organism: Enterococcus faecalis

substrate_name: Amikacin

verification_status: verified

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM Tris pH 7; cofactor NADH

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'amikacin'; column 'K_m (uM)' = 245 ± 27; column 'k_cat (s^-1)' = 2.46 ± 0.11; column 'K_i (mM)' = nd; column 'k_cat/K_m (M^-1 s^-1)' = 1.00 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.46 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2.46 s^(-1). Km: printed Table 3 cell 245 uM; 245 / 1000 = 0.245, so the paper value is 0.245 mM. kcat/Km: printed Table 3 cell 1.00 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.00 x 10^4 / 1000 = 10.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row amikacin: Km = 245 ± 27 uM; kcat = 2.46 ± 0.11 s^-1; printed kcat/Km = 1.00 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate row amikacin

substrate: Amikacin

status: verified


enzyme_display_name: kanamycin kinase

substrate_name: ATP

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM Tris pH 7; cofactor ATP

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'ATP'; column 'K_m (uM)' = 27.7 ± 3.7; column 'k_cat (s^-1)' = 1.76 ± 0.08; column 'K_i (mM)' = nd; column 'k_cat/K_m (M^-1 s^-1)' = 6.37 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.76 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1.76 s^(-1). Km: printed Table 3 cell 27.7 uM; 27.7 / 1000 = 0.0277, so the paper value is 0.0277 mM. kcat/Km: printed Table 3 cell 6.37 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.37 x 10^4 / 1000 = 63.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row ATP: Km = 27.7 ± 3.7 uM; kcat = 1.76 ± 0.08 s^-1; printed kcat/Km = 6.37 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate row ATP

data_origin: experimental

enzyme: kanamycin kinase

substrate: ATP

status: corrected

source: oed


substrate_name: ATP; Kanamycin A

kcat_over_km_display: Not reported

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

ki_unit: mM

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, recombinant enzyme, versus ATP

proof_lines: pH 7.5, 25°C, recombinant enzyme, versus kanamycin

substrate: ATP; Kanamycin A


substrate_name: Butirosin

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'butirosin'; column 'K_m (uM)' = 34.3 ± 3.1; column 'k_cat (s^-1)' = 2.02 ± 0.07; column 'K_i (mM)' = 2.17 ± 0.41; column 'k_cat/K_m (M^-1 s^-1)' = 5.87 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.02 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2.02 s^(-1). Km: printed Table 3 cell 34.3 uM; 34.3 / 1000 = 0.0343, so the paper value is 0.0343 mM. kcat/Km: printed Table 3 cell 5.87 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.87 x 10^4 / 1000 = 58.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row butirosin: Km = 34.3 ± 3.1 uM; kcat = 2.02 ± 0.07 s^-1; printed kcat/Km = 5.87 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate row butirosin

substrate: Butirosin


substrate_name: paromomycin

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'paromomycin'; column 'K_m (uM)' = 19.5 ± 3.5; column 'k_cat (s^-1)' = 3.62 ± 0.25; column 'K_i (mM)' = 0.53 ± 0.11; column 'k_cat/K_m (M^-1 s^-1)' = 1.86 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.62 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 3.62 s^(-1). Km: printed Table 3 cell 19.5 uM; 19.5 / 1000 = 0.0195, so the paper value is 0.0195 mM. kcat/Km: printed Table 3 cell 1.86 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.86 x 10^5 / 1000 = 186.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row paromomycin: Km = 19.5 ± 3.5 uM; kcat = 3.62 ± 0.25 s^-1; printed kcat/Km = 1.86 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row paromomycin

substrate: paromomycin


substrate_name: Kanamycin B

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'kanamycin B'; column 'K_m (uM)' = 19.4 ± 2.2; column 'k_cat (s^-1)' = 3.51 ± 0.19; column 'K_i (mM)' = nd; column 'k_cat/K_m (M^-1 s^-1)' = 1.81 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.51 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 3.51 s^(-1). Km: printed Table 3 cell 19.4 uM; 19.4 / 1000 = 0.0194, so the paper value is 0.0194 mM. kcat/Km: printed Table 3 cell 1.81 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.81 x 10^5 / 1000 = 181.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row kanamycin B: Km = 19.4 ± 2.2 uM; kcat = 3.51 ± 0.19 s^-1; printed kcat/Km = 1.81 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row kanamycin B

substrate: Kanamycin B


substrate_name: Lividomycin A

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'lividomycin A'; column 'K_m (uM)' = 31.6 ± 5.1; column 'k_cat (s^-1)' = 3.97 ± 0.25; column 'K_i (mM)' = 1.53 ± 0.42; column 'k_cat/K_m (M^-1 s^-1)' = 1.26 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.97 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 3.97 s^(-1). Km: printed Table 3 cell 31.6 uM; 31.6 / 1000 = 0.0316, so the paper value is 0.0316 mM. kcat/Km: printed Table 3 cell 1.26 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.26 x 10^5 / 1000 = 126.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row lividomycin A: Km = 31.6 ± 5.1 uM; kcat = 3.97 ± 0.25 s^-1; printed kcat/Km = 1.26 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row lividomycin A

substrate: Lividomycin A


substrate_name: Ribostamycin sulfate

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'ribostamycin'; column 'K_m (uM)' = 9.30 ± 1.8; column 'k_cat (s^-1)' = 1.89 ± 0.10; column 'K_i (mM)' = 1.73 ± 0.66; column 'k_cat/K_m (M^-1 s^-1)' = 2.03 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.89 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1.89 s^(-1). Km: printed Table 3 cell 9.30 uM; 9.30 / 1000 = 0.0093, so the paper value is 0.0093 mM. kcat/Km: printed Table 3 cell 2.03 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.03 x 10^5 / 1000 = 203.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row ribostamycin: Km = 9.30 ± 1.8 uM; kcat = 1.89 ± 0.10 s^-1; printed kcat/Km = 2.03 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row ribostamycin

substrate: Ribostamycin sulfate


substrate_name: Neomycin B

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'neomycin B'; column 'K_m (uM)' = 7.72 ± 0.9; column 'k_cat (s^-1)' = 2.08 ± 0.07; column 'K_i (mM)' = 2.65 ± 0.59; column 'k_cat/K_m (M^-1 s^-1)' = 2.69 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.08 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2.08 s^(-1). Km: printed Table 3 cell 7.72 uM; 7.72 / 1000 = 0.00772, so the paper value is 0.00772 mM. kcat/Km: printed Table 3 cell 2.69 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.69 x 10^5 / 1000 = 269.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row neomycin B: Km = 7.72 ± 0.9 uM; kcat = 2.08 ± 0.07 s^-1; printed kcat/Km = 2.69 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row neomycin B

substrate: Neomycin B


enzyme_display_name: glycerol kinase

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

substrate_name: ATP (at pH 7.5 and 80 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: kcat is 940 sec(-1) for glycerol (at pH 7.5 and 80 degrees Celsius).

enzyme: glycerol kinase

substrate: ATP (at pH 7.5 and 80 degrees Celsius)

source: uniprot


organism: Trypanosoma brucei brucei

assay_conditions_summary: cofactor ATP


enzyme_display_name: glutamate N-acetyltransferase

organism: Sinorhizobium meliloti

source_db: brenda

sequence_source: UniProtKB reviewed accession Q92MJ1; REST check https://rest.uniprot.org/uniprotkb/Q92MJ1.json

enzyme: glutamate N-acetyltransferase

source: brenda


organism: Streptomyces clavuligerus

substrate_name: L-Glutamate; N2-Acetyl-L-ornithine

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

sequence_source: UniProtKB reviewed accession Q9LCS7; REST check https://rest.uniprot.org/uniprotkb/Q9LCS7.json

substrate: L-Glutamate; N2-Acetyl-L-ornithine


organism: Thermotoga neapolitana

sequence_source: UniProtKB reviewed accession Q9Z4S1; REST check https://rest.uniprot.org/uniprotkb/Q9Z4S1.json


enzyme_display_name: phosphate propanoyltransferase

organism: Moorella thermoacetica

substrate_name: propanoyl-CoA

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

assay_conditions_summary: pH 7.6; 328.15 K; cofactor CoA

enzyme: phosphate propanoyltransferase

substrate: propanoyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: acetyl phosphate

