organism: unidentified prokaryotic organism

sequence_source: UniProtKB:A0A2I9 canonical sequence, REST release 2026_02

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

proof_lines: pH 7.0, 35°C, recombinant wild-type enz.yme


enzyme_display_name: sulfinoalanine decarboxylase

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:A0A2I9 canonical sequence, REST release 2026_02 and applied mutation signature V81L/F240S/I250S/D266L to reconstruct the assayed variant sequence.

data_origin: experimental

enzyme: sulfinoalanine decarboxylase

status: unverified

source: oed


source_db: brenda

kcat_over_km_display: Not reported

sequence_source: Reconstructed from UniProtKB:A0A2I9 canonical sequence, REST release 2026_02

proof_lines: pH 7.0, 35°C, recombinant mutant V81L/F240S/I250S/D266L enzyme

source: brenda


mutation_signature: Unknown

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


enzyme_display_name: sphinganine-1-phosphate aldolase

organism: Burkholderia pseudomallei

substrate_name: sphinganine 1-phosphate

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

enzyme: sphinganine-1-phosphate aldolase

substrate: sphinganine 1-phosphate


organism: Homo sapiens

substrate_name: Sphingosine 1-phosphate

kcat_display: Not reported

mutation_signature: Δ1

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

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

mutation_type: deletion

proof_lines: SABIO-RK modifier species: sphinganine-1-phosphate aldolase(Enzyme) mutant N-terminal truncated (delta1-61)

substrate: Sphingosine 1-phosphate


enzyme_display_name: chorismate lyase

organism: Escherichia coli

substrate_name: Chorismate

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:P26602 canonical sequence, REST release 2026_02

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

source_databases_merged: sabio_rk brenda skid

enzyme: chorismate lyase

substrate: Chorismate


proof_lines: SABIO-RK modifier species: chorismate lyase(Enzyme) mutant C14S, C81S


organism: Stenotrophomonas panacihumi

substrate_name: chorismate

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

substrate: chorismate


organism: Xylella fastidiosa


enzyme_display_name: methylglutaconyl-CoA hydratase

organism: Acinetobacter sp.

substrate_name: (E)-glutaconyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines: dehydration hydration

enzyme: methylglutaconyl-CoA hydratase

substrate: (E)-glutaconyl-CoA


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


enzyme_display_name: inositol-hexakisphosphate 5-kinase

organism: Glycine max

source_db: uniprot

enzyme: inositol-hexakisphosphate 5-kinase

source: uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Zea mays

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Haemophilus influenzae

substrate_name: D-ribulose 5-phosphate (in the presence of 50 uM CTP)

assay_conditions_summary: cofactor NADPH


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: CTP

substrate: CTP


organism: Rattus norvegicus

substrate_name: Unknown

km_display: Not reported

substrate: Unknown


substrate_name: (DL)-glycerol 3-phosphate

substrate: (DL)-glycerol 3-phosphate


enzyme_display_name: beta-agarase

organism: Agarivorans albus

substrate_name: agarose

sequence: ASLVTSFEEA

wild_type_sequence: ASLVTSFEEA

enzyme: beta-agarase

substrate: agarose


enzyme_display_name: creatininase

organism: Pseudomonas putida

substrate_name: creatinine

enzyme: creatininase

substrate: creatinine


enzyme_display_name: gamma-resorcylate decarboxylase

organism: Agrobacterium radiobacter

substrate_name: gamma-resorcylate (for decarboxylation)

enzyme: gamma-resorcylate decarboxylase

substrate: gamma-resorcylate (for decarboxylation)


organism: Rhizobium sp. (strain MTP-10005)


substrate_name: L-aspartate

substrate: L-aspartate


substrate_name: sphingosine 1-phosphate

substrate: sphingosine 1-phosphate


substrate_name: dihydrosphingosin 1-phosphate

substrate: dihydrosphingosin 1-phosphate


organism: Escherichia coli (strain K12)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Homo sapiens


enzyme_display_name: pentachlorophenol monooxygenase

organism: Sphingobium chlorophenolicum

substrate_name: pentachlorophenol

proof_lines: kcat is 0.024 sec(-1) with pentachlorophenol as substrate. kcat is 0.32 sec(-1) with 2,3,5,6-tetrachlorophenol as substrate.

enzyme: pentachlorophenol monooxygenase

substrate: pentachlorophenol


enzyme_display_name: cholestanetriol 26-monooxygenase

proof_lines: kcat/KM=0.005 umol/min for cholesterol and kcat/KM=0.018 umol/min for (25R)-cholest-5-ene-3beta,26-diol.

enzyme: cholestanetriol 26-monooxygenase


enzyme_display_name: pentalenolactone synthase

organism: Streptomyces arenae

substrate_name: pentalenolactone F

proof_lines: kcat is 8.8 min(-1) with pentalenolactone F as substrate.

enzyme: pentalenolactone synthase

substrate: pentalenolactone F


organism: Streptomyces exfoliatus

proof_lines: kcat is 10.5 min(-1) with pentalenolactone F as substrate.


organism: Streptomyces fradiae

proof_lines: kcat is 7.2 min(-1) with dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose as substrate. kcat is 32.5 min(-1) with TDP-3-N-methylamino-3,6-dideoxy-R-D-glucopyranose as substrate. kcat is 9.9 min(-1) with dTDP-3-amino-3,6-dideoxy-alpha-D-glu


enzyme_display_name: salicylate carboxymethyltransferase

organism: Arabidopsis thaliana

substrate_name: S-adenosyl-L-methionine

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

enzyme: salicylate carboxymethyltransferase

substrate: S-adenosyl-L-methionine


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


substrate_name: acetyl-CoA

proof_lines: kcat is 4.4 sec(-1) with acetyl-CoA as substrate (PubMed:15286288). kcat is 57.1 sec(-1) with benzoyl-CoA as substrate (in the presence of benzyl alcohol) (PubMed:15286288). kcat is 81.3 sec(-1) with benzoyl-CoA as substrate (in the presenc

substrate: acetyl-CoA


substrate_name: coniferyl alcohol (in the presence of acetyl CoA and at pH 6)

assay_conditions_summary: pH 6; cofactor CoA

proof_lines: kcat is 2.05 sec(-1) with coniferyl alcohol as substrate (in the presence of acetyl CoA and at pH 6) (PubMed:17241449). kcat is 2.32 sec(-1) with acetyl CoA as substrate (in the presence of coniferyl alcohol and at pH 6) (PubMed:17241449).


enzyme_display_name: anthocyanidin 3-O-glucosyltransferase

organism: Fragaria ananassa

substrate_name: pelargonidin

proof_lines: The kinetic constants are determined for the recombinant His(6)-tagged protein.

enzyme: anthocyanidin 3-O-glucosyltransferase

substrate: pelargonidin


organism: Zea mays

proof_lines: kcat is 11.6 sec(-1) for DIMBOA. kcat is 12.5 sec(-1) for DIBOA. kcat is 22.6 sec(-1) for UDPG.


organism: Humulus lupulus

substrate_name: phlorisovalerophenone

substrate: phlorisovalerophenone


substrate_name: naringenin chalcone

substrate: naringenin chalcone


enzyme_display_name: spermine synthase

substrate_name: S-adenosylmethionine

enzyme: spermine synthase

substrate: S-adenosylmethionine


enzyme_display_name: inositol-tetrakisphosphate 1-kinase

organism: Bos taurus

enzyme: inositol-tetrakisphosphate 1-kinase


organism: Glycine max


substrate_name: ATP

substrate: ATP


enzyme_display_name: hydroxymethylpyrimidine kinase

enzyme: hydroxymethylpyrimidine kinase


organism: Sus scrofa

substrate_name: prostamide H(2)

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

substrate: prostamide H(2)


enzyme_display_name: vitamin D 25-hydroxylase

substrate_name: vitamin D(2)

enzyme: vitamin D 25-hydroxylase

substrate: vitamin D(2)


organism: Pseudonocardia autotrophica

substrate_name: vitamin D(3)

substrate: vitamin D(3)


enzyme_display_name: L-methionine (R)-S-oxide reductase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: free methionine-R-sulfoxide

enzyme: L-methionine (R)-S-oxide reductase

substrate: free methionine-R-sulfoxide


organism: Clarkia breweri

substrate_name: benzylalcohol

substrate: benzylalcohol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


organism: Vitis vinifera

substrate_name: UDP-Glc (in the presence of quercitin)

substrate: UDP-Glc (in the presence of quercitin)


organism: Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)

substrate_name: agarose

substrate: agarose


organism: Polaromonas sp. (strain JS666 / ATCC BAA-500)

substrate_name: gamma-resorcylate

proof_lines: kcat is 0.44 sec(-1) with gamma-resorcylate as substrate. kcat is 0.47 sec(-1) with 2,3-dihydroxybenzoate as substrate. kcat is 0.18 sec(-1) with 2,4,6-trihydroxybenzoate as substrate. kcat is 0.38 sec(-1) with 2,6-dihydroxy-4-methylbenzoat

substrate: gamma-resorcylate


enzyme_display_name: sulfinoalanine decarboxylase

organism: Mus musculus

proof_lines: kcat is 3.6 sec(-1) with 3-sulfino-L-alanine (cysteine sulfinic acid) as substrate. kcat 1.3 sec(-1) is with L-aspartate as substrate.

enzyme: sulfinoalanine decarboxylase


proof_lines: kcat is 6.6 sec(-1) with 3-sulfino-L-alanine (cysteine sulfinic acid) as substrate. kcat is 0.14 sec(-1) with L-aspartate as substrate.


organism: Unknown prokaryotic organism

substrate_name: L-cysteine

proof_lines: kcat is 4.57 min(-1) with L-cysteine as substrate (Ref.2). kcat is 45.8 min(-1) with L-cysteine sulfinic acid as substrate (Ref.3).

substrate: L-cysteine


enzyme_display_name: galactarate dehydratase

organism: Escherichia coli (strain K12)

substrate_name: galactarate

enzyme: galactarate dehydratase

substrate: galactarate


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

substrate_name: L-talarate

proof_lines: kcat is 2.1 sec(-1) with L-talarate as substrate (PubMed:17649980). kcat is 3.6 sec(-1) with galactarate as substrate (PubMed:17649980). kcat is 4.8 sec(-1) with galactarate as substrate (PubMed:29248502).

substrate: L-talarate


enzyme_display_name: quercetin 2,3-dioxygenase

organism: Aspergillus flavus

substrate_name: quercetin

enzyme: quercetin 2,3-dioxygenase

substrate: quercetin


organism: Aspergillus niger


organism: Bacillus subtilis

sequence_source: UniProtKB:P42106 reviewed; direct EC+organism lookup

proof_lines: Mn quercetin 2,3-dioxygenase (1.8 atoms Mn/subunit)

proof_lines: Co quercetin 2,3-dioxygenase (0.65 atoms Co/subunit)


organism: Streptomyces sp.

assay_conditions_summary: pH 8; buffer pH 8

proof_lines: recombinant Co-QueD, 50 mM Tris-HCl buffer pH 8

proof_lines: recombinant Ni-QueD, 50 mM Tris-HCl buffer pH 8


organism: Bacillus tropicus

substrate_name: Pentachlorophenol

substrate: Pentachlorophenol


organism: Flavobacterium sp.


organism: Sphingobium chlorophenolicum

sequence_variant_note: Resolved canonical sequence from UniProtKB:P42535 reviewed; direct EC+organism lookup and applied mutation signature Y216F to reconstruct the assayed variant sequence.

