mutant G353D, electron acceptor: pterin

proof_lines: increased Km for mutant G353D, electron acceptor: 2,6-dichlorophenolindophenol


organism: Eubacterium barkeri

substrate_name: hypoxanthine

assay_conditions_summary: cofactor NADP+

proof_lines:
electron acceptor: NADP+
electron donor: hypoxanthine

substrate: hypoxanthine


organism: Gallus gallus

assay_conditions_summary: pH 7.9; cofactor NAD+

proof_lines: immobilized enzyme preparation, pH 7.9, pH dependence, minimum Km at pH 8.1, increasing values below and above

proof_lines: pH 7.9, pH dependence, increasing Km with increasing pH

proof_lines: pH 7.9, increasing Km with increasing pH


organism: Glycine max

substrate_name: H2O; NAD+; Xanthine

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: at pH 7.5, ping-pong-reaction mechanism, strongly pH-dependent

substrate: H2O; NAD+; Xanthine


organism: Rattus norvegicus

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NAD+

proof_lines: DTT-treated C-terminally truncated enzyme mutant, pH 7.8, 25°C


substrate_name: Xanthine; H2O; NAD+

substrate: Xanthine; H2O; NAD+


substrate_name: NAD+; Xanthine; H2O

proof_lines: SABIO-RK modifier species: xanthine dehydrogenase(Enzyme) mutant E232A

substrate: NAD+; Xanthine; H2O


substrate_name: NAD+; H2O; Xanthine

substrate: NAD+; H2O; Xanthine


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: DIBOA-beta-D-glucoside

proof_lines: kcat is 172 sec(-1) with DIBOA-beta-D-glucoside as substrate. kcat is 118 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 119 sec(-1) with DIMBOA-beta-D-glucoside as substrate. kcat is 158 sec(-1) with DI

substrate: DIBOA-beta-D-glucoside


substrate_name: DIBOA-beta-D-glucoside (with native hexamer)

proof_lines: kcat is 137 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 773 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 235.9 sec(-1) with p-nitrophenyl beta-D-glucopyranoside


proof_lines: kcat is 214 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 1201 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 128.2 sec(-1) with p-nitrophenyl beta-D-glucopyranosid

substrate: DIBOA-beta-D-glucoside (with native hexamer)


proof_lines: kcat is 48.8 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 338 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 99.2 sec(-1) with p-nitrophenyl beta-D-glucopyranoside


proof_lines: kcat is 5728 sec(-1) with DIBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat is 330 sec(-1) with DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme).


enzyme_display_name: methylthioadenosine nucleosidase

substrate_name: 5'-methylthioadenosine (MTA)

enzyme: methylthioadenosine nucleosidase

substrate: 5'-methylthioadenosine (MTA)


organism: Acinetobacter baumannii

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+

proof_lines:
electron acceptor: oxygen
electron acceptor: NAD+
pH 7.2, 25°C


organism: Colias eurytheme

substrate_name: Xanthopterin

proof_lines:
cosubstrate: NAD+
wing preparation, cosubstrate: NAD+
wing preparation, co substrate: NAD+

substrate: Xanthopterin


organism: Delftia acidovorans

proof_lines:
electron acceptor: NAD+
electron donor: xanthine
cosubstrate: hypoxanthine


assay_conditions_summary: pH 7; 323.15 K; cofactor NAD+

proof_lines: recombinant enzyme, electron acceptor: phenazine methosulfate-cytochrome c

proof_lines: pH 7.0, electron acceptor: methylene blue


substrate_name: H2O; Xanthine; NAD+

sequence_source: UniProtKB direct accession lookup P80457

substrate: H2O; Xanthine; NAD+


sequence_source: UniProtKB direct accession lookup Q8RLC1

proof_lines: coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25°C

proof_lines: coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25°C

proof_lines: coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25°C


organism: Escherichia coli

substrate_name: benzaldehyde

proof_lines:
wild-type, pH 5.5, 22°C
wild-type, pH 5.0, 22°C
wild-type, pH 4.5, 22°C

substrate: benzaldehyde


proof_lines:
mutant R440K, pH 5.5, 22°C
mutant R440K, pH 5.0, 22°C
mutant R440K, pH 4.5, 22°C


proof_lines:
mutant R440H, pH 5.0, 22°C
mutant R440H, pH 4.5, 22°C
mutant R440H, pH 5.5, 22°C


proof_lines: pH 7.8, 25°C, wild-type enzyme, with DCIP

proof_lines: pH 7.8, 25°C, wild-type enzyme, with NAD+


proof_lines:
pH 7.8, 25°C, mutant Q102G, with NAD+
pH 7.8, 25°C, mutant Q102G, with DCIP
pH 7.8, 25°C, mutant Q102G


substrate_name: DCPIP

substrate: DCPIP


proof_lines:
pH 7.8, 25°C, mutant Q102A, with NAD+
pH 7.8, 25°C, mutant Q102A, with DCIP
pH 7.8, 25°C, mutant Q102A


organism: Streptomyces cyanogenus

substrate_name: guanine

substrate: guanine


organism: Zea mays

substrate_name: DIMBOA-glucoside

proof_lines: pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)

proof_lines: pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)

proof_lines: pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)

substrate: DIMBOA-glucoside


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: licheninase

organism: Fibrobacter succinogenes

substrate_name: lichenan

enzyme: licheninase

substrate: lichenan


organism: Laetiporus sulphureus

proof_lines: pH 4.0, 75°C, substrate from Hordeum vulgare


organism: Paecilomyces sp.

substrate_name: Barley beta-glucan

proof_lines: calculated as D-glucose units released from beta-glucan

proof_lines: calculated as D-glucose units released from lichenan

substrate: Barley beta-glucan


organism: Paecilomyces sp. 'thermophila'


organism: Sus scrofa

substrate_name: xanthine

proof_lines: pH 7.4, 37°C, mutant S360P, Vmax (micromol/min/mg): 2.83

substrate: xanthine


proof_lines: pH 7.4, 37°C, mutant G47A, Vmax (micromol/min/mg): 7.91


proof_lines: pH 7.4, 37°C, mutant N352A, Vmax (micromol/min/mg): 7.69


organism: Triticum aestivum

substrate_name: NADH

proof_lines: electron acceptor: nitroblue tetrazolium

substrate: NADH


organism: Veillonella atypica

substrate_name: oxygen

proof_lines:
cosubstrate xanthine
electron acceptor: oxygen
electron acceptor: ferricyanide

substrate: oxygen


substrate_name: DIBOA-glucoside

substrate: DIBOA-glucoside


substrate_name: 4-nitrophenyl beta-D-glucoside

substrate: 4-nitrophenyl beta-D-glucoside


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8.5; cofactor NAD+


organism: Neurospora crassa

proof_lines:
xanthine dehydrogenase activity
diaphorase activity
oxidation of 2-amino-4-hydroxy-pterin


organism: Ovis aries

substrate_name: NAD+

substrate: NAD+


organism: Pseudomonas putida

substrate_name: hypoxanthine

substrate: hypoxanthine


organism: Rattus sp.

proof_lines:
oxidase type O, absence of NAD+
cosubstrate NAD+
dehydrogenase type D, absence of NAD+


organism: Rhodobacter capsulatus


organism: Gottschalkia acidurici

substrate_name: methyl viologen

proof_lines:
electron donor: xanthine
electron acceptor: methyl viologen

substrate: methyl viologen


organism: Gottschalkia purinilytica


organism: Homo sapiens


enzyme_display_name: 3-deoxy-7-phosphoheptulonate synthase

organism: Corynebacterium glutamicum

substrate_name: D-erythrose 4-phosphate

assay_conditions_summary: pH 7.5; 303.15 K; buffer context

proof_lines: isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C

proof_lines: isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C

proof_lines: isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5,at 30°C

enzyme: 3-deoxy-7-phosphoheptulonate synthase

substrate: D-erythrose 4-phosphate


organism: Aeropyrum pernix

substrate_name: phosphoenolpyruvate

source_db: brenda,skid

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

sequence_source: UniProtKB direct accession lookup Q9YEJ7 (REST FASTA/TSV, checked 2026-06-05)

proof_lines:
pH 7.0, 60°C
Raw SKiD Env: Temp=60°C, pH=7

source_databases_merged: brenda skid

substrate: phosphoenolpyruvate

source: brenda,skid


organism: Escherichia coli

substrate_name: H2O; Phosphoenolpyruvate; D-Erythrose 4-phosphate

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

sequence_source: UniProtKB direct accession lookup P0AB91 (REST FASTA/TSV, checked 2026-06-05)

proof_lines:
Phe-sensitive isozyme, pH 6.8, 25°C
sensitive to metal ion
Raw SKiD Env: Temp=25°C, pH=6.8

source_databases_merged: sabio_rk brenda skid


organism: Mycobacterium tuberculosis

substrate_name: Phosphoenolpyruvate; D-Erythrose 4-phosphate; H2O

sequence_source: UniProtKB direct accession lookup O53512 (REST FASTA/TSV, checked 2026-06-05)

proof_lines: results within factor two of this otherwise published value, 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5 with 100 microM MnCl2, 240 microM D-erythrose-4-phosphate (saturating), less than 10 microM phosphoenolpyr


organism: Paecilomyces sp. 'thermophila'


organism: Paenibacillus macerans


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P23904, reconstructed with RCSB 1MAC mature residue numbering offset +25 and applied mutation signature D105N with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed P23904 via RCSB 1MAC/SIFTS


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P23904, reconstructed with RCSB 1MAC mature residue numbering offset +25 and applied mutation signature W101F with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P23904, reconstructed with RCSB 1MAC mature residue numbering offset +25 and applied mutation signature E107D with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P23904, reconstructed with RCSB 1MAC mature residue numbering offset +25 and applied mutation signature E107H with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P23904, reconstructed with RCSB 1MAC mature residue numbering offset +25 and applied mutation signature W101Y with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


organism: Pectobacterium carotovorum

substrate_name: p-nitrophenyl-beta-D-glucopyranoside

substrate: p-nitrophenyl-beta-D-glucopyranoside


organism: Streptococcus pneumoniae

substrate_name: 4-nitrophenyl 6-phospho-beta-glucoside

substrate: 4-nitrophenyl 6-phospho-beta-glucoside


organism: Thermotoga maritima


organism: Acetabularia acetabulum


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7; 295.15 K; buffer 100 mM sodium phosphate

proof_lines: in 100 mM sodium phosphate buffer, pH 7.0


organism: Borreliella burgdorferi

assay_conditions_summary: pH 5

proof_lines:
Bgp protein, at pH 5.0
Pfs protein, at pH 5.0


organism: Penicillium occitanis (nom. inval.)


organism: Rhizopus homothallicus

substrate_name: Laminarin

sequence_source: NCBI Protein UEN71165.1 / nuccore MZ736416.1; Rhizopus homothallicus isolate RhGlu16B Glu16B mRNA partial CDS translation.