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

substrate: acetyl phosphate


organism: Listeria monocytogenes serotype 1/2a

sequence_source: UniProtKB REST direct check 2026-06-23; accession C0LNR0; reviewed Swiss-Prot entry FABH_LISM4

assay_conditions_summary: pH 7; 283.15 K; cofactor CoA

proof_lines:
pH 7, 10°C
pH 7, 30°C


substrate_name: isobutanoyl-CoA

verification_status: unverified

kcat_over_km_origin: calculated

substrate: isobutanoyl-CoA

status: unverified


substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


organism: Streptomyces glaucescens

sequence_source: UniProtKB REST direct check 2026-06-23; accession Q54206; reviewed Swiss-Prot entry FABH_STRGA

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA


organism: Streptomyces coelicolor

assay_conditions_summary: pH 7.2; 303.15 K; cofactor CoA

proof_lines: cosubstrate malonyl-[RedQ], pH 7.2, 30°C

proof_lines: cosubstrate isobutanoyl-CoA, pH 7.2, 30°C

proof_lines: cosubstrate malonyl-[FabC], pH 7.2, 30°C


organism: Chlamydomonas reinhardtii

substrate_name: L-glutamate

substrate: L-glutamate


organism: Chlorella vulgaris

substrate_name: alpha-N-acetyl-L-ornithine

substrate: alpha-N-acetyl-L-ornithine


organism: Citrullus lanatus

assay_conditions_summary: pH 7


organism: Geobacillus stearothermophilus


organism: Lathyrus oleraceus


organism: Methanocaldococcus jannaschii


organism: Saccharomyces cerevisiae


organism: Candida mycoderma

substrate_name: glycerol

assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP

substrate: glycerol


organism: Candida vini

substrate_name: Glycerol; ATP

substrate: Glycerol; ATP


organism: Cellulomonas sp.

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP

proof_lines:
pH 8.5, 30°C
ATP at 10.5 mM Mg2+, pH 8.5, 30°C
ATP at 21 mM Mg2+, pH 8.5, 30°C


organism: Cucumis sativus

substrate_name: UTP

substrate: UTP


organism: Elizabethkingia meningoseptica

substrate_name: ATP

substrate: ATP


organism: Epidermophyton floccosum


organism: Escherichia coli

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

mutation_type: substitution

proof_lines: E478C mutant protein, allosteric regulation


proof_lines: E478C/T428V/R429N mutant protein, allosteric regulation


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


substrate_name: N(2)-acetyl-L-ornithine (at pH 7.0)

substrate: N(2)-acetyl-L-ornithine (at pH 7.0)


substrate_name: acetyl-CoA (AGSase activity)

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

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA (AGSase activity)


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

substrate_name: N-acetyl-L-ornithine

substrate: N-acetyl-L-ornithine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: glutamate

substrate: glutamate


organism: Streptomyces clavuligerus

substrate_name: L-N-acetylornithine (at 37 degrees Celsius and pH 8.0)

assay_conditions_summary: pH 8


organism: Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E)


organism: Arabidopsis thaliana


organism: Escherichia coli (strain K12)


organism: Homo sapiens


organism: Enterococcus casseliflavus

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Thermococcus kodakarensis

sequence_variant_note: Resolved canonical sequence from UniProtKB:O93623 canonical sequence with row-specific K271E substitution; residue 271 checked directly from UniProt REST on 2026-06-23. and applied mutation signature K271E to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant enzyme mutant K271E


sequence_source: UniProtKB:O93623 canonical FASTA; RCSB SIFTS structure entries align to O93623 for Thermococcus kodakarensis glycerol kinase.


enzyme_display_name: 15-cis-phytoene synthase

organism: Capsicum annuum

substrate_name: geranylgeranyl diphosphate

enzyme: 15-cis-phytoene synthase

substrate: geranylgeranyl diphosphate


organism: Pantoea ananas

substrate_name: GGPP (at pH 8 and 37 degrees Celsius)

substrate: GGPP (at pH 8 and 37 degrees Celsius)


organism: Citrullus lanatus

substrate_name: L-Glutamate; N2-Acetyl-L-ornithine

sequence_source: UniProtKB:Q3C251 direct lookup

substrate: L-Glutamate; N2-Acetyl-L-ornithine


organism: Geobacillus stearothermophilus

sequence_source: UniProtKB:Q07908 direct lookup


organism: Methanocaldococcus jannaschii

substrate_name: N2-Acetyl-L-ornithine; L-Glutamate

sequence_source: UniProtKB:Q57645 direct lookup

substrate: N2-Acetyl-L-ornithine; L-Glutamate


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WPZ3 direct lookup

proof_lines: pH and temperature not specified in the publication, versus 1 mM of N2-acetyl-L-ornithine


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:Q04728 direct lookup


sequence_source: UniProtKB:Q9M8L4 direct lookup


organism: Bombyx mori

sequence_source: UniProtKB:B0I1G6 direct lookup

assay_conditions_summary: 278.15 K; cofactor ATP

proof_lines: enzyme source: crude extract from diapause eggs exposed to 5°C for 200 days, Bombyx mori has 3 glycerol kinase genes


organism: Cellulomonas sp.


proof_lines: mutant enzyme T386I/F388Y, at pH 7.5 and 37°C


proof_lines: mutant enzyme A344V/T386I/F388Y, at pH 7.5 and 37°C


smiles: OCC(O)CO


organism: Cucumis sativus

substrate_name: ATP; Glycerol

sequence_source: UniProtKB:A0A0A0KA32 direct lookup

substrate: ATP; Glycerol


organism: Enterococcus faecalis

sequence_source: UniProtKB:O34154 direct lookup


organism: Plasmodium falciparum

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:Q8IDI4 direct lookup

source_databases_merged: sabio_rk brenda skid


organism: Capsicum sp.

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


organism: Solanum lycopersicum

proof_lines: pH 8.0, 28°C, chloroplast enzyme and chromoplast enzyme


organism: Escherichia coli

substrate_name: dihydroxyacetone

proof_lines:
pH 7.0, 25°C
25°C, plus D-glyceraldehyde
ATP in form of MgATP2-

substrate: dihydroxyacetone


organism: Gallus gallus

proof_lines:
and also 0.22 mM, 30°C
and also 0.025 mM, 30°C


organism: Haemophilus influenzae

proof_lines:
and also 2.5 mM, pH 7.0, 25°C
and also 0.045 mM, pH 7.0, 25°C


organism: Mus musculus

proof_lines:
and also 1.5 mM, 30°C
and also 0.04 mM, 30°C


organism: Pediococcus pentosaceus


organism: Rattus norvegicus

proof_lines:
and also 1.26 mM, 30°C
pH 7.35, 37°C
and also 0.02 mM, 30°C


organism: Thermococcus kodakarensis

assay_conditions_summary: pH 8; 353.15 K; cofactor ATP


organism: Thermus thermophilus


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP


organism: Trypanosoma brucei gambiense

substrate_name: ADP

assay_conditions_summary: pH 6.8; 310.15 K; cofactor ADP

substrate: ADP


enzyme_display_name: lysozyme

proof_lines: human serum albumin-bound enzyme, pH 5.2, 37°C

enzyme: lysozyme


organism: Homo sapiens

km_display: Not reported


organism: Liolophura japonica


organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)

substrate_name: Unknown

substrate: Unknown


organism: Ruditapes philippinarum

substrate_name: p-nitrophenyl beta 1,4-linked pentamer of N-acetyl-D-glucosamine ((GlcNAc)5-PNP) at pH 5 and 40 degrees Celsius

assay_conditions_summary: pH 5


enzyme_display_name: deoxynogalonate monooxygenase

organism: Streptomyces nogalater

substrate_name: dithranol

proof_lines: kcat is 1.5 sec(-1) for monooxygenase activity with dithranol as substrate.

