substrate_name: N-Acetylneuraminate 9-phosphate; H2O

sequence_source: UniProtKB:Q8TBE9 exact accession lookup on 2026-06-24

substrate: N-Acetylneuraminate 9-phosphate; H2O


organism: Rattus norvegicus

substrate_name: H2O; N-Acetylneuraminate 9-phosphate

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

sequence_source: UniProtKB:Q5M969 exact accession lookup on 2026-06-24

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

substrate: H2O; N-Acetylneuraminate 9-phosphate


enzyme_display_name: baicalin-beta-D-glucuronidase

organism: Scutellaria baicalensis

source_db: brenda

source_license: CC BY 4.0

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9LRC8 exact accession lookup on 2026-06-24 and applied mutation signature E329A to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: baicalin-beta-D-glucuronidase

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9LRC8 exact accession lookup on 2026-06-24 and applied mutation signature Y281A to reconstruct the assayed variant sequence.


source_db: oed

verification_status: unverified

sequence_source: UniProtKB:Q9LRC8 exact accession lookup on 2026-06-24

data_origin: experimental

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9LRC8 exact accession lookup on 2026-06-24 and applied mutation signature E212A to reconstruct the assayed variant sequence.


kcat_over_km_origin: calculated


enzyme_display_name: protodioscin 26-O-beta-D-glucosidase

organism: Hellenia speciosa

substrate_name: protogracillin

sequence_source: UniProtKB:Q42707 exact accession lookup on 2026-06-24

enzyme: protodioscin 26-O-beta-D-glucosidase

substrate: protogracillin


organism: Solanum torvum

substrate_name: 4-nitrophenyl beta-D-glucoside

sequence_source: UniProtKB:P0DKH4 exact accession lookup on 2026-06-24

substrate: 4-nitrophenyl beta-D-glucoside


substrate_name: torvoside A

substrate: torvoside A


proof_lines: recombinant His-tagged enzyme, pH 5.0, 37°C


enzyme_display_name: glycolaldehyde dehydrogenase

organism: Escherichia coli

substrate_name: NADPH

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

assay_conditions_summary: cofactor NADP+

proof_lines:
isozyme B
isozyme C
isozyme A

enzyme: glycolaldehyde dehydrogenase

substrate: NADPH


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

proof_lines: isozyme A from vitamin B6 auxotroph mutant strain WG3


enzyme_display_name: acetyl-CoA carboxytransferase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetyl-CoA (in the presence of alpha3 subunit)

source_db: uniprot

assay_conditions_summary: cofactor CoA

enzyme: acetyl-CoA carboxytransferase

source: uniprot


substrate: acetyl-CoA (in the presence of alpha3 subunit)


organism: Pisum sativum

substrate_name: Unknown

km_display: Not reported

substrate: Unknown


enzyme_display_name: sphingosine N-acyltransferase

organism: Homo sapiens

substrate_name: sphinganine

enzyme: sphingosine N-acyltransferase

substrate: sphinganine


substrate_name: sphinganine (with octadecanoyl-CoA as substrate)


organism: Mus musculus


substrate_name: acetyl-CoA

assay_conditions_summary: cofactor NADPH

substrate: acetyl-CoA


substrate_name: malonyl-CoA

substrate: malonyl-CoA


enzyme_display_name: lactose synthase

organism: Bos taurus

substrate_name: UDP-galactose

enzyme: lactose synthase

substrate: UDP-galactose


substrate_name: GlcNAc-B-S-pNP

substrate: GlcNAc-B-S-pNP


substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


enzyme_display_name: glycine transaminase

organism: Arabidopsis thaliana

substrate_name: glutamate

enzyme: glycine transaminase

substrate: glutamate


substrate_name: aminoadipate

substrate: aminoadipate


substrate_name: L-kynurenine

substrate: L-kynurenine


enzyme_display_name: serine--pyruvate transaminase

substrate_name: L-alanine (with the His-AGXT construct)

enzyme: serine--pyruvate transaminase

substrate: L-alanine (with the His-AGXT construct)


enzyme_display_name: purine nucleosidase

organism: Trypanosoma vivax

substrate_name: guanosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9GPQ4 direct REST accession lookup, 2026-06-24 and applied mutation signature L250P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM potassium phosphate

proof_lines: mutant enzyme L250P, in 50 mM potassium phosphate buffer, at 25°C and pH 7.0

enzyme: purine nucleosidase

substrate: guanosine


organism: Zea mays

substrate_name: Xanthosine

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

proof_lines:
pH 7.5, 30°C, recombinant enzyme
Raw SKiD Env: Temp=30°C, pH=7.5

source_databases_merged: brenda skid

substrate: Xanthosine


substrate_name: adenosine 5'-phosphoramidate

sequence_source: UniProtKB:A0A2H1ZE58 direct REST accession lookup, 2026-06-24

substrate: adenosine 5'-phosphoramidate


sequence_source: UniProtKB:Q7Z2E3 direct REST accession lookup, 2026-06-24


proof_lines: nicked DNA substrate, pH 7.5, 25-37°C, recombinant His-tagged wild-type enzyme

proof_lines: blunt DNA substrate, pH 7.5, 25-37°C, recombinant His-tagged wild-type enzyme


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:Q08702 direct REST accession lookup, 2026-06-24


enzyme_display_name: 2-oxo-3-hexenedioate decarboxylase

organism: Pseudomonas putida

sequence_source: UniProtKB:Q1XGK3 direct REST accession lookup, 2026-06-24

enzyme: 2-oxo-3-hexenedioate decarboxylase


organism: Candida albicans

substrate_name: D-Ribulose 5-phosphate

sequence_source: UniProtKB:Q5A3V6 direct REST accession lookup, 2026-06-24

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

proof_lines: SABIO-RK modifier species: 3,4-dihydroxy-2-butanone-4-phosphate synthase(Enzyme) mutant C87A

substrate: D-Ribulose 5-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5A3V6 direct REST accession lookup, 2026-06-24 and applied mutation signature C59A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3,4-dihydroxy-2-butanone-4-phosphate synthase(Enzyme) mutant C59A


organism: Methanocaldococcus jannaschii

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q60364 direct REST accession lookup, 2026-06-24 and applied mutation signature H147S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3,4-dihydroxy-2-butanone-4-phosphate synthase(Enzyme) mutant H147S


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q60364 direct REST accession lookup, 2026-06-24 and applied mutation signature D23S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3,4-dihydroxy-2-butanone-4-phosphate synthase(Enzyme) mutant D23S


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q60364 direct REST accession lookup, 2026-06-24 and applied mutation signature D118S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3,4-dihydroxy-2-butanone-4-phosphate synthase(Enzyme) mutant D118S


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


organism: Escherichia coli (strain K12)

substrate_name: CTP

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

substrate: CTP


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: C55-P (at pH 8 and at 65 degrees Celsius)

assay_conditions_summary: pH 8


organism: Cricetulus griseus

substrate_name: CDP-diacylglycerol

substrate: CDP-diacylglycerol


enzyme_display_name: aryl-sulfate sulfotransferase

organism: Lelliottia amnigena

substrate_name: p-nitrophenyl sulfate

enzyme: aryl-sulfate sulfotransferase

substrate: p-nitrophenyl sulfate


substrate_name: N-acetylneuraminate 9-P

substrate: N-acetylneuraminate 9-P


organism: Hellenia speciosa

substrate_name: protogracillin

substrate: protogracillin


enzyme_display_name: hyaluronoglucosaminidase

organism: Bothrops atrox

substrate_name: hyaluronic acid

enzyme: hyaluronoglucosaminidase

substrate: hyaluronic acid


organism: Homo sapiens

substrate_name: AppppA

substrate: AppppA


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)


organism: Uncultured bacterium HF130_AEPn_1

proof_lines: kcat is 11 min(-1) for (R)-2-amino-1-hydroxyethylphosphonic acid as substrate. kcat is 7 min(-1) for (R,R)-2-amino-1-hydroxypropylphosphonic acid as substrate.


organism: Pseudomonas aeruginosa (strain UCBPP-PA14)

proof_lines: kcat is 1.2 min(-1) for hydroxylation with oxygen (at 37 degrees Celsius). kcat is 2.7 min(-1) for hydroxylation with 2-heptyl-4-quinolone (at 37 degrees Celsius). kcat is 3.2 min(-1) for hydroxylation with NADH (at 37 degrees Celsius). kca


enzyme_display_name: cholesterol 24-hydroxylase

proof_lines: kcat/KM=8.4 mM/min for cholesterol, kcat/KM=8.5 mM/min for cholesta-5,7-dien-3beta-ol/7-dehydrocholesterol and kcat/KM=3.5 mM/min for cholesta-5,24-dien-3beta-ol/desmosterol.

enzyme: cholesterol 24-hydroxylase


substrate_name: L-lactaldehyde

proof_lines: kcat is 761 sec(-1) with L-lactaldehyde as substrate (PubMed:27671251). kcat is 52 sec(-1) with glycolaldehyde as substrate (PubMed:31850327). kcat is 1100 min(-1) with glycolaldehyde as substrate. kcat is 37 min(-1) with acetaldehyde as su

substrate: L-lactaldehyde


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: adenosine 5'-phosphosulfate

substrate: adenosine 5'-phosphosulfate


organism: Rhizobium meliloti (strain 1021)

substrate_name: APS

proof_lines: Km for phosphoadenosine-5'-phosphosulfate (PAPS) is above 100 uM and Vmax is lower than 0.21 pmol/min/mg.

substrate: APS


enzyme_display_name: theobromine synthase

organism: Camellia sinensis var. assamica

substrate_name: 1,3,7-trimethyluric acid

proof_lines: kcat is 0.00018 sec(-1) with 1,3,7-trimethyluric acid as substrate.

enzyme: theobromine synthase

substrate: 1,3,7-trimethyluric acid


enzyme_display_name: quercetin 3-O-methyltransferase

organism: Solanum habrochaites

substrate_name: myricetin (in the presence of S-adenosylmethionine)

proof_lines: kcat is 0.82 sec(-1) with myricetin as substrate (in the presence of S-adenosylmethionine) (PubMed:22711283). kcat is 1.66 sec(-1) with 3'-methyl myricetin as substrate (in the presence of S-adenosylmethionine) (PubMed:22711283). kcat is 0.

enzyme: quercetin 3-O-methyltransferase


organism: Pisum sativum

substrate_name: Unknown

substrate: Unknown


organism: Arabidopsis thaliana

substrate_name: alanine (with recombinant enzyme, in the presence of 20 mM glyoxylate)

proof_lines: kcat is 6.4 sec(-1) for L-serine. kcat is 2.86 sec(-1) for L-alanine.


substrate_name: PtdIns (in the absence of phosphatidylserine)

assay_conditions_summary: cofactor ATP

proof_lines: In the absence of the carrier phosphatidylserine, enzymatic kinetics toward PtdIns4P are non-linear.