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

substrate: Laminarin


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


organism: Synechocystis sp. PCC 6803

substrate_name: 4-methylumbelliferyl cellobiose

sequence_source: NCBI Protein BAF51695.1; endo-1,3;1,4-beta-glucanase from Synechocystis sp. PCC 6803.

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

proof_lines: calculated as D-glucose units released from lichenan

substrate: 4-methylumbelliferyl cellobiose


organism: Fusobacterium mortiferum

sequence_source: UniProtKB P94793 / EMBL AAB49339.1; phospho-beta-glucosidase pbgA from Fusobacterium mortiferum, flagged as Fragment.


organism: Klebsiella aerogenes

substrate_name: arbutin 6-phosphate

substrate: arbutin 6-phosphate


organism: Salmonella enterica

proof_lines: in 100 mM HEPES, 50 mM KCl (pH 7.5), at 25°C


organism: Solanum lycopersicum


substrate_name: Unknown

substrate: Unknown


organism: Vibrio cholerae serotype O1

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM phosphate

proof_lines: at 25°C, in 100 mM HEPES, pH 7.5, and 50 mM KCl


assay_conditions_summary: pH 7; buffer 100 mM sodium phosphate


substrate_name: S-adenosyl-L-homocysteine

proof_lines:
Pfs protein, at pH 5.0
Bgp protein, at pH 5.0

substrate: S-adenosyl-L-homocysteine


organism: Sus scrofa

substrate_name: xanthine

protein_accession_database: NCBI Protein

sequence_source: NCBI GenBank JN896312.1 CDS protein_id AEW10559.1 direct lookup

proof_lines: pH 7.4, 37°C, wild-type, Vmax (micromol/min/mg): 7.74

substrate: xanthine


sequence_variant_note: Resolved canonical sequence from NCBI GenBank JN896312.1 CDS protein_id AEW10559.1 direct lookup plus R427E reconstruction and applied mutation signature R427E to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant R427E, Vmax (micromol/min/mg): 7.75


sequence_variant_note: Resolved canonical sequence from NCBI GenBank JN896312.1 CDS protein_id AEW10559.1 direct lookup plus D431A reconstruction and applied mutation signature D431A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant D431A, Vmax (micromol/min/mg): 8.52


sequence_variant_note: Resolved canonical sequence from NCBI GenBank JN896312.1 CDS protein_id AEW10559.1 direct lookup plus K1230A reconstruction and applied mutation signature K1230A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant K1230A, Vmax (micromol/min/mg): 4.02


sequence_variant_note: Resolved canonical sequence from NCBI GenBank JN896312.1 CDS protein_id AEW10559.1 direct lookup plus S1227A reconstruction and applied mutation signature S1227A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant S1227A, Vmax (micromol/min/mg): 3.94


sequence_variant_note: Resolved canonical sequence from NCBI GenBank JN896312.1 CDS protein_id AEW10559.1 direct lookup plus D430H reconstruction and applied mutation signature D430H to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant D430H, Vmax (micromol/min/mg): 7.47


organism: Brucella melitensis

sequence_source: UniProt Q8YBL1 via PMID 24657441/PDB 4PR3 SIFTS mapping; variant sequence reconstructed only where stated.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 via PMID 24657441/PDB 4PR3 SIFTS mapping; variant sequence reconstructed only where stated. and applied mutation signature M144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 via PMID 24657441/PDB 4PR3 SIFTS mapping; variant sequence reconstructed only where stated. and applied mutation signature R164A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 via PMID 24657441/PDB 4PR3 SIFTS mapping; variant sequence reconstructed only where stated. and applied mutation signature Y134F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 via PMID 24657441/PDB 4PR3 SIFTS mapping; variant sequence reconstructed only where stated. and applied mutation signature Y134A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 via PMID 24657441/PDB 4PR3 SIFTS mapping; variant sequence reconstructed only where stated. and applied mutation signature R85A to reconstruct the assayed variant sequence.


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


organism: Burkholderia thailandensis

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


organism: Escherichia coli

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM potassium phosphate

proof_lines:
pH 7.5, 25°C
recombinant nucleosidase
native nucleosidase


mutation_signature: truncated enzyme / truncated enzyme

proof_lines: rMTAN-8, truncated enzyme, lacking first 8 amino acids


organism: Helicobacter pylori

assay_conditions_summary: pH 7.2; 310.15 K; buffer HEPES/KCl

proof_lines: mutant enzyme F107A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C


organism: Catharanthus roseus


organism: Homo sapiens

substrate_name: H2O; 5'-Deoxy-5'-(methylthio)adenosine

substrate: H2O; 5'-Deoxy-5'-(methylthio)adenosine


organism: Lupinus luteus


organism: Neisseria meningitidis

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: alanine transaminase

organism: Arabidopsis thaliana

substrate_name: L-Glutamate; Pyruvate

sequence_source: UniProtKB REST direct lookup for reviewed accession Q9S7E9, fetched 2026-06-05

enzyme: alanine transaminase

substrate: L-Glutamate; Pyruvate


substrate_name: Pyruvate; L-Glutamate

sequence_source: UniProtKB REST direct lookup for reviewed accession Q9LR30, fetched 2026-06-05

substrate: Pyruvate; L-Glutamate


substrate_name: L-Alanine; 2-Oxoglutarate

substrate: L-Alanine; 2-Oxoglutarate


substrate_name: L-Alanine

substrate: L-Alanine


substrate_name: L-Glutamate

substrate: L-Glutamate


enzyme_display_name: LL-diaminopimelate aminotransferase, chloroplastic (AtDAP-AT) (DAP-AT) (DAP-aminotransferase) (LL-DAP-aminotransferase) (EC 2.6.1.83) (Protein ABERRANT GROWTH AND DEATH 2)

sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession lookup, retrieved 2026-06-05 and applied mutation signature P398S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: alanine transaminase(Enzyme) mutant His6-AGD2 P398S


enzyme_display_name: Aminotransferase ALD1, chloroplastic (EC 2.6.1.-) (AGD2-like defense response protein 1)

verification_status: verified

sequence_source: UniProtKB REST exact accession lookup, retrieved 2026-06-05

assay_conditions_summary: pH 8; 310.15 K; buffer an assay

column_label: Table 3. Kinetic Parameters of Recombinant AGD2- and ALD1-Catalyzed Reactions for Amino Acid Degradation Using Either Lys, Ala, or Arg with 2-Oxoglutarate (The Plant Cell 16, 353-366, 2004); printed columns Substrate, Cosubstrate (mM), Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); enzyme row 'ALD1', Substrate column Ala, Cosubstrate (mM) column 2-oxoglutarate (100 mM); column 'Km (mM)' = 5.56; column 'kcat (s^-1)' = 2.15; column 'kcat/Km (mM^-1 s^-1)' = 0.39.

normalized_value_unit_evidence: Km: printed cell 5.56 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 5.56 mM. kcat: printed cell 2.15 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 2.15 s^(-1). kcat/Km: printed cell 0.39 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 0.39 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 2.15 / 5.56 = 0.3866906474820144 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'ALD1', Substrate column Ala, Cosubstrate (mM) column 2-oxoglutarate (100 mM): Km = 5.56 mM; kcat = 2.15 s^-1; printed kcat/Km = 0.39 mM^-1 s^-1.

row_label: Table 3, enzyme row 'ALD1' with Substrate column Ala and Cosubstrate (mM) column 2-oxoglutarate (100 mM)

status: verified


column_label: Table 4. Kinetic Parameters of Recombinant AGD2- and ALD1-Catalyzed Reactions for Ala Synthesis Using Glutamate and Pyruvate as Cosubstrates (The Plant Cell 16, 353-366, 2004); printed columns Substrate, Cosubstrate (mM), Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); enzyme row 'ALD1', Substrate column Glutamate, Cosubstrate (mM) column Pyruvate (50 mM); column 'Km (mM)' = 37.0; column 'kcat (s^-1)' = 5.80; column 'kcat/Km (mM^-1 s^-1)' = 0.16.

normalized_value_unit_evidence: Km: printed cell 37.0 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 37.0 mM. kcat: printed cell 5.80 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 5.8 s^(-1). kcat/Km: printed cell 0.16 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 0.16 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 5.8 / 37.0 = 0.15675675675675677 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row 'ALD1', Substrate column Glutamate, Cosubstrate (mM) column Pyruvate (50 mM): Km = 37.0 mM; kcat = 5.80 s^-1; printed kcat/Km = 0.16 mM^-1 s^-1.

row_label: Table 4, enzyme row 'ALD1' with Substrate column Glutamate and Cosubstrate (mM) column Pyruvate (50 mM)

enzyme: Aminotransferase ALD1, chloroplastic (EC 2.6.1.-) (AGD2-like defense response protein 1)


enzyme_display_name: Alanine aminotransferase 2, mitochondrial (AtAlaAT2) (AtAlaATm) (EC 2.6.1.2) (Alanine-2-oxoglutarate aminotransferase 3) (EC 2.6.1.-)


enzyme_display_name: Alanine aminotransferase 1, mitochondrial (AtAlaAT1) (AtAlaATc) (EC 2.6.1.2) (Alanine-2-oxoglutarate aminotransferase 4) (EC 2.6.1.-)

substrate_name: L-alanine

substrate: L-alanine


enzyme_display_name: Glutamate-pyruvate aminotransferase AlaA (EC 2.6.1.2)


enzyme_display_name: Glutamate-pyruvate aminotransferase AlaC (EC 2.6.1.2)


enzyme_display_name: Alanine aminotransferase 1 (ALT1) (EC 2.6.1.2) (Glutamate pyruvate transaminase 1) (GPT 1) (Glutamic--alanine transaminase 1) (Glutamic--pyruvic transaminase 1)

substrate_name: glyoxylate

proof_lines:
pH 7.4, 37°C, cosubstrate: L-alanine
pH 7.4, 37°C, cosubstrate: L-glutamate

substrate: glyoxylate


organism: Trypanosoma cruzi

substrate_name: 2-Oxoglutarate; L-Alanine

proof_lines: SABIO-RK modifier species: alanine transaminase(Enzyme) mutant R20A

substrate: 2-Oxoglutarate; L-Alanine


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


proof_lines: SABIO-RK modifier species: alanine transaminase(Enzyme) mutant N17S


organism: Atriplex spongiosa

substrate_name: glutamate

proof_lines:
pH 7.5, 22°C, isoenzyme 1
pH 7.5, 22°C, isoenzyme 2
pH 7.5, 22°C, isoenzyme 3