mutation_type: substitution


sequence_source: UniProtKB:P42535 reviewed; direct EC+organism lookup

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P42535 reviewed; direct EC+organism lookup and applied mutation signature R235K to reconstruct the assayed variant sequence.


organism: Homo sapiens

substrate_name: vitamin D2

sequence_source: UniProtKB:Q6VVX0 reviewed; direct EC+organism lookup

substrate: vitamin D2


organism: Citrus sinensis

substrate_name: salicylate

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

substrate: salicylate


organism: Glycine max


organism: Solanum lycopersicum

substrate_name: S-adenosyl-L-methionine

proof_lines: in 50 mM Tris-HCl, pH 7.5, 100 mM KCl, at 25°C

substrate: S-adenosyl-L-methionine


enzyme_display_name: selenocysteine Se-methyltransferase

organism: Astragalus bisulcatus

substrate_name: L-selenocysteine

proof_lines: app. Km-value with [methyl-14C]S-adenosyl-L-methionine, pH 6.0, 30°C

enzyme: selenocysteine Se-methyltransferase

substrate: L-selenocysteine


organism: Clarkia breweri

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: isoform BEAT-1, in 250 mM Tris-HCl pH 7.5, 25 mM MgCl2, 25 mM KC1, 10 mM 2-mercaptoethanol, at 30°C

proof_lines: isoform BEAT-2, in 250 mM Tris-HCl pH 7.5, 25 mM MgCl2, 25 mM KC1, 10 mM 2-mercaptoethanol, at 30°C

substrate: acetyl-CoA


organism: Rattus norvegicus

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


organism: Sus scrofa

substrate_name: bufuralol

substrate: bufuralol


proof_lines: pH 7.4, 37°C, kcat for the conversion of (24S)-3beta-hydroxy-methyl-5alpha-cholesta-8(14),22-dien-15-one into side chain oxygenated products


organism: Streptomyces arenae

substrate_name: pentalenolactone F

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

substrate: pentalenolactone F


organism: Streptomyces exfoliatus


enzyme_display_name: methionine synthase

organism: Bos taurus

enzyme: methionine synthase


organism: Candida albicans

substrate_name: L-homocysteine

proof_lines: in 50 mM potassium phosphate (pH 7.2), 50 mM Tris-HCl (pH 7.2), 0.1 mM MgSO4, and 10 mM dithiothreitol, at 37°C

substrate: L-homocysteine


organism: Phaseolus vulgaris


organism: Zea mays

proof_lines: kcat is 22.7 sec(-1) for DIMBOA. kcat is 12.5 sec(-1) for DIBOA. kcat is 22.6 sec(-1) for UDPG.


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

substrate_name: norspermidine (at pH 9 and 37 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: kcat is 0.73 sec(-1) for aminopropyl transferase activity with S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees Celsius). kcat is 0.65 sec(-1) for aminopropyl transferase activity with spermidine as substrate (at pH 9 and 37 de


enzyme_display_name: mevalonate 3-kinase

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

substrate_name: ATP

proof_lines: kcat is 1.9 sec(-1) for mevalonate as substrate. kcat is 0.1 sec(-1) for 3-hydroxyisovalerate (3-HIV) as substrate. kcat is 0.1 sec(-1) for 3-hydroxybutyrate (3-HB) as substrate.

enzyme: mevalonate 3-kinase

substrate: ATP


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: (R)-mevalonate

proof_lines: kcat is 5.3 sec(-1) for ATP as substrate (PubMed:25422158). kcat is 5 sec(-1) for (R)-mevalonate as substrate (PubMed:24914732).

substrate: (R)-mevalonate


organism: Acinetobacter baumannii (strain IS-123)

substrate_name: HMP

proof_lines: kcat is 0.19 sec(-1) with HMP as substrate.

substrate: HMP


organism: Haemophilus influenzae

substrate_name: D-ribulose 5-phosphate

proof_lines: kcat is 22 sec(-1) for the reductase reaction. kcat is 13 sec(-1) for the cytidyltransferase reaction.

substrate: D-ribulose 5-phosphate


enzyme_display_name: [protein-PII] uridylyltransferase

organism: Escherichia coli (strain K12)

substrate_name: GlnB protein

proof_lines: kcat is 137 min(-1) for the UTase reaction. kcat is 2.7 min(-1) for the UR reaction in the absence of glutamine, and 6.5 min(-1) in the presence of 2.5 mM glutamine.

enzyme: [protein-PII] uridylyltransferase

substrate: GlnB protein


enzyme_display_name: apo-salmochelin esterase

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

substrate_name: Ent

proof_lines: kcat is 375 min(-1) with Ent as substrate. kcat is 3.0 min(-1) with Fe-Ent as substrate. kcat is 430 min(-1) with MGE as substrate. kcat is 3.2 min(-1) with Fe-MGE as substrate. kcat is 320 min(-1) with DGE as substrate. kcat is 2.5 min(-1)

enzyme: apo-salmochelin esterase

substrate: Ent


organism: Mus musculus

proof_lines: kcat is 0.1 sec(-1) with glycerol-3-phosphate.


enzyme_display_name: beta-agarase

organism: Microbulbifer thermotolerans

substrate_name: agar

proof_lines: The catalytic efficiency for agar is 3 orders of magnitude greater than that for neoagarohexaose.

enzyme: beta-agarase

substrate: agar


organism: Wenyingzhuangia aestuarii

substrate_name: funoran

proof_lines: kcat is 3.95 sec(-1) with funoran as substrate (PubMed:37479453). kcat is 176.74 sec(-1) with agarose as substrate (PubMed:32578425).

substrate: funoran


organism: Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)

substrate_name: agarose

substrate: agarose


substrate_name: S-adenosylmethioninamine; spermidine

substrate: S-adenosylmethioninamine; spermidine


organism: Homo sapiens


proof_lines: mutant enzyme S165D/L175E/T178H/C206R, at pH 7.5 and 37°C


organism: Mammalia

substrate_name: S-Adenosylmethioninamine; Spermidine

ki_unit: mM

substrate: S-Adenosylmethioninamine; Spermidine


substrate_name: Unknown

substrate: Unknown


organism: Rattus norvegicus

substrate_name: 7-Monofluorospermidine; S-adenosylmethioninamine; spermidine; fluorinated spermidine analogues


organism: Glycine max

substrate_name: ATP; myo-inositol-1,3,4-trisphosphate

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

substrate: ATP; myo-inositol-1,3,4-trisphosphate


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

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Escherichia coli

substrate_name: pyridoxine; ATP; 2-methyl-4-amino-5-hydroxymethylpyrimidine; pyridoxamine; pyridoxal

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


organism: Plasmodium falciparum

assay_conditions_summary: pH 7.5; buffer 100 mM triethanolamine or 50 mM potassium phosphate; cofactor ATP

proof_lines: apparent value, in 100 mM triethanolamine or 50 mM potassium phosphate buffer, pH 7.5, 1 mM MgCl2, 500 mM ATP and 100 mM substrate


enzyme_display_name: inositol-hexakisphosphate 5-kinase

substrate_name: ATP; Inositol hexakisphosphate; ADP; 5-diphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate

assay_conditions_summary: pH 6.8; 310.15 K; cofactor ATP

proof_lines: pH and temperature not specified in the publication

enzyme: inositol-hexakisphosphate 5-kinase


organism: Clarkia concinna

substrate_name: benzyl alcohol

proof_lines: isoform BEAT-1, in 250 mM Tris-HCl pH 7.5, 25 mM MgCl2, 25 mM KC1, 10 mM 2-mercaptoethanol, at 30°C

proof_lines: isoform BEAT-2, in 250 mM Tris-HCl pH 7.5, 25 mM MgCl2, 25 mM KC1, 10 mM 2-mercaptoethanol, at 30°C

substrate: benzyl alcohol


organism: Jasminum sambac

substrate_name: acetyl-CoA

proof_lines:
isoform BEAT2, pH 7.5, 30°C
isoform BEAT1, pH 7.5, 30°C

substrate: acetyl-CoA


organism: Brassica oleracea

substrate_name: cyanidin

substrate: cyanidin


organism: Daucus carota


organism: Pericallis hybrida

substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Silene dioica

substrate_name: UDPglucose

substrate: UDPglucose


organism: Vitis vinifera


organism: Xanthisma gracile


organism: Zea mays

proof_lines: reaction with 2,4-dihydroxy-1,4-benzoxazin-3-one, enzyme in peak 2


enzyme_display_name: kaempferol 3-O-galactosyltransferase

organism: Eriobotrya japonica

substrate_name: quercetin

enzyme: kaempferol 3-O-galactosyltransferase

substrate: quercetin


organism: Petunia sp.

substrate_name: UDP

proof_lines: cosubstrate kaempferol 3-O-beta-D-galactoside, reverse reaction

substrate: UDP


organism: Vigna mungo

substrate_name: kaempferol

proof_lines:
pH 8, 30°C
pH 8, 30°C, cosubstrate kaempferol

substrate: kaempferol


organism: Saccharomyces cerevisiae

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


organism: Trypanosoma cruzi

substrate_name: p-nitrophenyl-alpha-D-mannoside

substrate: p-nitrophenyl-alpha-D-mannoside


organism: Alteromonas sp.

substrate_name: neoagarohexaose

substrate: neoagarohexaose


organism: Microbulbifer elongatus

substrate_name: beta-4-nitrophenyl galactopyranoside

substrate: beta-4-nitrophenyl galactopyranoside


organism: Saccharophagus degradans

substrate_name: agarose

assay_conditions_summary: pH 7; 303.15 K; buffer 20 mM Tris-HCl

proof_lines: in 20 mM Tris-HCl buffer (pH 7.0), at 30°C


organism: Streptomyces coelicolor

assay_conditions_summary: pH 7; 313.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer, pH 7.0, 40°C


organism: Zobellia galactanivorans

substrate_name: liquid-phase agarose

proof_lines: AgaB AgaAc

substrate: liquid-phase agarose


enzyme_display_name: bacillolysin

organism: Geobacillus stearothermophilus

substrate_name: Unknown

enzyme: bacillolysin


organism: Priestia megaterium

substrate_name: plasminogen

substrate: plasminogen


enzyme_display_name: creatininase

organism: Homo sapiens

substrate_name: creatinine

enzyme: creatininase

substrate: creatinine


organism: Paenarthrobacter ureafaciens


organism: Pseudomonas putida


organism: Phycomyces blakesleeanus

substrate_name: dihydroxyacetone phosphate

substrate: dihydroxyacetone phosphate


substrate_name: NADH; Glycerone phosphate

assay_conditions_summary: cofactor NADH

substrate: NADH; Glycerone phosphate


substrate_name: H2O; Glycerol 3-phosphate

proof_lines:
for Gpp1p
for Gpp2p

substrate: H2O; Glycerol 3-phosphate


organism: Aspergillus phoenicis

sequence_variant_note: Resolved canonical sequence from UniProtKB Q12563 reviewed canonical sequence; C363A reconstructed during review from PMID 16306691 mutation label and applied mutation signature C363A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q12563 reviewed canonical sequence; C443A reconstructed during review from PMID 16306691 mutation label and applied mutation signature C443A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q12563 reviewed canonical sequence anchored by PMID 16306691 wild-type Aspergillus saitoi/A. phoenicis enzyme context


sequence_variant_note: Resolved canonical sequence from UniProtKB Q12563 reviewed canonical sequence; C334A reconstructed during review from PMID 16306691 mutation label and applied mutation signature C334A to reconstruct the assayed variant sequence.