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

substrate_name: KDG (at 50 degrees Celsius)

proof_lines: kcat is 8.26 sec(-1) with KDG as substrate. kcat is 26.3 sec(-1) with KG as substrate.

substrate: KDG (at 50 degrees Celsius)


organism: Pseudomonas putida

substrate_name: OT-CoA (at pH 9 and at 25 degrees Celsius)

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

assay_conditions_summary: pH 9; cofactor CoA


enzyme_display_name: mitogen-activated protein kinase kinase kinase

substrate_name: ATP

substrate: ATP


enzyme: mitogen-activated protein kinase kinase kinase


organism: Rattus norvegicus


enzyme_display_name: protein-ribulosamine 3-kinase

substrate_name: ribuloselysine

enzyme: protein-ribulosamine 3-kinase

substrate: ribuloselysine


substrate_name: deoxymorpholinopsicose

substrate: deoxymorpholinopsicose


substrate_name: deoxymorpholinofructose

substrate: deoxymorpholinofructose


enzyme_display_name: levoglucosan kinase

organism: Lipomyces starkeyi

substrate_name: levoglucosan

enzyme: levoglucosan kinase

substrate: levoglucosan


organism: Escherichia coli (strain K12)


organism: Thermoproteus tenax

substrate_name: KDG (at 70 degrees Celsius and pH 7)

assay_conditions_summary: pH 7

substrate: KDG (at 70 degrees Celsius and pH 7)


organism: Salmonella typhi

substrate_name: CTP-glucose (at pH 8)

substrate: CTP-glucose (at pH 8)


enzyme_display_name: L-rhamnonate dehydratase

substrate_name: L-rhamnonate

proof_lines: The catalytic efficiency observed with L-rhamnonate as substrate is 70- and 16-fold higher than that observed with L-lyxonate and L-mannonate, respectively.

enzyme: L-rhamnonate dehydratase

substrate: L-rhamnonate


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

proof_lines: The catalytic efficiency observed with L-rhamnonate as substrate is 533- and 8-fold higher than that observed with L-lyxonate and L-mannonate, respectively.


organism: Sphingomonas sp. (strain SKA58)

proof_lines: kcat is 21.3 min(-1) with L-rhamnonate as substrate (PubMed:19187228). kcat is 11.0 min(-1) with L-lyxonate as substrate (PubMed:19187228). kcat is 10.8 min(-1) with L-mannonate as substrate (PubMed:19187228).


organism: uncultured bacterium


enzyme_display_name: Renilla-type luciferase

organism: Aequorea forskalea

substrate_name: coelenterazine

enzyme: Renilla-type luciferase

substrate: coelenterazine


organism: Renilla reniformis

substrate_name: methyl luciferin

substrate: methyl luciferin


organism: Renilla sp.


organism: Microbulbifer sp. HZ11

substrate_name: NADH

assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADH

substrate: NADH


organism: Homo sapiens

substrate_name: cholesterol

substrate: cholesterol


enzyme_display_name: (+)-pinoresinol reductase

organism: Forsythia x intermedia

substrate_name: (+)-pinoresinol

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

enzyme: (+)-pinoresinol reductase

substrate: (+)-pinoresinol


organism: Thuja plicata

proof_lines: mutant G267V of isoform PLR2, at pH 8.0 and 30°C


organism: Bos taurus

substrate_name: phospholipid hydroperoxide

substrate: phospholipid hydroperoxide


organism: Oryza sativa

proof_lines:
cosubstrate: glutathione
cosubstrate: thioredoxin


organism: Trypanosoma cruzi

substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


enzyme_display_name: 3-hydroxyanthranilate 3,4-dioxygenase

substrate_name: 3-hydroxyanthranilic acid

proof_lines:
for the pI 5.6 enzyme
for the pI 4.98 enzyme

enzyme: 3-hydroxyanthranilate 3,4-dioxygenase

substrate: 3-hydroxyanthranilic acid


organism: Cupriavidus metallidurans

sequence_variant_note: Resolved canonical sequence from Reconstructed R99A variant from UniProtKB Q1LCS4 using the selected BRENDA mutant note and residue check. and applied mutation signature R99A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q1LCS4; RCSB PDB 1YFU/1YFW/1YFX/1YFY map to Q1LCS4 with full sequence coverage.


sequence_variant_note: Resolved canonical sequence from Reconstructed R47A variant from UniProtKB Q1LCS4 using the selected BRENDA mutant note and residue check. and applied mutation signature R47A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed E110A variant from UniProtKB Q1LCS4 using the selected BRENDA mutant note and residue check. and applied mutation signature E110A to reconstruct the assayed variant sequence.


organism: Papio ursinus

substrate_name: 4-Propyl-3-hydroxyanthranilic acid

substrate: 4-Propyl-3-hydroxyanthranilic acid


organism: Rattus norvegicus


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9LD14 canonical PLR1 sequence plus reconstructed V268G/L272F substitutions from the selected BRENDA note and applied mutation signature V268G/L272F to reconstruct the assayed variant sequence.

proof_lines: mutant V268G/L272F of isoform PLR1, at pH 8.0 and 30°C


proof_lines: wild type isoform PLR2, at pH 8.0 and 30°C

proof_lines: wild type isoform PLR1, at pH 8.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9LD14 canonical PLR1 sequence plus reconstructed V268G substitution from the selected BRENDA note and applied mutation signature V268G to reconstruct the assayed variant sequence.

proof_lines: mutant V268G of isoform PLR1, at pH 8.0 and 30°C


enzyme_display_name: glycolaldehyde dehydrogenase

organism: Bacillus subtilis

substrate_name: acetaldehyde

enzyme: glycolaldehyde dehydrogenase

substrate: acetaldehyde


organism: Mycobacterium tuberculosis

substrate_name: 5'-adenylyl sulfate

proof_lines: levulinate/-hydroxy-4-methyl-2H-chromen-2-one-based assay, pH 7.5, 22°C

proof_lines: levulinate/rhodol-based assay, pH 7.5, 22°C

substrate: 5'-adenylyl sulfate


organism: Pseudomonas aeruginosa

substrate_name: thioredoxin

substrate: thioredoxin


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

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


organism: Coffea arabica

substrate_name: paraxanthine

substrate: paraxanthine


organism: Paullinia cupana

proof_lines: native enzyme from seeds, at pH 8.0 and 28°C


organism: Chrysosplenium americanum

substrate_name: quercetin

substrate: quercetin


organism: Citrus sinensis


organism: Serratula tinctoria

substrate_name: S-Adenosyl-L-methionine; Quercetin

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

ki_unit: mM

substrate: S-Adenosyl-L-methionine; Quercetin


organism: Solanum habrochaites

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: acetyl-CoA carboxytransferase

organism: Escherichia coli

substrate_name: [biotin carboxyl-carrier protein 87]-N6-carboxybiotinyl-L-lysine

proof_lines: pH and temperature not specified in the publication

enzyme: acetyl-CoA carboxytransferase


organism: Staphylococcus aureus

substrate_name: Malonyl-CoA; Holo-[carboxylase]

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: at pH 8.0, temperature not specified in the publication

substrate: Malonyl-CoA; Holo-[carboxylase]


enzyme_display_name: curcumin synthase

organism: Curcuma longa

substrate_name: feruloyl-CoA

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: pH 8.0, 37°C, with cinnamoyl-diketide-N-acetylcysteaminyl-CoA

enzyme: curcumin synthase

substrate: feruloyl-CoA


enzyme_display_name: sphingosine N-acyltransferase

organism: Bos taurus

substrate_name: Hexanoyl-CoA; D-Sphingosine

enzyme: sphingosine N-acyltransferase

substrate: Hexanoyl-CoA; D-Sphingosine


substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Spinacia oleracea


organism: Streptomyces collinus

substrate_name: n+1 n+1 n+1 Coenzyme A; Acetoacetyl-CoA

proof_lines: SABIO-RK modifier species: [acyl-carrier-protein] S-acetyltransferase(Enzyme) mutant C92S His-tagged

substrate: n+1 n+1 n+1 Coenzyme A; Acetoacetyl-CoA


proof_lines: native wild-type, crude E. coli [acyl-carrier-protein]

proof_lines: recombinant wild-type, crude Streptomyces glaucescens [acyl-carrier-protein]


substrate_name: Holo-[acyl-carrier protein]; Acetyl-CoA

substrate: Holo-[acyl-carrier protein]; Acetyl-CoA


organism: Homo sapiens

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme with wild-type apolipoprotein A-I, HDL with a surface charge of -8.2 mV

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme with mutant A154D/A158D/T161D/A164D apolipoprotein A-I, HDL with a surface charge of -11.3 mV


proof_lines: phospholipase activity of recombinant enzyme devoid of sialic acid, expressed in baby hamster kidney cells

proof_lines: phospholipase activity of recombinant enzyme expressed in baby hamster kidney cells


enzyme_display_name: lactose synthase

substrate_name: UDPgalactose

proof_lines: reaction in absence of alpha-lactalbumin

enzyme: lactose synthase

substrate: UDPgalactose


substrate_name: glucose

substrate: glucose


organism: Mus musculus


organism: Rattus norvegicus

proof_lines:
serum
liver, Golgi apparatus


enzyme_display_name: glycine transaminase

organism: Arabidopsis thaliana

substrate_name: Glyoxylate; L-Glutamate

enzyme: glycine transaminase

substrate: Glyoxylate; L-Glutamate


substrate_name: glyoxylate

substrate: glyoxylate


organism: Lactiplantibacillus plantarum


substrate_name: glutamate

substrate: glutamate


organism: Rhodopseudomonas palustris

substrate_name: L-glutamate

substrate: L-glutamate


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: KDG (at 35 degrees Celsius and pH 7.4)

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

proof_lines: kcat is 11 sec(-1) for KDG and 2.2 sec(-1) for 2-keto-D-gluconate (at 35 degrees Celsius and pH 7.4).

substrate: KDG (at 35 degrees Celsius and pH 7.4)


enzyme_display_name: aryl-sulfate sulfotransferase

organism: Dehalobacterium formicoaceticum

substrate_name: pNPS with phenol

proof_lines: kcat is 6.3 sec(-1) for pNPS with phenol. kcat is 155.2 sec(-1) for pNPS with catechol.

enzyme: aryl-sulfate sulfotransferase

substrate: pNPS with phenol


organism: Desulfitobacterium dehalogenans (strain ATCC 51507 / DSM 9161 / JW/IU-DC1)

proof_lines: kcat is 25.3 sec(-1) for pNPS with phenol. kcat is 230.7 sec(-1) for pNPS with catechol.


organism: Desulfitobacterium hafniense

proof_lines: kcat is 0.7 sec(-1) for pNPS with phenol. kcat is 14.0 sec(-1) for pNPS with catechol.


organism: Desulfitobacterium hafniense (strain DSM 10664 / DCB-2)

proof_lines: kcat is 61.2 sec(-1) for pNPS with phenol. kcat is 70.3 sec(-1) for pNPS with catechol.


proof_lines: kcat is 26.9 sec(-1) for pNPS with phenol. kcat is 129.5 sec(-1) for pNPS with catechol.


organism: Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628 / Singapore I)

proof_lines: kcat is 0.6 sec(-1) for pNPS with pNPS with phenol. kcat is 11.9 sec(-1) for catechol.


organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

substrate_name: phenol (at pH 8.0)

proof_lines: kcat is 48.6 sec(-1) with phenol and 4-methylumbelliferylsulfate as substrates (at pH 8.0).

substrate: phenol (at pH 8.0)


organism: Hungatella effluvii

proof_lines: kcat is 46.9 sec(-1) for pNPS with phenol. kcat is 10.7 sec(-1) for pNPS with catechol.


enzyme_display_name: iron(III) salmochelin esterase

substrate_name: Ent

proof_lines: kcat is 1060 min(-1) with Ent as substrate. kcat is 74 min(-1) with Fe-Ent as substrate. kcat is 3720 min(-1) with MGE as substrate. kcat is 46 min(-1) with Fe-MGE as substrate. kcat is 6500 min(-1) with DGE as substrate. kcat is 32 min(-1)

enzyme: iron(III) salmochelin esterase

substrate: Ent


enzyme_display_name: baicalin-beta-D-glucuronidase

organism: Scutellaria baicalensis

substrate_name: luteolin 3'-O-beta-D-glucuronide

proof_lines: kcat is 639 sec(-1) for baicalein 7-O-beta-D-glucuronide.

enzyme: baicalin-beta-D-glucuronidase

substrate: luteolin 3'-O-beta-D-glucuronide


enzyme_display_name: protodioscin 26-O-beta-D-glucosidase

organism: Solanum torvum

substrate_name: torvoside A

proof_lines: kcat is 8.6 sec(-1) for torvoside A. kcat is 7.7 sec(-1) for torvoside B. kcat is 9.1 sec(-1) for p-nitrophenyl-beta-glucoside. kcat is 8.3 sec(-1) for 4-methylumbelliferyl-beta-glucoside.

enzyme: protodioscin 26-O-beta-D-glucosidase

substrate: torvoside A


organism: Spinacia oleracea


enzyme_display_name: serine--pyruvate transaminase

organism: Canis familiaris

substrate_name: Pyruvate; L-Serine

enzyme: serine--pyruvate transaminase

substrate: Pyruvate; L-Serine


organism: Canis lupus familiaris

substrate_name: pyruvate

proof_lines: pH 8.0, 37°C, pyruvate as amino acceptor

substrate: pyruvate


organism: Felis catus

substrate_name: serine

substrate: serine


organism: Mus musculus


organism: Oncorhynchus mykiss

proof_lines: pH 8.4-9.2, 15°C, Km increases with rising temperature, remains constant over the range 5-30°C


organism: Phaseolus vulgaris


organism: Rattus norvegicus

proof_lines:
pH 8.0, 37°C, serine as amino donor
pH 7.4, 37°C
pH 8.0, 30°C, recombinant enzyme


enzyme_display_name: mitogen-activated protein kinase kinase kinase

organism: Homo sapiens

substrate_name: ATP

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines: recombinant COT30-467/p105DELTAN, pH 7.5, 22°C, with 10 mM Mg2+

proof_lines: recombinant COT30-397, pH 7.5, 22°C, with 5 mM Mn2+

proof_lines: recombinant COT30-397/p105DELTAN, pH 7.5, 22°C, with 5 mM Mn2+

substrate: ATP


organism: Bacillus licheniformis

substrate_name: sn-glycerol 3-phosphate

substrate: sn-glycerol 3-phosphate


organism: Clostridium perfringens


organism: Cricetulus griseus

substrate_name: CDP-diacylglycerol

substrate: CDP-diacylglycerol


organism: Escherichia coli


organism: Glycine max


organism: Oryctolagus cuniculus

substrate_name: CMP

substrate: CMP


organism: Saccharomyces cerevisiae

substrate_name: glycerol 3-phosphate

substrate: glycerol 3-phosphate


organism: Schizosaccharomyces pombe


organism: Eubacterium sp.