substrate: glutamate


organism: Hordeum vulgare

sequence_source: UniProtKB:P52894 direct REST lookup on 2026-06-05

proof_lines:
cofactor: L-glutamate, 25°C, pH 8.0
cofactor: pyruvate, 25°C, pH 8.0
cofactor: L-alanine, 25°C, pH 8.0


organism: Lachancea kluyveri

substrate_name: beta-Alanine

substrate: beta-Alanine


organism: Mus musculus

substrate_name: pyruvate

sequence_source: UniProtKB:Q8QZR5 direct REST lookup on 2026-06-05

substrate: pyruvate


organism: Panicum miliaceum

sequence_source: UniProtKB:P34106 direct REST lookup on 2026-06-05


organism: Pyrococcus furiosus

sequence_source: UniProtKB:Q9P9M8 direct REST lookup on 2026-06-05

proof_lines:
pH 7.2, 80°C, native enzyme
pH 7.2, 80°C, recombinant enzyme
pH 8.0, 20°C


organism: Rattus norvegicus

sequence_source: UniProtKB:P25409 direct REST lookup on 2026-06-05


organism: Clarias batrachus


organism: Halalkalibacterium halodurans


substrate_name: alanine

proof_lines:
pH 7.8, 30°C, cytosolic enzyme
pH 7.4, 37°C
pH 7.8, 30°C, mitochondrial enzyme

substrate: alanine


organism: Hydrogenobacter thermophilus


organism: Kluyveromyces lactis


organism: Bombyx mori


organism: Bos taurus

proof_lines: pH 7.5, mitochondrial alanine aminotransferase

proof_lines: pH 7.5 mitochondrial alanine aminotransferase

proof_lines: pH 7.5, cytosolic alanine aminotransferase


organism: Camellia sinensis

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


organism: Candida maltosa


organism: Chlamydomonas reinhardtii


enzyme_display_name: 6,7-dimethyl-8-ribityllumazine synthase

organism: Aquifex aeolicus

sequence_source: UniProtKB reviewed entry O66529 direct accession lookup

enzyme: 6,7-dimethyl-8-ribityllumazine synthase


organism: Bacillus subtilis

substrate_name: L-3,4-dihydroxybutan-2-one 4-phosphate

sequence_source: UniProtKB reviewed entry P11998 direct accession lookup

substrate: L-3,4-dihydroxybutan-2-one 4-phosphate


organism: Escherichia coli

sequence_source: UniProtKB reviewed entry P61714 direct accession lookup


organism: Mesorhizobium loti

sequence_source: UniProtKB reviewed entry Q986N2 direct accession lookup

proof_lines:
isoform RibH1, pH 7.0, 37°C
Raw SKiD Env: Temp=37°C, pH=7


sequence_source: UniProtKB reviewed entry Q983B0 direct accession lookup


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB reviewed entry Q57751 direct accession lookup


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB reviewed entry P50861 direct accession lookup


organism: Schizosaccharomyces pombe

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q9UUB1 direct accession lookup plus W27Y reconstruction from selected mutation signature and applied mutation signature W27Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6,7-dimethyl-8-ribityllumazine synthase(Enzyme) mutant W27Y


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UUB1 canonical sequence; reconstructed W27H variant from source mutation note and applied mutation signature W27H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6,7-dimethyl-8-ribityllumazine synthase(Enzyme) mutant W27H


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UUB1 canonical sequence; reconstructed W27I variant from source mutation note and applied mutation signature W27I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6,7-dimethyl-8-ribityllumazine synthase(Enzyme) mutant W27I


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UUB1 canonical sequence; reconstructed W27G variant from source mutation note and applied mutation signature W27G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6,7-dimethyl-8-ribityllumazine synthase(Enzyme) mutant W27G


sequence_source: UniProtKB:Q9UUB1 canonical wild-type sequence

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UUB1 canonical sequence; reconstructed W27S variant from source mutation note and applied mutation signature W27S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6,7-dimethyl-8-ribityllumazine synthase(Enzyme) mutant W27S


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UUB1 canonical sequence; reconstructed W27F variant from source mutation note and applied mutation signature W27F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6,7-dimethyl-8-ribityllumazine synthase(Enzyme) mutant W27F


sequence_source: UniProtKB:Q9UUB1 canonical sequence

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

proof_lines:
pH 7.0, 27°C
Raw SKiD Env: Temp=37°C, pH=7


organism: Bacillus subtilis (strain 168)


organism: Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M)

substrate_name: 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius and pH 7.0)

assay_conditions_summary: pH 7

proof_lines: kcat is 0.003 sec(-1) (at 37 degrees Celsius and pH 7.0).


organism: Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)

proof_lines: kcat is 0.040 sec(-1) (at 37 degrees Celsius and pH 7.0).

substrate: 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius and pH 7.0)


proof_lines: kcat is inferior to 0.0003 sec(-1) (at 37 degrees Celsius and pH 7.0).


organism: Aquifex aeolicus (strain VF5)


organism: Brucella abortus (strain 2308)


organism: Escherichia coli (strain K12)


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


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: glutathione dehydrogenase (ascorbate)

organism: Arabidopsis thaliana

substrate_name: Reduced glutathione; Dehydroascorbate

sequence_source: UniProtKB reviewed Q8LE52 (DHAR3_ARATH), accessed 2026-06-05

enzyme: glutathione dehydrogenase (ascorbate)

substrate: Reduced glutathione; Dehydroascorbate


substrate_name: Dehydroascorbate; Reduced glutathione

sequence_source: UniProtKB reviewed Q9FWR4 (DHAR1_ARATH), accessed 2026-06-05

substrate: Dehydroascorbate; Reduced glutathione


organism: Caenorhabditis elegans

sequence_source: UniProtKB reviewed P34345 (GSTO1_CAEEL), accessed 2026-06-05


organism: Cenchrus americanus

substrate_name: dehydroascorbate

sequence_source: UniProtKB unreviewed U5XYA0 (U5XYA0_CENAM), accessed 2026-06-05

proof_lines: pH and temperature not specified in the publication, cytosolic isozyme

substrate: dehydroascorbate


organism: Chlamydomonas reinhardtii

sequence_source: UniProtKB unreviewed A8IYH1 (A8IYH1_CHLRE), accessed 2026-06-05

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


proof_lines: pH 7.0, temperature not specified in the publication


sequence_source: UniProtKB unreviewed A8I0K9 (A8I0K9_CHLRE), accessed 2026-06-05

proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme


substrate_name: glutathione

sequence_source: UniProtKB REST accession A8I0K9 direct lookup on 2026-06-05

substrate: glutathione


organism: Homo sapiens

proof_lines:
allelic variant D142 of GSTO2-2
allelic variant N142 of GSTO2-2


mutation_signature: six cysteine-to-serine mutations plus C-terminal FGLC deletion context from selected source notes

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

mutation_type: deletion

proof_lines: mutant containing six cysteine-to-serine mutations, with C-terminal residues FGLC deleted, pH 6.9, 30°C

proof_lines: mutant containing six cysteine-to-serine mutations with the C-terminal cysteine residue deleted, pH 6.9, 30°C

proof_lines: mutant with C-terminal residues FGLC deleted, pH 6.9, 30°C


sequence_source: UniProtKB REST accession Q9H4Y5 direct lookup on 2026-06-05


sequence_source: UniProtKB REST accession P78417 direct lookup on 2026-06-05


organism: Ipomoea batatas

sequence_source: UniProtKB REST accession D2CGD4 direct lookup on 2026-06-05


organism: Populus trichocarpa

proof_lines: pH and temperature not specified in the publication, chloroplastic isozyme DHAR3B


organism: Actinidia chinensis

proof_lines: pH and temperature not specified in the publication, cytosolic isozyme DHAR1

proof_lines: pH and temperature not specified in the publication, plastidic isozyme DHAR2


organism: Unknown


organism: Populus tomentosa

sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA direct lookup for J9WN12 on 2026-06-05; variant sequence reconstructed from the accession sequence. and applied mutation signature D72A to reconstruct the assayed variant sequence.

proof_lines: mutant D72A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA direct lookup for J9WN12 on 2026-06-05; variant sequence reconstructed from the accession sequence. and applied mutation signature K8A to reconstruct the assayed variant sequence.

proof_lines: mutant K8A, pH not specified in the publication, temperature not specified in the publication


sequence_source: UniProtKB REST/FASTA direct lookup for J9WN12 on 2026-06-05.

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


proof_lines: pH and temperature not specified in the publication, cytosolic isozyme DHAR2


sequence_source: UniProtKB REST/FASTA direct lookup for J9WNR5 on 2026-06-05.

proof_lines: pH and temperature not specified in the publication, cytosolic isozyme DHAR3


sequence_source: UniProtKB REST/FASTA direct lookup for J9WQY6 on 2026-06-05.

proof_lines: pH and temperature not specified in the publication, chloroplastic isozyme DHAR1


sequence_source: UniProtKB REST/FASTA direct lookup for D2WL73 on 2026-06-05.


sequence_source: UniProtKB REST/FASTA direct lookup for D2WL74 on 2026-06-05.