substrate_name: mannobiose

assay_conditions_summary: pH 5

substrate: mannobiose


organism: Candida albicans


organism: Penicillium citrinum

substrate: Unknown


organism: Rattus norvegicus


organism: Ricinus communis


organism: Pseudomonas sp.


enzyme_display_name: UDP-sugar diphosphatase

organism: Escherichia coli

substrate_name: UDP-glucose

proof_lines:
pH 7.5, 37°C
with 5 mM CoSO4, pH 8.0, 37 °C
with 5 mM MgCl2, pH 8.0, 25 °C

enzyme: UDP-sugar diphosphatase


organism: Saccharomyces cerevisiae


enzyme_display_name: gamma-resorcylate decarboxylase

organism: Agrobacterium tumefaciens

enzyme: gamma-resorcylate decarboxylase


organism: Aedes aegypti

substrate_name: L-cysteine sulfinate

proof_lines: mutant Q37L, 25°C, pH not specified in the publication

substrate: L-cysteine sulfinate


proof_lines: mutant Q377L, 25°C, pH not specified in the publication


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


organism: Bos taurus

substrate_name: cysteine sulfinic acids

substrate: cysteine sulfinic acids


substrate_name: cysteine sulfinate

proof_lines:
minor enzyme form
liver enzyme
brain enzyme

substrate: cysteine sulfinate


organism: Sus scrofa

proof_lines: CSADII fusion protein with beta-galactosidase

proof_lines: CSADI fusion protein with beta-galactosidase


enzyme_display_name: sphinganine-1-phosphate aldolase

assay_conditions_summary: pH 10.6; 310.15 K; buffer conditions

proof_lines: in 0.6 mM EDTA, 0.4 mM pyridoxal 5-phosphate, 3 mM dithiothreitol mM sucrose, 36 mM potassium phosphate buffer, and 36 mM NaF containing 0.08% Triton X-100

enzyme: sphinganine-1-phosphate aldolase


organism: Mus musculus

substrate_name: sphingosine 1-phosphate

proof_lines: in 35 mM potassium phosphate buffer (pH 7.4), 0.6 mM EDTA, 70 mM sucrose, 36 mM sodium fluoride, 0.57 mM pyridoxal 5-phosphate, at 37°C

substrate: sphingosine 1-phosphate


organism: Xenopus sp.

substrate_name: Inositol hexakisphosphate

substrate: Inositol hexakisphosphate


organism: Arabidopsis thaliana

substrate_name: DL-glycerol 3-phosphate

assay_conditions_summary: pH 7

proof_lines: Gpp2, in 20 mM Tris-HCl pH 7.0, 5 mM MgCl2, and 10 mM DL-glycerol-3-phosphate

proof_lines: Gpp1, in 20 mM Tris-HCl pH 7.0, 5 mM MgCl2, and 10 mM DL-glycerol-3-phosphate

substrate: DL-glycerol 3-phosphate


organism: Corynebacterium glutamicum

substrate_name: L-glycerol 3-phosphate

proof_lines: with DL-glycerol-3-phosphate as substrate, at 30°C, pH 7.5, in 100 mM HEPES

proof_lines: with L-glycerol-3-phosphate as substrate, at 30°C, pH 7.5, in 100 mM HEPES

substrate: L-glycerol 3-phosphate


organism: Dunaliella salina


organism: Dunaliella tertiolecta


proof_lines: in 20 mM MES buffer pH 6.5, containing 10 mM MgSO4, and 1 mM dithioerythritol, at 30°C


organism: Osmerus mordax

substrate_name: glycerol 3-phosphate

proof_lines: at pH 5.5, temperature not specified in the publication

substrate: glycerol 3-phosphate


organism: Tetrahymena pyriformis

substrate_name: sphinganine 1-phosphate

substrate: sphinganine 1-phosphate


enzyme_display_name: chorismate lyase

substrate_name: chorismate

sequence_source: UniProt:P26602; PubMed:11825618 literature cross-reference

proof_lines: pH 7.5, wild-type enzyme, initial rate analysis

proof_lines: pH 7.5, wild-type enzyme, progress curve analysis

enzyme: chorismate lyase

substrate: chorismate


proof_lines: pH 7.5, mutant enzyme C14S/C81S, initial rate analysis

proof_lines: pH 7.5, mutant enzyme C14S/C81S, progress curve analysis


organism: Mycobacterium tuberculosis

sequence_source: UniProt:P9WIC5; PubMed:16210318 literature cross-reference

proof_lines: pH 7.5, 37°C, recombinant enzyme produced in Mycobacterium smegmatis

proof_lines: pH 7.5, 37°C, recombinant enzyme produced in Escherichia coli


organism: Stenotrophomonas maltophilia

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


enzyme_display_name: methylglutaconyl-CoA hydratase

organism: Homo sapiens

assay_conditions_summary: cofactor CoA

proof_lines:
lymphocyte enzyme
fibroblast enzyme

enzyme: methylglutaconyl-CoA hydratase


organism: Pseudomonas putida

assay_conditions_summary: pH 7.9; 298.15 K; cofactor CoA

proof_lines:
pH 7.9, 25°C, wild-type enzyme
pH 7.09, 25°C, wild-type enzyme


enzyme_display_name: galactarate dehydratase

substrate_name: meso-galactarate

sequence_source: UniProt:A9CG74; PubMed:24926996 abstract accession/locus anchor

enzyme: galactarate dehydratase

substrate: meso-galactarate


organism: Escherichia coli

substrate_name: galactarate

sequence_source: UniProt:P39829; PubMed:9772162 literature cross-reference

substrate: galactarate


organism: Oceanobacillus iheyensis

sequence_source: UniProtKB Q8EMJ9 canonical sequence; RCSB 3HPF/PMID 19883118 identity anchor

assay_conditions_summary: pH 8

proof_lines: wild-type, in 50 mM Hepes, pH 8.0, 5 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8EMJ9 canonical sequence; RCSB 3HPF/PMID 19883118 identity anchor and applied mutation signature H45Q to reconstruct the assayed variant sequence.

proof_lines: mutant H45Q, in 50 mM Hepes, pH 8.0, 5 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8EMJ9 canonical sequence; RCSB 3HPF/PMID 19883118 identity anchor and applied mutation signature Y90F to reconstruct the assayed variant sequence.

proof_lines: mutant Y90F, in 50 mM Hepes, pH 8.0, 5 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8EMJ9 canonical sequence; RCSB 3HPF/PMID 19883118 identity anchor and applied mutation signature R162N to reconstruct the assayed variant sequence.

proof_lines: mutant R162N, in 50 mM Hepes, pH 8.0, 5 mM MgCl2


enzyme_display_name: ferric-chelate reductase (NADH)

organism: Paracoccus denitrificans

substrate_name: Fe(3+)EGTA and NADH

sequence: MVKTVAVMVGSLRKDSLAHKLMKVLQK

wild_type_sequence: MVKTVAVMVGSLRKDSLAHKLMKVLQK

enzyme: ferric-chelate reductase (NADH)

substrate: Fe(3+)EGTA and NADH


organism: Vibrio vulnificus

substrate_name: Unknown


organism: Beta vulgaris

substrate_name: Fe3+; NADH; H+

substrate: Fe3+; NADH; H+


substrate_name: NADH

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH

substrate: NADH


substrate_name: NADH; Fe3+; H+

sequence: SRLPPATRDKLADEITFFPA

wild_type_sequence: SRLPPATRDKLADEITFFPA

substrate: NADH; Fe3+; H+


organism: Solanum lycopersicum

substrate_name: NADH; H+; Fe3+

substrate: NADH; H+; Fe3+


substrate_name: glutaredoxin 1

substrate: glutaredoxin 1


organism: Myxococcus xanthus

substrate_name: arsenate

proof_lines: at pH 9.0, temperature not specified in the publication

substrate: arsenate


organism: Pteris vittata


organism: Saccharomyces cerevisiae

substrate_name: glutaredoxin

proof_lines: glutaredoxin 1p from Saccharomyces cerevisiae or glutaredoxin 1 from E. coli

substrate: glutaredoxin


enzyme_display_name: cyanuric acid amidohydrolase

organism: Neomoorella thermoacetica

substrate_name: cyanuric acid

enzyme: cyanuric acid amidohydrolase

substrate: cyanuric acid


organism: Paracidovorax citrulli


organism: Pseudomonas sp.

assay_conditions_summary: pH 8; cofactor ADP


enzyme_display_name: L-lysine 6-transaminase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

sequence_source: UniProt P9WQ77; RCSB 2CJH entity 1/SIFTS maps the PMID 16950391 structure to P9WQ77

enzyme: L-lysine 6-transaminase


enzyme_display_name: sedoheptulose-bisphosphatase

organism: Spinacia oleracea

substrate_name: Fructose 1,6-bisphosphate

enzyme: sedoheptulose-bisphosphatase

substrate: Fructose 1,6-bisphosphate


substrate_name: sedoheptulose 1,7-bisphosphate

substrate: sedoheptulose 1,7-bisphosphate


organism: Synechocystis sp.


organism: Acidovorax citrulli

substrate_name: Cyanuric acid; H2O

substrate: Cyanuric acid; H2O


organism: Azorhizobium caulinodans

verification_status: verified

column_label: Table 2 (Kinetic constants of various cyanuric acid hydrolase/barbiturase family enzymes, using cyanuric acid as a substrate) prints one enzyme-label column, 'Enzyme name and /or organism (reference)', followed by three numeric columns whose heads are kcat (s^-1), Km (uM) and kcat/Km (s^-1 M^-1) in that printed order. The cited cell set is Table 2, enzyme row Azorhizobium caulinodans ORS 571 locus AZC_3892: kcat (s^-1) = 50; Km (uM) = 370; kcat/Km (s^-1 M^-1) = 1.3 x 10^5. The printed uncertainties of that row are kcat 50 +/- 9, Km 370 +/- 90 and kcat/Km (1.3 +/- 0.6) x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 50 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 50.0 s^(-1). Km: printed Table 2 cell 370 uM; 370 / 1000 = 0.37, so the paper value is 0.37 mM. kcat/Km: printed Table 2 cell 1.3 x 10^5 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^5 / 1000 = 130.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row Azorhizobium caulinodans ORS 571 locus AZC_3892: kcat = 50 s-1; Km = 370 uM; printed kcat/Km = 1.3 x 10^5 s-1 M-1.

table_label: Table 2: Kinetic constants of various cyanuric acid hydrolase/barbiturase family enzymes, using cyanuric acid as a substrate (J Bacteriol 2012, 194(17):4579-4588)

status: verified


organism: Bradyrhizobium diazoefficiens

substrate_name: H2O; Cyanuric acid

column_label: Table 2 (Kinetic constants of various cyanuric acid hydrolase/barbiturase family enzymes, using cyanuric acid as a substrate) prints one enzyme-label column, 'Enzyme name and /or organism (reference)', followed by three numeric columns whose heads are kcat (s^-1), Km (uM) and kcat/Km (s^-1 M^-1) in that printed order. The cited cell set is Table 2, enzyme row Bradyrhizobium japonicum USDA 110: kcat (s^-1) = 9.3; Km (uM) = 50; kcat/Km (s^-1 M^-1) = 1.9 x 10^5. The printed uncertainties of that row are kcat 9.3 +/- 0.7, Km 50 +/- 10 and kcat/Km (1.9 +/- 0.5) x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 9.3 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 9.3 s^(-1). Km: printed Table 2 cell 50 uM; 50 / 1000 = 0.05, so the paper value is 0.05 mM. kcat/Km: printed Table 2 cell 1.9 x 10^5 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^5 / 1000 = 190.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row Bradyrhizobium japonicum USDA 110: kcat = 9.3 s-1; Km = 50 uM; printed kcat/Km = 1.9 x 10^5 s-1 M-1.