enzyme: deoxynogalonate monooxygenase

substrate: dithranol


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O54259 and applied mutation signature N63A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1). Printed enzyme line 'Asn63Ala'; column 'Vmax (umol min^-1 mg^-1)' = 0.07; column 'relative Vmax (%)' = 1.1; column 'kcat (s^-1)' = 0.02; column 'KM (uM)' = 68; column 'kcat/KM (M^-1 s^-1)' = 2.3 x 10^2. The value printed after the plus/minus sign beside the Vmax and KM cells of this line is the printed standard error and is not a catalog metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.02 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.02 s^(-1). Km: printed Table 3 cell 68 in a column headed KM (uM); 1 uM is 0.001 mM, so 68 / 1000 = 0.068 mM. kcat/Km: printed Table 3 cell 2.3 x 10^2 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 229.99999999999997 / 1000 = 0.22999999999999998 s^-1 mM^-1. The catalog values for this identity are kcat 0.02 s^(-1), Km 0.068 mM; this identity stores no kcat_over_km field.

raw_value_unit_evidence: Table 3, printed enzyme line 'Asn63Ala': kcat = 0.02 s^-1; KM = 68 uM; printed kcat/KM = 2.3 x 10^2 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 3, printed enzyme line 'Asn63Ala'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O54259 and applied mutation signature H49A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1). Printed enzyme line 'His49Ala'; column 'Vmax (umol min^-1 mg^-1)' = 1.3; column 'relative Vmax (%)' = 20.6; column 'kcat (s^-1)' = 0.3; column 'KM (uM)' = 150; column 'kcat/KM (M^-1 s^-1)' = 2.0 x 10^3. The value printed after the plus/minus sign beside the Vmax and KM cells of this line is the printed standard error and is not a catalog metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.3 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.3 s^(-1). Km: printed Table 3 cell 150 in a column headed KM (uM); 1 uM is 0.001 mM, so 150 / 1000 = 0.15 mM. kcat/Km: printed Table 3 cell 2.0 x 10^3 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2000.0 / 1000 = 2.0 s^-1 mM^-1. The catalog values for this identity are kcat 0.3 s^(-1), Km 0.15 mM; this identity stores no kcat_over_km field.

raw_value_unit_evidence: Table 3, printed enzyme line 'His49Ala': kcat = 0.3 s^-1; KM = 150 uM; printed kcat/KM = 2.0 x 10^3 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 3, printed enzyme line 'His49Ala'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O54259 and applied mutation signature N18A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1). Printed enzyme line 'Asn18Ala'; column 'Vmax (umol min^-1 mg^-1)' = 0.1; column 'relative Vmax (%)' = 1.6; column 'kcat (s^-1)' = 0.03; column 'KM (uM)' = 120; column 'kcat/KM (M^-1 s^-1)' = 2.2 x 10^2. The value printed after the plus/minus sign beside the Vmax and KM cells of this line is the printed standard error and is not a catalog metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.03 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.03 s^(-1). Km: printed Table 3 cell 120 in a column headed KM (uM); 1 uM is 0.001 mM, so 120 / 1000 = 0.12 mM. kcat/Km: printed Table 3 cell 2.2 x 10^2 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 220.00000000000003 / 1000 = 0.22000000000000003 s^-1 mM^-1. The catalog values for this identity are kcat 0.03 s^(-1), Km 0.12 mM and kcat_over_km 0.25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed enzyme line 'Asn18Ala': kcat = 0.03 s^-1; KM = 120 uM; printed kcat/KM = 2.2 x 10^2 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 3, printed enzyme line 'Asn18Ala'


sequence_variant_note: Resolved canonical sequence from UniProt O54259 FASTA direct lookup plus validated R90E substitution on the canonical sequence. and applied mutation signature R90E to reconstruct the assayed variant sequence.


normalized_value_unit_evidence: kcat: printed Table 3 cell 0.03 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.03 s^(-1). Km: printed Table 3 cell 120 in a column headed KM (uM); 1 uM is 0.001 mM, so 120 / 1000 = 0.12 mM. kcat/Km: printed Table 3 cell 2.2 x 10^2 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 220.00000000000003 / 1000 = 0.22000000000000003 s^-1 mM^-1. The catalog values for this identity are kcat 0.03 s^(-1), Km 0.12 mM; this identity stores no kcat_over_km field.

table_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1).


normalized_value_unit_evidence: kcat: printed Table 3 cell 0.3 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.3 s^(-1). Km: printed Table 3 cell 150 in a column headed KM (uM); 1 uM is 0.001 mM, so 150 / 1000 = 0.15 mM. kcat/Km: printed Table 3 cell 2.0 x 10^3 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2000.0 / 1000 = 2.0 s^-1 mM^-1. The catalog values for this identity are kcat 0.3 s^(-1), Km 0.15 mM and kcat_over_km 2.0 s^(-1)*mM^(-1).


sequence_source: UniProt O54259 FASTA direct lookup.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1). Printed enzyme line 'SnoaB-N'; column 'Vmax (umol min^-1 mg^-1)' = 6.3; column 'relative Vmax (%)' = 100; column 'kcat (s^-1)' = 1.5; column 'KM (uM)' = 140; column 'kcat/KM (M^-1 s^-1)' = 1.1 x 10^4. The value printed after the plus/minus sign beside the Vmax and KM cells of this line is the printed standard error and is not a catalog metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.5 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.5 s^(-1). Km: printed Table 3 cell 140 in a column headed KM (uM); 1 uM is 0.001 mM, so 140 / 1000 = 0.14 mM. kcat/Km: printed Table 3 cell 1.1 x 10^4 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11000.0 / 1000 = 11.0 s^-1 mM^-1. The catalog values for this identity are kcat 1.5 s^(-1), Km 0.14 mM and kcat_over_km 10.714285714285714 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed enzyme line 'SnoaB-N': kcat = 1.5 s^-1; KM = 140 uM; printed kcat/KM = 1.1 x 10^4 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 3, printed enzyme line 'SnoaB-N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O54259 and applied mutation signature W67F to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1). Printed enzyme line 'Trp67Phe'; column 'Vmax (umol min^-1 mg^-1)' = 0.06; column 'relative Vmax (%)' = 1.0; column 'kcat (s^-1)' = 0.02; column 'KM (uM)' = 220; column 'kcat/KM (M^-1 s^-1)' = 68. The value printed after the plus/minus sign beside the Vmax and KM cells of this line is the printed standard error and is not a catalog metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.02 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.02 s^(-1). Km: printed Table 3 cell 220 in a column headed KM (uM); 1 uM is 0.001 mM, so 220 / 1000 = 0.22 mM. kcat/Km: printed Table 3 cell 68 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 68.0 / 1000 = 0.068 s^-1 mM^-1. The catalog values for this identity are kcat 0.02 s^(-1), Km 0.22 mM; this identity stores no kcat_over_km field.

raw_value_unit_evidence: Table 3, printed enzyme line 'Trp67Phe': kcat = 0.02 s^-1; KM = 220 uM; printed kcat/KM = 68 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 3, printed enzyme line 'Trp67Phe'


normalized_value_unit_evidence: kcat: printed Table 3 cell 0.02 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.02 s^(-1). Km: printed Table 3 cell 220 in a column headed KM (uM); 1 uM is 0.001 mM, so 220 / 1000 = 0.22 mM. kcat/Km: printed Table 3 cell 68 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 68.0 / 1000 = 0.068 s^-1 mM^-1. The catalog values for this identity are kcat 0.02 s^(-1), Km 0.22 mM and kcat_over_km 0.09090909090909091 s^(-1)*mM^(-1).


proof_lines: pH 7.0, 22°C, wild-type enzyme, recombinant enzyme construct with a His tag at the C-terminus

proof_lines: pH 7.0, 22°C, wild-type enzyme, recombinant enzyme with N-terminal polyhistidine tag


normalized_value_unit_evidence: kcat: printed Table 3 cell 0.02 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.02 s^(-1). Km: printed Table 3 cell 68 in a column headed KM (uM); 1 uM is 0.001 mM, so 68 / 1000 = 0.068 mM. kcat/Km: printed Table 3 cell 2.3 x 10^2 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 229.99999999999997 / 1000 = 0.22999999999999998 s^-1 mM^-1. The catalog values for this identity are kcat 0.02 s^(-1), Km 0.068 mM and kcat_over_km 0.29411764705882354 s^(-1)*mM^(-1).