sequence_source: UniProtKB D2WL75 direct accession lookup on 2026-06-05

proof_lines: pH and temperature not specified in the publication, cytosolic isozyme DHAR3A


organism: Solanum lycopersicum

sequence_source: UniProtKB Q4VDN8 direct accession lookup on 2026-06-05

proof_lines: pH 6.3, temperature not specified in the publication


organism: Solanum tuberosum

sequence_source: UniProtKB M1BA41 direct accession lookup on 2026-06-05

proof_lines: pH and temperature not specified in the publication, cytosolic isozyme


organism: Spinacia oleracea

sequence_source: UniProtKB Q9FVE4 direct accession lookup on 2026-06-05


proof_lines: pH and temperature not specified in the publication, chloroplastic isozyme


proof_lines: SABIO-RK modifier species: glutathione dehydrogenase (ascorbate)(Enzyme) mutant C9/26S


proof_lines: SABIO-RK modifier species: glutathione dehydrogenase (ascorbate)(Enzyme) mutant C9S


proof_lines: SABIO-RK modifier species: glutathione dehydrogenase (ascorbate)(Enzyme) mutant C26S


organism: Euglena gracilis


organism: Oryza sativa


organism: Picea abies

proof_lines:
isoform DHAR2, at pH 6.5 and 25°C
isoform DHAR1, at pH 6.5 and 25°C


organism: Pleurotus ostreatus


organism: Rattus norvegicus


organism: Selaginella moellendorffii

proof_lines:
isoform DHAR1, at pH 6.5 and 25°C
isoform DHAR2, at pH 6.5 and 25°C


substrate_name: GSH

substrate: GSH


proof_lines: pH 6.8, in presence of 0.5 mM dehydroascorbate


enzyme_display_name: tryptophan 5-monooxygenase

sequence_source: UniProtKB:P17752 canonical sequence direct lookup 2026-06-05

smiles: O=O

enzyme: tryptophan 5-monooxygenase


substrate_name: L-Tryptophan

sequence_source: UniProtKB:Q8IWU9 canonical sequence direct lookup 2026-06-05

substrate: L-Tryptophan


organism: Mus musculus

substrate_name: L-tryptophan

sequence_source: UniProtKB:Q8CGV2 canonical sequence direct lookup 2026-06-05

proof_lines: TPH2, with 0.004-0.4 mM tetrahydrobiopterin

substrate: L-tryptophan


sequence_source: UniProtKB:P17532 canonical sequence direct lookup 2026-06-05


organism: Oryctolagus cuniculus

sequence_source: UniProtKB:P17290 canonical sequence direct lookup 2026-06-05


organism: Pseudomonas fluorescens


organism: Homo sapiens

sequence_source: UniProtKB reviewed accession Q8IWU9 direct FASTA lookup

sequence_variant_note: Mutation signature ΔC17 could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant TPH2 delta C17 (aa 1-473)


proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant chimeric TPH1-2 (N1-44(Q8IWU9)-TPH1)


substrate_name: L-Tryptophan; Tetrahydrobiopterin; O2

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant R441H His6-tagged

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant R441H MBP-His6-tagged

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant R441H N-terminal 6xHis-MBP-fusion

substrate: L-Tryptophan; Tetrahydrobiopterin; O2


substrate_name: Tetrahydrobiopterin; O2; L-Tryptophan

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant P206S His6-tagged

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant P206S MBP-His6-tagged

substrate: Tetrahydrobiopterin; O2; L-Tryptophan


proof_lines: pH 7.0, 30°C, recombinant phosphorylated wild-type TPH2

proof_lines: pH 7.0, 30°C, recombinant wild-type TPH2 fusion enzyme

proof_lines: pH 7.0, 30°C, recombinant non-phosphorylated wild-type TPH2


substrate_name: Tetrahydrobiopterin

sequence_source: UniProtKB reviewed accession P17752 direct FASTA lookup

substrate: Tetrahydrobiopterin


organism: Gallus gallus

substrate_name: tetrahydrobiopterin

sequence_source: UniProt REST exact accession P70080, TPH1_CHICK, reviewed, EC 1.14.16.4, Gallus gallus

proof_lines:
pH 7.0, 15°C, recombinant TPH1
Raw SKiD Env: Temp=15°C, pH=7

substrate: tetrahydrobiopterin


mutation_signature: doubly truncated enzyme form DELTANH102-DELTACOOH402 doubly truncated enzyme form DELTANH102-DELTACOOH402

sequence_source: RCSB PDB 1MLW entity 1, mapped by SIFTS to UniProt P17752 residues 102-402

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


substrate_name: Tetrahydrobiopterin; L-Tryptophan; O2

sequence_source: UniProt REST exact accession Q8IWU9, TPH2_HUMAN, reviewed, EC 1.14.16.4, Homo sapiens

proof_lines: 0.02 mM ferrous ammonium, 0.5 mM (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin, 30°C

substrate: Tetrahydrobiopterin; L-Tryptophan; O2


sequence_source: Canonical parent sequence from UniProt REST exact accession P17752; row-specific HPTrx-TPH1 Ndelta90 construct sequence not resolved

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant HPTrx-TPH1 Ndelta90


substrate_name: O2; Tetrahydrobiopterin; L-Tryptophan

sequence_source: UniProt REST exact accession P17752, TPH1_HUMAN, reviewed, EC 1.14.16.4, Homo sapiens

proof_lines:
catalytic domain of TPH1
Raw SKiD Env: Temp=-----, pH=-----

substrate: O2; Tetrahydrobiopterin; L-Tryptophan


substrate_name: L-Tryptophan; O2; Tetrahydrobiopterin

sequence_source: Canonical parent sequence from UniProt REST exact accession P17752; row-specific HPTrx-TPH1 Ndelta90 F313W construct sequence not resolved

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant HPTrx-TPH1 Ndelta90 F313W

substrate: L-Tryptophan; O2; Tetrahydrobiopterin


sequence_source: Canonical parent sequence from UniProt REST exact accession Q8IWU9; row-specific P449R fusion/detagged construct sequence not resolved

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant P449R N-terminal 6xHis-MBP-fusion

proof_lines: pH 7.0, 30°C, recombinant mutant P449R fusion enzyme


sequence_source: Reconstructed from UniProt REST exact accession Q8IWU9 using selected source note TPH2 delta C19 (aa 1-471)

sequence_variant_note: Mutation signature ΔC19 could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: tryptophan 5-monooxygenase(Enzyme) mutant TPH2 delta C19 (aa 1-471)


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Arabidopsis thaliana

substrate_name: glutamate

substrate: glutamate


organism: Escherichia coli (strain K12)

substrate_name: pyruvate (at 37 degrees Celsius and pH 8.5)


substrate: pyruvate (at 37 degrees Celsius and pH 8.5)


organism: Unknown


sequence_source: UniProtKB P17752 canonical sequence after PMID 10525150 TPH1 context check

proof_lines: TPH1. in vitro transcription and translation product


organism: Nilaparvata lugens

sequence_variant_note: Resolved canonical sequence from UniProtKB:J9Q3Y4 REST direct check on 2026-06-05 and applied mutation signature R176A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:J9Q3Y4 REST direct check on 2026-06-05


sequence_variant_note: Resolved canonical sequence from UniProtKB:J9Q3Y4 REST direct check on 2026-06-05 and applied mutation signature C29A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:J9Q3Y4 REST direct check on 2026-06-05 and applied mutation signature F28A to reconstruct the assayed variant sequence.


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


organism: Oryza sativa Japonica Group

sequence_source: UniProtKB:Q65XA0 REST direct check on 2026-06-05

proof_lines: pH and temperature not specified in the publication, cytosolic isozyme


organism: Pinus bungeana

sequence_source: UniProtKB:B2ZHM6 REST direct check on 2026-06-05


organism: Populus tomentosa

sequence_variant_note: Resolved canonical sequence from uniprot_accession:J9WN12; reconstructed_variant:S73A and applied mutation signature S73A to reconstruct the assayed variant sequence.

proof_lines: mutant S73A, pH not specified in the publication, temperature not specified in the publication


substrate_name: 2-hydroxyethyl disulfide (HEDS)

sequence_source: source_record; UniProt O00299 direct check

substrate: 2-hydroxyethyl disulfide (HEDS)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: reduced glutathione (GSH)

sequence_source: source_record; UniProt P36156 direct check

substrate: reduced glutathione (GSH)


sequence_source: source_record; UniProt P48239 direct check


organism: Schistosoma mansoni

sequence_source: UniProtKB:O96370 direct REST lookup


organism: Liriodendron chinense

sequence_source: UniProtKB:A0A6C0W973 direct REST lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:J9Q3Y4 direct REST lookup plus reviewed mutation reconstruction and applied mutation signature P30A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:J9Q3Y4 direct REST lookup plus reviewed mutation reconstruction and applied mutation signature F28A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:J9Q3Y4 direct REST lookup plus reviewed mutation reconstruction


sequence_source: UniProtKB:J9Q3Y4 direct REST lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:J9Q3Y4 direct REST lookup plus reviewed mutation reconstruction and applied mutation signature L225A to reconstruct the assayed variant sequence.


organism: Neisseria meningitidis

substrate_name: phosphoenolpyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q9K169 canonical sequence with RCSB structure cross-checks and applied mutation signature S213G to reconstruct the assayed variant sequence.

substrate: phosphoenolpyruvate


sequence_source: UniProtKB REST Q9K169 canonical sequence with RCSB structure cross-checks

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

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


proof_lines:
pH 6.8, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=6.8
Raw SKiD Env: Temp=30°C, pH=6.8


substrate_name: D-erythrose 4-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q9K169 canonical sequence with RCSB structure cross-checks and applied mutation signature R126S to reconstruct the assayed variant sequence.

substrate: D-erythrose 4-phosphate


proof_lines:
pH 6.8, 25°C, mutant R126S
pH 6.8, 30°C, mutant R126S


organism: Corynebacterium glutamicum

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

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM Tris-HCl

proof_lines: isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C

proof_lines: isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C

proof_lines: isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5,at 30°C


organism: Amycolatopsis mediterranei

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


organism: Amycolatopsis methanolica

sequence_source: GenBank AY382157.1 / protein AAQ89574.1; A. methanolica aroF DAHP-synthase direct CDS translation, mapped to DS2/AroF by PMID 14600244.

proof_lines:
isozyme DS II, pH 7.5, 37°C
DS II isozyme, pH 7.5, 37°C


organism: Daucus carota

proof_lines:
pH 7.0, 25°C
cytosolic isozyme, pH 8.6


organism: Actinosynnema pretiosum subsp. auranticum


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


organism: Aeropyrum pernix

proof_lines:
pH 7.0, 60°C
Raw SKiD Env: Temp=60°C, pH=7


organism: Escherichia coli

substrate_name: H2O; Phosphoenolpyruvate; D-Erythrose 4-phosphate

proof_lines:
Phe-sensitive isozyme, pH 6.8, 25°C
sensitive to metal ion
Raw SKiD Env: Temp=25°C, pH=6.8


organism: Mycobacterium tuberculosis

substrate_name: Phosphoenolpyruvate; D-Erythrose 4-phosphate; H2O

proof_lines: results within factor two of this otherwise published value, 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5 with 100 microM MnCl2, 240 microM D-erythrose-4-phosphate (saturating), less than 10 microM phosphoenolpyr


organism: Pyrococcus furiosus

sequence_source: UniProt REST FASTA Q8U0A9 direct lookup

sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA Q8U0A9 direct lookup and applied mutation signature I181D to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

sequence_source: UniProt REST FASTA Q9WYH8 direct lookup

sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA Q9WYH8 direct lookup and applied mutation signature H29A to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, temperature not specified in the publication, mutant H29A


sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA Q9WYH8 direct lookup and applied mutation signature H29S/S31H to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, temperature not specified in the publication, mutant H29S/S31H


sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA Q9WYH8 direct lookup and applied mutation signature S31G to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, temperature not specified in the publication, mutant S31G


proof_lines: pH 7.3, temperature not specified in the publication, wild-type enzyme