substrate: H2O; Cyanuric acid


organism: Bradyrhizobium sp.


organism: Methylobacterium sp.

column_label: Table 2 (Kinetic constants of various cyanuric acid hydrolase/barbiturase family enzymes, using cyanuric acid as a substrate) prints one enzyme-label column, 'Enzyme name and /or organism (reference)', followed by three numeric columns whose heads are kcat (s^-1), Km (uM) and kcat/Km (s^-1 M^-1) in that printed order. The cited cell set is Table 2, enzyme row Methylobacterium sp. 4-46: kcat (s^-1) = 17; Km (uM) = 69; kcat/Km (s^-1 M^-1) = 2.5 x 10^5. The printed uncertainties of that row are kcat 17 +/- 2, Km 69 +/- 16 and kcat/Km (2.5 +/- 0.9) x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 17 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 17.0 s^(-1). Km: printed Table 2 cell 69 uM; 69 / 1000 = 0.069, so the paper value is 0.069 mM. kcat/Km: printed Table 2 cell 2.5 x 10^5 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 x 10^5 / 1000 = 250.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row Methylobacterium sp. 4-46: kcat = 17 s-1; Km = 69 uM; printed kcat/Km = 2.5 x 10^5 s-1 M-1.


organism: Moorella thermoacetica


organism: Nocardioides sp.


organism: Pseudomonas pseudoalcaligenes


assay_conditions_summary: pH 8; 295.15 K; cofactor ADP


organism: Homo sapiens

substrate_name: GPC

substrate: GPC


organism: Oryza sativa

substrate_name: Reduced glutaredoxin; Arsenate; H+; Reduced glutathione

sequence_variant_note: Resolved canonical sequence from direct UniProt lookup Q10SX6 with C70S reconstruction and applied mutation signature C70S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arsenate reductase (glutaredoxin)(Enzyme) mutant C70S ACR2.2, N-terminal His-tag


substrate_name: Reduced glutaredoxin; H+; Arsenate; Reduced glutathione

proof_lines: SABIO-RK modifier species: arsenate reductase (glutaredoxin)(Enzyme) mutant C71S ACR2.1, N-terminal His-tag


sequence_source: direct UniProt lookup Q336V5

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

substrate: Reduced glutaredoxin; H+; Arsenate; Reduced glutathione


sequence_source: direct UniProt lookup Q10SX6


organism: Pteris vittata

sequence_source: direct UniProt lookup Q1A5X4


organism: Saccharomyces cerevisiae

substrate_name: Reduced glutathione; Reduced glutaredoxin; H+; Arsenate

sequence_variant_note: Resolved canonical sequence from direct UniProt lookup Q06597 with H118A reconstruction and applied mutation signature H118A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arsenate reductase (glutaredoxin)(Enzyme) mutant H118A


substrate_name: Reduced glutathione; H+; Reduced glutaredoxin; Arsenate

sequence_variant_note: Resolved canonical sequence from direct UniProt lookup Q06597 with C106S reconstruction and applied mutation signature C106S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arsenate reductase (glutaredoxin)(Enzyme) mutant C106S


substrate_name: Arsenate; Reduced glutaredoxin; Reduced glutathione; H+

sequence_variant_note: Resolved canonical sequence from direct UniProt lookup Q06597 with C119S reconstruction and applied mutation signature C119S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arsenate reductase (glutaredoxin)(Enzyme) mutant C119S


substrate_name: Reduced glutathione; Arsenate; H+; Reduced glutaredoxin

sequence_variant_note: Resolved canonical sequence from direct UniProt lookup Q06597 with H75A reconstruction and applied mutation signature H75A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arsenate reductase (glutaredoxin)(Enzyme) mutant H75A


sequence_variant_note: Resolved canonical sequence from direct UniProt lookup Q06597 with R120A reconstruction and applied mutation signature R120A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arsenate reductase (glutaredoxin)(Enzyme) mutant R120A

substrate: Reduced glutathione; H+; Reduced glutaredoxin; Arsenate


substrate_name: Arsenate; Reduced glutaredoxin; H+; Reduced glutathione

sequence_source: direct UniProt lookup Q06597

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


organism: Staphylococcus aureus

sequence_variant_note: Resolved canonical sequence from direct UniProt lookup P0A006 with D105A reconstruction and applied mutation signature D105A to reconstruct the assayed variant sequence.


substrate_name: Arsenate; Reduced thioredoxin

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: arsenate reductase (glutaredoxin)(Enzyme) mutant D105A

substrate: Arsenate; Reduced thioredoxin


sequence_source: direct UniProt lookup P74313

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


sequence_variant_note: Resolved canonical sequence from direct UniProt lookup P74313 with C35A reconstruction and applied mutation signature C35A to reconstruct the assayed variant sequence.

proof_lines: mutant C35A, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct UniProt lookup P74313 with C13A reconstruction and applied mutation signature C13A to reconstruct the assayed variant sequence.

proof_lines: mutant C13A, pH 7.5, temperature not specified in the publication


organism: Arabidopsis thaliana

substrate_name: para-nitrophenyl phosphate

substrate: para-nitrophenyl phosphate


organism: Oryza sativa subsp. japonica

substrate_name: arsenate


organism: Rhizobium meliloti (strain 1021)


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

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: sedoheptulose 1,7-bisphosphate (SBP)

substrate: sedoheptulose 1,7-bisphosphate (SBP)


organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

substrate_name: fructose-1,6-bisphosphate (at pH 8)

substrate: fructose-1,6-bisphosphate (at pH 8)


organism: Bos taurus

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


organism: Pseudomonas sp.

substrate_name: cyanuric acid

sequence_source: identity_reuse_cache accession:P58329 plus direct UniProt REST accession lookup

column_label: Table 2 (Kinetic constants of various cyanuric acid hydrolase/barbiturase family enzymes, using cyanuric acid as a substrate) prints one enzyme-label column, 'Enzyme name and /or organism (reference)', followed by three numeric columns whose heads are kcat (s^-1), Km (uM) and kcat/Km (s^-1 M^-1) in that printed order. The cited cell set is Table 2, enzyme row Pseudomonas sp. ADP AtzD (this study): kcat (s^-1) = 73; Km (uM) = 23; kcat/Km (s^-1 M^-1) = 3.2 x 10^6. The printed uncertainties of that row are kcat 73 +/- 6, Km 23 +/- 7 and kcat/Km (3.2 +/- 1.2) x 10^6.

normalized_value_unit_evidence: kcat: printed Table 2 cell 73 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 73.0 s^(-1). Km: printed Table 2 cell 23 uM; 23 / 1000 = 0.023, so the paper value is 0.023 mM. kcat/Km: printed Table 2 cell 3.2 x 10^6 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.2 x 10^6 / 1000 = 3200.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row Pseudomonas sp. ADP AtzD (this study): kcat = 73 s-1; Km = 23 uM; printed kcat/Km = 3.2 x 10^6 s-1 M-1.


organism: Pseudomonas sp. ADP

assay_conditions_summary: pH 9; 295.15 K; cofactor ADP


proof_lines: pH 9, 22°C, purified from Pseudomonas sp. ADP


organism: Pseudonocardia dioxanivorans

sequence_source: identity_reuse_cache accession:F4CUJ4 plus direct UniProt REST accession lookup


organism: Rhizobium leguminosarum

sequence_source: identity_reuse_cache accession:Q1M7F3 plus direct UniProt REST accession lookup

column_label: Table 2 (Kinetic constants of various cyanuric acid hydrolase/barbiturase family enzymes, using cyanuric acid as a substrate) prints one enzyme-label column, 'Enzyme name and /or organism (reference)', followed by three numeric columns whose heads are kcat (s^-1), Km (uM) and kcat/Km (s^-1 M^-1) in that printed order. The cited cell set is Table 2, enzyme row Rhizobium leguminosarum bv. viciae 3841: kcat (s^-1) = 5; Km (uM) = 130; kcat/Km (s^-1 M^-1) = 3.8 x 10^4. The printed uncertainties of that row are kcat 5 +/- 1, Km 130 +/- 60 and kcat/Km (3.8 +/- 2.5) x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 5.0 s^(-1). Km: printed Table 2 cell 130 uM; 130 / 1000 = 0.13, so the paper value is 0.13 mM. kcat/Km: printed Table 2 cell 3.8 x 10^4 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.8 x 10^4 / 1000 = 38.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row Rhizobium leguminosarum bv. viciae 3841: kcat = 5 s-1; Km = 130 uM; printed kcat/Km = 3.8 x 10^4 s-1 M-1.


sequence_source: direct UniProt REST accession lookup


enzyme_display_name: linoleate 11-lipoxygenase

organism: Fusarium oxysporum

substrate_name: linolenate

assay_conditions_summary: pH 9

proof_lines: pH 9.0, temperature not specified in the publication, recombinant enzyme

enzyme: linoleate 11-lipoxygenase

substrate: linolenate


organism: Gaeumannomyces graminis

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

proof_lines: pH 9.0, temperature not specified in the publication, mutants L336A and L336F


proof_lines: pH 9.0, temperature not specified in the publication, mutant F337I


proof_lines: pH 9.0, temperature not specified in the publication, mutant L336V


proof_lines: pH 9.0, temperature not specified in the publication, wild-type enzyme


substrate_name: linoleic acid

proof_lines:
pH 7.5, 18:3n-3 substrate
pH 9.0, 21°C

substrate: linoleic acid


organism: Cyberlindnera jadinii

substrate_name: L-lysine

substrate: L-lysine


organism: [Flavobacterium] lutescens

proof_lines:
pH 8.0, 37°C
L-lysine, pH 8.0, 37°C
cosubstrate L-ornithine, pH 8.0, 37°C


organism: Haemophilus influenzae

substrate_name: D-ribitol 5-phosphate

substrate: D-ribitol 5-phosphate


substrate_name: D-Ribitol 5-phosphate; CTP

substrate: D-Ribitol 5-phosphate; CTP


sequence_source: UniProtKB reviewed accession Q8X150


substrate_name: (13R)-hydroperoxylinolenic acid

sequence_source: UniProtKB reviewed accession Q8X151

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8X151 and applied mutation signature G316A to reconstruct the assayed variant sequence.

substrate: (13R)-hydroperoxylinolenic acid


substrate_name: linoleate

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

substrate: linoleate


substrate_name: O2; alpha-Linolenate

substrate: O2; alpha-Linolenate


smiles: O=O


substrate_name: alpha-Linolenate

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

substrate: alpha-Linolenate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q93ZN9 and applied mutation signature P398S to reconstruct the assayed variant sequence.