sequence_source: UniProt O54259 FASTA direct lookup plus validated R90E substitution on the canonical sequence.


proof_lines:
at pH 6.3 and 20°C
at pH 9.8 and 20°C


enzyme_display_name: aromatase

organism: Aptenodytes forsteri

proof_lines: pH 7.4, temperature not specified in the publication

enzyme: aromatase


substrate_name: NADPH; O2; Testosterone; H+

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

assay_conditions_summary: cofactor NADP+

proof_lines: SABIO-RK modifier species: aromatase(Enzyme) mutant D509A

substrate: NADPH; O2; Testosterone; H+


enzyme_display_name: glucose-1,6-bisphosphate synthase

substrate_name: alpha-D-glucose 1-phosphate (for glucose 1,6-bisphosphate synthase activity)

enzyme: glucose-1,6-bisphosphate synthase


enzyme_display_name: Aromatase

substrate_name: H+; Testosterone; NADPH; O2

sequence_source: UniProtKB REST release 2026_02 (release date 2026-06-10; API deployment 2026-06-12); accession P11511

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

enzyme: Aromatase

substrate: H+; Testosterone; NADPH; O2


organism: Neomoorella thermoacetica

substrate_name: propanoyl-CoA

assay_conditions_summary: pH 7.6; 328.15 K; cofactor CoA

substrate: propanoyl-CoA


substrate_name: propionyl-CoA

substrate: propionyl-CoA


enzyme_display_name: Bifunctional 15-cis-phytoene synthase, chromoplastic

organism: Capsicum annuum

substrate_name: Geranylgeranyl diphosphate

sequence_source: UniProtKB REST release 2026_02 (release date 2026-06-10; API deployment 2026-06-12); accession P37272

substrate: Geranylgeranyl diphosphate


organism: Pantoea ananas

sequence_source: UniProtKB REST release 2026_02 (release date 2026-06-10; API deployment 2026-06-12); accession P21683


enzyme_display_name: Phytoene synthase 1, chloroplastic

organism: Solanum lycopersicum

sequence_source: UniProtKB REST release 2026_02 (release date 2026-06-10; API deployment 2026-06-12); accession P08196

assay_conditions_summary: pH 6.5; cofactor FAD

proof_lines: in 400 mM Tris (pH 6.5), 10 mM sodium ascorbate, 5 mM MgCl2, 0.5 mM MnCl2, 3 mM ATP and 0.02 mM FAD

enzyme: Phytoene synthase 1, chloroplastic


enzyme_display_name: Phytoene synthase 2, chloroplastic

sequence_source: UniProtKB REST release 2026_02 (release date 2026-06-10; API deployment 2026-06-12); accession P37273

enzyme: Phytoene synthase 2, chloroplastic


enzyme_display_name: Glucose 1,6-bisphosphate synthase

substrate_name: Glycerate 1,3-bisphosphate; Glucose 1-phosphate

sequence_source: UniProtKB REST release 2026_02 (release date 2026-06-10; API deployment 2026-06-12); accession Q6PCE3

enzyme: Glucose 1,6-bisphosphate synthase


substrate_name: Glycerate 1,3-bisphosphate; Glucose 6-phosphate

sequence_source: UniProtKB:Q96G03 REST lookup in worker run


organism: Mus musculus

substrate_name: Glycerate 1,3-bisphosphate; D-Glucose 1-phosphate

sequence_source: UniProtKB:Q8CAA7 REST lookup in worker run


enzyme_display_name: ceramide kinase

substrate_name: ATP; N-Acylsphingosine

sequence_source: UniProtKB:Q8TCT0 REST lookup in worker run

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

proof_lines: pH 7.2, 30°C, recombinant ceramide kinase

enzyme: ceramide kinase

substrate: ATP; N-Acylsphingosine


sequence_source: UniProtKB:Q53H12 REST lookup in worker run

assay_conditions_summary: cofactor ATP


sequence_source: UniProtKB:Q9ESW4 REST lookup in worker run


organism: Gallus gallus

sequence_source: UniProtKB:P00698 REST lookup in worker run


organism: Schistocerca gregaria

substrate_name: H2O; Peptidoglycan

sequence_source: UniProtKB:H2EQQ0 REST lookup in worker run

substrate: H2O; Peptidoglycan


organism: Arabidopsis thaliana

substrate_name: C8 ceramide

substrate: C8 ceramide


substrate_name: diacylglycerol

substrate: diacylglycerol


organism: Oryza sativa subsp. japonica

substrate_name: C6 ceramide

substrate: C6 ceramide


proof_lines: substrate androst-4-ene-3,17-dione, pH 7.0, 37°C

proof_lines: substrate 19-hydroxyandrost-4-ene-3,17-dione, pH 7.0, 37°C


organism: Salmonella enterica

substrate_name: propanoyl phosphate

proof_lines: reverse reaction, pH and temperature not specified in the publication

substrate: propanoyl phosphate


organism: Bos taurus

proof_lines: 23°C, pH 8, Mg2+- and Zn2+-enzyme in brain

substrate: Glycerate 1,3-bisphosphate; D-Glucose 1-phosphate


organism: Homo sapiens

substrate_name: ceramide

assay_conditions_summary: pH 7; 295.15 K; cofactor ATP

proof_lines:
pH 7.0, 22°C
recombinant enzyme

substrate: ceramide


organism: Rattus norvegicus

substrate_name: ATP; N-Stearoyl-D-sphingosine

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: pH 7.4, 30°, in the presence of 0.010 mM Ca2+

substrate: ATP; N-Stearoyl-D-sphingosine


substrate_name: LDL

proof_lines: Affinity for LDL is 2.3 to 4-fold lower than for HDL. Relative reactivities are 16% for HDL(3), 1.3% for HDL(2) and 6.5% for LDL.

substrate: LDL


enzyme_display_name: phospholipase A1

organism: Mesocricetus auratus

enzyme: phospholipase A1


proof_lines:
native vesicles, pH 5.4, 37°C
delipidated vesicles, pH 5.4, 37°C


organism: Serratia marcescens

substrate_name: soybean lecithin

sequence_source: NCBI Protein CDG14854.1 from GenBank HG326223.1, linked by PMID 31681748/PMC6811509

substrate: soybean lecithin


organism: Thermomyces lanuginosus

substrate_name: triacylglycerol

substrate: triacylglycerol


organism: Haloferax volcanii

substrate_name: D-Fructose 1-phosphate

sequence_source: UniProt direct accession lookup D4GYE6

assay_conditions_summary: pH 7.5; 315.15 K; cofactor ATP

proof_lines: in 100 mM Tris-HCl, pH 7.5, 7 mM MgCl2, 0.5 M KCl, at 42°C

substrate: D-Fructose 1-phosphate


organism: Serratia sp. (in: enterobacteria)

substrate_name: phosphatidylcholine

sequence_source: UniProt direct accession lookup Q9X9D8

substrate: phosphatidylcholine


organism: Streptomyces albidoflavus

substrate_name: phosphatidic acid

substrate: phosphatidic acid


organism: Clostridium difficile

substrate_name: D-Fructose 1-phosphate; ATP

substrate: D-Fructose 1-phosphate; ATP


organism: Clostridium pasteurianum

substrate_name: ATP; D-Fructose 1-phosphate

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

substrate: ATP; D-Fructose 1-phosphate


organism: Escherichia coli

substrate_name: ATP

assay_conditions_summary: pH 7.1; 303.15 K; cofactor ATP

proof_lines: pH 7.1, 30°C, in the presence of 50 mM KCl

proof_lines: pH 7.1, 30°C, in the presence of 5 mM KCl

substrate: ATP


organism: Haloarcula vallismortis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Klebsiella aerogenes