organism: uncultured bacterium


organism: Neurospora crassa

substrate_name: Unknown

proof_lines: slope, tryptophan-sensitive isozyme, versus D-erythrose 4-phosphate, pH 7.4, 37°C

proof_lines: intercept, tryptophan-sensitive isozyme, versus phosphoenolpyruvate, pH 7.4, 37°C

proof_lines: slope, tryptophan-sensitive isozyme, versus phosphoenolpyruvate, pH 7.4, 37°C

substrate: Unknown


assay_conditions_summary: pH 6.8; 298.15 K; buffer bis-tris-propane, 50 mM, pH 6

proof_lines:
pH 6.8
Trp-sensitive isozyme, pH 7.0, 25°C
pH 7.0, 37°C, MW 79000 assumed

substrate: Phosphoenolpyruvate; D-Erythrose 4-phosphate; H2O


organism: Saccharomyces cerevisiae

proof_lines:
Tyr-sensitive isozyme, pH 6.8
Phe-sensitive isozyme, pH 6.8, 30°C


organism: Spinacia oleracea

substrate_name: D-erythrose

substrate: D-erythrose


organism: Pseudomonas aeruginosa

proof_lines: synthase-trp isozyme, versus D-erythrose 4-phosphate, 37°C, pH 7.0


organism: Homo sapiens

substrate_name: L-tryptophan

substrate: L-tryptophan


organism: Arabidopsis thaliana

substrate_name: DHA (at pH 6.5 and 30 degrees Celsius)

substrate: DHA (at pH 6.5 and 30 degrees Celsius)


organism: Caenorhabditis elegans


sequence_source: UniProtKB:G3XCJ9 direct accession lookup

proof_lines:
pH 7.5, 37°C, presence of Co2+
Raw SKiD Env: Temp=37°C, pH=7.5


sequence_source: UniProtKB:Q8U0A9 direct accession lookup

proof_lines: pH 6.8, 60°C, cosubstrate 2-deoxy-D-erythrose 4-phosphate

proof_lines: pH 6.8, 60°C, cosubstrate D-erythrose 4-phosphate

proof_lines: pH 6.8, 60°C, cosubstrate 2-deoxy-D-ribose 5-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8U0A9 direct accession lookup and applied mutation signature I181D to reconstruct the assayed variant sequence.


enzyme_display_name: peptidylglycine monooxygenase

organism: Unknown

substrate_name: N-acetylglycine

enzyme: peptidylglycine monooxygenase

substrate: N-acetylglycine


organism: Streptomyces coelicolor

sequence_source: UniProtKB:P80574; PMID:8760910; BRENDA literature 639779


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: D-erythrose 4-phosphate (E4P)

sequence_source: source_record; UniProt O53512 direct check

substrate: D-erythrose 4-phosphate (E4P)


organism: Bos taurus

sequence_source: UniProtKB REST direct accession lookup: P10731


substrate_name: ascorbate

proof_lines: pH 7.75, monomeric enzyme, temperature not specified in the publication

substrate: ascorbate


substrate_name: N-dansyl-Tyr-Val-Gly

sequence_source: UniProtKB REST direct accession lookup: P19021

proof_lines: pH and temperature not specified in the publication

substrate: N-dansyl-Tyr-Val-Gly


organism: Rattus norvegicus

sequence_source: UniProtKB REST direct accession lookup: P14925

proof_lines:
apparent KM
protiated
deuterated


organism: Oryctolagus cuniculus


substrate_name: L-phenylalanine

mutation_signature: recombinant N- and C-terminal truncated enzyme / cofactor tetrahydrobiopterin recombinant N- and C-terminal truncated enzyme

proof_lines: recombinant N- and C-terminal truncated enzyme, cofactor tetrahydrobiopterin

substrate: L-phenylalanine


mutation_signature: recombinant N- and C-terminal truncated enzyme / cofactor 6-methyltetrahydrobipterin recombinant N- and C-terminal truncated enzyme

proof_lines: recombinant N- and C-terminal truncated enzyme, cofactor 6-methyltetrahydrobipterin


substrate_name: tetrahydrobiopterin

mutation_signature: recombinant N- and C-terminal truncated enzyme / substrate tryptophan recombinant N- and C-terminal truncated enzyme

proof_lines: recombinant N- and C-terminal truncated enzyme, substrate tryptophan

substrate: tetrahydrobiopterin


mutation_signature: recombinant N- and C-terminal truncated enzyme / cofactor 6-methyltetrahydropterin recombinant N- and C-terminal truncated enzyme

proof_lines: recombinant N- and C-terminal truncated enzyme, cofactor 6-methyltetrahydropterin


mutation_signature: recombinant N- and C-terminal truncated enzyme / substrate phenylalanine recombinant N- and C-terminal truncated enzyme

proof_lines: recombinant N- and C-terminal truncated enzyme, substrate phenylalanine


substrate_name: dansyl-L-Tyr-L-Val-Gly

proof_lines: mutant enzyme H108A, in100 mM MES pH 5.5, at 37°C

substrate: dansyl-L-Tyr-L-Val-Gly


proof_lines: mutant enzyme M109I, in100 mM MES pH 5.5, at 37°C


proof_lines: mutant enzyme H107A, in100 mM MES pH 5.5, at 37°C


organism: Ovis aries

substrate_name: D-Tyr-Pro-Gly-Gly

proof_lines: assayed without ascorbate and catalase, brain enzyme

proof_lines: assayed with ascorbate and 0.1mg/ml catalase, pituitary enzyme

proof_lines: assayed without ascorbate and catalase, pituitary enzyme

substrate: D-Tyr-Pro-Gly-Gly


substrate_name: N-benzoylglycine

proof_lines: 100 mM MES, pH 5.5, 0.2 mM dansyl-D-Tyr-Val-Gly, 5 microM CuSO4, ascorbate

substrate: N-benzoylglycine


substrate_name: hippuric acid

proof_lines: pH 6.0, 37°C, [1H2]-hippuric acid, mutant Y318F

proof_lines: pH 6.0, 37°C, [2H2]-hippuric acid, mutant Y318F

substrate: hippuric acid


proof_lines:
tryptohan hydroxylase form I
tryptophan hydroxylase form I


organism: Thunnus albacares


substrate_name: N-dansyl-L-Tyr-L-Val-Gly

assay_conditions_summary: pH 6

proof_lines: 100 mM MES/NaOH, pH 6.0, 30 mM NaCl, 1% (v/v) ethanol, 0.001% (v/v) Triton X-100, 1 microM Cu(NO3)2, 10 mg/l catalase, 6 mM ascorbate, 8 microM N-dansyl-Tyr-Val-Gly

substrate: N-dansyl-L-Tyr-L-Val-Gly


organism: Cricetulus griseus

substrate_name: alpha-hydroxyhippuric acid

proof_lines: 0.4 mM ferrocyanide, 100 mM MES pH 6.0, 30 mM KCl, 1 microM CuSO4

proof_lines: 4 mM alpha-hydroxyhippuric acid, 0.21 mM O2, 100 mM MES pH 6.0, 30 mM KCl, 1 microM CuSO4

proof_lines: 40 mM alpha-hydroxyhippuric acid, 0.95 mM O2, 100 mM MES pH 6.0, 30 mM KCl, 1 microM CuSO4

substrate: alpha-hydroxyhippuric acid


proof_lines: pH and temperature not specified in the publication


proof_lines: wild type enzyme, in100 mM MES pH 5.5, at 37°C


organism: Drosophila melanogaster

substrate_name: alpha-N-acetyl-Tyr-Val-Gly

substrate: alpha-N-acetyl-Tyr-Val-Gly


proof_lines: enzyme from pineal gland, cofactor tetrahydrobiopterin


organism: Cavia porcellus

proof_lines: enzyme from crude mitochondrial fraction


proof_lines: F313W mutant, recombinant N-terminal truncated enzyme


mutation_signature: recombinant N-terminal truncated enzyme recombinant N-terminal truncated enzyme


substrate_name: Unknown

mutation_signature: recombinant truncated enzyme recombinant truncated enzyme

substrate: Unknown


organism: Mus musculus


organism: Taiwanofungus camphoratus

substrate_name: dehydroascorbate

substrate: dehydroascorbate


organism: Triticum aestivum


organism: Zea mays

substrate_name: glutathione

proof_lines:
isoform DHAR1, at pH 6.5 and 25°C
isoform DHAR3, at pH 6.5 and 25°C
isoform DHAR4, at pH 6.5 and 25°C

substrate: glutathione


organism: Bacillus subtilis

substrate_name: phosphoenolpyruvate

proof_lines:
pH 7.5, 37°C
at 37°C

substrate: phosphoenolpyruvate


organism: Corynebacterium glutamicum

proof_lines:
recombinant wild-type, 30°C, pH 6.5
wild-type, pH 7.9, 30°C


organism: Cupriavidus necator

substrate_name: D-erythrose 4-phosphate

substrate: D-erythrose 4-phosphate


substrate_name: N-acetyl-Tyr-Val-Gly

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P14925 and applied mutation signature Y79W to reconstruct the assayed variant sequence.

proof_lines: purified recombinant mutant Y79W, pH 7.0

proof_lines: purified recombinant mutant Y79W, pH 5.5

substrate: N-acetyl-Tyr-Val-Gly


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P14925 and applied mutation signature Q170A to reconstruct the assayed variant sequence.

proof_lines: purified recombinant mutant Q170A, pH 5.5

proof_lines: purified recombinant mutant Q170A, pH 7.0


proof_lines: purified recombinant wild-type enzyme, pH 5.5

proof_lines: purified recombinant wild-type enzyme, pH 7.0

proof_lines: pH 6.0, 37°C, [2H2]-hippuric acid, wild-type enzyme


substrate_name: peptidylglycine

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P14925 and applied mutation signature Q170E to reconstruct the assayed variant sequence.