substrate_name: 4-nitrophenyl sulfate

proof_lines: with tyramine as second substrate, pH 8, 37°C

proof_lines: with 4-nitrophenyl sulfate as second substrate, pH 8, 37°C

substrate: 4-nitrophenyl sulfate


organism: Haemophilus sp.

proof_lines: pH 10, 37°C, with phenol as second substrate

proof_lines: pH 10, 37°C, with 4-nitrophenyl sulfate as second substrate


substrate_name: dopamine

substrate: dopamine


organism: Klebsiella sp.

proof_lines: with phenol as second substrate, pH 8, 37°C


substrate_name: salmochelin S4

substrate: salmochelin S4


substrate_name: N-acetylneuraminate 9-phosphate

proof_lines: in 25 mM HEPES, pH 7.4, 25 mM KCl, 1 mM MgCl2, 1 mM dithiothreitol, at 37°C

proof_lines: in 25 mM HEPES pH 7.5, 25 mM KCl, 1 mM MgCl2, 1 mM dithiothreitol, at 30°C

substrate: N-acetylneuraminate 9-phosphate


proof_lines: calcium alginate-encapsulated enzyme, at pH 7.0 and 37°C


organism: Levilactobacillus brevis

substrate_name: Baicalin

proof_lines: recombinant His-tagged enzyme, pH 5.0, 37°C

substrate: Baicalin


organism: Scutellaria baicalensis


organism: Solanum torvum

substrate_name: torvoside H

substrate: torvoside H


enzyme_display_name: hyaluronoglucosaminidase

organism: Bos taurus

substrate_name: hyaluronic acid

proof_lines: in 5 mM ammonium acetate, at 37°C and pH 5.0

enzyme: hyaluronoglucosaminidase

substrate: hyaluronic acid


organism: Caenorhabditis elegans

substrate_name: chondroitin

proof_lines: apparent KM, substrate calculated as disaccharide

substrate: chondroitin


organism: Homo sapiens

substrate_name: hyaluronan

substrate: hyaluronan


enzyme_display_name: purine nucleosidase

organism: Crithidia fasciculata

substrate_name: Inosine

enzyme: purine nucleosidase

substrate: Inosine


organism: Giardia duodenalis


substrate_name: Unknown

substrate: Unknown


organism: Lathyrus oleraceus


organism: Lentilactobacillus buchneri


organism: Neurospora crassa

substrate_name: GMP

substrate: GMP


organism: Oryza sativa Japonica Group

substrate_name: adenosine

substrate: adenosine


organism: Saccharolobus solfataricus


organism: Salmonella enterica


organism: Trypanosoma brucei

proof_lines: noncompetitive, recombinant enzyme, pH 7.3, 37°C


organism: Trypanosoma brucei brucei

substrate_name: cytidine

proof_lines: Km less than 0.001 mM, at pH 7.0 and 35°C

substrate: cytidine


organism: Mus musculus

substrate_name: chondroitin sulfate D; chondroitin sulfate A; chondroitin sulfate C


organism: Palamneus gravimanus


organism: Streptococcus pyogenes phage

substrate_name: n H2O; Hyaluronate

substrate: n H2O; Hyaluronate


organism: Arabidopsis thaliana

substrate_name: adenosine; Inosine

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

substrate: adenosine; Inosine


organism: Aspergillus niger

substrate_name: NAD+; adenosine; Inosine; 5'-AMP; guanosine

assay_conditions_summary: cofactor NAD+


organism: Aspergillus terricola

substrate_name: adenosine; Inosine; guanosine

substrate: adenosine; Inosine; guanosine


organism: Bos taurus


organism: Brucella anthropi

substrate_name: adenosine; Xanthosine; Inosine; guanosine


organism: Caenorhabditis elegans

substrate_name: cytidine; guanosine; adenosine; Inosine; Xanthosine; uridine


organism: Escherichia coli


organism: Sulfurisphaera tokodaii

sequence_source: UniProtKB Q96XN9, direct EC 2.7.1.45 plus Sulfurisphaera tokodaii lookup; reviewed Swiss-Prot entry for kdgK.

assay_conditions_summary: pH 8.5; 323.15 K; cofactor ATP

proof_lines: in 50 mM Tris/HCl (pH 8.5) at 50°C, with 2-keto-D-gluconate as substrate

proof_lines: in 50 mM Tris/HCl (pH 8.5) at 50°C, with 2-dehydro-3-deoxy-D-gluconate as substrate


organism: Thermus thermophilus

sequence_source: UniProtKB Q53W83, direct EC 2.7.1.45 plus Thermus thermophilus lookup; reviewed Swiss-Prot entry for kdgK.

proof_lines: pH 7.4, 35°C, in presence of 5 mM MgCl2 and 0.1 M KCl


organism: Azotobacter vinelandii

substrate_name: diphosphate

sequence_source: UniProtKB Q7M0S5, direct EC 2.7.7.33 plus Azotobacter vinelandii lookup; unreviewed TrEMBL entry.

proof_lines: diphosphate in form of magnesium diphosphate

substrate: diphosphate


substrate_name: CTP

substrate: CTP


organism: Salmonella enterica subsp. enterica serovar Paratyphi A


organism: Salmonella enterica subsp. enterica serovar Typhi


organism: Streptomyces glaucescens


organism: Yersinia pseudotuberculosis

substrate_name: CDP-D-glucose

substrate: CDP-D-glucose


proof_lines: 1 mM MnCl2 pH 7.2, temperature not specified in the publication

proof_lines: 1 mM MgCl2 pH 7.2, temperature not specified in the publication


substrate_name: UDP-N-acetyl-D-glucosamine

proof_lines: wild type enzyme, in 50 mM of Tris-HCl (pH 8.0), 40 mM of MgCl2, at 37°C

substrate: UDP-N-acetyl-D-glucosamine


proof_lines: mutant enzyme, in 50 mM of Tris-HCl (pH 8.0), 40 mM of MgCl2, at 37°C


enzyme_display_name: levoglucosan kinase

organism: Alternaria alternata

proof_lines: pH and temperature not specified in the publication

enzyme: levoglucosan kinase


substrate_name: ATP

assay_conditions_summary: pH 9.3; 303.15 K; cofactor ATP

substrate: ATP


organism: Buckleyzyma aurantiaca


organism: Hannaella luteola


organism: Papiliotrema flavescens


organism: Papiliotrema laurentii


organism: Penicillium herquei


organism: Penicillium javanicum


organism: Sporobolomyces salmonicolor


organism: Trypanosoma vivax

substrate_name: guanosine

sequence_variant_note: Resolved canonical sequence from direct_uniprot_followup and applied mutation signature D40A to reconstruct the assayed variant sequence.

substrate: guanosine


substrate_name: 7-methyl guanosine

substrate: 7-methyl guanosine


sequence_variant_note: Resolved canonical sequence from direct_uniprot_followup and applied mutation signature R252A to reconstruct the assayed variant sequence.


substrate_name: Unknown

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


organism: Vigna unguiculata

substrate_name: Xanthosine

substrate: Xanthosine


enzyme_display_name: 2-oxo-3-hexenedioate decarboxylase

organism: Pseudomonas putida

enzyme: 2-oxo-3-hexenedioate decarboxylase


proof_lines: wild-type, in complex with vinylpuruvate hydratase


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

proof_lines: mutant E109Q, in complex with vinylpuruvate hydratase


proof_lines: mutant E111Q, in complex with vinylpuruvate hydratase


enzyme_display_name: L-rhamnonate dehydratase

substrate_name: L-Rhamnonate

enzyme: L-rhamnonate dehydratase

substrate: L-Rhamnonate


organism: Haloferax volcanii


organism: Scheffersomyces stipitis


organism: Saccharomyces cerevisiae


enzyme_display_name: rhamnulose-1-phosphate aldolase

organism: Escherichia coli (strain K12)

substrate_name: L-rhamnulose 1-phosphate (at 37 degrees Celsius)

enzyme: rhamnulose-1-phosphate aldolase


enzyme_display_name: IkappaB kinase

organism: Homo sapiens

sequence_source: UniProtKB reviewed accession O14920 direct REST lookup on 2026-06-24

enzyme: IkappaB kinase


sequence_source: UniProtKB reviewed accession O15111 direct REST lookup on 2026-06-24


sequence_source: UniProtKB reviewed accession Q14164 direct REST lookup on 2026-06-24


organism: Bos taurus

substrate_name: ATP; AMP

sequence_source: UniProtKB:P08760 direct REST lookup; release 2026_02

substrate: ATP; AMP


organism: Clonorchis sinensis

substrate_name: AMP

sequence_source: UniProtKB:Q564A6 direct REST lookup; release 2026_02

substrate: AMP


substrate_name: AMP; ATP

substrate: AMP; ATP


organism: Plasmodium falciparum

sequence_source: UniProtKB:Q8I1T1 direct REST lookup; Q964H2 inactive MERGED to Q8I1T1; release 2026_02


organism: Escherichia coli

substrate_name: L-Rhamnulose 1-phosphate

sequence_source: UniProtKB:P32169 direct REST lookup; release 2026_02

substrate: L-Rhamnulose 1-phosphate


substrate_name: L-rhamnulose 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P32169 direct REST lookup plus K15Y reconstruction; release 2026_02 and applied mutation signature K15Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K15Y, in 60 mM Tris-HCl pH 7.5, 60 mM KCl

substrate: L-rhamnulose 1-phosphate


substrate_name: dihydroxyacetone phosphate

proof_lines: wild type enzyme, apparent value, at pH 7.0 and 25°C

proof_lines: wild type enzyme, in 60 mM Tris-HCl pH 7.5, 60 mM KCl

substrate: dihydroxyacetone phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32169 direct REST lookup plus L84W reconstruction; release 2026_02 and applied mutation signature L84W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L84W, in 60 mM Tris-HCl pH 7.5, 60 mM KCl


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32169 direct REST lookup plus K15W reconstruction; release 2026_02 and applied mutation signature K15W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K15W, in 60 mM Tris-HCl pH 7.5, 60 mM KCl


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32169 direct REST lookup plus Q11W reconstruction; release 2026_02 and applied mutation signature Q11W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q11W, in 60 mM Tris-HCl pH 7.5, 60 mM KCl


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32169 direct REST lookup plus N29D reconstruction; release 2026_02 and applied mutation signature N29D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N29D, apparent value, at pH 7.0 and 25°C


assay_conditions_summary: pH 8; cofactor ATP

proof_lines:
pH 8.0, with of AMP
pH 8.0, with ADP
pH 8.0, with GDP


organism: Thermotoga maritima


substrate_name: GTP

sequence_source: source_record; UniProt Q9UIJ7 direct REST cross-check

proof_lines: kcat is 57 sec(-1) with GTP as phosphate donor.

substrate: GTP


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: AMP (at 25 degrees Celsius and pH 6)

sequence_source: source_record; UniProt Q8I1T1 direct REST cross-check

assay_conditions_summary: pH 6

proof_lines: kcat is 46 sec(-1) (at 25 degrees Celsius and pH 6).

substrate: AMP (at 25 degrees Celsius and pH 6)


enzyme_display_name: phenylalanine 2-monooxygenase

organism: Pseudomonas sp.