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Oceanimonas doudoroffii


organism: Pseudomonas doudoroffii


organism: Pseudomonas putida


substrate_name: phosphatidylglycerol

substrate: phosphatidylglycerol


substrate_name: high-density lipoprotein

substrate: high-density lipoprotein


organism: Escherichia coli (strain K12)

substrate_name: fructose 1-phosphate

substrate: fructose 1-phosphate


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)


organism: Dolichovespula maculata

substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens

substrate_name: dipalmitoyl-PC

substrate: dipalmitoyl-PC


organism: Mus musculus


organism: Polistes gallicus


organism: Rattus norvegicus


organism: Vespa tropica


organism: Bos taurus

substrate_name: N-deacetylase K5-polysaccharide

substrate: N-deacetylase K5-polysaccharide


substrate_name: Glucuronyl-N-acetylglucosamine; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C486A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C486A

substrate: Glucuronyl-N-acetylglucosamine; H2O


substrate_name: H2O; Glucuronyl-N-acetylglucosamine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C56A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C56A

substrate: H2O; Glucuronyl-N-acetylglucosamine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C751A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C751A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C818A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C818A


proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C496W


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C486F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C486F


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C486V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C486V


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C586A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C586A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C601A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C601A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C159A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C159A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C486G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C486G


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02353 and applied mutation signature C828A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: [heparan sulfate]-glucosamine N-sulfotransferase(Enzyme) mutant C828A


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


substrate_name: K5 polysaccharide

substrate: K5 polysaccharide


substrate_name: K5 polysaccharide (for deacetylase activity)


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


proof_lines: apparent value, in 50 mM HEPES, pH 7.0, at 37°C


organism: Mycobacterium tuberculosis


enzyme_display_name: inositol oxygenase

organism: Unknown

substrate_name: Inositol

enzyme: inositol oxygenase

substrate: Inositol


enzyme_display_name: venombin A

organism: Daboia russelii russelii

substrate_name: human plasma fibrinogen

proof_lines:
pH 7.4, 37°C, isozyme RV-FVPgamma
pH 7.4, 37°C, isozyme RV-FVPdelta
pH 7.4, 37°C, isozyme RV-FVPbeta

enzyme: venombin A

substrate: human plasma fibrinogen


substrate_name: D-Phe-L-pipecoyl-L-Arg 4-nitroanilide

substrate: D-Phe-L-pipecoyl-L-Arg 4-nitroanilide


substrate_name: myo-Inositol; O2

sequence_source: UniProt Q9UGB7 direct accession lookup

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

proof_lines: MIOX activity present in peak 1 of hydrophobic-interaction chromatography on Resource-PHE column

proof_lines: MIOX activity present in peak 3 of hydrophobic-interaction chromatography on Resource-PHE column

substrate: myo-Inositol; O2


substrate_name: O2; myo-Inositol

sequence_source: UniProt Q9QXN5 direct accession lookup

proof_lines: MIOX activity present in peak 2 of hydrophobic-interaction chromatography on Resource-PHE column

substrate: O2; myo-Inositol


substrate_name: myo-inositol

sequence_variant_note: Resolved canonical sequence from UniProt Q9QXN5 direct accession lookup plus validated mutation reconstruction and applied mutation signature L240M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L240M, at 37°C, pH not specified in the publication

substrate: myo-inositol


sequence_variant_note: Resolved canonical sequence from UniProt Q9QXN5 direct accession lookup plus validated mutation reconstruction and applied mutation signature S173N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S173N, at 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt Q9QXN5 direct accession lookup plus validated mutation reconstruction and applied mutation signature D82Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D82Y, at 37°C, pH not specified in the publication


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


sequence_variant_note: Resolved canonical sequence from UniProt Q9QXN5 direct accession lookup plus validated mutation reconstruction and applied mutation signature D82Y/S173N/L240M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D82Y/S173N/L240M, at 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt Q9QXN5 direct accession lookup plus validated mutation reconstruction and applied mutation signature Q62H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q62H, at 37°C, pH not specified in the publication


sequence_source: UniProt Q9QXN4 direct accession lookup


organism: Sus scrofa

sequence_source: UniProt Q8WN98 direct accession lookup

proof_lines: with Fe(2+) and L-cysteine as activators


substrate_name: Histone H3(1-24)-[dimethyl]K9; 2-Oxoglutarate; O2

sequence_source: UniProt Q9UPP1 direct accession lookup; reconstructed PHF8 residues 1-447 from source construct note

proof_lines: SABIO-RK modifier species: [histone H3]-dimethyl-L-lysine9 demethylase(Enzyme) mutant PHF8(1-447)


substrate_name: O2; 2-Oxoglutarate; Histone H3(1-24)-[dimethyl]K9

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: [histone H3]-dimethyl-L-lysine9 demethylase(Enzyme) mutant KIAA1718(96-488)

proof_lines: SABIO-RK modifier species: [histone H3]-dimethyl-L-lysine9 demethylase(Enzyme) mutant KIAA1718(1-488)


substrate_name: not preserved in the selected batch

sequence_source: UniProt Q6ZMT4 direct accession lookup

proof_lines: pH and temperature not specified in the publication

substrate: not preserved in the selected batch


substrate_name: [histone H3]-N6-methyl-L-lysine9

sequence_source: UniProt Q9Y4C1 direct accession lookup

substrate: [histone H3]-N6-methyl-L-lysine9


sequence_source: UniProt O60341 direct accession lookup

assay_conditions_summary: pH 7.5; 298.15 K; cofactor FAD

proof_lines:
pH 7.5, 25°C
pH 7.5, 25°C, recombinant enzyme


substrate_name: H3 monomethyl-K4

proof_lines: kcat is 7.35 sec(-1) with H3 monomethyl-K4 as substrate when part of a complex with RCOR1 (at 25 degrees Celsius).

proof_lines: kcat is 5.47 sec(-1) with H3 monomethyl-K4 as substrate when part of a complex with RCOR1 (at 25 degrees Celsius).

proof_lines: kcat is 9.4 sec(-1) with H3 monomethyl-K4 as substrate when part of a complex with RCOR1 (at 25 degrees Celsius).

substrate: H3 monomethyl-K4


enzyme_display_name: (2Z,6E)-farnesyl diphosphate synthase

organism: Thermobifida fusca (strain YX)

substrate_name: geranyl diphosphate (at 37 degrees Celsius and at pH 7.5)

proof_lines: kcat is 229 sec(-1) with geranyl diphosphate as substrate and 282 sec(-1) with isopentenyl diphosphate as substrate.

enzyme: (2Z,6E)-farnesyl diphosphate synthase


enzyme_display_name: acetyl-CoA hydrolase

substrate_name: acetyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 7000 sec(-1) for the hydrolysis of acetyl-CoA.

enzyme: acetyl-CoA hydrolase

substrate: acetyl-CoA


substrate_name: acetoacetyl-CoA

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

substrate: acetoacetyl-CoA


proof_lines: In summary, KM for medium- to long-chain acyl CoAs is in the order 1.4-6.7 uM, and with short-chain acyl CoAs range from 8 to 30 uM. KM for bile acid-CoA esters is in the range 6-15 uM.


proof_lines: with Fe(II) and quinolinic acid as activators

proof_lines: with Fe(II) and L-cysteine as activators


organism: Acetoanaerobium sticklandii

substrate_name: nicotinic acid mononucleotide

proof_lines:
cosubstrate adenine
cosubstrate benzimidazole

substrate: nicotinic acid mononucleotide


organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: benzimidazole

substrate: benzimidazole


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: NAD+

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

proof_lines:
pH 7.0, 37°C
or less

substrate: NAD+


organism: Corynebacterium efficiens

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


organism: Corynebacterium glutamicum

substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


organism: Thermobifida fusca


organism: Salmonella enterica

substrate_name: beta-nicotinate D-ribonucleotide

source_db: skid

source_license: CC BY-NC-ND 4.0

substrate: beta-nicotinate D-ribonucleotide

source: skid


organism: Sporomusa ovata

substrate_name: phenol

substrate: phenol


sequence_variant_note: Resolved canonical sequence from direct_uniprot_rest:P9WFF5_plus_computed_L84A_L85F and applied mutation signature L84A/L85F to reconstruct the assayed variant sequence.