proof_lines: transiently expressed mutant Q170E, pH 5.5

substrate: peptidylglycine


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

proof_lines: transiently expressed mutants Q170A and Y79W, pH 5.5


proof_lines: transiently expressed mutants Q170N and Q170L, pH 5.5


organism: Vigna radiata

substrate_name: D-Erythrose 4-phosphate; Phosphoenolpyruvate; H2O


organism: Aquifex aeolicus


organism: Bacillus anthracis

proof_lines: pH 7.0, temperature not specified in the publication


organism: Delftia acidovorans

proof_lines:
DAHP synthase-tyr, pH 7.0, 37°C
DAHP synthase-phe, pH 7.0, 37°C


organism: Escherichia coli


mutation_signature: N-terminal deletion mutant

proof_lines: N-terminal deletion mutant, 25°C, pH 6.4


organism: Helicobacter pylori

sequence_source: UniProtKB Q9ZMU5, linked by PMID 15853768 / DOI 10.1042/BJ20050259 to H. pylori strain J99 DAH7P synthase

proof_lines: pH 7.5, 30°C, cosubstrate erythrose 4-phosphate

proof_lines: pH 7.5, 30°C, cosubstrate phosphoenolpyruvate


organism: Sus scrofa


organism: Xenopus laevis

substrate_name: N-trinitrophenyl-D-Tyr-Val-Gly

proof_lines:
pH 6.0, 37°C, recombinant enzyme
pH 5.0, 37°C, recombinant enzyme
pH 7.5, 37°C, recombinant enzyme

substrate: N-trinitrophenyl-D-Tyr-Val-Gly


substrate_name: N-dansyl-L-Tyr-L-Phe-Gly

substrate: N-dansyl-L-Tyr-L-Phe-Gly


organism: Spinacia oleracea

substrate_name: GSH

substrate: GSH


substrate_name: Reduced glutathione; Dehydroascorbate

proof_lines: SABIO-RK modifier species: glutathione dehydrogenase (ascorbate)(Enzyme) mutant C25S

proof_lines: glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin), C25S mutant

substrate: Reduced glutathione; Dehydroascorbate


proof_lines: glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)


organism: Kitasatospora aureofaciens


organism: Porphyromonas gingivalis


organism: Pyrococcus furiosus

substrate_name: H2O; D-Erythrose 4-phosphate; Phosphoenolpyruvate


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Streptomyces rimosus


organism: Thermotoga maritima


enzyme_display_name: serine O-acetyltransferase

organism: Arabidopsis thaliana

substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProt REST direct lookup for reviewed accession Q39218 plus local G354A substitution check. and applied mutation signature G354A to reconstruct the assayed variant sequence.

enzyme: serine O-acetyltransferase

substrate: acetyl-CoA


substrate_name: L-Serine

substrate: L-Serine


substrate_name: Acetyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: Acetyl-CoA


organism: Haemophilus influenzae

substrate_name: Coenzyme A

sequence_source: UniProtKB P43886 direct REST lookup.

assay_conditions_summary: pH 6.5; 298.15 K; cofactor CoA

substrate: Coenzyme A


sequence_source: UniProtKB:P0A9D4 direct accession lookup


sequence_source: UniProtKB Q42588 reviewed entry SAT1_ARATH; direct accession lookup on 2026-06-06.


substrate_name: L-serine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P43886; row-specific variant reconstructed from canonical sequence and mutation signature and applied mutation signature H189N to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor CoA

substrate: L-serine


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJY9; row-specific variant reconstructed from canonical sequence and mutation signature and applied mutation signature A59G to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, serine O-acetyltransferase activity, mutant enzyme A59G


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJY9; row-specific variant reconstructed from canonical sequence and mutation signature and applied mutation signature A59G/G62P to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, serine O-acetyltransferase activity, mutant enzyme A59G/G62P


proof_lines: pH 7.5, 25°C, serine O-acetyltransferase activity, wild-type enzyme


sequence_source: UniProt REST direct lookup: P0A9D4/P0A9D5/P0A9D6

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


substrate_name: L-Ser (at pH 8 and 30 degrees Celsius); acetyl-CoA (at pH 8 and 30 degrees Celsius)

assay_conditions_summary: pH 8; cofactor CoA


substrate: L-Ser (at pH 8 and 30 degrees Celsius); acetyl-CoA (at pH 8 and 30 degrees Celsius)


substrate_name: L-Ser (at pH 8 and 37 degrees Celsius); acetyl-CoA (at pH 8 and 37 degrees Celsius)


substrate: L-Ser (at pH 8 and 37 degrees Celsius); acetyl-CoA (at pH 8 and 37 degrees Celsius)


organism: Lacticaseibacillus casei

substrate_name: L-serine; acetyl-CoA

substrate: L-serine; acetyl-CoA


enzyme_display_name: L-serine/homoserine O-acetyltransferase

organism: Streptomyces lavendulae

sequence_source: UniProtKB:D2Z028 direct lookup

assay_conditions_summary: pH 8; 303.15 K; buffer 60 mM Tris-HCl; cofactor CoA

column_label: Table 2 (Kinetic parameters of DcsE and its mutants). Enzyme row 'Wild type'. The table splits into two substrate column groups headed 'L-Serine' and 'L-Homoserine'; this record reads the 'L-Serine' group. Inside that group the printed column heads are 'Km (mM)' = 4.9, 'kcat (min^-1)' = 95 and 'kcat/Km (min^-1 mM^-1)' = 19. The final 'Specificity' column of the table is the ratio of the two kcat/Km cells of the row (table footnote b) and belongs to neither substrate group.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.9 mM; the printed unit is already mM, so no unit conversion applies, giving 4.9 mM. kcat: printed Table 2 cell 95 min^-1; one min^-1 is 1/60 s^-1, so 95 / 60 = 1.5833333333333333 s^(-1). kcat/Km: printed Table 2 cell 19 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 19 / 60 = 0.31666666666666665 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Enzyme row 'Wild type', L-Serine column group: Km (mM) = 4.9; kcat (min^-1) = 95; kcat/Km (min^-1 mM^-1) = 19.

row_label: Table 2, Enzyme row 'Wild type', L-Serine column group (Km, kcat and kcat/Km columns for L-Serine)

table_label: Table 2: Kinetic parameters of DcsE and its mutants (Journal of Bacteriology 2013, 195(8):1741-1749)

enzyme: L-serine/homoserine O-acetyltransferase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D2Z028 and applied mutation signature P55G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of DcsE and its mutants). Enzyme row 'P55G'. The table splits into two substrate column groups headed 'L-Serine' and 'L-Homoserine'; this record reads the 'L-Serine' group. Inside that group the printed column heads are 'Km (mM)' = 0.50, 'kcat (min^-1)' = 37 and 'kcat/Km (min^-1 mM^-1)' = 74. The final 'Specificity' column of the table is the ratio of the two kcat/Km cells of the row (table footnote b) and belongs to neither substrate group.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.50 mM; the printed unit is already mM, so no unit conversion applies, giving 0.5 mM. kcat: printed Table 2 cell 37 min^-1; one min^-1 is 1/60 s^-1, so 37 / 60 = 0.6166666666666667 s^(-1). kcat/Km: printed Table 2 cell 74 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 74 / 60 = 1.2333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Enzyme row 'P55G', L-Serine column group: Km (mM) = 0.50; kcat (min^-1) = 37; kcat/Km (min^-1 mM^-1) = 74.

row_label: Table 2, Enzyme row 'P55G', L-Serine column group (Km, kcat and kcat/Km columns for L-Serine)


organism: Rattus norvegicus

proof_lines: kcat is 15 sec(-1) with Ac-Tyr-Val-Gly peptide as substrate.


substrate_name: L-serine (at 30 degrees Celsius and pH 8)

assay_conditions_summary: pH 8

proof_lines: kcat is 95 min(-1) and 88 min(-1) for L-serine and L-homoserine, respectively (at 30 degrees Celsius and pH 8).


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

substrate_name: L-serine as isolated subunit

substrate: L-serine as isolated subunit


organism: Allium cepa

substrate_name: acetyl-CoA; L-serine

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

substrate: acetyl-CoA; L-serine


organism: Entamoeba histolytica

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

proof_lines: 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C

proof_lines: 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C

proof_lines: competitive inhibition with L-serine but no inhibition with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 25°C


organism: Escherichia coli

substrate_name: L-Threonine; Acetyl-CoA; L-Serine; Propanoyl-CoA

source_db: sabio_rk; brenda

source: sabio_rk; brenda


organism: Glycine max

substrate_name: acetyl-CoA; L-Ser

proof_lines:
pH 8.0
versus acetyl-CoA
versus L-Ser

substrate: acetyl-CoA; L-Ser


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from UniProtKB P11998 FASTA plus PubMed 12581640/UniProt mutagenesis reference; variant sequence reconstructed during review when mutation_signature is present. and applied mutation signature A56S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P11998 FASTA plus PubMed 12581640/UniProt mutagenesis reference; variant sequence reconstructed during review when mutation_signature is present. and applied mutation signature D138A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P11998 FASTA plus PubMed 12581640/UniProt mutagenesis reference; variant sequence reconstructed during review when mutation_signature is present. and applied mutation signature F57S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P11998 FASTA plus PubMed 12581640/UniProt mutagenesis reference; variant sequence reconstructed during review when mutation_signature is present. and applied mutation signature F22V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P11998 FASTA plus PubMed 12581640/UniProt mutagenesis reference; variant sequence reconstructed during review when mutation_signature is present. and applied mutation signature F22S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P11998 FASTA plus PubMed 12581640/UniProt mutagenesis reference; variant sequence reconstructed during review when mutation_signature is present.


sequence_variant_note: Resolved canonical sequence from UniProtKB P11998 FASTA plus direct H88K reconstruction from selected mutation_signature and applied mutation signature H88K to reconstruct the assayed variant sequence.