substrate_name: L-phenylalanine

proof_lines: active enzyme comparable to native enzyme, 20 mM Tris-HCl, pH 8.0, 25°C

proof_lines: calculation from oxygen consumption due to oxidation and/or oxygenation

enzyme: phenylalanine 2-monooxygenase

substrate: L-phenylalanine


proof_lines: M142A mutant (elevated compared to 1.8 mM for wild-type), 20 mM Tris-HCl, pH 8.0, 25°C


enzyme_display_name: gluconolactonase

substrate_name: gluconolactone (with Zn(2+) as cofactor)

enzyme: gluconolactonase


organism: Rattus norvegicus

substrate_name: gluconolactone

substrate: gluconolactone


enzyme_display_name: malolactic enzyme

organism: Oenococcus oeni

substrate_name: L-Malate

sequence_source: UniProtKB Q48796

enzyme: malolactic enzyme

substrate: L-Malate


organism: Lactiplantibacillus plantarum

substrate_name: L-malate

substrate: L-malate


organism: Leuconostoc mesenteroides

proof_lines: pH 6.0, temperature not specified in the publication


organism: Ligilactobacillus murinus

substrate_name: (S)-malate

substrate: (S)-malate


organism: Secundilactobacillus collinoides

substrate_name: DL-malate

substrate: DL-malate


organism: Bacillus subtilis (strain 168)

substrate_name: malate

substrate: malate


organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)

substrate_name: manganese

substrate: manganese


substrate_name: NAD

substrate: NAD


proof_lines: kcat is 187 sec(-1) with manganese as substrate. kcat is 227 sec(-1) with NAD as substrate. kcat is 234 sec(-1) with (S)-malate as substrate.


enzyme_display_name: biotin synthase

organism: Unknown

substrate_name: dethiobiotin

enzyme: biotin synthase

substrate: dethiobiotin


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Escherichia coli (strain K12)


enzyme_display_name: protein-ribulosamine 3-kinase

organism: Homo sapiens

sequence_source: UniProtKB reviewed direct accession lookup Q9HA64 on 2026-06-24

proof_lines: pH 7.4, 37°C, recombinant enzyme FN3K-RP

enzyme: protein-ribulosamine 3-kinase


organism: Arabidopsis thaliana

substrate_name: NADH

assay_conditions_summary: pH 8; cofactor NADPH

substrate: NADH


organism: Escherichia coli

substrate_name: Dethiobiotin; reduced [2Fe-2S] Ferredoxin; Sulfur-(sulfur carrier); S-Adenosyl-L-methionine

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 reviewed direct accession lookup P12996 on 2026-06-24

proof_lines: pH and temperature not specified in the publication

source_databases_merged: sabio_rk brenda skid


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed direct accession lookup P9WPQ7 on 2026-06-24

proof_lines:
pH 8.0, 37°C
approximate value, pH 8.0, 37°C


organism: Enterococcus faecium

substrate_name: ATP; Ribuloselysine

substrate: ATP; Ribuloselysine


organism: Lactobacillus plantarum

substrate_name: Ribuloselysine; ATP

substrate: Ribuloselysine; ATP


organism: Spinacia oleracea


organism: Staphylococcus aureus


organism: Thermus thermophilus


organism: Bacillus subtilis


proof_lines:
pH 7.5, 37°C
pH 7.5, 30°C, cell free extract
pH 8, 37°C


organism: Lysinibacillus sphaericus


substrate_name: IkB-alpha; ATP

substrate: IkB-alpha; ATP


substrate_name: ATP; p65

substrate: ATP; p65


substrate_name: IkB-beta; ATP

substrate: IkB-beta; ATP


substrate_name: p65; ATP

substrate: p65; ATP


substrate_name: ATP; IkB-alpha

substrate: ATP; IkB-alpha


organism: Euglena gracilis

sequence_source: UniProtKB A9CPS8 REST/FASTA direct lookup on 2026-06-24


organism: Xanthomonas campestris

sequence_source: UniProtKB B0RN69 REST/FASTA direct lookup on 2026-06-24

assay_conditions_summary: pH 7; buffer 1 mM potassium phosphate

proof_lines: in 1 mM potassium phosphate buffer (pH 7.0) with 0.075 mM CaCl2


organism: Bos taurus


organism: Gluconobacter oxydans


organism: Rattus norvegicus

substrate_name: H2O; D-Gulonolactone

substrate: H2O; D-Gulonolactone


organism: Sus scrofa


enzyme_display_name: Delta(7)-sterol 5(6)-desaturase

enzyme: Delta(7)-sterol 5(6)-desaturase


verification_status: corrected

sequence_source: UniProtKB Q9EQS5 exact EC+organism lookup

proof_lines: reconstituted enzyme system consisting of: cytochrome b5, cytochrome b5 reductase and egg lecithin liposomes

status: corrected


enzyme_display_name: leghemoglobin reductase

organism: Vigna unguiculata

substrate_name: ferrileghemoglobin

enzyme: leghemoglobin reductase

substrate: ferrileghemoglobin


organism: Glycine max

substrate_name: Lipoamide; NADH; H+

sequence_source: UniProtKB O81413 direct REST/FASTA accession check on 2026-06-24

assay_conditions_summary: cofactor NADH

substrate: Lipoamide; NADH; H+


substrate_name: Lipoamide

sequence_source: UniProtKB reviewed accession Q41219 FASTA; UniProt reference PMID 8159785 reports soybean FLbR cDNA/protein sequence.

proof_lines:
recombinant enzyme
native enzyme
lipoamide-dependent NADH oxidation

substrate: Lipoamide


sequence_source: UniProtKB reviewed accession Q9SPB1 FASTA; UniProt reference PMID 10729615 reports cowpea FLbR sequence/function/catalytic activity.

proof_lines:
cowpea ferrileghemoglobin
soybean ferrileghemoglobin


enzyme_display_name: sinapine esterase

organism: Brassica napus

substrate_name: sinapine

enzyme: sinapine esterase

substrate: sinapine


enzyme_display_name: 2,4,6-trihydroxybenzophenone synthase

organism: Garcinia mangostana

substrate_name: malonyl-CoA

sequence_source: UniProt REST L7NCQ3; reviewed EC 2.3.1.220 entry for Garcinia mangostana

enzyme: 2,4,6-trihydroxybenzophenone synthase

substrate: malonyl-CoA


substrate_name: benzoyl-CoA

substrate: benzoyl-CoA


organism: Hypericum androsaemum

sequence_source: UniProt REST Q8SAS8; reviewed EC 2.3.1.220 entry for Hypericum androsaemum


organism: Hypericum perforatum


assay_conditions_summary: cofactor CoA

proof_lines: kcat is 2.97 min(-1) with benzoyl-CoA as substrate. kcat is 3.49 min(-1) with malonyl-CoA as substrate.


proof_lines: kcat is 9.66 min(-1) with benzoyl-CoA as substrate.


enzyme_display_name: linoleate 9S-lipoxygenase

organism: Mus musculus

substrate_name: arachidonate (at pH 7.4 and 25 degrees Celsius)

proof_lines: The highest catalytic efficiency is observed with arachidonate followed by (8S)-HPETE and(15S)-HPETE with similar efficiencies (PubMed:16112079). kcat is 0.22 sec(-1) for (5Z,8Z,11Z,14Z)-eicosatetraenoate. kcat is 0.045 sec(-1) for (8Z,11Z,

enzyme: linoleate 9S-lipoxygenase


organism: Pseudomonas aeruginosa

substrate_name: linoleate (Ref.4)

proof_lines: kcat is 96 sec(-1) with linoleate as substrate (Ref.4).

substrate: linoleate (Ref.4)


enzyme_display_name: Linoleate 9S-lipoxygenase 1

enzyme_name_source: UniProtKB Q06327 direct accession lookup

organism: Arabidopsis thaliana

substrate_name: linoleate

enzyme: Linoleate 9S-lipoxygenase 1

substrate: linoleate


enzyme_display_name: Lipoxygenase

enzyme_name_source: UniProtKB D3TTH9 direct accession lookup

organism: Capsicum annuum

smiles: CCCCC/C=C\C/C=C\CCCCCCCC(=O)O

enzyme: Lipoxygenase


substrate_name: arachidonate

sequence_source: UniProtKB D3TTH9 direct accession lookup

smiles: CCCCC/C=C\C/C=C\C/C=C\C/C=C\CCCC(=O)O

substrate: arachidonate


enzyme_display_name: Delta(7)-sterol-C5(6)-desaturase 1

enzyme_name_source: UniProtKB Q39208 direct accession lookup

substrate_name: O2; 5alpha-Cholest-7-en-3beta-ol; H+; Ferrocytochrome b5

sequence_variant_note: Resolved canonical sequence from UniProtKB Q39208 canonical sequence plus direct residue substitution reconstruction and applied mutation signature P175V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Delta(7)-sterol 5-desaturase(Enzyme) mutant P175V

enzyme: Delta(7)-sterol-C5(6)-desaturase 1


substrate_name: Ferrocytochrome b5; H+; O2; 5alpha-Cholest-7-en-3beta-ol

sequence_variant_note: Resolved canonical sequence from UniProtKB Q39208 canonical sequence plus direct residue substitution reconstruction and applied mutation signature P201A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Delta(7)-sterol 5-desaturase(Enzyme) mutant P201A


substrate_name: 5alpha-Cholest-7-en-3beta-ol; O2; H+; Ferrocytochrome b5

sequence_variant_note: Resolved canonical sequence from UniProtKB Q39208 canonical sequence plus direct residue substitution reconstruction and applied mutation signature K115L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Delta(7)-sterol 5-desaturase(Enzyme) mutant K115L


sequence_source: UniProtKB Q39208 direct accession lookup


substrate_name: H+; 5alpha-Cholest-7-en-3beta-ol; Ferrocytochrome b5; O2

sequence_variant_note: Resolved canonical sequence from UniProtKB Q39208 canonical sequence plus direct residue substitution reconstruction and applied mutation signature T114I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Delta(7)-sterol 5-desaturase(Enzyme) mutant T114I


substrate_name: H+; Ferrocytochrome b5; O2; 5alpha-Cholest-7-en-3beta-ol

sequence_variant_note: Resolved canonical sequence from UniProtKB Q39208 canonical sequence plus direct residue substitution reconstruction and applied mutation signature H203L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Delta(7)-sterol 5-desaturase(Enzyme) mutant H203L


substrate_name: 5alpha-Cholest-7-en-3beta-ol; H+; Ferrocytochrome b5; O2

sequence_variant_note: Resolved canonical sequence from UniProtKB Q39208 canonical sequence plus direct residue substitution reconstruction and applied mutation signature H222E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Delta(7)-sterol 5-desaturase(Enzyme) mutant H222E


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

substrate: O2; 5alpha-Cholest-7-en-3beta-ol; H+; Ferrocytochrome b5


sequence_variant_note: Resolved canonical sequence from UniProtKB Q39208 canonical sequence plus direct residue substitution reconstruction and applied mutation signature T114S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Delta(7)-sterol 5-desaturase(Enzyme) mutant T114S


sequence_variant_note: Resolved canonical sequence from UniProtKB Q39208 canonical sequence plus direct residue substitution reconstruction and applied mutation signature P175A to reconstruct the assayed variant sequence.


substrate_name: 5alpha-Cholest-7-en-3beta-ol; Ferrocytochrome b5; H+; O2

sequence_source: UniProtKB Q39208 canonical sequence plus direct residue substitution reconstruction

proof_lines: SABIO-RK modifier species: Delta(7)-sterol 5-desaturase(Enzyme) mutant P175A


substrate_name: H+; O2; Ferrocytochrome b5; 5alpha-Cholest-7-en-3beta-ol

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q39208 reviewed canonical sequence, with G234D reconstructed from the selected mutation_signature and UniProt mutagenesis evidence for PMID 10651635. and applied mutation signature G234D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Delta(7)-sterol 5-desaturase(Enzyme) mutant G234D


organism: Saccharomyces cerevisiae

substrate_name: Ferrocytochrome b5; 5alpha-Cholest-7-en-3beta-ol; H+; O2

sequence_source: UniProtKB:P32353 reviewed canonical sequence from direct UniProt lookup on 2026-06-24.