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

assay_conditions_summary: pH 8; 310.15 K; buffer an assay

column_label: Table 3. Kinetic Parameters of Recombinant AGD2- and ALD1-Catalyzed Reactions for Amino Acid Degradation Using Either Lys, Ala, or Arg with 2-Oxoglutarate (The Plant Cell 16, 353-366, 2004); printed columns Substrate, Cosubstrate (mM), Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); enzyme row 'AGD2P398S', Substrate column 2-oxoglutarate, Cosubstrate (mM) column Lys (100 mM); column 'Km (mM)' = 1.92; column 'kcat (s^-1)' = 1.83; column 'kcat/Km (mM^-1 s^-1)' = 0.95.

normalized_value_unit_evidence: Km: printed cell 1.92 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 1.92 mM. kcat: printed cell 1.83 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 1.83 s^(-1). kcat/Km: printed cell 0.95 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 0.95 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 1.83 / 1.92 = 0.9531250000000001 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'AGD2P398S', Substrate column 2-oxoglutarate, Cosubstrate (mM) column Lys (100 mM): Km = 1.92 mM; kcat = 1.83 s^-1; printed kcat/Km = 0.95 mM^-1 s^-1.

row_label: Table 3, enzyme row 'AGD2P398S' with Substrate column 2-oxoglutarate and Cosubstrate (mM) column Lys (100 mM)


substrate_name: L-Lysine

column_label: Table 3. Kinetic Parameters of Recombinant AGD2- and ALD1-Catalyzed Reactions for Amino Acid Degradation Using Either Lys, Ala, or Arg with 2-Oxoglutarate (The Plant Cell 16, 353-366, 2004); printed columns Substrate, Cosubstrate (mM), Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); enzyme row 'AGD2P398S', Substrate column Lys, Cosubstrate (mM) column 2-oxoglutarate (100 mM); column 'Km (mM)' = 71.4; column 'kcat (s^-1)' = 2.87; column 'kcat/Km (mM^-1 s^-1)' = 0.040.

normalized_value_unit_evidence: Km: printed cell 71.4 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 71.4 mM. kcat: printed cell 2.87 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 2.87 s^(-1). kcat/Km: printed cell 0.040 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 0.04 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 2.87 / 71.4 = 0.040196078431372545 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'AGD2P398S', Substrate column Lys, Cosubstrate (mM) column 2-oxoglutarate (100 mM): Km = 71.4 mM; kcat = 2.87 s^-1; printed kcat/Km = 0.040 mM^-1 s^-1.

row_label: Table 3, enzyme row 'AGD2P398S' with Substrate column Lys and Cosubstrate (mM) column 2-oxoglutarate (100 mM)

substrate: L-Lysine


sequence_source: UniProtKB reviewed accession Q9ZQI7

column_label: Table 3. Kinetic Parameters of Recombinant AGD2- and ALD1-Catalyzed Reactions for Amino Acid Degradation Using Either Lys, Ala, or Arg with 2-Oxoglutarate (The Plant Cell 16, 353-366, 2004); printed columns Substrate, Cosubstrate (mM), Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); enzyme row 'ALD1', Substrate column 2-oxoglutarate, Cosubstrate (mM) column Lys (100 mM); column 'Km (mM)' = 2.63; column 'kcat (s^-1)' = 3.75; column 'kcat/Km (mM^-1 s^-1)' = 1.43.

normalized_value_unit_evidence: Km: printed cell 2.63 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 2.63 mM. kcat: printed cell 3.75 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 3.75 s^(-1). kcat/Km: printed cell 1.43 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 1.43 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 3.75 / 2.63 = 1.4258555133079849 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'ALD1', Substrate column 2-oxoglutarate, Cosubstrate (mM) column Lys (100 mM): Km = 2.63 mM; kcat = 3.75 s^-1; printed kcat/Km = 1.43 mM^-1 s^-1.

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


column_label: Table 3. Kinetic Parameters of Recombinant AGD2- and ALD1-Catalyzed Reactions for Amino Acid Degradation Using Either Lys, Ala, or Arg with 2-Oxoglutarate (The Plant Cell 16, 353-366, 2004); printed columns Substrate, Cosubstrate (mM), Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); enzyme row 'ALD1', Substrate column Lys, Cosubstrate (mM) column 2-oxoglutarate (50 mM); column 'Km (mM)' = 0.53; column 'kcat (s^-1)' = 4.42; column 'kcat/Km (mM^-1 s^-1)' = 8.34.

normalized_value_unit_evidence: Km: printed cell 0.53 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 0.53 mM. kcat: printed cell 4.42 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 4.42 s^(-1). kcat/Km: printed cell 8.34 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 8.34 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 4.42 / 0.53 = 8.339622641509433 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'ALD1', Substrate column Lys, Cosubstrate (mM) column 2-oxoglutarate (50 mM): Km = 0.53 mM; kcat = 4.42 s^-1; printed kcat/Km = 8.34 mM^-1 s^-1.

row_label: Table 3, enzyme row 'ALD1' with Substrate column Lys and Cosubstrate (mM) column 2-oxoglutarate (50 mM)


substrate_name: 2-Oxoglutarate; L-Lysine

sequence_source: UniProtKB reviewed accession Q93ZN9

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q93ZN9 and applied mutation signature P398S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-lysine 6-transaminase(Enzyme) mutant His6-AGD2 P398S

substrate: 2-Oxoglutarate; L-Lysine


substrate_name: L-Lysine; 2-Oxoglutarate

substrate: L-Lysine; 2-Oxoglutarate


column_label: Table 3. Kinetic Parameters of Recombinant AGD2- and ALD1-Catalyzed Reactions for Amino Acid Degradation Using Either Lys, Ala, or Arg with 2-Oxoglutarate (The Plant Cell 16, 353-366, 2004); printed columns Substrate, Cosubstrate (mM), Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); enzyme row 'AGD2', Substrate column Lys, Cosubstrate (mM) column 2-oxoglutarate (100 mM); column 'Km (mM)' = 58.8; column 'kcat (s^-1)' = 5.33; column 'kcat/Km (mM^-1 s^-1)' = 0.091.

normalized_value_unit_evidence: Km: printed cell 58.8 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 58.8 mM. kcat: printed cell 5.33 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 5.33 s^(-1). kcat/Km: printed cell 0.091 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 0.091 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 5.33 / 58.8 = 0.09064625850340137 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'AGD2', Substrate column Lys, Cosubstrate (mM) column 2-oxoglutarate (100 mM): Km = 58.8 mM; kcat = 5.33 s^-1; printed kcat/Km = 0.091 mM^-1 s^-1.

row_label: Table 3, enzyme row 'AGD2' with Substrate column Lys and Cosubstrate (mM) column 2-oxoglutarate (100 mM)


column_label: Table 3. Kinetic Parameters of Recombinant AGD2- and ALD1-Catalyzed Reactions for Amino Acid Degradation Using Either Lys, Ala, or Arg with 2-Oxoglutarate (The Plant Cell 16, 353-366, 2004); printed columns Substrate, Cosubstrate (mM), Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); enzyme row 'AGD2', Substrate column 2-oxoglutarate, Cosubstrate (mM) column Lys (100 mM); column 'Km (mM)' = 1.82; column 'kcat (s^-1)' = 2.83; column 'kcat/Km (mM^-1 s^-1)' = 1.55.

normalized_value_unit_evidence: Km: printed cell 1.82 mM; the printed column head is Km (mM), so no unit conversion applies and the paper value is 1.82 mM. kcat: printed cell 2.83 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 2.83 s^(-1). kcat/Km: printed cell 1.55 mM^-1 s^-1; the printed column head is kcat/Km (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 1.55 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 2.83 / 1.82 = 1.554945054945055 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'AGD2', Substrate column 2-oxoglutarate, Cosubstrate (mM) column Lys (100 mM): Km = 1.82 mM; kcat = 2.83 s^-1; printed kcat/Km = 1.55 mM^-1 s^-1.

row_label: Table 3, enzyme row 'AGD2' with Substrate column 2-oxoglutarate and Cosubstrate (mM) column Lys (100 mM)


organism: Fusarium oxysporum (strain Fo5176)


organism: Gaeumannomyces avenae

substrate_name: alpha-linoleate

substrate: alpha-linoleate


organism: Gaeumannomyces tritici


organism: Streptomyces clavuligerus

substrate_name: lysine

substrate: lysine


substrate_name: lysophosphatidylcholine

substrate: lysophosphatidylcholine


organism: Escherichia coli

substrate_name: arsenate

proof_lines: kcat is 0.53 sec(-1) with arsenate as substrate. kcat is 0.218 sec(-1) with Grx2 as substrate.

substrate: arsenate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 55 min(-1) with L-lysine as substrate. kcat is 86 min(-1) with alpha-ketoglutarate as substrate.


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: L-ornithine (in the presence of 5 mM 2-oxoglutarate)

proof_lines: kcat is 77.6 sec(-1) with L-ornithine as substrate. kcat is 86.4 sec(-1) with L-lysine as substrate. kcat is 95.8 sec(-1) with 2-oxoglutarate as substrate. kcat is 124 sec(-1) with 2-oxoadipate as substrate.


organism: Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB 13405 / ORS 571)

substrate_name: cyanuric acid

row_label: Table 2, enzyme row Azorhizobium caulinodans ORS 571 locus AZC_3892

substrate: cyanuric acid


organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)

row_label: Table 2, enzyme row Bradyrhizobium japonicum USDA 110


organism: Bradyrhizobium sp. (strain ORS 375)

substrate_name: Unknown

proof_lines: kcat/KM is with cyanuric acid as substrate.

substrate: Unknown


organism: Ectopseudomonas oleovorans (strain CECT 5344)

proof_lines: kcat is 2.2 sec(-1) with cyanuric acid as substrate.


organism: Methylobacterium sp. (strain 4-46)

row_label: Table 2, enzyme row Methylobacterium sp. 4-46


organism: Moorella thermoacetica (strain ATCC 39073 / JCM 9320)

proof_lines: kcat is 10.6 sec(-1) with cyanuric acid as substrate (PubMed:19767460). kcat is 5.2 sec(-1) with cyanuric acid as substrate (PubMed:28235873).


organism: Pseudomonas sp

verification_status: corrected

column_label: Table 2 (Kinetic constants of various cyanuric acid hydrolase/barbiturase family enzymes, using cyanuric acid as a substrate) prints one enzyme-label column, 'Enzyme name and /or organism (reference)', followed by three numeric columns whose heads are kcat (s^-1), Km (uM) and kcat/Km (s^-1 M^-1) in that printed order. The cited cell set is Table 2, enzyme row TrzD (this study): kcat (s^-1) = 14.2; Km (uM) = 58; kcat/Km (s^-1 M^-1) = 2.5 x 10^5. The printed uncertainties of that row are kcat 14.2 +/- 0.4, Km 58 +/- 7 and kcat/Km (2.5 +/- 0.4) x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 14.2 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 14.2 s^(-1). Km: printed Table 2 cell 58 uM; 58 / 1000 = 0.058, so the paper value is 0.058 mM. kcat/Km: printed Table 2 cell 2.5 x 10^5 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 x 10^5 / 1000 = 250.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row TrzD (this study): kcat = 14.2 s-1; Km = 58 uM; printed kcat/Km = 2.5 x 10^5 s-1 M-1.

row_label: Table 2, enzyme row TrzD (this study)

status: corrected


organism: Pseudomonas sp. (strain ADP)

row_label: Table 2, enzyme row Pseudomonas sp. ADP AtzD (this study)


organism: Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 / CB1190)

proof_lines: kcat is 56.3 sec(-1) with cyanuric acid as substrate.


organism: Staphylococcus aureus


organism: Mus musculus

substrate_name: p-nitrophenylphosphocholine

proof_lines: pH 10, 20°C, hydrolysis of sn-glycero-3-phosphocholine

proof_lines: pH 10, 20°C, hydrolysis of p-nitrophenylphosphocholine

substrate: p-nitrophenylphosphocholine


organism: Rattus norvegicus

substrate_name: p-nitrophenylphosphorylthymidine

substrate: p-nitrophenylphosphorylthymidine


organism: Mycobacterium tuberculosis

substrate_name: L-lysine

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

sequence_source: UniProtKB:P9WQ77 REST direct accession check on 2026-06-15; sequence version 1

source_databases_merged: brenda skid

substrate: L-lysine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WQ77 REST direct accession check on 2026-06-15; sequence version 1 and applied mutation signature E243A to reconstruct the assayed variant sequence.