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


substrate_name: L-3,4-dihydroxybutan-2-one 4-phosphate

assay_conditions_summary: pH 7; 310.15 K; buffer pH 7

proof_lines:
hollow beta60 capsid, pH 7.0, 37°C
native enzyme complex, pH 7.0, 37°C
pH 7.0, 37°C, phosphate buffer

substrate: L-3,4-dihydroxybutan-2-one 4-phosphate


organism: Brucella melitensis


organism: Brucella sp.


organism: Candida albicans

substrate_name: Unknown

substrate: Unknown


proof_lines: pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione


organism: Pyricularia grisea


organism: Saccharomyces cerevisiae


organism: Schizosaccharomyces pombe

assay_conditions_summary: pH 7; 300.15 K; buffer pH 7

proof_lines:
pH 7.0, 27°C
pH 7.0, 37°C, phosphate buffer
pH 7.0, 37°C


organism: Spinacia oleracea

sequence_source: UniProtKB reviewed accession Q9XH32 from direct EC 2.5.1.78 + Spinacia oleracea lookup; entry cites PMID 10419541.


organism: Labeo rohita


organism: Lachancea kluyveri

substrate_name: L-alanine

proof_lines: pH and temperature not specified in the publication

substrate: L-alanine


organism: Leptosphaeria michotii


organism: Medicago truncatula

proof_lines:
isoform AlaAT2, pH 8.0, 20°C
isoform AlaAT1, pH 8.0, 20°C


organism: Mustela vison

substrate_name: 2-Oxoglutarate; L-Alanine

substrate: 2-Oxoglutarate; L-Alanine


organism: Oryctolagus cuniculus

proof_lines: pH 8.8, 37°C, cosubstrate 2-oxoglutarate


organism: Oryza sativa

substrate_name: pyruvate

proof_lines:
cofactor: L-glutamate, 25°C, pH 8.0
cofactor: pyruvate, 25°C, pH 8.0
cofactor: L-alanine, 25°C, pH 8.0

substrate: pyruvate


organism: Panicum miliaceum


organism: Pseudomonas putida


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.1 M phosphate

proof_lines: 200 mM L-alanine and 2 mM 2-oxoglutarate in 0.1 M phosphate buffer, pH 7.4, at 37°C


organism: Rhodopseudomonas palustris

proof_lines:
cofactor: L-alanine, 25°C, pH 8.0
cofactor: 2-oxoglutarate, 25°C, pH 8.0
cofactor: L-glutamate, 25°C, pH 8.0


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P11998 using selected mutation signature and applied mutation signature F22W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P11998 using selected mutation signature and applied mutation signature T80V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P11998 using selected mutation signature and applied mutation signature S142L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P11998 using selected mutation signature and applied mutation signature F113S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P11998 using selected mutation signature and applied mutation signature E58Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P11998 using selected mutation signature and applied mutation signature N23S to reconstruct the assayed variant sequence.


organism: Triticum aestivum

proof_lines: AlaAT2, cosubstrate: L-alanine, pH 7.3, 25°C

proof_lines: AlaAT2, cosubstrate: 2-oxoglutarate, pH 7.3, 25°C

proof_lines: AlaAT2, cosubstrate: L-glutamate, pH 7.3, 25°C


organism: Zea mays


enzyme_display_name: adenosylhomocysteine nucleosidase

organism: Helicobacter pylori

substrate_name: S-adenosyl-L-homocysteine

assay_conditions_summary: pH 7.2; 310.15 K; buffer 100 mM HEPES and 50 mM KCl

proof_lines: wild type enzyme, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C

substrate: S-adenosyl-L-homocysteine


proof_lines: mutant enzyme H109A, in 100 mM HEPES and 50 mM KCl buffer (pH 7.2), at 37°C


organism: Klebsiella pneumoniae


organism: Neisseria meningitidis


organism: Saccharomyces cerevisiae

proof_lines:
at pH 7.5 and 25°C
cofactor: L-glutamate, 25°C, pH 8.0
cofactor: pyruvate, 25°C, pH 8.0


organism: Sagmatias obliquidens


organism: Schistocerca gregaria


organism: Solanum lycopersicum


organism: Sus scrofa

proof_lines: pH 7.8, 30°C, mitochondrial alanine aminotransferase


organism: Trichoderma viride

substrate_name: DL-alanine

substrate: DL-alanine


organism: Rattus rattus


organism: Streptococcus pneumoniae


organism: Vibrio cholerae serotype O1

assay_conditions_summary: pH 7.5; 298.15 K; buffer 100 mM HEPES

proof_lines: at 25°C, in 100 mM HEPES, pH 7.5, and 50 mM KCl

proof_lines: at 25°C, in 100 mM HEPES buffer, pH 7.5, 50 mM KCl

proof_lines: at 25°C, in 50 mM phosphate buffer, pH 7.9, and 10 mM KCl


enzyme_display_name: soluble epoxide hydrolase

organism: Agrobacterium tumefaciens

enzyme: soluble epoxide hydrolase


substrate_name: (R)-styrene oxide

substrate: (R)-styrene oxide


organism: Gallus gallus

substrate_name: (3-phenyl-oxiranyl)-acetic acid cyano-(6-methoxy-naphthalen-2-yl)-methyl ester


organism: Glycine max

proof_lines:
soluble enzyme
microsomal enzyme


organism: Homo sapiens

substrate_name: trans-2-Methylstyrene 7,8-oxide; H2O

proof_lines:
pH 7.4, 37°C
30°C
microsomal enzyme

substrate: trans-2-Methylstyrene 7,8-oxide; H2O


organism: Mus musculus

proof_lines:
30°C
pH 7.4, 25°C
enzyme from untreated animals


organism: Oryctolagus cuniculus

substrate_name: styrene oxide

substrate: styrene oxide


organism: Rattus norvegicus

substrate_name: trans-stilbene oxide

proof_lines:
native enzyme
pH 7.4, 37°C
30°C

substrate: trans-stilbene oxide


organism: Arabidopsis thaliana


organism: Aspergillus niger

substrate_name: (S)-4-nitrostyrene oxide

substrate: (S)-4-nitrostyrene oxide


organism: Brassica napus


organism: Cavia porcellus


sequence_variant_note: Resolved canonical sequence from UniProt P80299 reviewed rat soluble epoxide hydrolase plus H332Q reconstruction from PMID 8626766 mutagenesis evidence and applied mutation signature H332Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P80299 reviewed rat soluble epoxide hydrolase plus W540L reconstruction from PMID 8626766 mutagenesis evidence and applied mutation signature W540L to reconstruct the assayed variant sequence.


organism: Solanum tuberosum

proof_lines: pH 7.4, 37°C, recombinant enzyme, noncompetitive inhibition type


organism: Vibrio vulnificus

substrate_name: 3-Phenyl-cyano(6-methoxy-2-naphthalenyl)methyl ester-2-oxiraneacetic acid; H2O


organism: Xenopus laevis

substrate_name: 3-phenyl-cyano(6-methoxy-2-naphthalenyl)methyl ester 2-oxiraneacetic acid

sequence_source: UniProt Q6DCH2 Xenopus laevis bifunctional epoxide hydrolase 2, nucleotide-sequence reference PMID 24681163

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


enzyme_display_name: bacterial leucyl aminopeptidase

organism: Aeromonas caviae

substrate_name: Val-beta-naphthylamide

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

enzyme: bacterial leucyl aminopeptidase

substrate: Val-beta-naphthylamide


organism: Brevibacterium linens

proof_lines:
pH 8.5, 45°C, API
pH 8.0, 37°C, APII


organism: Escherichia coli


organism: Fasciola hepatica

assay_conditions_summary: pH 8.5; 310.15 K; buffer 0.1 M glycine

proof_lines: recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C

proof_lines: recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C


organism: Geobacillus kaustophilus

proof_lines: pH 8.0, 55°C, recombinant wild-type enzyme


organism: Geobacillus stearothermophilus

assay_conditions_summary: pH 8; 333.15 K; buffer 25 mM Tris-HCl

proof_lines: mutant enzyme D380E, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C


proof_lines: wild type enzyme, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P24828 plus PMID:18286359 mutation label; residue 352 was checked as Y before substitution. and applied mutation signature Y352D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y352D, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P24828 plus PMID:18286359 mutation label; residue 352 was checked as Y before substitution. and applied mutation signature Y352L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y352L, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P24828 plus PMID:18286359 mutation label; residue 380 was checked as D before substitution. and applied mutation signature D380N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D380N, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P24828 plus PMID:18286359 mutation label; residue 380 was checked as D before substitution. and applied mutation signature D380V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D380V, in 25 mM Tris-HCl buffer, pH 8.0, at 60°C


organism: Geobacillus thermoleovorans


organism: Streptomyces septatus

substrate_name: L-cystinyl-p-nitroanilide

proof_lines: mutant enzyme D198I/F221W, at pH 8.0 and 37°C

substrate: L-cystinyl-p-nitroanilide


substrate_name: L-Arg-p-nitroanilide

proof_lines: mutant enzyme D198P/F221E, at pH 8.0 and 37°C

substrate: L-Arg-p-nitroanilide


substrate_name: L-Leu-p-nitroanilide

proof_lines: mutant enzyme D198F/F221I, at pH 8.0 and 37°C

substrate: L-Leu-p-nitroanilide


organism: Treponema denticola

sequence_source: UniProtKB Q73QZ3 direct lookup; reviewed Treponema denticola strain ATCC 35405 PepA sequence with leucine aminopeptidase alternative EC 3.4.11.10.

proof_lines:
recombinant enzyme, at pH 7.3
recombinant enzyme, at pH 8.0
native enzyme, at pH 7.3


organism: Vibrio proteolyticus

substrate_name: L-leucine 4-nitroanilide

sequence_source: UniProtKB Q01693 direct lookup; reviewed Vibrio proteolyticus bacterial leucyl aminopeptidase, EC 3.4.11.10.

assay_conditions_summary: pH 8; 298.15 K; buffer dependent

proof_lines: pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound

proof_lines: pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound

substrate: L-leucine 4-nitroanilide


enzyme_display_name: membrane alanyl aminopeptidase

organism: Bombyx mori

enzyme: membrane alanyl aminopeptidase


organism: Bos taurus

substrate_name: Unknown


organism: Cucumis sativus


organism: Homo sapiens

proof_lines: Ala-, Met-, Tyr-, Leu-, Phe-, Arg-, Lys-, Gly-derivatives


organism: Hordeum vulgare


organism: Spodoptera litura


organism: Streptococcus salivarius

substrate_name: Lys-4-methylcoumarin 7-amide

substrate: Lys-4-methylcoumarin 7-amide


organism: Streptomyces sp.