proof_lines:
mutant L84A/L85F
pH 7.9, 37°C, mutant enzyme L84A/L85F


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

source_databases_merged: brenda skid


organism: Cerastes cerastes

substrate_name: H2O; N-Benzoyl-L-arginine ethyl ester

sequence: VIGGDEXDINEHRSLALMYXSWSHRFIXXGXLI

wild_type_sequence: VIGGDEXDINEHRSLALMYXSWSHRFIXXGXLI

substrate: H2O; N-Benzoyl-L-arginine ethyl ester


organism: Homo sapiens

substrate_name: histone H3 H3K9Me2

substrate: histone H3 H3K9Me2


enzyme_display_name: diglucosylglycerate octanoyltransferase

organism: Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)

substrate_name: diglucosylglycerate (at 37 degrees Celsius)

enzyme: diglucosylglycerate octanoyltransferase


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate: diglucosylglycerate (at 37 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: neryl diphosphate (at pH 7.9 and 37 degrees Celsius)


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


organism: Rattus norvegicus


organism: Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8)

substrate_name: acetyl-CoA (for acetyl-CoA hydrolase reaction)


organism: Bothrops leucurus

substrate_name: H-D-Val-Leu-Arg-pNA (S-2266)

substrate: H-D-Val-Leu-Arg-pNA (S-2266)


organism: Lachesis muta rhombeata

substrate_name: N-p-tosyl-L-arginine methyl ester (TAME)

sequence: VIGGDECNINEHRFLVALYDGLSGTFLCGG

wild_type_sequence: VIGGDECNINEHRFLVALYDGLSGTFLCGG


substrate_name: H2O; Acetyl-CoA

assay_conditions_summary: pH 7.4; cofactor CoA

proof_lines: tetrameric enzyme, in presence of 2mM ATP

substrate: H2O; Acetyl-CoA


organism: Bothrops jararaca

sequence_source: UniProtKB reviewed accession P81661 from direct EC 3.4.21.74 and Bothrops jararaca lookup


organism: Crotalus adamanteus

substrate_name: D-phenylglycyl-Phe-Arg 4-nitroanilide

sequence_source: UniProtKB reviewed accession F8S114 from direct EC 3.4.21.74 and Crotalus adamanteus lookup

substrate: D-phenylglycyl-Phe-Arg 4-nitroanilide


organism: Mycolicibacterium hassiacum

substrate_name: octanoyl-CoA

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: 37°C, pH 8.0, cosubstrate: 20 mM 2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-D-glycerate

proof_lines: 37°C, pH 8.0, cosubstrate: 0.1 mM hexanoyl-CoA

proof_lines: 37°C, pH 8.0, cosubstrate: 20 mM 2-O-(alpha-D-glucopyranosyl)-D-glycerate

substrate: octanoyl-CoA


assay_conditions_summary: pH 8; 310.15 K; buffer reactions performed in 50 mM BTP; cofactor CoA

column_label: Table 2 (Apparent kinetic parameters of M. hassiacum and M. smegmatis OctTs), line with OctT 'Mh', substrate 'Oct-CoA' and fixed co-substrate 'DGG 20 mM'; column 'Km (mM)' = 0.06; column 'Vmax (nmol/min/mg)' = 162; column 'kcat (min^-1)' = 0.12; column 'kcat/Km (mM^-1 min^-1)' = 1.9. Table 2 prints no Ki column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.06 mM; the printed head is millimolar, so no unit conversion applies and the paper value is 0.06 mM, which is the exported Km. kcat: printed Table 2 cell 0.12 min^-1; the printed head is per minute, so 0.12 / 60 = 0.002 s^(-1), which is the exported kcat. kcat/Km: printed Table 2 cell 1.9 mM^-1 min^-1; one per-minute efficiency is one sixtieth of the same per-second efficiency, so 1.9 / 60 = 0.03166666666666666 s^(-1)*mM^(-1); the proposed kcat/Km is 0.03166666666666666 s^(-1)*mM^(-1), which is the paper's own independently fitted efficiency cell.

raw_value_unit_evidence: Table 2, line with OctT 'Mh', substrate 'Oct-CoA' and fixed co-substrate 'DGG 20 mM': Km cell = 0.06 mM; Vmax cell = 162 nmol/min/mg; kcat cell = 0.12 min^-1; printed kcat/Km cell = 1.9 mM^-1 min^-1.

table_label: Table 2: Apparent kinetic parameters of M. hassiacum and M. smegmatis OctTs (Scientific Reports 2015, volume 5, article 13610), PDF page 4 of 18; printed column heads OctT, Substrate, Co-substrate concentration (fixed), Km (mM), Vmax (nmol/min/mg), kcat (min^-1) and kcat/Km (mM^-1 min^-1)


substrate_name: hexanoyl-CoA

column_label: Table 2 (Apparent kinetic parameters of M. hassiacum and M. smegmatis OctTs), line with OctT 'Mh', substrate 'Hex-CoA' and fixed co-substrate 'DGG 20 mM'; column 'Km (mM)' = 0.02; column 'Vmax (nmol/min/mg)' = 59; column 'kcat (min^-1)' = 0.04; column 'kcat/Km (mM^-1 min^-1)' = 2.1. Table 2 prints no Ki column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.02 mM; the printed head is millimolar, so no unit conversion applies and the paper value is 0.02 mM, which is the exported Km. kcat: printed Table 2 cell 0.04 min^-1; the printed head is per minute, so 0.04 / 60 = 0.0006666666666666666 s^(-1); the proposed kcat is the full-precision value 0.0006666666666666666 s^(-1) in place of the two-significant-figure value 0.00067 s^(-1) the catalog holds. kcat/Km: printed Table 2 cell 2.1 mM^-1 min^-1; one per-minute efficiency is one sixtieth of the same per-second efficiency, so 2.1 / 60 = 0.035 s^(-1)*mM^(-1); the proposed kcat/Km is 0.035 s^(-1)*mM^(-1), which is the paper's own independently fitted efficiency cell.

raw_value_unit_evidence: Table 2, line with OctT 'Mh', substrate 'Hex-CoA' and fixed co-substrate 'DGG 20 mM': Km cell = 0.02 mM; Vmax cell = 59 nmol/min/mg; kcat cell = 0.04 min^-1; printed kcat/Km cell = 2.1 mM^-1 min^-1.

substrate: hexanoyl-CoA


organism: Mycolicibacterium smegmatis

column_label: Table 2 (Apparent kinetic parameters of M. hassiacum and M. smegmatis OctTs), line with OctT 'Ms', substrate 'Oct-CoA' and fixed co-substrate 'DGG 45 mM'; column 'Km (mM)' = 0.03; column 'Vmax (nmol/min/mg)' = 1898; column 'kcat (min^-1)' = 2.2; column 'kcat/Km (mM^-1 min^-1)' = 86. Table 2 prints no Ki column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.03 mM; the printed head is millimolar, so no unit conversion applies and the paper value is 0.03 mM, which is the exported Km. kcat: printed Table 2 cell 2.2 min^-1; the printed head is per minute, so 2.2 / 60 = 0.03666666666666667 s^(-1); the proposed kcat is the full-precision value 0.03666666666666667 s^(-1) in place of the two-significant-figure value 0.037 s^(-1) the catalog holds. kcat/Km: printed Table 2 cell 86 mM^-1 min^-1; one per-minute efficiency is one sixtieth of the same per-second efficiency, so 86 / 60 = 1.4333333333333333 s^(-1)*mM^(-1); the proposed kcat/Km is 1.4333333333333333 s^(-1)*mM^(-1), which is the paper's own independently fitted efficiency cell.

raw_value_unit_evidence: Table 2, line with OctT 'Ms', substrate 'Oct-CoA' and fixed co-substrate 'DGG 45 mM': Km cell = 0.03 mM; Vmax cell = 1898 nmol/min/mg; kcat cell = 2.2 min^-1; printed kcat/Km cell = 86 mM^-1 min^-1.