proof_lines: mutant E243A, pH not specified in the publication, temperature not specified in the publication


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


organism: Haemophilus influenzae

substrate_name: CTP; D-Ribitol 5-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q48230 REST direct accession check on 2026-06-15; sequence version 1 and applied mutation signature K386A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-ribitol-5-phosphate cytidylyltransferase(Enzyme) mutant K386A His-tagged

substrate: CTP; D-Ribitol 5-phosphate


substrate_name: D-Ribitol 5-phosphate; CTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q48230 REST direct accession check on 2026-06-15; sequence version 1 and applied mutation signature R18A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-ribitol-5-phosphate cytidylyltransferase(Enzyme) mutant R18A His-tagged

substrate: D-Ribitol 5-phosphate; CTP


sequence_source: UniProtKB:Q48230 REST direct accession check on 2026-06-15; sequence version 1


sequence_source: UniProtKB:Q2G2C4 REST direct accession check on 2026-06-15; sequence version 2


organism: Bos taurus

sequence_source: UniProtKB:F1N5C8 REST direct accession check on 2026-06-15; sequence version 2


substrate_name: Sphingosyl-phosphocholine

substrate: Sphingosyl-phosphocholine


substrate_name: H2O; sn-Glycero-3-phosphocholine

substrate: H2O; sn-Glycero-3-phosphocholine


substrate_name: 4-Nitrophenyl phosphocholine

substrate: 4-Nitrophenyl phosphocholine


organism: Streptomyces sanglieri


enzyme_display_name: propionate kinase

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

substrate_name: ATP (at 25 degrees Celsius and pH 7.5)

assay_conditions_summary: cofactor ATP

enzyme: propionate kinase

substrate: ATP (at 25 degrees Celsius and pH 7.5)


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: propionate

sequence_source: UniProtKB reviewed O06961; RCSB 1X3N primary citation PMID 16139298 maps the TdcD structure entity to O06961

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: propionate


enzyme_display_name: kojibiose hydrolase

organism: Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101)

substrate_name: kojibiose

proof_lines: kcat is 108 sec(-1) with kojibiose as substrate. kcat is 46.5 sec(-1) with kojitriose as substrate. kcat is 67.5 sec(-1) with kojitetraose as substrate. kcat is 44.5 sec(-1) with kojipentaose as substrate. kcat is 72.8 sec(-1) with G2G6G as

enzyme: kojibiose hydrolase

substrate: kojibiose


organism: Mucilaginibacter mallensis

substrate_name: kojibiose (at pH 4.5 and 30 degrees Celsius)

proof_lines: kcat is 9.9 sec(-1) with kojibiose as substrate (at pH 4.5 and 30 degrees Celsius).


organism: Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841)

row_label: Table 2, enzyme row Rhizobium leguminosarum bv. viciae 3841


organism: Sarocladium sp

proof_lines: kcat is 3.4 sec(-1) with cyanuric acid as substrate.


organism: Weissella viridescens

substrate_name: tRNA(Ala)

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

substrate: tRNA(Ala)


enzyme_display_name: 2'-5' oligoadenylate synthase

organism: Homo sapiens

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P29728 fetched from rest.uniprot.org on 2026-06-15; variant sequence reconstructed from selected batch mutation annotation. and applied mutation signature D408A/D410A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2'-5' oligoadenylate synthase(Enzyme) mutant heterodimer wt His6-tagged/DADA (D408A,D410A) FLAG-tagged

proof_lines: SABIO-RK modifier species: 2'-5' oligoadenylate synthase(Enzyme) mutant DADA (D408A,D410A) FLAG-tagged

enzyme: 2'-5' oligoadenylate synthase

substrate: ATP


substrate_name: P1,P3-Bis(5'-adenosyl) triphosphate

sequence_source: UniProtKB reviewed accession P29728 fetched from rest.uniprot.org on 2026-06-15; variant sequence reconstructed from selected batch mutation annotation.

substrate: P1,P3-Bis(5'-adenosyl) triphosphate


sequence_source: UniProtKB reviewed accession P00973 fetched from rest.uniprot.org on 2026-06-15.

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


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


sequence_source: UniProtKB reviewed accession Q9Z2F2 fetched from rest.uniprot.org on 2026-06-15.


organism: Sus scrofa

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q29599 fetched from rest.uniprot.org on 2026-06-15; variant sequence reconstructed from selected batch mutation annotation. and applied mutation signature S62A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+

proof_lines: OAS1 mutant S62A, with ATP and NAD+ as substrates, pH and temperature not specified in the publication

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q29599 fetched from rest.uniprot.org on 2026-06-15; variant sequence reconstructed from selected batch mutation annotation. and applied mutation signature S63A to reconstruct the assayed variant sequence.

proof_lines: OAS1 mutant S63A, with ATP and NAD+ as substrates, pH and temperature not specified in the publication


sequence_source: UniProtKB reviewed accession Q29599 fetched from rest.uniprot.org on 2026-06-15; variant sequence reconstructed from selected batch mutation annotation.

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

proof_lines: wild-type OAS1, with ATP as sole substrate, pH and temperature not specified in the publication

proof_lines: wild-type OAS1, with ATP and NAD+ as substrates, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q29599 fetched from rest.uniprot.org on 2026-06-15; variant sequence reconstructed from selected batch mutation annotation. and applied mutation signature K212A to reconstruct the assayed variant sequence.

proof_lines: OAS1 mutant K212A, with ATP as sole substrate, pH and temperature not specified in the publication


organism: Flavobacterium johnsoniae

substrate_name: kojitriose

sequence_source: UniProtKB reviewed accession A5FBJ5 fetched from rest.uniprot.org on 2026-06-15.

substrate: kojitriose


substrate_name: alpha-D-glucopyranosyl fluoride

substrate: alpha-D-glucopyranosyl fluoride


substrate_name: kojitetraose

substrate: kojitetraose


substrate_name: kojipentaose

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

substrate: kojipentaose


substrate_name: L-alanyl-tRNAAla

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9EY50 canonical sequence plus selected-record mutation signature and applied mutation signature E320Q to reconstruct the assayed variant sequence.

proof_lines: Ala-tRNAAla from E. coli, recombinant mutant E320Q

substrate: L-alanyl-tRNAAla


proof_lines: Ala-tRNAAla from E. coli, recombinant wild-type


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9EY50 canonical sequence plus selected-record mutation signature and applied mutation signature D109N to reconstruct the assayed variant sequence.

proof_lines: Ala-tRNAAla from E. coli, recombinant mutant D109N


substrate_name: L-alanyl-tRNA

proof_lines:
pH 7.5, 30°C
product inhibition
versus UDP-acetylmuramoylpentapeptide

substrate: L-alanyl-tRNA


enzyme_display_name: inositol 3-kinase

organism: Zea mays

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

proof_lines: in 20 mM HEPES (pH 7.2), 6 mM MgCl2, 10 mM LiCl, 1 mM dithiothreitol, at 30°C

enzyme: inositol 3-kinase


organism: Lactobacillus viridescens

substrate_name: L-Alanyl-tRNA(Ala)

sequence_source: UniProtKB Q9EY50 REST direct sequence checked 2026-06-15.

substrate: L-Alanyl-tRNA(Ala)


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9EY50 REST direct canonical sequence checked 2026-06-15 plus selected mutation E320Q. and applied mutation signature E320Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9EY50 REST direct canonical sequence checked 2026-06-15 plus selected mutation E320Q.

proof_lines: SABIO-RK modifier species: UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase(Enzyme) mutant E320Q 6His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9EY50 REST direct canonical sequence checked 2026-06-15 plus selected mutation D109N. and applied mutation signature D109N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9EY50 REST direct canonical sequence checked 2026-06-15 plus selected mutation D109N.

proof_lines: SABIO-RK modifier species: UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase(Enzyme) mutant D109N 6His-tagged


enzyme_display_name: dimethylallylcistransferase

organism: Solanum habrochaites

substrate_name: neryl diphosphate

sequence_source: UniProtKB W0J9X7 REST direct sequence checked 2026-06-15; selected row is variant_unspecified so canonical sequence is context only.

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

proof_lines:
pH 7.6, 30°C, mutant NDPS1-M10
pH 7.6, 30°C, mutant NDPS1-M4

enzyme: dimethylallylcistransferase

substrate: neryl diphosphate


substrate_name: isopentenyl diphosphate

sequence_source: UniProtKB W0J9X7 REST direct sequence checked 2026-06-15.

substrate: isopentenyl diphosphate


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


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


organism: Solanum lycopersicum

sequence_source: UniProtKB C1K5M2 REST direct sequence checked 2026-06-15.


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


enzyme_display_name: allose kinase

organism: Escherichia coli

substrate_name: D-Allose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32718 and applied mutation signature F145L to reconstruct the assayed variant sequence.

column_label: Table 2, F145L AlsK column, D-allose block; kcat cell = 49 s-1; Km cell = 1.5 x 10^-4 M; kcat/Km cell = 3.2 x 10^5 M^-1 s^-1. captured primary segment: F145L AlsK | D-allose | Table 2, F145L AlsK column, D-allose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, F145L AlsK column, D-allose block, kcat = 49 s-1 | Table 2, F145L AlsK column, D-allose block, Km = 1.5 x 10^-4 M | Table 2, F145L AlsK column, D-allose block, kcat/Km = 3.2 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 49 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 49.0 s^(-1). Km: printed cell 1.5 x 10^-4 M; 1 M is 1000 mM, so 1.5 x 10^-4 x 1000 = 0.15 mM. kcat/Km: printed cell 3.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.2 x 10^5 / 1000 = 320.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 49.0 / 0.15 = 326.6666666666667 s^-1 mM^-1, against the printed efficiency cell 320.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, F145L AlsK column, D-allose block: kcat = 49 s-1; Km = 1.5 x 10^-4 M; kcat/Km = 3.2 x 10^5 M^-1 s^-1.

table_label: Table 2: Kinetic Parameters for Phosphorylation of Native and Ambiguous Substrates by Wild-Type AlsK and Selected Variants (Biochemistry 2007, 46, 13564-13572); printed row heads kcat, sugar (s-1) | Km, sugar (M) | Km, ATP (M) | kcat/Km, sugar (M-1 s-1)

enzyme: allose kinase

substrate: D-Allose


substrate_name: D-Glucose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32718 and applied mutation signature A73G to reconstruct the assayed variant sequence.

column_label: Table 2, A73G AlsK column, D-glucose block; kcat cell = 13 s-1; Km cell = 6.5 x 10^-4 M; kcat/Km cell = 2.1 x 10^4 M^-1 s^-1. captured primary segment: A73G AlsK | D-glucose | Table 2, A73G AlsK column, D-glucose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, A73G AlsK column, D-glucose block, kcat = 13 s-1 | Table 2, A73G AlsK column, D-glucose block, Km = 6.5 x 10^-4 M | Table 2, A73G AlsK column, D-glucose block, kcat/Km = 2.1 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 13 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 13.0 s^(-1). Km: printed cell 6.5 x 10^-4 M; 1 M is 1000 mM, so 6.5 x 10^-4 x 1000 = 0.65 mM. kcat/Km: printed cell 2.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.1 x 10^4 / 1000 = 21.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 13.0 / 0.65 = 20.0 s^-1 mM^-1, against the printed efficiency cell 21.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, A73G AlsK column, D-glucose block: kcat = 13 s-1; Km = 6.5 x 10^-4 M; kcat/Km = 2.1 x 10^4 M^-1 s^-1.