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


organism: Homo sapiens

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


organism: Mangifera indica

substrate_name: linolenic acid

substrate: linolenic acid


organism: Musa acuminata


organism: Myxococcus xanthus

substrate_name: gamma-linolenic acid

substrate: gamma-linolenic acid


organism: Nicotiana benthamiana


organism: Rattus norvegicus


organism: Zea mays

substrate_name: avenasterol

substrate: avenasterol


enzyme_display_name: acetylserotonin O-methyltransferase

organism: Oryza sativa subsp. japonica

substrate_name: quercetin

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

enzyme: acetylserotonin O-methyltransferase

substrate: quercetin


substrate_name: serotonin

substrate: serotonin


substrate_name: N-acetylserotonin

substrate: N-acetylserotonin


organism: Gallus gallus


substrate_name: N-acetylserotonin (at 55 degrees Celsius)


proof_lines: isoform ASMT3, pH and temperature not specified in the publication


organism: Nicotiana tabacum


organism: Oryza sativa

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


organism: Ovibos moschatus


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


organism: Conioselinum anthriscoides

sequence_source: UniProtKB REST direct accession check for A0A0K1YW34 on 2026-06-24


organism: Mus musculus

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB REST direct accession check for D3KU66 on 2026-06-24

proof_lines:
enzyme from pineal gland, pH 7.9, 30°C
enzyme from retina, pH 7.9, 30°C

substrate: S-adenosyl-L-methionine


sequence_source: UniProtKB REST direct accession check for Q6EPG8 on 2026-06-24


organism: Brassica napus

substrate_name: Sinapoylcholine; H2O

sequence_source: UniProtKB reviewed accession Q3ZFI4 direct REST/FASTA lookup

substrate: Sinapoylcholine; H2O


organism: Barbarea intermedia

substrate_name: p-Coumaroylcholine

substrate: p-Coumaroylcholine


proof_lines:
cv. Line
cv. Gulliver


organism: Brassica nigra

substrate_name: isoferuloylcholine

substrate: isoferuloylcholine


organism: Brassica rapa subsp. oleifera


organism: Raphanus sativus

substrate_name: Sinapoylcholine

substrate: Sinapoylcholine


organism: Sinapis alba


enzyme_display_name: gallate 1-beta-glucosyltransferase

organism: Quercus rubra

substrate_name: UDPglucose

enzyme: gallate 1-beta-glucosyltransferase

substrate: UDPglucose


organism: Quercus robur

substrate_name: gallate

substrate: gallate


organism: Eucalyptus camaldulensis

substrate_name: protocatechuate

substrate: protocatechuate


substrate_name: vanillate

substrate: vanillate


sequence_source: UniProtKB REST accessions endpoint, A0A2Z5V6P3, checked 2026-06-24


sequence_source: UniProtKB REST accessions endpoint, A0A2Z5VC92, checked 2026-06-24


organism: Punica granatum

substrate_name: gallic acid (at pH 5.0 and 30 degrees Celsius)

proof_lines: kcat is 0.55 sec(-1) with gallic acid as substrate. kcat is 0.6 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec(-1) with caffeic acid as substrate. kcat is


proof_lines: kcat is 0.52 sec(-1) with gallic acid as substrate. kcat is 0.61 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 0.76 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.64 sec(-1) with caffeic acid as substrate. kcat is

substrate: gallic acid (at pH 5.0 and 30 degrees Celsius)


enzyme_display_name: retinol O-fatty-acyltransferase

organism: Homo sapiens

substrate_name: retinol

enzyme: retinol O-fatty-acyltransferase

substrate: retinol


enzyme_display_name: thiamine-phosphate kinase

organism: Escherichia coli (strain K12)

substrate_name: thiamine-monophosphate

sequence_source: UniProtKB reviewed accession P0AGG0 direct REST check on 2026-06-24; matches the selected source_record sequence.

assay_conditions_summary: cofactor ATP

enzyme: thiamine-phosphate kinase

substrate: thiamine-monophosphate


organism: Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)

substrate_name: thiamine phosphate (at pH 7.0 and 100 degrees Celsius)

assay_conditions_summary: pH 7; cofactor ATP

proof_lines: kcat is 0.063 sec(-1) (at pH 7.0 and 100 degrees Celsius).


organism: Pyrobaculum calidifontis

substrate_name: thiamine phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot A3MTW6 REST FASTA/JSON, checked 2026-06-24 and applied mutation signature R136M to reconstruct the assayed variant sequence.

substrate: thiamine phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot A3MTW6 REST FASTA/JSON, checked 2026-06-24 and applied mutation signature S196A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Swiss-Prot A3MTW6 REST FASTA/JSON, checked 2026-06-24


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

substrate_name: ManGlcNAc (at pH 5.5 and 30 degrees Celsius)

proof_lines: kcat is 37 sec(-1) for phosphorylase activity with GlcNAc (at pH 5.5 and 30 degrees Celsius). kcat is 22 sec(-1) for phosphorylase activity with GlcNAc2 (at pH 5.5 and 30 degrees Celsius). kcat is 210 sec(-1) for phosphorylase activity with


organism: Bacteroides thetaiotaomicron


sequence_source: UniProtKB direct lookup: Q8A8Y4


substrate_name: N-Acetyl-D-glucosamine

column_label: Table 1 (Kinetic parameters for the synthetic reactions catalyzed by BT1033), acceptor row 'GlcNAc': column 'Km (mM)' = 3.8; column 'kcat (s^-1)' = 37; column 'kcat/Km (s^-1 mM^-1)' = 9.6.

normalized_value_unit_evidence: kcat: printed cell 37 s^-1; already in s^-1, no unit conversion applies; normalized 37.0 s^(-1). Km: printed cell 3.8 mM; already in mM, no unit conversion applies; normalized 3.8 mM. kcat/Km: printed cell 9.6 s^-1 mM^-1; already in s^-1 mM^-1, no unit conversion applies; normalized 9.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, journal page 27370, Table 1, acceptor row 'GlcNAc': kcat = 37 s^-1; Km = 3.8 mM; printed kcat/Km = 9.6 s^-1 mM^-1.

row_label: Table 1, acceptor row 'GlcNAc'

table_label: Table 1: Kinetic parameters for the synthetic reactions catalyzed by BT1033 (J. Biol. Chem. 2013, 288(38):27366-27374, journal page 27370)

substrate: N-Acetyl-D-glucosamine


column_label: Table 2 (Kinetic parameters for the phosphorolytic reactions catalyzed by BT1033), substrate row 'ManGlcNAc': column 'kcat (s^-1)' = 240; column 'KmA (mM)' = 2.1; column 'KmB (mM)' = 0.6; column 'KiA (mM)' = 1.7; column 'kcat/KmA (s^-1 mM^-1)' = 110.

normalized_value_unit_evidence: kcat: printed cell 240 s^-1; already in s^-1, no unit conversion applies; normalized 240.0 s^(-1). Km: printed cell 2.1 mM; already in mM, no unit conversion applies; normalized 2.1 mM. kcat/Km: printed cell 110 s^-1 mM^-1; already in s^-1 mM^-1, no unit conversion applies; normalized 110.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, journal page 27371, Table 2, substrate row 'ManGlcNAc': kcat = 240 s^-1; Km = 2.1 mM; printed kcat/Km = 110 s^-1 mM^-1.

row_label: Table 2, substrate row 'ManGlcNAc'

table_label: Table 2: Kinetic parameters for the phosphorolytic reactions catalyzed by BT1033 (J. Biol. Chem. 2013, 288(38):27366-27374, journal page 27371)


substrate_name: alpha-D-Mannose 1-phosphate

verification_status: verified

column_label: Table 1 (Kinetic parameters for the synthetic reactions catalyzed by BT1033), donor row 'alpha-Man1P': column 'Km (mM)' = 2.6; column 'kcat (s^-1)' = 25; column 'kcat/Km (s^-1 mM^-1)' = 9.6.

normalized_value_unit_evidence: kcat: printed cell 25 s^-1; already in s^-1, no unit conversion applies; normalized 25.0 s^(-1). Km: printed cell 2.6 mM; already in mM, no unit conversion applies; normalized 2.6 mM. kcat/Km: printed cell 9.6 s^-1 mM^-1 is 9.6 s^(-1)*mM^(-1); the exact quotient of the same two printed cells, 25.0 / 2.6, is 9.615384615384615 s^(-1)*mM^(-1), which is the value this row carries.

raw_value_unit_evidence: Table 1, journal page 27370, Table 1, donor row 'alpha-Man1P': kcat = 25 s^-1; Km = 2.6 mM; printed kcat/Km = 9.6 s^-1 mM^-1.

row_label: Table 1, donor row 'alpha-Man1P'

substrate: alpha-D-Mannose 1-phosphate

status: verified


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


proof_lines: pH 5.5, 30°C, cosubstrate: N-acetyl-D-glucosamine, synthetic reaction

proof_lines: pH 5.5, 30°C, cosubstrate: 4-O-beta-D-mannopyranosyl-N-acetyl-D-glucosamine, phosphorolytic reaction


substrate_name: N,N'-diacetylchitobiose

substrate: N,N'-diacetylchitobiose


substrate_name: N,N'-Diacetylchitobiose

column_label: Table 1 (Kinetic parameters for the synthetic reactions catalyzed by BT1033), acceptor row 'GlcNAc2': column 'Km (mM)' = 27; column 'kcat (s^-1)' = 22; column 'kcat/Km (s^-1 mM^-1)' = 0.8.

normalized_value_unit_evidence: kcat: printed cell 22 s^-1; already in s^-1, no unit conversion applies; normalized 22.0 s^(-1). Km: printed cell 27 mM; already in mM, no unit conversion applies; normalized 27.0 mM. kcat/Km: printed cell 0.8 s^-1 mM^-1 is 0.8 s^(-1)*mM^(-1); the exact quotient of the same two printed cells, 22.0 / 27.0, is 0.8148148148148148 s^(-1)*mM^(-1), which is the value this row carries.

raw_value_unit_evidence: Table 1, journal page 27370, Table 1, acceptor row 'GlcNAc2': kcat = 22 s^-1; Km = 27 mM; printed kcat/Km = 0.8 s^-1 mM^-1.

row_label: Table 1, acceptor row 'GlcNAc2'

substrate: N,N'-Diacetylchitobiose


substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


substrate_name: Retinol; Palmitoyl-CoA

substrate: Retinol; Palmitoyl-CoA


assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: ARAT activity of recombinant acyl coenzyme A:diacylglycerol acyltransferase isozyme 1, pH 7.4, 37°C

proof_lines: ARAT activity of acyl coenzyme A:diacylglycerol acyltransferase isozyme 1, pH 7.4, 37°C


organism: Bos taurus

proof_lines: pH 7.5, 37°C, retinal pigment epithelium microsomes


organism: Gallus gallus


organism: Salvelinus fontinalis


enzyme_display_name: phosphatidylinositol 3-kinase

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

sequence_source: UniProtKB reviewed Swiss-Prot P32871, fetched by UniProt REST on 2026-06-24

enzyme: phosphatidylinositol 3-kinase

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


sequence_source: UniProtKB reviewed Swiss-Prot O00443, fetched by UniProt REST on 2026-06-24


column_label: Table 1; row/segment WT PI3Kalpha; metric/detail PIP2 Km; raw 1.77 +/- 0.03 micromolar; normalized 0.00177 mM.

raw_value_unit_evidence: Table 1; WT PI3Kalpha; PIP2 Km: 1.77 +/- 0.03 micromolar.

row_label: WT PI3Kalpha

table_label: Table 1


substrate_name: PtdIns (in the absence of phosphatidylserine)

proof_lines: In the absence of the carrier phosphatidylserine, enzymatic kinetics toward PtdIns4P are non-linear.


organism: Corynebacterium sp.

substrate_name: NADPH; 2-Dehydro-L-idonate; H+

assay_conditions_summary: cofactor NADPH

proof_lines: SABIO-RK modifier species: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)(Enzyme) mutant F22Y

substrate: NADPH; 2-Dehydro-L-idonate; H+


proof_lines: SABIO-RK modifier species: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)(Enzyme) mutant Q192R


assay_conditions_summary: pH 7; 373.15 K; cofactor ATP

proof_lines: pH 7.0, 100°C, recombinant His-tagged mutant R136M


proof_lines: with ATP, pH 7.0, 100°C, recombinant His-tagged wild-type enzyme

proof_lines: with thiamine phosphate, pH 7.0, 100°C, recombinant His-tagged wild-type enzyme


proof_lines: pH 7.0, 100°C, recombinant His-tagged mutant S196A


organism: Acinetobacter baumannii

substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


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


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


enzyme_display_name: glucan endo-1,6-beta-glucosidase

enzyme: glucan endo-1,6-beta-glucosidase


organism: Saccharophagus degradans

substrate_name: Laminarin

substrate: Laminarin


organism: Trichoderma harzianum

substrate_name: Pustulan; H2O

substrate: Pustulan; H2O


substrate_name: pustulan

substrate: pustulan


organism: Sphingobium chlorophenolicum

sequence_source: UniProtKB:Q03520 direct FASTA/JSON lookup; canonical sequence retained only as context because the row-specific variant was not reconstructed.