proof_lines: 37°C, pH 8.0, cosubstrate: 45 mM 2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-D-glycerate

proof_lines: 37°C, pH 8.0, cosubstrate: 0.1 mM octanoyl-CoA

proof_lines: 37°C, pH 8.0, cosubstrate: 45 mM 2-O-(alpha-D-glucopyranosyl)-D-glycerate


organism: Pseudomonas denitrificans


organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: nicotinic acid mononucleotide


organism: Salmonella enterica

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q05603 and applied mutation signature C160A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q05603 and applied mutation signature G320D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q05603 and applied mutation signature G257D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q05603 and applied mutation signature G257A to reconstruct the assayed variant sequence.


enzyme_display_name: curcumin synthase

organism: Curcuma longa

substrate_name: feruloyl-CoA

proof_lines: kcat is 1.1 min(-1) with feruloyl-CoA. kcat is 0.85 min(-1) with p-coumaroyl-CoA.

enzyme: curcumin synthase

substrate: feruloyl-CoA


proof_lines: kcat is 0.19 min(-1) with feruloyl-CoA. kcat is 0.36 min(-1) with p-coumaroyl-CoA.


proof_lines: kcat is 0.41 min(-1) with feruloyl-CoA. kcat is 0.94 min(-1) with p-coumaroyl-CoA.


enzyme_display_name: alternansucrase

organism: Leuconostoc citreum

substrate_name: sucrose

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

proof_lines: pH 4.0, 40°C, transglycosylation, mutant enzyme W675Y

enzyme: alternansucrase

substrate: sucrose


proof_lines: pH 4.0, 40°C, transglycosylation, mutant enzyme W675L


proof_lines: pH 4.0, 40°C, transglycosylation, mutant enzyme W675I


proof_lines: pH 4.0, 40°C, transglycosylation, mutant enzyme W675S


proof_lines: pH 4.0, 40°C, transglycosylation, wild-type enzyme


proof_lines: pH 4.0, 40°C, transglycosylation, mutant enzyme W675H


proof_lines: pH 4.0, 40°C, transglycosylation, mutant enzyme W675N


proof_lines: pH 4.0, 40°C, transglycosylation, mutant enzyme W675F


proof_lines: pH 4.0, 40°C, transglycosylation, mutant enzyme W675D


substrate_name: Sucrose; alpha-D-Glucan

substrate: Sucrose; alpha-D-Glucan


organism: Streptococcus mutans

substrate_name: Sucrose; Dextran

substrate: Sucrose; Dextran


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


substrate_name: cinnamoyl-diketide-N-acetylcysteamine

sequence_source: UniProtKB:C0SVZ6 direct lookup with source-record identity cache

substrate: cinnamoyl-diketide-N-acetylcysteamine


substrate_name: 3-oxo-5-phenyl-4-pentenoic acid

substrate: 3-oxo-5-phenyl-4-pentenoic acid


proof_lines: pH 4.0, 40°C, transglycosylation, mutant enzyme W675A


organism: Unknown

substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Lathyrus oleraceus


organism: Mesocricetus auratus


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: tetrameric enzyme, in presence of 2mM ATP


organism: Gallus gallus


substrate_name: Acetyl-CoA; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P23228 and applied mutation signature H264N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA hydrolase(Enzyme) mutant H264N

substrate: Acetyl-CoA; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23228 and applied mutation signature H264A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA hydrolase(Enzyme) mutant H264A


enzyme_display_name: Acetyl-coenzyme A thioesterase

organism: Mus musculus

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

proof_lines: pH 8, 37°C, Vmax: 44 micromol/min/mg, wild-type

proof_lines: pH 8, 37°C, Vmax: 30 micromol/min/mg, wild-type

enzyme: Acetyl-coenzyme A thioesterase


proof_lines: pH 8, 37°C, mutant form lacking START domain

proof_lines: pH 8, 37°C, Vmax: 23.4 micromol/min/mg, mutant form lacking START domain


assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA

proof_lines:
25°C, native enzyme
25°C, recombinant enzyme
pH 7.4


enzyme_display_name: Ethanol acetyltransferase 1

organism: Wickerhamomyces anomalus

enzyme: Ethanol acetyltransferase 1


enzyme_display_name: purine nucleosidase

organism: Caenorhabditis elegans

substrate_name: inosine (at pH 7.0 and 37 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: kcat is 0.79 sec(-1) with inosine as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:12777783). kcat is 0.203 sec(-1) with inosine as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:28218438). kcat is 0.78 sec(-1) with adenosine a

enzyme: purine nucleosidase


organism: Arabidopsis thaliana

substrate_name: inosine

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

substrate: inosine


substrate_name: Inosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9XWN7 and applied mutation signature C42A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer containing 20 mM Hepes pH 7

column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C42A block, substrate row Inosine: kcat (s^-1) = 0.024; KM (uM) = 215; kcat/KM (M^-1 s^-1) = 112.

normalized_value_unit_evidence: kcat: printed Table II cell 0.024 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.024 s^(-1). KM: printed Table II cell 215 uM; 215 / 1000 = 0.215, so the paper value is 0.215 mM. kcat/KM: printed Table II cell 112 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 112 / 1000 = 0.112 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C42A block, substrate row Inosine: kcat = 0.024 s^-1; KM = 215 uM; printed kcat/KM = 112 M^-1 s^-1.

table_label: Table II: Kinetic Constants of Wild-Type and Mutant CeNH (Protein Science 2017, 26:985-996)

substrate: Inosine


substrate_name: adenosine

column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C42A block, substrate row Adenosine: kcat (s^-1) = 0.023; KM (uM) = 94; kcat/KM (M^-1 s^-1) = 245.

normalized_value_unit_evidence: kcat: printed Table II cell 0.023 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.023 s^(-1). KM: printed Table II cell 94 uM; 94 / 1000 = 0.094, so the paper value is 0.094 mM. kcat/KM: printed Table II cell 245 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 245 / 1000 = 0.245 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C42A block, substrate row Adenosine: kcat = 0.023 s^-1; KM = 94 uM; printed kcat/KM = 245 M^-1 s^-1.

substrate: adenosine


substrate_name: guanosine

sequence_source: UniProt REST direct lookup Q9XWN7 on 2026-06-24; selected accession context

column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH Wild-type block, substrate row Guanosine: kcat (s^-1) = 0.143; KM (uM) = 68; kcat/KM (M^-1 s^-1) = 2,103.

normalized_value_unit_evidence: kcat: printed Table II cell 0.143 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.143 s^(-1). KM: printed Table II cell 68 uM; 68 / 1000 = 0.068, so the paper value is 0.068 mM. kcat/KM: printed Table II cell 2,103 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2,103 / 1000 = 2.103 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH Wild-type block, substrate row Guanosine: kcat = 0.143 s^-1; KM = 68 uM; printed kcat/KM = 2,103 M^-1 s^-1.

substrate: guanosine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9XWN7 and applied mutation signature C253A to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C253A block, substrate row Guanosine: kcat (s^-1) = 0.0051; KM (uM) = 300; kcat/KM (M^-1 s^-1) = 17.

normalized_value_unit_evidence: kcat: printed Table II cell 0.0051 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0051 s^(-1). KM: printed Table II cell 300 uM; 300 / 1000 = 0.3, so the paper value is 0.3 mM. kcat/KM: printed Table II cell 17 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 17 / 1000 = 0.017 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C253A block, substrate row Guanosine: kcat = 0.0051 s^-1; KM = 300 uM; printed kcat/KM = 17 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C253A block, substrate row p-NPR: kcat (s^-1) = 0.017; KM (uM) = 9; kcat/KM (M^-1 s^-1) = 1,889.

normalized_value_unit_evidence: kcat: printed Table II cell 0.017 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.017 s^(-1). KM: printed Table II cell 9 uM; 9 / 1000 = 0.009, so the paper value is 0.009 mM. kcat/KM: printed Table II cell 1,889 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1,889 / 1000 = 1.889 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C253A block, substrate row p-NPR: kcat = 0.017 s^-1; KM = 9 uM; printed kcat/KM = 1,889 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C253A block, substrate row Inosine: kcat (s^-1) = 0.0043; KM (uM) = 343; kcat/KM (M^-1 s^-1) = 13.