substrate: D-Glucose


sequence_source: UniProtKB P32718 REST direct sequence checked 2026-06-15.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


substrate_name: ATP; D-Allose

column_label: Table 2, A73G AlsK column, D-allose block, ATP axis; kcat cell = 40 s-1; Km, ATP cell = 6.0 x 10^-5 M; kcat/Km cell: Table 2 carries none on the ATP axis. captured primary segment: A73G AlsK | ATP | Table 2, A73G AlsK column, D-allose block, ATP axis | 0.2 M Tris, pH 7.6 at 25 C | Table 2, A73G AlsK column, D-allose block, ATP axis, kcat = 40 s-1 | Table 2, A73G AlsK column, D-allose block, ATP axis, Km, ATP = 6.0 x 10^-5 M | kcat/Km: Table 2 prints no kcat/Km cell on the ATP axis of this measurement

normalized_value_unit_evidence: kcat: printed cell 40 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 40.0 s^(-1). Km: printed cell 6.0 x 10^-5 M; 1 M is 1000 mM, so 6.0 x 10^-5 x 1000 = 0.060000000000000005 mM. kcat/Km: the paper prints no efficiency cell on this ATP axis, so the ratio typed on this record is the arithmetic quotient of the two printed cells of this same measurement, 40.0 / 0.060000000000000005 = 666.6666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, A73G AlsK column, D-allose block, ATP axis: kcat = 40 s-1; Km, ATP = 6.0 x 10^-5 M; Table 2 carries no kcat/Km cell on the ATP axis.

substrate: ATP; D-Allose


sequence_source: UniProtKB P32718 direct FASTA/JSON lookup; reviewed Swiss-Prot D-allose kinase, EC 2.7.1.55, Escherichia coli K-12.

column_label: Table 2, wt AlsK column, D-allose block; kcat cell = 47 s-1; Km cell = 1.9 x 10^-4 M; kcat/Km cell = 2.5 x 10^5 M^-1 s^-1. captured primary segment: wt AlsK | D-allose | Table 2, wt AlsK column, D-allose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, wt AlsK column, D-allose block, kcat = 47 s-1 | Table 2, wt AlsK column, D-allose block, Km = 1.9 x 10^-4 M | Table 2, wt AlsK column, D-allose block, kcat/Km = 2.5 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 47 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 47.0 s^(-1). Km: printed cell 1.9 x 10^-4 M; 1 M is 1000 mM, so 1.9 x 10^-4 x 1000 = 0.19 mM. kcat/Km: printed cell 2.5 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 x 10^5 / 1000 = 250.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 47.0 / 0.19 = 247.3684210526316 s^-1 mM^-1, against the printed efficiency cell 250.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, wt AlsK column, D-allose block: kcat = 47 s-1; Km = 1.9 x 10^-4 M; kcat/Km = 2.5 x 10^5 M^-1 s^-1.

row_label: Table 2, wt AlsK column, D-allose block


column_label: Table 2, A73G AlsK column, D-glucose block, ATP axis; kcat cell = 13 s-1; Km, ATP cell = 4.5 x 10^-4 M; kcat/Km cell: Table 2 carries none on the ATP axis. captured primary segment: A73G AlsK | ATP | Table 2, A73G AlsK column, D-glucose block, ATP axis | 0.2 M Tris, pH 7.6 at 25 C | Table 2, A73G AlsK column, D-glucose block, ATP axis, kcat = 13 s-1 | Table 2, A73G AlsK column, D-glucose block, ATP axis, Km, ATP = 4.5 x 10^-4 M | kcat/Km: Table 2 prints no kcat/Km cell on the ATP axis of this measurement

normalized_value_unit_evidence: kcat: printed cell 13 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 13.0 s^(-1). Km: printed cell 4.5 x 10^-4 M; 1 M is 1000 mM, so 4.5 x 10^-4 x 1000 = 0.45 mM. kcat/Km: the paper prints no efficiency cell on this ATP axis, so the ratio typed on this record is the arithmetic quotient of the two printed cells of this same measurement, 13.0 / 0.45 = 28.88888888888889 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, A73G AlsK column, D-glucose block, ATP axis: kcat = 13 s-1; Km, ATP = 4.5 x 10^-4 M; Table 2 carries no kcat/Km cell on the ATP axis.


substrate_name: D-Altrose

column_label: Table 3, A73G AlsK section, D-altrose row; kcat cell = 94 s-1; Km cell = 4.8 x 10^-2 M; kcat/Km cell = 2.0 x 10^3 M^-1 s^-1. captured primary segment: A73G AlsK | D-altrose | Table 3, A73G AlsK section, D-altrose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, A73G AlsK section, D-altrose row, kcat = 94 s-1 | Table 3, A73G AlsK section, D-altrose row, Km = 4.8 x 10^-2 M | Table 3, A73G AlsK section, D-altrose row, kcat/Km = 2.0 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 94 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 94.0 s^(-1). Km: printed cell 4.8 x 10^-2 M; 1 M is 1000 mM, so 4.8 x 10^-2 x 1000 = 48.0 mM. kcat/Km: printed cell 2.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.0 x 10^3 / 1000 = 2.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 94.0 / 48.0 = 1.9583333333333333 s^-1 mM^-1, against the printed efficiency cell 2.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, A73G AlsK section, D-altrose row: kcat = 94 s-1; Km = 4.8 x 10^-2 M; kcat/Km = 2.0 x 10^3 M^-1 s^-1.

table_label: Table 3: Specificity Profiles of Wild-Type and A73G AlsK (Biochemistry 2007, 46, 13564-13572); printed column heads substrate | kcat (s-1) | Km (M) | kcat/Km (M-1 s-1) | x-fold change in kcat/Km

substrate: D-Altrose


sequence_variant_note: Resolved canonical sequence from UniProtKB P32718 direct FASTA/JSON lookup; reviewed Swiss-Prot D-allose kinase, EC 2.7.1.55, Escherichia coli K-12. Variant reconstructed by direct residue check for A73G. and applied mutation signature A73G to reconstruct the assayed variant sequence.


substrate_name: D-Mannose

column_label: Table 3, A73G AlsK section, D-mannose row; kcat cell = 9.5 s-1; Km cell = 2.1 x 10^-1 M; kcat/Km cell = 4.5 x 10^1 M^-1 s^-1. captured primary segment: A73G AlsK | D-mannose | Table 3, A73G AlsK section, D-mannose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, A73G AlsK section, D-mannose row, kcat = 9.5 s-1 | Table 3, A73G AlsK section, D-mannose row, Km = 2.1 x 10^-1 M | Table 3, A73G AlsK section, D-mannose row, kcat/Km = 4.5 x 10^1 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 9.5 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 9.5 s^(-1). Km: printed cell 2.1 x 10^-1 M; 1 M is 1000 mM, so 2.1 x 10^-1 x 1000 = 210.0 mM. kcat/Km: printed cell 4.5 x 10^1 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.5 x 10^1 / 1000 = 0.045 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 9.5 / 210.0 = 0.04523809523809524 s^-1 mM^-1, against the printed efficiency cell 0.045 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, A73G AlsK section, D-mannose row: kcat = 9.5 s-1; Km = 2.1 x 10^-1 M; kcat/Km = 4.5 x 10^1 M^-1 s^-1.

substrate: D-Mannose


column_label: Table 2, wt AlsK column, D-glucose block; kcat cell = 10 s-1; Km cell = 2.9 x 10^-2 M; kcat/Km cell = 3.4 x 10^2 M^-1 s^-1. captured primary segment: wt AlsK | D-glucose | Table 2, wt AlsK column, D-glucose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, wt AlsK column, D-glucose block, kcat = 10 s-1 | Table 2, wt AlsK column, D-glucose block, Km = 2.9 x 10^-2 M | Table 2, wt AlsK column, D-glucose block, kcat/Km = 3.4 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 10 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 10.0 s^(-1). Km: printed cell 2.9 x 10^-2 M; 1 M is 1000 mM, so 2.9 x 10^-2 x 1000 = 29.0 mM. kcat/Km: printed cell 3.4 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.4 x 10^2 / 1000 = 0.34 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 10.0 / 29.0 = 0.3448275862068966 s^-1 mM^-1, against the printed efficiency cell 0.34 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, wt AlsK column, D-glucose block: kcat = 10 s-1; Km = 2.9 x 10^-2 M; kcat/Km = 3.4 x 10^2 M^-1 s^-1.


substrate_name: ATP

column_label: Table 2, F145L AlsK column, D-glucose block, ATP axis; kcat cell = 28 s-1; Km, ATP cell = 9.6 x 10^-4 M; kcat/Km cell: Table 2 carries none on the ATP axis. captured primary segment: F145L AlsK | ATP | Table 2, F145L AlsK column, D-glucose block, ATP axis | 0.2 M Tris, pH 7.6 at 25 C | Table 2, F145L AlsK column, D-glucose block, ATP axis, kcat = 28 s-1 | Table 2, F145L AlsK column, D-glucose block, ATP axis, Km, ATP = 9.6 x 10^-4 M | kcat/Km: Table 2 prints no kcat/Km cell on the ATP axis of this measurement

normalized_value_unit_evidence: kcat: printed cell 28 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 28.0 s^(-1). Km: printed cell 9.6 x 10^-4 M; 1 M is 1000 mM, so 9.6 x 10^-4 x 1000 = 0.9600000000000001 mM. kcat/Km: the paper prints no efficiency cell on this ATP axis, so the ratio typed on this record is the arithmetic quotient of the two printed cells of this same measurement, 28.0 / 0.9600000000000001 = 29.166666666666664 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, F145L AlsK column, D-glucose block, ATP axis: kcat = 28 s-1; Km, ATP = 9.6 x 10^-4 M; Table 2 carries no kcat/Km cell on the ATP axis.

substrate: ATP


column_label: Table 2, F145L AlsK column, D-glucose block; kcat cell = 28 s-1; Km cell = 7.2 x 10^-3 M; kcat/Km cell = 3.9 x 10^3 M^-1 s^-1. captured primary segment: F145L AlsK | D-glucose | Table 2, F145L AlsK column, D-glucose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, F145L AlsK column, D-glucose block, kcat = 28 s-1 | Table 2, F145L AlsK column, D-glucose block, Km = 7.2 x 10^-3 M | Table 2, F145L AlsK column, D-glucose block, kcat/Km = 3.9 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 28 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 28.0 s^(-1). Km: printed cell 7.2 x 10^-3 M; 1 M is 1000 mM, so 7.2 x 10^-3 x 1000 = 7.2 mM. kcat/Km: printed cell 3.9 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.9 x 10^3 / 1000 = 3.9 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 28.0 / 7.2 = 3.888888888888889 s^-1 mM^-1, against the printed efficiency cell 3.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, F145L AlsK column, D-glucose block: kcat = 28 s-1; Km = 7.2 x 10^-3 M; kcat/Km = 3.9 x 10^3 M^-1 s^-1.


column_label: Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row; kcat cell = 1.5 s-1; Km cell = 3.8 x 10^-1 M; kcat/Km cell = 4.1 M^-1 s^-1. captured primary segment: wild-type AlsK | 2'-deoxy-D-glucose | Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row, kcat = 1.5 s-1 | Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row, Km = 3.8 x 10^-1 M | Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row, kcat/Km = 4.1 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 1.5 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 1.5 s^(-1). Km: printed cell 3.8 x 10^-1 M; 1 M is 1000 mM, so 3.8 x 10^-1 x 1000 = 380.0 mM. kcat/Km: printed cell 4.1 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.1 / 1000 = 0.0040999999999999995 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 1.5 / 380.0 = 0.003947368421052632 s^-1 mM^-1, against the printed efficiency cell 0.0040999999999999995 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row: kcat = 1.5 s-1; Km = 3.8 x 10^-1 M; kcat/Km = 4.1 M^-1 s^-1.