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


substrate_name: Unknown

substrate: Unknown


organism: Sphingobium sp. UG30

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q937X0 direct FASTA/JSON lookup plus deterministic mutation reconstruction. and applied mutation signature C14A to reconstruct the assayed variant sequence.


substrate_name: glutathione

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q937X0 direct FASTA/JSON lookup plus deterministic mutation reconstruction. and applied mutation signature S15A to reconstruct the assayed variant sequence.

substrate: glutathione


sequence_source: UniProtKB:Q937X0 direct FASTA/JSON lookup plus deterministic mutation reconstruction.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q937X0 direct FASTA/JSON lookup plus deterministic mutation reconstruction. and applied mutation signature S12A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q937X0 direct FASTA/JSON lookup.

proof_lines:
pH 8.7, 37°, wild-type enzyme
pH 8.7, 37°C, wild-type enzyme


enzyme_display_name: factor independent urate hydroxylase

organism: Arthrobacter globiformis

substrate_name: Urate

sequence_variant_note: Resolved canonical sequence from UniProtKB:D0VWQ1 direct FASTA/JSON lookup plus deterministic mutation reconstruction. and applied mutation signature K12C/E286C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K12C/E286C, at pH 7.4, temperature not specified in the publication

enzyme: factor independent urate hydroxylase

substrate: Urate


sequence_variant_note: Resolved canonical sequence from UniProtKB:D0VWQ1 direct FASTA/JSON lookup plus deterministic mutation reconstruction. and applied mutation signature S296C/C302S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S296C/C302S, at pH 7.4, temperature not specified in the publication


sequence_source: UniProtKB:D0VWQ1 direct FASTA/JSON lookup.

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


organism: Aspergillus flavus

sequence_source: UniProtKB:Q00511 direct FASTA/JSON lookup.

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


organism: Bacillus subtilis

substrate_name: H2O; Urate; O2

proof_lines: SABIO-RK modifier species: factor-independent urate hydroxylase(Enzyme) mutant T69A/K9M

substrate: H2O; Urate; O2


substrate_name: Urate; O2; H2O

proof_lines: SABIO-RK modifier species: factor-independent urate hydroxylase(Enzyme) mutant T69V

substrate: Urate; O2; H2O


sequence_source: UniProtKB:O32141 direct REST/FASTA check


substrate_name: H2O; O2; Urate

proof_lines: SABIO-RK modifier species: factor-independent urate hydroxylase(Enzyme) mutant K9M

substrate: H2O; O2; Urate


proof_lines: SABIO-RK modifier species: factor-independent urate hydroxylase(Enzyme) mutant D70A


substrate_name: O2; H2O; Urate

proof_lines: SABIO-RK modifier species: factor-independent urate hydroxylase(Enzyme) mutant T69A

substrate: O2; H2O; Urate


organism: Canis lupus familiaris

sequence_source: UniProtKB:Q5FZI9 direct REST/FASTA check


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5FZI9 direct REST/FASTA check plus selected mutation_signature and applied mutation signature H245L/E252A/M253I/R291K/A296V/A301S/K303R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5FZI9 direct REST/FASTA check plus selected mutation_signature and applied mutation signature R291K/A296V/A301S/K303R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q5FZI9 direct REST/FASTA check plus selected mutation_signature


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5FZI9 direct REST/FASTA check plus selected mutation_signature and applied mutation signature A296V to reconstruct the assayed variant sequence.


enzyme_display_name: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase

organism: Escherichia coli

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

enzyme: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase


substrate_name: salicylyl-CoA

substrate: salicylyl-CoA


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


organism: Listeria monocytogenes serotype 1/2a

assay_conditions_summary: pH 8; 296.15 K; cofactor CoA


enzyme_display_name: acrosin

organism: Meleagris gallopavo

substrate_name: Bz-Arg-p-nitroanilide; H2O

enzyme: acrosin

substrate: Bz-Arg-p-nitroanilide; H2O


organism: Cicer arietinum

proof_lines:
GST-uricase fusion protein
GST-free recombinant uricase


organism: Cyberlindnera jadinii


organism: Latimeria menadoensis

assay_conditions_summary: pH 8; 303.15 K; buffer 50 mM sodium borate

column_label: Table 3 (Specific activity, kinetic parameters and production yield of WT and LM-UOX mutants), variant row 'WT'; column 'Km (uM)' = 18.43 ± 0.4; column 'kcat (s-1)' = 29.89 ± 0.3; column 'kcat/Km (uM-1 s-1)' = 1.62; column 'Specific Activity (unit/mg)' = 10.45 ± 0.14; column 'Yield (mg/1-L Culture)' = 132.1.

normalized_value_unit_evidence: Km: printed Table 3 cell 18.43 uM; 18.43 / 1000 = 0.01843 mM; the exported value is 0.01843 mM. kcat: printed Table 3 cell 29.89 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 29.89 s^(-1). kcat/Km: printed Table 3 cell 1.62 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.62 x 1000 = 1620.0 s^-1 mM^-1. This catalog row (source_db brenda) stores no kcat_over_km, so the printed efficiency cell is carried as typed primary ratio provenance only and no ratio value is exported from this record.

raw_value_unit_evidence: Table 3, variant row 'WT': Km = 18.43 uM (printed 18.43 ± 0.4); kcat = 29.89 s^-1 (printed 29.89 ± 0.3); printed kcat/Km = 1.62 uM^-1 s^-1.

row_label: Table 3, canonical-order row for the enzyme form 'WT'

table_label: Table 3: Specific activity, kinetic parameters and production yield of WT and LM-UOX mutants (International Journal of Molecular Sciences 2019, 20(6):1269)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:U4KJC3 and applied mutation signature A132C/A225C to reconstruct the assayed variant sequence.

column_label: Table 3 (Specific activity, kinetic parameters and production yield of WT and LM-UOX mutants), variant row 'A132C/A225C'; column 'Km (uM)' = 39.19 ± 0.5; column 'kcat (s-1)' = 58.19 ± 0.6; column 'kcat/Km (uM-1 s-1)' = 1.49; column 'Specific Activity (unit/mg)' = 15.38 ± 0.12; column 'Yield (mg/1-L Culture)' = 40.5.

normalized_value_unit_evidence: Km: printed Table 3 cell 39.19 uM; 39.19 / 1000 = 0.03919 mM; the exported value is 0.03919 mM. kcat: printed Table 3 cell 58.19 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 58.19 s^(-1). kcat/Km: printed Table 3 cell 1.49 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.49 x 1000 = 1490.0 s^-1 mM^-1. The exported kcat_over_km 1484.8175554988516 s^(-1)*mM^(-1) is instead the full-precision quotient of the row's own kcat and Km cells (58.19 / 0.03919 = 1484.8175554988516); the paper's printed efficiency cell 1.49 uM^-1 s^-1 = 1490.0 s^(-1)*mM^(-1) does not equal that quotient rounded to the paper's own two decimal places (1.4848175554988516 rounds to 1.48, not 1.49), so the printed primary cell replaces the stored quotient.

row_label: Table 3, canonical-order row for the enzyme form 'A132C/A225C'


sequence_variant_note: Resolved canonical sequence from UniProtKB:U4KJC3 plus reconstructed I27C/N289C variant and applied mutation signature I27C/N289C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:U4KJC3 plus reconstructed S136C variant and applied mutation signature S136C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:U4KJC3 plus reconstructed S136C variant


sequence_variant_note: Resolved canonical sequence from UniProtKB:U4KJC3 plus reconstructed A132C/A225C variant and applied mutation signature A132C/A225C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A132C/A225C, at pH 8.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:U4KJC3 plus reconstructed N289C variant and applied mutation signature N289C to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:U4KJC3 plus reconstructed D288C variant and applied mutation signature D288C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:U4KJC3 plus reconstructed D288C variant


sequence_source: UniProtKB:U4KJC3 plus reconstructed I27C/N289C variant

proof_lines: mutant enzyme I27C/N289C, at pH 8.0 and 30°C


sequence_source: UniProtKB:U4KJC3 plus reconstructed N289C variant


organism: Metabacillus fastidiosus

proof_lines: unmodified enzyme, 50 mM borate buffer, 40°C, pH 9.2

proof_lines: unmodified enzyme, 50 mM borate buffer, 25°C, pH 9.2


sequence_source: UniProt REST direct accession C5HDG5 (unreviewed canonical wild-type sequence)

proof_lines:
wild-type, pH 9.2, 27°C
wild type enzyme, at pH 9.2 and 25°C
wild type enzyme, at pH 7.4 and 25°C


proof_lines:
mutant enzyme V144A, at pH 9.2 and 25°C
mutant enzyme V144A, at pH 7.4 and 25°C


proof_lines:
mutant enzyme Y319R, at pH 7.4 and 25°C
mutant enzyme Y319R, at pH 9.2 and 25°C


proof_lines: mutant enzyme V144A/Y319R, at pH 7.4 and 25°C

proof_lines: mutant enzyme V144A/Y319R, at pH 9.2 and 25°C


enzyme_display_name: benzoate O-methyltransferase

organism: Antirrhinum majus

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProt REST direct accession Q8H6N2 (unreviewed canonical accession sequence)

proof_lines:
with benzoic acid, pH 7.5, 20°C
pH 7.5, 20°C

enzyme: benzoate O-methyltransferase

substrate: S-adenosyl-L-methionine


organism: Arabidopsis lyrata

substrate_name: benzoic acid

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

substrate: benzoic acid


proof_lines:
pH 7.7, 30°C
apparent Km-value, pH 7.7, 30°C


organism: Arabidopsis thaliana

sequence_source: UniProt REST direct accession Q6XMI3 (reviewed canonical sequence)


organism: Clarkia breweri

substrate_name: salicylate

substrate: salicylate


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


enzyme_display_name: exoribonuclease II

substrate_name: Poly(A)

sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession P30850 with reconstructed E542A substitution and applied mutation signature E542A to reconstruct the assayed variant sequence.

enzyme: exoribonuclease II

substrate: Poly(A)


sequence_source: UniProt REST direct accession P30850 (reviewed canonical wild-type sequence)


enzyme_display_name: 2-aminophenol 1,6-dioxygenase

organism: Comamonas testosteroni

assay_conditions_summary: pH 8

proof_lines: at pH 8.0, temperature not specified in the publication

enzyme: 2-aminophenol 1,6-dioxygenase


organism: Ectopseudomonas oleovorans


organism: Pseudomonas sp.

proof_lines: pH and temperature not specified in the publication


organism: Brevibacterium ketosoreductum

substrate_name: NADPH

assay_conditions_summary: pH 6.4; 303.15 K; cofactor NADPH

substrate: NADPH


organism: Corynebacterium sp.

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: mutant enzyme F22Y/K232G/R235G/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C


proof_lines: mutant enzyme K232G/R238H, in 100 mM Bis-Tris, pH 7.0, at 25°C


proof_lines: wild type enzyme, in 100 mM Bis-Tris, pH 7.0, at 25°C


proof_lines: mutant enzyme F22Y/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C


proof_lines: mutant enzyme F22Y/S233T/R235S/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C


proof_lines: mutant enzyme F22Y/K232G/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C


assay_conditions_summary: pH 6.4; 298.15 K; cofactor NADP+

proof_lines: isoform 2,5-diketo-D-gluconate reductase I, at pH 7.0 and 30°C

proof_lines: isoform 2,5-diketo-D-gluconate reductase II, at pH 7.0 and 30°C


substrate_name: ethyl 2-methylacetoacetate

substrate: ethyl 2-methylacetoacetate


organism: Escherichia coli (strain K12)

substrate_name: methylglyoxal

proof_lines: kcat is 1749 min(-1) with methylglyoxal as substrate (PubMed:16077126). kcat is 368 min(-1) with glyoxal as substrate (PubMed:23990306). kcat is 22 min(-1) with glycolaldehyde as substrate (PubMed:23990306).

substrate: methylglyoxal


proof_lines: kcat is 1657 min(-1) with methylglyoxal as substrate (PubMed:16077126). kcat is 296 min(-1) with glyoxal as substrate (PubMed:23990306). kcat is 15 min(-1) with glycolaldehyde as substrate (PubMed:23990306).


proof_lines: kcat is 0.19 sec(-1) for benzoic acid. kcat is 0.07 sec(-1) for salicylic acid.