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


organism: Sus scrofa

proof_lines: recombinant wild-type enzyme, pH 7.4, 35°C

substrate: Unknown


substrate_name: VVYPWTQRF

proof_lines: Km is pH-dependent between pH 6 and pH 9, maximum affinity at pH 7.0-7.3

substrate: VVYPWTQRF


enzyme_display_name: Xaa-Pro aminopeptidase

substrate_name: Arg-Pro-Pro

enzyme: Xaa-Pro aminopeptidase

substrate: Arg-Pro-Pro


organism: Mizuhopecten yessoensis


organism: Neisseria meningitidis

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, value higher than
pH 7.5, 37°C, value above


organism: Novosphingobium capsulatum


organism: Oryctolagus cuniculus


organism: Plasmodium falciparum

proof_lines: pH and temperature not specified in the publication


organism: Rattus norvegicus

proof_lines:
from brain
from kidney
pH 7.4, 35°C


organism: Escherichia coli

substrate_name: bradykinin

substrate: bradykinin


organism: Caenorhabditis elegans

sequence_source: UniProtKB reviewed O44750 direct EC+organism lookup; entry cites PMID 11606206 and ORF W03G9.4


organism: Cavia porcellus

substrate_name: Arg-Pro-Pro-benzylamide

substrate: Arg-Pro-Pro-benzylamide


proof_lines: wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C


organism: Lactococcus lactis

substrate_name: Leu-Pro-Pro

substrate: Leu-Pro-Pro


organism: Lactococcus lactis subsp. lactis

substrate_name: L-Ile-L-Pro-L-Pro

assay_conditions_summary: pH 7

proof_lines: pH 7, temperature not specified in the publication

substrate: L-Ile-L-Pro-L-Pro


sequence_source: UniProtKB:A0A144A2H0 via direct EC 3.4.11.9 + Plasmodium falciparum lookup


substrate_name: Arg-Pro-Pro-Gly-Phe

sequence_source: UniProtKB:Q99MA2; PubMed 7669781 membrane-bound rat lung aminopeptidase P context

proof_lines:
in presence of 4 mM Mn2+
without 4 mM Mn2+
without Mn2+

substrate: Arg-Pro-Pro-Gly-Phe


organism: Streptomyces lavendulae

sequence_source: UniProtKB:M4MBM1 / EMBL KC292272 / NCBI protein AGG68151.1

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


organism: Streptomyces lividans

proof_lines:
recombinant enzyme, pH 7.4, 30°C
chimera th-sl cAPP, pH 7.0, 30°C
chimera sl-th cAPP, pH 8.2, 30°C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q95333 using selected mutation H519K and applied mutation signature H519K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q95333 using selected mutation H519L and applied mutation signature H519L to reconstruct the assayed variant sequence.


enzyme_display_name: Xaa-Pro dipeptidase

organism: Macaca radiata

substrate_name: Gly-L-Pro; Pro-Hyp; Gly-Hyp

enzyme: Xaa-Pro dipeptidase

substrate: Gly-L-Pro; Pro-Hyp; Gly-Hyp


organism: Neurospora crassa

substrate_name: L-Val-L-Pro; Gly-L-Pro; Met-Pro

substrate: L-Val-L-Pro; Gly-L-Pro; Met-Pro


organism: Pyrococcus furiosus

substrate_name: Met-Pro

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P81535 using selected mutation G39E and applied mutation signature G39E to reconstruct the assayed variant sequence.

proof_lines:
pH 7.0, 100°C, recombinant mutant G39E
pH 7.0, 35°C, recombinant mutant G39E
pH 7.0, 70°C, recombinant mutant G39E

substrate: Met-Pro


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P81535 using selected mutation R19G/G39E/K71E/S229T and applied mutation signature R19G/G39E/K71E/S229T to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 35°C, recombinant mutant R19G/G39E/K71E/S229T

proof_lines: pH 7.0, 70°C, recombinant mutant R19G/G39E/K71E/S229T

proof_lines: pH 7.0, 100°C, recombinant mutant R19G/G39E/K71E/S229T


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P81535 using selected mutation R19G/K71E/S229T and applied mutation signature R19G/K71E/S229T to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 35°C, recombinant mutant R19G/K71E/S229T

proof_lines: pH 7.0, 70°C, recombinant mutant R19G/K71E/S229T

proof_lines: pH 7.0, 100°C, recombinant mutant R19G/K71E/S229T


sequence_source: UniProtKB:P81535 via direct EC 3.4.13.9 + Pyrococcus furiosus lookup and RCSB 1PV9 cross-check

proof_lines: pH 7.0, 70°C, recombinant wild-type enzyme

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

proof_lines: pH 7.0, 100°C, recombinant wild-type enzyme


organism: Homo sapiens

substrate_name: Ala-Pro

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

proof_lines: pH 7.8, 37°C, recombinant His-tagged mutant H859A

substrate: Ala-Pro


proof_lines: pH 7.8, 37°C, recombinant His-tagged mutant Y844A


substrate_name: Gly-Pro

assay_conditions_summary: pH 7.8; 310.15 K; buffer 30 mM phosphate

proof_lines: pH 7.8, 37°C, presence of 20 mM D-valine, prolidase I

proof_lines: pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine

substrate: Gly-Pro


organism: Lacticaseibacillus casei

substrate_name: Leu-Pro

substrate: Leu-Pro


organism: Lactobacillus delbrueckii


organism: Lactococcus cremoris

substrate_name: Val-Pro

substrate: Val-Pro


organism: Sus scrofa

sequence_source: UniProtKB reviewed accession Q95333 (XPP2_PIG), matched by Sus scrofa, EC 3.4.11.9, membrane-bound aminopeptidase P, kidney/membrane context, and bradykinin AP-P function.


substrate_name: Gly-Pro-Hyp

sequence_source: UniProtKB reviewed accession Q95333 (XPP2_PIG), matched by Sus scrofa, EC 3.4.11.9, pig kidney membrane-bound AP-P context, and Gly-Pro-Hyp substrate context.

substrate: Gly-Pro-Hyp


organism: Trichinella spiralis

sequence_source: GenBank protein EFV57850.1 from the PMID 36089006 TsAPP source paper; sequence also matches UniProtKB TrEMBL E5SBI8.

proof_lines: pH and temperature not specified in the publication


organism: Aspergillus phoenicis


organism: Bos taurus

substrate_name: L-Val-L-Pro

substrate: L-Val-L-Pro


substrate_name: L-Met-L-Pro

substrate: L-Met-L-Pro


enzyme_display_name: pepsin A

organism: Micropterus salmoides

substrate_name: Substance P

proof_lines:
isoform PG1-1, at pH 3.0 and 37°C
isoform PG2-2, at pH 3.0 and 37°C

enzyme: pepsin A

substrate: Substance P


organism: Monopterus albus

substrate_name: hemoglobin

assay_conditions_summary: pH 3; 310.15 K; buffer sodium acetate

proof_lines: isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C

substrate: hemoglobin


organism: Oncorhynchus mykiss

substrate_name: Acid-denatured hemoglobin

proof_lines:
isoform P-III, at pH 2.0 and 37°C
isoform P-I, at pH 2.0 and 37°C
isoform P-II, at pH 2.0 and 37°C

substrate: Acid-denatured hemoglobin


organism: Ovis aries

substrate_name: N,N-dimethylcasein

substrate: N,N-dimethylcasein


organism: Saurida micropectoralis

proof_lines:
pepsinogen III, pH 2.0, 40°C
pepsinogen II, pH 2.0, 40°C
pepsinogen I, pH 2.0, 40°C


proof_lines:
pH 2.1, 37°C, mutant enzyme G76A
pH 3.95, 37°C, mutant enzyme G76A


substrate_name: Phe-Pro

sequence_source: UniProtKB:P81535 direct EC+organism lookup; UniProt reference list links P81535 to PMID 9733678.

proof_lines:
native prolidase
recombinant prolidase

substrate: Phe-Pro


enzyme_display_name: angiotensin-converting enzyme 2

substrate_name: angiotensin I

sequence_source: UniProtKB:Q9BYF1 direct EC+organism lookup for human ACE2.

enzyme: angiotensin-converting enzyme 2

substrate: angiotensin I


organism: Albatrossia pectoralis


organism: Gallus gallus

substrate_name: casein

proof_lines: A B

substrate: casein


assay_conditions_summary: pH 4; 310.15 K; buffer 0.2 M sodium formate

proof_lines: in 0.2 M sodium formate buffer, pH 4.0, at 37°C


proof_lines:
pH 3.5, 25°C, wild-type enzyme
pH 3.95, 37°C, wild-type enzyme
wild-type, pH 2.0


proof_lines: pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M


proof_lines: pH 3.95, 37°C, mutant enzyme L10M/T12A/E13S


proof_lines:
pH 2.1, 37°C, mutant enzyme G76V
pH 3.95, 37°C, mutant enzyme G76V


proof_lines:
pH 3.95, 37°C, mutant enzyme G76S
pH 2.1, 37°C, mutant enzyme G76S


proof_lines: pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M


proof_lines: pH 3.95, 37°C, mutant enzyme G2S/D3Y/L10M/T12A/E13S


proof_lines: pH 3.95, 37°C, mutant enzyme DELTA240-246/+GD


assay_conditions_summary: pH 2

proof_lines: unglycosylated mutant E244N/V246T, pH 2.0


proof_lines:
glycosylated mutant T77N, pH 2.0
unglycosylated mutant T77N, pH 2.0


proof_lines: unglycosylated mutant S110N/L112T, pH 2.0


organism: Lactococcus lactis

substrate_name: L-Leu-L-Pro

proof_lines: mutant enzyme R293S/S307G, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C

substrate: L-Leu-L-Pro


proof_lines: mutant enzyme R293S, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines: mutant enzyme S307G, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines: mutant enzyme S307R, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines: wild type enzyme, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines: mutant enzyme S307D, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines:
unglycosylated mutant S281N, pH 2.0
glycosylated mutant S281N, pH 2.0


proof_lines: in 0.2 M sodium formate buffer, pH 4.0, at 37°C


proof_lines:
T77D/G78(S)S79 double mutant
T77D mutant


organism: Alcaligenes sp.

substrate_name: N-formyl-D-aspartate

substrate: N-formyl-D-aspartate


organism: Aspergillus melleus

substrate_name: N-acetyl-L-methionine

proof_lines: pH 8.0, 40°C, immobilized, cross-linked enzyme-bovine serum albumin aggregate

substrate: N-acetyl-L-methionine


organism: Bacillus sp. (in: firmicutes)

proof_lines:
addition of 0.2 mM Co2+
addition of 0.2 mM Mn2+


organism: Corynebacterium striatum


organism: Mycobacterium sp.

substrate_name: palmitoylaspartate

substrate: palmitoylaspartate


organism: Pseudomonas sp. AK2

substrate_name: N-acetyl-L-pipecolic acid

proof_lines: pH and temperature not specified in the publication

substrate: N-acetyl-L-pipecolic acid


organism: Rattus norvegicus

substrate_name: N-acetylmethionine

substrate: N-acetylmethionine


organism: Stenotrophomonas maltophilia

substrate_name: N-acetyl-DL-aspartate

substrate: N-acetyl-DL-aspartate


organism: Streptomyces ambofaciens

substrate_name: lauric acid

substrate: lauric acid


organism: Sus scrofa

substrate_name: N-isopentanoyl-L-methionine

assay_conditions_summary: buffer hydrolysis in D2O

proof_lines: kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1

proof_lines: kcat for the hydrolysis of N-acetyl-L-glutamate substrates by pAcy1

proof_lines: hydrolysis of N-acyl-L-methionine substrates by pAcy1

substrate: N-isopentanoyl-L-methionine


organism: Homo sapiens

substrate_name: Nalpha-acetylmethionine

substrate: Nalpha-acetylmethionine


substrate_name: N-alpha-acetyl-L-phenylalanine

substrate: N-alpha-acetyl-L-phenylalanine


organism: Mus musculus

substrate_name: N-acetyl-L-aspartate

proof_lines: E167R mutant protein, pH not specified in the publication, temperature not specified in the publication

substrate: N-acetyl-L-aspartate