column_label: Table 3, A73G AlsK section, 2'-deoxy-D-glucose row; kcat cell = 19 s-1; Km cell = 5.1 x 10^-2 M; kcat/Km cell = 3.7 x 10^2 M^-1 s^-1. captured primary segment: A73G AlsK | 2'-deoxy-D-glucose | Table 3, A73G AlsK section, 2'-deoxy-D-glucose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, A73G AlsK section, 2'-deoxy-D-glucose row, kcat = 19 s-1 | Table 3, A73G AlsK section, 2'-deoxy-D-glucose row, Km = 5.1 x 10^-2 M | Table 3, A73G AlsK section, 2'-deoxy-D-glucose row, kcat/Km = 3.7 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 19 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 19.0 s^(-1). Km: printed cell 5.1 x 10^-2 M; 1 M is 1000 mM, so 5.1 x 10^-2 x 1000 = 51.0 mM. kcat/Km: printed cell 3.7 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.7 x 10^2 / 1000 = 0.37 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 19.0 / 51.0 = 0.37254901960784315 s^-1 mM^-1, against the printed efficiency cell 0.37 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, A73G AlsK section, 2'-deoxy-D-glucose row: kcat = 19 s-1; Km = 5.1 x 10^-2 M; kcat/Km = 3.7 x 10^2 M^-1 s^-1.


column_label: Table 3, wild-type AlsK section, D-altrose row; kcat cell = 34 s-1; Km cell = 2.1 x 10^-1 M; kcat/Km cell = 1.6 x 10^2 M^-1 s^-1. captured primary segment: wild-type AlsK | D-altrose | Table 3, wild-type AlsK section, D-altrose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, wild-type AlsK section, D-altrose row, kcat = 34 s-1 | Table 3, wild-type AlsK section, D-altrose row, Km = 2.1 x 10^-1 M | Table 3, wild-type AlsK section, D-altrose row, kcat/Km = 1.6 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 34 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 34.0 s^(-1). Km: printed cell 2.1 x 10^-1 M; 1 M is 1000 mM, so 2.1 x 10^-1 x 1000 = 210.0 mM. kcat/Km: printed cell 1.6 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^2 / 1000 = 0.16 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 34.0 / 210.0 = 0.1619047619047619 s^-1 mM^-1, against the printed efficiency cell 0.16 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, wild-type AlsK section, D-altrose row: kcat = 34 s-1; Km = 2.1 x 10^-1 M; kcat/Km = 1.6 x 10^2 M^-1 s^-1.


column_label: Table 3, wild-type AlsK section, D-mannose row; kcat cell = 0.5 s-1; Km cell = 3.9 x 10^-1 M; kcat/Km cell = 1.2 M^-1 s^-1. captured primary segment: wild-type AlsK | D-mannose | Table 3, wild-type AlsK section, D-mannose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, wild-type AlsK section, D-mannose row, kcat = 0.5 s-1 | Table 3, wild-type AlsK section, D-mannose row, Km = 3.9 x 10^-1 M | Table 3, wild-type AlsK section, D-mannose row, kcat/Km = 1.2 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.5 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.5 s^(-1). Km: printed cell 3.9 x 10^-1 M; 1 M is 1000 mM, so 3.9 x 10^-1 x 1000 = 390.0 mM. kcat/Km: printed cell 1.2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 / 1000 = 0.0012 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 0.5 / 390.0 = 0.001282051282051282 s^-1 mM^-1, against the printed efficiency cell 0.0012 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, wild-type AlsK section, D-mannose row: kcat = 0.5 s-1; Km = 3.9 x 10^-1 M; kcat/Km = 1.2 M^-1 s^-1.


substrate_name: D-Allose; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB P32718 direct FASTA/JSON lookup; reviewed Swiss-Prot D-allose kinase, EC 2.7.1.55, Escherichia coli K-12. Variant reconstructed by direct residue check for F145L. and applied mutation signature F145L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: allose kinase(Enzyme) mutant AlsK F145L

substrate: D-Allose; ATP


organism: Thermococcus kodakarensis

substrate_name: D-Xylose

sequence_source: UniProtKB Q5JDA3 direct FASTA/JSON lookup; live TrEMBL TK2285 PfkB-family kinase from Thermococcus kodakarensis KOD1 with BRENDA cross-reference EC 2.7.1.64.

assay_conditions_summary: pH 7.5; 358.15 K; buffer solution; cofactor ATP

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Xylose': column 'kcat, s^-1' = 5.6; column 'Km, mM' = 418; column 'kcat/Km, s^-1 mM^-1' = 0.013. The kcat and Km cells are printed with their standard deviations (5.6 +/- 0.3 and 418 +/- 50); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.6 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 5.6 s^(-1). Km: printed Table 3 cell 418 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 418.0 mM. kcat/Km: printed Table 3 cell 0.013 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.013 s^(-1)*mM^(-1), which is the exact same-row quotient 5.6 / 418 = 0.013397129186602871 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Xylose': kcat = 5.6 s^-1; Km = 418 mM; printed kcat/Km = 0.013 s^-1 mM^-1.

table_label: Table 3: Kinetic parameters of TK2285 toward various monosaccharides and myo-inositol (J. Biol. Chem. 2013, 288(29):20856-20867)

substrate: D-Xylose


substrate_name: D-Talose

sequence_source: UniProtKB direct lookup Q5JDA3

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Talose': column 'kcat, s^-1' = 13.1; column 'Km, mM' = 438; column 'kcat/Km, s^-1 mM^-1' = 0.030. The kcat and Km cells are printed with their standard deviations (13.1 +/- 0.1 and 438 +/- 39); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 13.1 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 13.1 s^(-1). Km: printed Table 3 cell 438 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 438.0 mM. kcat/Km: printed Table 3 cell 0.030 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.03 s^(-1)*mM^(-1), which is the exact same-row quotient 13.1 / 438 = 0.029908675799086758 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Talose': kcat = 13.1 s^-1; Km = 438 mM; printed kcat/Km = 0.030 s^-1 mM^-1.

substrate: D-Talose


substrate_name: D-allose

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Allose': column 'kcat, s^-1' = 18.3; column 'Km, mM' = 863; column 'kcat/Km, s^-1 mM^-1' = 0.021. The kcat and Km cells are printed with their standard deviations (18.3 +/- 0.6 and 863 +/- 51); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 18.3 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 18.3 s^(-1). Km: printed Table 3 cell 863 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 863.0 mM. kcat/Km: printed Table 3 cell 0.021 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.021 s^(-1)*mM^(-1), which is the exact same-row quotient 18.3 / 863 = 0.021205098493626885 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Allose': kcat = 18.3 s^-1; Km = 863 mM; printed kcat/Km = 0.021 s^-1 mM^-1.

substrate: D-allose


substrate_name: D-Lyxose

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Lyxose': column 'kcat, s^-1' = 3.9; column 'Km, mM' = 171; column 'kcat/Km, s^-1 mM^-1' = 0.023. The kcat and Km cells are printed with their standard deviations (3.9 +/- 0.1 and 171 +/- 17); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.9 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 3.9 s^(-1). Km: printed Table 3 cell 171 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 171.0 mM. kcat/Km: printed Table 3 cell 0.023 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.023 s^(-1)*mM^(-1), which is the exact same-row quotient 3.9 / 171 = 0.02280701754385965 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Lyxose': kcat = 3.9 s^-1; Km = 171 mM; printed kcat/Km = 0.023 s^-1 mM^-1.

substrate: D-Lyxose


substrate_name: D-ribose

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Ribose': column 'kcat, s^-1' = 5.1; column 'Km, mM' = 951; column 'kcat/Km, s^-1 mM^-1' = 0.005. The kcat and Km cells are printed with their standard deviations (5.1 +/- 0.4 and 951 +/- 119); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.1 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 5.1 s^(-1). Km: printed Table 3 cell 951 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 951.0 mM. kcat/Km: printed Table 3 cell 0.005 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.005 s^(-1)*mM^(-1), which is the exact same-row quotient 5.1 / 951 = 0.005362776025236593 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Ribose': kcat = 5.1 s^-1; Km = 951 mM; printed kcat/Km = 0.005 s^-1 mM^-1.

substrate: D-ribose


substrate_name: D-tagatose

substrate: D-tagatose


substrate_name: myo-inositol

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'myo-Inositol': column 'kcat, s^-1' = 23.2; column 'Km, mM' = 0.36; column 'kcat/Km, s^-1 mM^-1' = 64.9. The kcat and Km cells are printed with their standard deviations (23.2 +/- 0.5 and 0.36 +/- 0.03); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 23.2 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 23.2 s^(-1). Km: printed Table 3 cell 0.36 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 0.36 mM. kcat/Km: printed Table 3 cell 64.9 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 64.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'myo-Inositol': kcat = 23.2 s^-1; Km = 0.36 mM; printed kcat/Km = 64.9 s^-1 mM^-1.

substrate: myo-inositol


column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Tagatose': column 'kcat, s^-1' = 1.5; column 'Km, mM' = 53; column 'kcat/Km, s^-1 mM^-1' = 0.028. The kcat and Km cells are printed with their standard deviations (1.5 +/- 0.1 and 53 +/- 9); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.5 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 1.5 s^(-1). Km: printed Table 3 cell 53 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 53.0 mM. kcat/Km: printed Table 3 cell 0.028 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.028 s^(-1)*mM^(-1), which is the exact same-row quotient 1.5 / 53 = 0.02830188679245283 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Tagatose': kcat = 1.5 s^-1; Km = 53 mM; printed kcat/Km = 0.028 s^-1 mM^-1.


substrate_name: D-Xylulose

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Xylulose': column 'kcat, s^-1' = 11.6; column 'Km, mM' = 524; column 'kcat/Km, s^-1 mM^-1' = 0.022. The kcat and Km cells are printed with their standard deviations (11.6 +/- 0.4 and 524 +/- 38); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 11.6 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 11.6 s^(-1). Km: printed Table 3 cell 524 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 524.0 mM. kcat/Km: printed Table 3 cell 0.022 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.022 s^(-1)*mM^(-1), which is the exact same-row quotient 11.6 / 524 = 0.022137404580152672 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Xylulose': kcat = 11.6 s^-1; Km = 524 mM; printed kcat/Km = 0.022 s^-1 mM^-1.

substrate: D-Xylulose


substrate_name: myo-Inositol; ATP

sequence_source: UniProtKB direct lookup Q5GA22

substrate: myo-Inositol; ATP


substrate_name: GTP

sequence_source: UniProtKB direct lookup O06961

substrate: GTP


substrate_name: CTP

substrate: CTP


substrate_name: propanoate

smiles: CCC(=O)O

substrate: propanoate


substrate_name: UTP

substrate: UTP


substrate_name: Butyrate

smiles: CCCC(=O)O

substrate: Butyrate


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


enzyme_display_name: teichoic acid poly(glycerol phosphate) polymerase

organism: Bacillus subtilis

substrate_name: CDPglycerol

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13485 direct accession lookup on 2026-06-15 and applied mutation signature D645A to reconstruct the assayed variant sequence.

substrate: CDPglycerol