organism: Petunia hybrida

proof_lines: kcat is 0.0057 sec(-1) with S-adenosyl-L-methionine (in the presence of salicylic acid) (PubMed:14630969). kcat is 0.0079 sec(-1) with S-adenosyl-L-methionine (in the presence of benzoic acid) (PubMed:14630969). kcat is 0.004 sec(-1) with s


proof_lines: kcat is 0.0145 sec(-1) with S-adenosyl-L-methionine (in the presence of salicylic acid) (PubMed:14630969). kcat is 0.0075 sec(-1) with S-adenosyl-L-methionine (in the presence of benzoic acid) (PubMed:14630969). kcat is 0.012 sec(-1) with s


proof_lines: kcat is 6.2 sec(-1) with 1,4-dihydroxy-2-naphthoyl-CoA (PubMed:23564174). kcat is 1.6 sec(-1) with 1,4-dihydroxy-2-naphthoyl-CoA (PubMed:24992697). kcat is 0.12 sec(-1) with oleoyl-CoA. kcat is 0.62 sec(-1) with myristoyl-CoA. kcat is 0.004


organism: Listeria monocytogenes serotype 1/2a (strain 10403S)

substrate_name: DHNA-CoA

substrate: DHNA-CoA


organism: Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)

substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Pseudomonas sp


organism: Corynebacterium sp. (strain ATCC 31090)


organism: Danio rerio

substrate_name: urate

substrate: urate


organism: Puccinia recondita f. sp. triseti

substrate_name: Urate

sequence: APFSLATA

wild_type_sequence: APFSLATA

substrate: Urate


organism: Rattus norvegicus


organism: Zea mays


organism: Trichoderma harzianum

substrate_name: Unknown

substrate: Unknown


organism: Meleagris gallopavo

substrate_name: N-alpha-benzoyl-DL-arginine-p-nitroanilide (at 25 degrees Celsius)


organism: Rhizorhabdus dicambivorans


organism: Arthrobacter globiformis


organism: Bacillus sp. (in: firmicutes)

substrate_name: uric acid

proof_lines:
enzyme with histidine tag
enzyme without histidine tag

substrate: uric acid


organism: Bacillus subtilis

assay_conditions_summary: pH 8; buffer air-saturated

proof_lines: mutant enzyme K9M, apparent Km in air-saturated buffer


proof_lines: wild type enzyme, apparent Km in air-saturated buffer


assay_conditions_summary: buffer air-saturated

proof_lines: mutant enzyme F179A, apparent Km in air-saturated buffer


proof_lines: mutant enzyme F179Y, apparent Km in air-saturated buffer


proof_lines: competitive inhibitor versus urate at pH 8.0


organism: Cytobacillus firmus


organism: Enterobacter cloacae


organism: Geobacillus thermocatenulatus

proof_lines: 0.1 M sodium borate, pH 8.5 containing 2 mM uric acid, 30 mM 4-aminoantipyrine, 1.5% phenol and peroxidase (15 U/ml), 37°C, 20 min


organism: Glycine max

substrate_name: Urate; O2; H2O

substrate: Urate; O2; H2O


organism: Metabacillus fastidiosus

proof_lines: native uricase, monomethoxypoly(ethylene glycol) N-leucine-OSu-uricase and branched monomethoxypoly(ethylene glycol) N-leucine-OSu-uricase


organism: Microbacterium sp.


organism: Penicillium purpurescens


organism: Sphingobacterium thalpophilum


organism: synthetic construct


organism: Uromyces phaseoli


organism: Uromyces viciae-fabae


organism: Antirrhinum majus

proof_lines: apparent Km-value of plant-purified protein, pH 7.5, 20°C

proof_lines: apparent Km-value of recombinant protein, pH 7.5, 20°C

proof_lines: for S-adenosyl-L-methionine, pH 7.5, 20°C


organism: Bos taurus

substrate_name: ATP

substrate: ATP


organism: Homo sapiens


organism: Mus musculus

assay_conditions_summary: pH 7.4; cofactor ATP


organism: Rattus norvegicus

proof_lines: with phosphatidylinositol 4-phosphate or phosphatidylinositol 4,5-bisphosphate as cosubstrate

proof_lines: with phosphatidylinositol as cosubstrate


organism: Sus scrofa

substrate_name: phosphatidylinositol 4-phosphate

proof_lines: reaction with phosphatidylinositol 4,5-diphosphate

proof_lines: reaction with phosphatidylinositol 4-phosphate

substrate: phosphatidylinositol 4-phosphate


organism: Escherichia coli

substrate_name: thiamine phosphate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: thiamine phosphate


organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, temperature not specified in the publication


organism: Neisseria meningitidis

sequence_source: UniProtKB H2VFI5 FASTA, anchored by PMID 15518580 MC58 SiaA/NeuC abstract

proof_lines: wild-type, 37°C, pH not specified in the publication


proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, hexamer


organism: Acremonium persicinum

substrate_name: Pustulan; H2O

substrate: Pustulan; H2O


organism: Eupenicillium brefeldianum

substrate_name: H2O; Pustulan

substrate: H2O; Pustulan


organism: Fusarium fujikuroi

substrate_name: Gentiotetraose

proof_lines: assumed molecular weight for lutean 650000 Da

substrate: Gentiotetraose


organism: Trichoderma harzianum


organism: Verruciconidia persicina

substrate_name: pustulan

proof_lines: assumed molecular weight for pustulan 17000 Da, or KM of 1.28 mg/ml

substrate: pustulan


organism: Capra hircus

substrate_name: Nalpha-tosyl-L-arginine methyl ester

substrate: Nalpha-tosyl-L-arginine methyl ester


organism: Ovis aries


enzyme_display_name: nitrate reductase (cytochrome)

organism: Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB)

substrate_name: nitrate (in the presence of NaCl)

enzyme: nitrate reductase (cytochrome)

substrate: nitrate (in the presence of NaCl)


organism: Oryza sativa subsp. japonica


organism: Pisum sativum

substrate_name: galactinol for the raffinose synthesis activity

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


organism: Campylobacter jejuni

substrate_name: nitrate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5HV12 direct lookup plus mutation reconstruction and applied mutation signature C176S to reconstruct the assayed variant sequence.

substrate: nitrate


sequence_source: UniProtKB:Q5HV12 direct lookup


organism: Cereibacter sphaeroides f. sp. denitrificans

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

proof_lines:
mutant K56H, 25°C, pH 6
mutant K56H, 25°C, pH 5


sequence_source: UniProtKB:O88111 direct lookup

proof_lines:
wild-type, 25°C, pH 6
wild-type, 25°C, pH 5
wild-type, 25°C, pH 7


proof_lines:
mutant K56M, 25°C, pH 6
mutant K56M, 25°C, pH 7


sequence_source: UniProtKB:O88111 direct lookup selected from source accession bundle


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q9SYJ4 direct lookup

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme


organism: Beta vulgaris

substrate_name: sucrose; galactinol

sequence_source: UniProtKB:A0A1S7IYZ8 direct lookup

substrate: sucrose; galactinol


organism: Lathyrus oleraceus

substrate_name: galactinol; sucrose

sequence_source: UniProtKB:Q8VWN6 direct lookup

proof_lines: partially purified native enzyme, raffinose synthesis

proof_lines: recombinant enzyme in Sf21 cell extract, raffinose synthesis

substrate: galactinol; sucrose


organism: Escherichia coli

substrate_name: Poly(A)

sequence_variant_note: Resolved canonical sequence from Reconstructed E542A from UniProtKB reviewed canonical sequence P30850 (RNB_ECOLI), direct REST lookup and applied mutation signature E542A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; buffer 20 mM Tris-HCl

proof_lines: 35-nt poly(A), mutant E542A, at 37°C, in 20 mM Tris-HCl buffer, pH 8, 100 mM KCl, 1 mM MgCl2, and 1 mM dithiothreitol

substrate: Poly(A)


sequence_source: UniProtKB reviewed canonical sequence P30850 (RNB_ECOLI), direct REST lookup

proof_lines: 35-nt poly(A), wild-type, at 37°C, in 20 mM Tris-HCl buffer, pH 8, 100 mM KCl, 1 mM MgCl2, and 1 mM dithiothreitol


organism: Escherichia coli (strain K12)

substrate_name: S-adenosylmethionine

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

substrate: S-adenosylmethionine


substrate_name: Unknown

substrate: Unknown


organism: Achromobacter sp. MMT


organism: Cupriavidus necator


organism: Paracoccus pantotrophus

assay_conditions_summary: pH 7

proof_lines: pH 7, NapAB catalysed nitrate reduction driven by direct electron transfer from the electrode to NapAB, protein film voltammetry


organism: Oryza sativa


organism: Vicia faba

proof_lines:
+ sucrose
cosubstrate galactinol
+ sucrose, exchange reaction


substrate_name: polyadenosine

proof_lines: malE-malF mRNA transcripts incubated at 37°C

substrate: polyadenosine


organism: Homo sapiens


enzyme_display_name: methionine transaminase

substrate_name: indole-3-pyruvic acid (at pH 8.5 and 37 degrees Celsius)

proof_lines: kcat is 2.5 min(-1) with indole-3-pyruvic acid as substrate. kcat is 1.9 min(-1) with L-Met as substrate. kcat is 3.16 min(-1) with L-Phe as substrate (at pH 8.5 and 37 degrees Celsius).

enzyme: methionine transaminase


substrate_name: 2-oxo acid 4-methylthio-2-oxobutyrate (MTOB)


substrate_name: 4-methyl-2-oxopentanoate (4MOP)

substrate: 4-methyl-2-oxopentanoate (4MOP)


substrate_name: S-adenosyl-L-methionine

proof_lines: in 100 mM glycylglycine (pH 8.7), 100 mM EDTA, 100 mM KCl, 0.5 mM dithiothreitol, at 37°C

proof_lines: competitive inhibition against 7-(aminomethyl)-7-deazaguanine-tRNATyr, in 100 mM glycylglycine (pH 8.7), 100 mM KCl, 0.5 mM dithiothreitol, 100 mM EDTA, at 37°C

substrate: S-adenosyl-L-methionine


enzyme_display_name: histidine kinase

organism: Anaeromyxobacter sp.

substrate_name: ATP

sequence_source: UniProtKB:A7HD43 REST JSON direct lookup; reviewed Swiss-Prot; organism Anaeromyxobacter sp. (strain Fw109-5); EC 2.7.13.3

assay_conditions_summary: pH 8; 293.15 K; cofactor ATP

enzyme: histidine kinase

substrate: ATP


sequence_source: UniProtKB:P23837 REST JSON direct lookup; reviewed Swiss-Prot; organism Escherichia coli (strain K12); EC 2.7.13.3

assay_conditions_summary: pH 8; 295.15 K; cofactor ATP


organism: Bos taurus

assay_conditions_summary: cofactor ATP


substrate_name: ATP (at 22 degrees Celsius and pH 8, in the presence of 50 mM KCl and 1 mM MgCl(2))


substrate_name: IDP

substrate: IDP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


substrate_name: ATP for autophosphorylation by deoxy-DosT


substrate_name: ATP for autophosphorylation by deoxy-DevS


organism: Rattus norvegicus


organism: Solanum tuberosum


organism: Anaeromyxobacter sp. (strain Fw109-5)

substrate_name: ATP (with the Fe(III)-OH(-) bound form of the enzyme)

sequence_source: source_record; UniProt REST FASTA A7HD43 matched selected sequence

proof_lines: kcat is 1.1 min(-1) for the autophosphorylation reaction with the Fe(III)-OH(-) bound form of the enzyme. kcat is 1.2 min(-1) with the Fe(III)-CN(-) bound form of the enzyme. kcat is 1.1 min(-1) with the Fe(III)-imidazole bound form of the


organism: Staphylococcus aureus

sequence_source: source_record; UniProt REST FASTA Q9RDT3 matched selected sequence

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

mutation_type: truncation

proof_lines: Kinetic parameters were determined with a truncated form of WalK, which includes only the cytoplasmic domain and not the sensor domain and the transmembrane region.


organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

substrate_name: ATP (at pH 7.8 and 25 degrees Celsius)

sequence_source: source_record; UniProt REST FASTA Q8DPL8 matched selected full-entry sequence

assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines: Kinetic parameters were determined with a truncated form of WalK, which includes only the cytoplasmic domain and not the short extracellular domain and the transmembrane region. kcat is 0.08 sec(-1) for ATP (at pH 7.8 and 25 degrees Celsius

substrate: ATP (at pH 7.8 and 25 degrees Celsius)


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:O07778 HK1_MYCTU; direct UniProt FASTA check; BRENDA literature 679855 and PubMed 17434492 identify HK1.


organism: Myxococcus xanthus

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4VPT3 rodK canonical sequence with D657N/D782N/D909N reconstructed after direct position check. and applied mutation signature D657N/D782N/D909N to reconstruct the assayed variant sequence.


organism: Thermotoga maritima


enzyme_display_name: cholesterol 7alpha-monooxygenase

substrate_name: cholesterol

proof_lines:
isoenzyme I
isoenzyme II
reconstituted enzyme complex

enzyme: cholesterol 7alpha-monooxygenase

substrate: cholesterol


enzyme_display_name: uroporphyrinogen-III synthase

substrate_name: hydroxymethylbilane

enzyme: uroporphyrinogen-III synthase

substrate: hydroxymethylbilane


substrate_name: O2; NADPH; H+; Cholesterol

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

sequence_source: UniProtKB reviewed accession P22680; direct lookup 2026-06-25

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

substrate: O2; NADPH; H+; Cholesterol


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P22680; direct lookup 2026-06-25 and applied mutation signature T104L to reconstruct the assayed variant sequence.


substrate_name: Cholesterol; O2; NADPH; H+

sequence_source: UniProtKB reviewed accession P18125; direct lookup 2026-06-25

assay_conditions_summary: cofactor NADPH

substrate: Cholesterol; O2; NADPH; H+


organism: Arabidopsis thaliana

substrate_name: 2-Oxoglutarate; L-Methionine

sequence_source: UniProtKB reviewed accession Q9LE06; direct lookup 2026-06-25

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

substrate: 2-Oxoglutarate; L-Methionine


sequence_source: UniProtKB reviewed accession Q9M401; direct lookup 2026-06-25


enzyme_display_name: iron(III) enterobactin esterase

organism: Geobacillus thermodenitrificans

substrate_name: 4-nitrophenyl butyrate

enzyme: iron(III) enterobactin esterase

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl caprylate

substrate: 4-nitrophenyl caprylate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Escherichia coli

substrate_name: Hydroxymethylbilane

sequence_source: UniProtKB reviewed accession P09126; direct lookup 2026-06-25

substrate: Hydroxymethylbilane


sequence_source: UniProtKB reviewed accession P10746; direct lookup 2026-06-25


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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P10746; direct lookup 2026-06-25 and applied mutation signature C73R/A69E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C73R/A69E, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P10746; direct lookup 2026-06-25 and applied mutation signature C73R/L43D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C73R/L43D, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P10746; direct lookup 2026-06-25 and applied mutation signature C73R to reconstruct the assayed variant sequence.

proof_lines: Km above 10 mM, mutant enzyme C73R, pH and temperature not specified in the publication

proof_lines: kcat/Km less than 1 1/sec*mM, mutant enzyme C73R, pH and temperature not specified in the publication


proof_lines: 7-oxocholestanol formation, pH 7.4, 30°C


organism: Klebsiella pneumoniae

assay_conditions_summary: pH 7.4; 310.15 K; buffer phosphate

proof_lines: recombinant enzyme, with L-tyrosine as cosubstrate, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5-phosphate, at 37°C

proof_lines: recombinant enzyme, in 10 mM phosphate buffer (pH 7.4), 50 mM pyridoxal 5-phosphate, at 37°C


substrate_name: L-leucine

proof_lines: apparent Km value, with L-leucine as cosubstrate, at pH 7.4, 37°C

proof_lines: Ki above 0.2 mM, uncompetitive inhibition, at pH 7.4, 37°C

substrate: L-leucine


organism: Bacillus subtilis


organism: Euglena gracilis


organism: Homo sapiens

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


proof_lines: kcat is 3.7 min(-1) with 5alpha-cholest-7-en-3beta-ol (lathosterol) as substrate. kcat is 2.2 min(-1) with cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol) as substrate.


organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

substrate_name: MGE

proof_lines: kcat is 9 min(-1) with Fe-Ent as substrate. kcat is 850 min(-1) with MGE as substrate. kcat is 1.4 min(-1) with Fe-MGE as substrate.

substrate: MGE


organism: Sinorhizobium sp

substrate_name: S-adenosyl-L-methionine


organism: Rattus norvegicus

proof_lines: inhibition of the last step in the synthesis of phosphatidylcholine


organism: Saccharomyces cerevisiae

substrate_name: phosphatidyl-N-dimethylethanolamine

proof_lines: phosphatidyl-N-dimethylethanolamine as substrate, noncompetitive inhibition

proof_lines: phosphatidyl-N-monomethylethanolamine as substrate, noncompetitive inhibition

proof_lines: phosphatidyl-N-monomethylethanolamine as substrate, competitive inhibition

substrate: phosphatidyl-N-dimethylethanolamine


substrate_name: diglucosyl-enterobactin

substrate: diglucosyl-enterobactin


organism: Methanobacterium ivanovii

substrate_name: uroporphyrinogen III

substrate: uroporphyrinogen III


organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

substrate_name: S-adenosyl-L-methionine (in presence of phosphatidyl-N-methylethanolamine (PMME) as substrate)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: S-adenosyl-L-methionine (in presence of phosphatidylethanolamine (PE) as substrate)


organism: Staphylococcus aureus

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication


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

assay_conditions_summary: cofactor CoA


substrate_name: lysophosphatidylethanolamine

substrate: lysophosphatidylethanolamine


organism: Mus musculus


substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Nitratidesulfovibrio vulgaris


sequence_source: UniProtKB reviewed Q3TFD2 / PCAT1_MOUSE, sequence version 1


proof_lines: total membrane fractions of mesangial cells


organism: Oryctolagus cuniculus

proof_lines:
microsomal fraction
neuronal nuclear fraction


substrate_name: hexanoyl-CoA

proof_lines: Km is induced to 0.118 mM in presence of Ca2+

substrate: hexanoyl-CoA


organism: Sus scrofa


enzyme_display_name: procollagen galactosyltransferase

substrate_name: UDP-galactose

enzyme: procollagen galactosyltransferase

substrate: UDP-galactose


substrate_name: UDP-galactose (at 37 degrees Celsius and pH 7.4)


enzyme_display_name: ribosylnicotinamide kinase

organism: Escherichia coli (strain K12)

substrate_name: NMN

enzyme: ribosylnicotinamide kinase

substrate: NMN


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)


substrate_name: nicotinamide riboside (with ATP as cosubstrate)


substrate: nicotinamide riboside (with ATP as cosubstrate)


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

substrate_name: ribosylnicotinamide

substrate: ribosylnicotinamide


substrate_name: 5-Hydroxy-L-lysine; UDPgalactose

sequence_source: UniProtKB Q8NBJ5 direct lookup

substrate: 5-Hydroxy-L-lysine; UDPgalactose


substrate_name: UDPgalactose; 5-Hydroxy-L-lysine

sequence_source: UniProtKB Q8IYK4 direct lookup

substrate: UDPgalactose; 5-Hydroxy-L-lysine


organism: Amphimedon queenslandica

substrate_name: Collagen

substrate: Collagen


organism: Gallus gallus

substrate_name: UDPgalactose

substrate: UDPgalactose


organism: Homo sapiens

proof_lines: value based on actual amount of galactosylhydroxylysyl-residues in ichthyocol

proof_lines: value based on actual amount of galactosylhydroxylysyl-residues in calf skin collagen


organism: Haemophilus influenzae

substrate_name: nicotinamide mononucleotide

proof_lines: pH 7.5, 37°C, nicotinamide mononucleotide adenylyltransferase activity

substrate: nicotinamide mononucleotide


sequence_source: UniProtKB reviewed accession Q9NWW6 direct REST lookup

proof_lines: pH and temperature not specified in the publication, with GTP

proof_lines: pH and temperature not specified in the publication, with ATP


sequence_source: UniProtKB reviewed accession Q9NPI5 direct REST lookup

proof_lines: with GTP, pH and temperature not specified in the publication

proof_lines: with ATP, pH and temperature not specified in the publication


organism: Salmonella enterica

substrate_name: N-Ribosylnicotinamide; ATP

sequence_source: UniProtKB reviewed accession P24518 direct REST lookup

substrate: N-Ribosylnicotinamide; ATP


substrate_name: ATP; N-Ribosylnicotinamide

proof_lines: SABIO-RK modifier species: ribosylnicotinamide kinase(Enzyme) mutant (R212C) N-terminal His-tag

substrate: ATP; N-Ribosylnicotinamide


substrate_name: ATP

sequence_source: UniProtKB reviewed accession P24518 (NADR_SALTY), matched to PMID 15805524 paper strain/gene context.

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: D-aminoacyl-tRNA deacylase

organism: Arabidopsis thaliana

substrate_name: H2O; D-Tyrosyl-tRNA(Tyr)

sequence_source: UniProtKB REST direct lookup Q9ZPQ3 (UniProtKB reviewed (Swiss-Prot)); accessed 2026-06-25

enzyme: D-aminoacyl-tRNA deacylase

substrate: H2O; D-Tyrosyl-tRNA(Tyr)


organism: Escherichia coli

substrate_name: D-Tyrosyl-tRNA(Tyr); H2O

sequence_source: UniProtKB REST direct lookup P0A6M4 (UniProtKB reviewed (Swiss-Prot)); accessed 2026-06-25

substrate: D-Tyrosyl-tRNA(Tyr); H2O


organism: Pyrococcus abyssi

sequence_source: UniProtKB REST direct lookup Q9V2R8 (UniProtKB reviewed (Swiss-Prot)); accessed 2026-06-25


organism: Synechocystis sp.

substrate_name: D-tyrosyl-tRNATyr

sequence_source: UniProtKB REST direct lookup P73335 (UniProtKB reviewed (Swiss-Prot)); accessed 2026-06-25

substrate: D-tyrosyl-tRNATyr


organism: Thermus thermophilus

substrate_name: D-Tyr-tRNATyr

sequence_source: UniProtKB REST direct lookup Q72K35 (UniProtKB reviewed (Swiss-Prot)); accessed 2026-06-25

substrate: D-Tyr-tRNATyr


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q72K35 (UniProtKB reviewed (Swiss-Prot)); accessed 2026-06-25 and applied mutation signature Y125F to reconstruct the assayed variant sequence.


enzyme_display_name: glycoprotein endo-alpha-1,2-mannosidase

organism: Bacteroides thetaiotaomicron

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q8A109 (UniProtKB unreviewed (TrEMBL)); accessed 2026-06-25 and applied mutation signature E332A to reconstruct the assayed variant sequence.

enzyme: glycoprotein endo-alpha-1,2-mannosidase


sequence_source: UniProtKB REST direct lookup Q8A109 (UniProtKB unreviewed (TrEMBL)); accessed 2026-06-25

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


organism: Bacteroides xylanisolvens

sequence_source: UniProtKB REST direct lookup D6D1V7 (UniProtKB unreviewed (TrEMBL)); accessed 2026-06-25


enzyme_display_name: diaminobutyrate decarboxylase

organism: Trichormus variabilis

substrate_name: L-lysine

sequence_source: UniProtKB REST direct lookup Q3M985 (UniProtKB unreviewed (TrEMBL)); accessed 2026-06-25

enzyme: diaminobutyrate decarboxylase

substrate: L-lysine


substrate_name: D-tyrosyl-tRNA(Tyr)

substrate: D-tyrosyl-tRNA(Tyr)


proof_lines: kcat/KM is 6 uM(-1)sec(-1) for D-tyrosyl-tRNA(Tyr) (PubMed:10383414). kcat/KM is 2.8 uM(-1)sec(-1) for D-tryptophanyl-tRNA(Trp) (PubMed:10918062). kcat/KM is 12 uM(-1)sec(-1) for D-aspartyl-tRNA(Asp) (PubMed:10918062). kcat/KM is 10 uM (-1)


organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)


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

proof_lines: wild type enzyme, in 25 mM HEPES pH 7.0, 100 mM NaCl, at 37°C


organism: Acinetobacter calcoaceticus


organism: Klebsiella aerogenes


organism: Serratia marcescens


organism: Vibrio alginolyticus


organism: Vibrio cholerae


organism: Vibrio cholerae serotype O1

proof_lines:
DABA AT//DC fusion protein
DABA AT/DC fusion protein


enzyme_display_name: carbonic anhydrase

organism: Stylophora pistillata

sequence_source: UniProtKB B5SU02 REST direct lookup, 2026-06-25

assay_conditions_summary: pH 7.5; 293.15 K; buffer but no exact kinetic metric/table value

proof_lines: at 20°C and pH 7.5 in 10 mM HEPES buffer

enzyme: carbonic anhydrase


organism: Methanosarcina thermophila

sequence_variant_note: Resolved canonical sequence from UniProtKB:P40881 with PMID 10924116 mature-chain E84A reconstruction and applied mutation signature E84A with inferred residue-numbering offset +34 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer the reconstructed sequence. Remaining blocker: selected BRENDA snippets list

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS-Ac buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM IMID buffer