normalized_value_unit_evidence: kcat: printed Table II cell 0.0043 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0043 s^(-1). KM: printed Table II cell 343 uM; 343 / 1000 = 0.343, so the paper value is 0.343 mM. kcat/KM: printed Table II cell 13 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 13 / 1000 = 0.013 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C253A block, substrate row Inosine: kcat = 0.0043 s^-1; KM = 343 uM; printed kcat/KM = 13 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C253A block, substrate row Adenosine: kcat (s^-1) = 0.0042; KM (uM) = 96; kcat/KM (M^-1 s^-1) = 44.

normalized_value_unit_evidence: kcat: printed Table II cell 0.0042 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0042 s^(-1). KM: printed Table II cell 96 uM; 96 / 1000 = 0.096, so the paper value is 0.096 mM. kcat/KM: printed Table II cell 44 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 44 / 1000 = 0.044 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C253A block, substrate row Adenosine: kcat = 0.0042 s^-1; KM = 96 uM; printed kcat/KM = 44 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C42A block, substrate row Guanosine: kcat (s^-1) = 0.011; KM (uM) = 54; kcat/KM (M^-1 s^-1) = 202.

normalized_value_unit_evidence: kcat: printed Table II cell 0.011 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.011 s^(-1). KM: printed Table II cell 54 uM; 54 / 1000 = 0.054, so the paper value is 0.054 mM. kcat/KM: printed Table II cell 202 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 202 / 1000 = 0.202 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C42A block, substrate row Guanosine: kcat = 0.011 s^-1; KM = 54 uM; printed kcat/KM = 202 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C42A block, substrate row 7-Methylguanosine: kcat (s^-1) = 2.4; KM (uM) = 53; kcat/KM (M^-1 s^-1) = 45,283.

normalized_value_unit_evidence: kcat: printed Table II cell 2.4 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2.4 s^(-1). KM: printed Table II cell 53 uM; 53 / 1000 = 0.053, so the paper value is 0.053 mM. kcat/KM: printed Table II cell 45,283 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 45,283 / 1000 = 45.283 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C42A block, substrate row 7-Methylguanosine: kcat = 2.4 s^-1; KM = 53 uM; printed kcat/KM = 45,283 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH Wild-type block, substrate row p-NPR: kcat (s^-1) = 0.039; KM (uM) = 0.32; kcat/KM (M^-1 s^-1) = 121,875.

normalized_value_unit_evidence: kcat: printed Table II cell 0.039 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.039 s^(-1). KM: printed Table II cell 0.32 uM; 0.32 / 1000 = 0.00032, so the paper value is 0.00032 mM. kcat/KM: printed Table II cell 121,875 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 121,875 / 1000 = 121.875 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH Wild-type block, substrate row p-NPR: kcat = 0.039 s^-1; KM = 0.32 uM; printed kcat/KM = 121,875 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH Wild-type block, substrate row 7-Methylguanosine: kcat (s^-1) = 1.090; KM (uM) = 37; kcat/KM (M^-1 s^-1) = 29,459.

normalized_value_unit_evidence: kcat: printed Table II cell 1.090 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1.09 s^(-1). KM: printed Table II cell 37 uM; 37 / 1000 = 0.037, so the paper value is 0.037 mM. kcat/KM: printed Table II cell 29,459 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 29,459 / 1000 = 29.459 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH Wild-type block, substrate row 7-Methylguanosine: kcat = 1.090 s^-1; KM = 37 uM; printed kcat/KM = 29,459 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C42A block, substrate row p-NPR: kcat (s^-1) = 0.0260; KM (uM) = 0.64; kcat/KM (M^-1 s^-1) = 40,625.

normalized_value_unit_evidence: kcat: printed Table II cell 0.0260 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.026 s^(-1). KM: printed Table II cell 0.64 uM; 0.64 / 1000 = 0.00064, so the paper value is 0.00064 mM. kcat/KM: printed Table II cell 40,625 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 40,625 / 1000 = 40.625 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C42A block, substrate row p-NPR: kcat = 0.0260 s^-1; KM = 0.64 uM; printed kcat/KM = 40,625 M^-1 s^-1.


sequence_source: UniProt Q9XWN7 direct FASTA sequence

column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH Wild-type block, substrate row Adenosine: kcat (s^-1) = 0.418; KM (uM) = 77; kcat/KM (M^-1 s^-1) = 5,429.

normalized_value_unit_evidence: kcat: printed Table II cell 0.418 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.418 s^(-1). KM: printed Table II cell 77 uM; 77 / 1000 = 0.077, so the paper value is 0.077 mM. kcat/KM: printed Table II cell 5,429 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5,429 / 1000 = 5.429 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH Wild-type block, substrate row Adenosine: kcat = 0.418 s^-1; KM = 77 uM; printed kcat/KM = 5,429 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH C253A block, substrate row 7-Methylguanosine: kcat (s^-1) = 1.98; KM (uM) = 51; kcat/KM (M^-1 s^-1) = 38,823.

normalized_value_unit_evidence: kcat: printed Table II cell 1.98 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1.98 s^(-1). KM: printed Table II cell 51 uM; 51 / 1000 = 0.051, so the paper value is 0.051 mM. kcat/KM: printed Table II cell 38,823 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 38,823 / 1000 = 38.823 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH C253A block, substrate row 7-Methylguanosine: kcat = 1.98 s^-1; KM = 51 uM; printed kcat/KM = 38,823 M^-1 s^-1.


column_label: Table II (Kinetic Constants of Wild-Type and Mutant CeNH) prints one substrate-label column followed by three numeric columns whose printed heads are kcat (s^-1), KM (uM) and kcat/KM (M^-1 s^-1) in that printed order, repeated under each of the three enzyme block headings CeNH Wild-type, CeNH C42A and CeNH C253A. The cited cell set is the CeNH Wild-type block, substrate row Inosine: kcat (s^-1) = 0.203; KM (uM) = 129; kcat/KM (M^-1 s^-1) = 1,574.

normalized_value_unit_evidence: kcat: printed Table II cell 0.203 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.203 s^(-1). KM: printed Table II cell 129 uM; 129 / 1000 = 0.129, so the paper value is 0.129 mM. kcat/KM: printed Table II cell 1,574 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1,574 / 1000 = 1.574 s^-1 mM^-1.

raw_value_unit_evidence: Table II, CeNH Wild-type block, substrate row Inosine: kcat = 0.203 s^-1; KM = 129 uM; printed kcat/KM = 1,574 M^-1 s^-1.


organism: Physcomitrium patens

substrate_name: Xanthosine

sequence_variant_note: Resolved canonical sequence from UniProt A9TXA6 canonical sequence plus validated D252A reconstruction and applied mutation signature D252A to reconstruct the assayed variant sequence.

substrate: Xanthosine


sequence_variant_note: Resolved canonical sequence from UniProt A9TXA6 canonical sequence plus validated E247A reconstruction and applied mutation signature E247A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9TXA6 and applied mutation signature Y241A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 200 mM Tris-HCl

column_label: Table III: Kinetic parameters for PpNRH1 and mutant proteins with the potential natural substrates inosine and xanthosine (Plant Physiology 2013, 163(4):1568-1583); printed column heads Enzyme, Relative Rate Inosine/Xanthosine (%), then per substrate column group Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1). Table III, enzyme row Y241A, Xanthosine column group; column Km (uM) = 487; column kcat (s^-1) = 0.19; column kcat/Km (s^-1 M^-1) = 4.0 x 10^2. captured primary segment: Table III | Xanthosine | PpNRH1 Y241A | Km 487 uM | kcat 0.19 s^-1 | kcat/Km 4.0 x 10^2 s^-1 M^-1 | 200 mM Tris-HCl buffer (pH 7.5), 30 C

normalized_value_unit_evidence: Km: printed Table III cell 487 uM; 1 uM is 1/1000 mM, so 487 / 1000 = 0.487 mM. kcat: printed Table III cell 0.19 s^-1; the printed unit is already the canonical unit and no unit conversion applies, so the value is 0.19 s^(-1). kcat/Km: printed Table III cell 4.0 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.0 x 10^2 / 1000 = 0.4 s^-1 mM^-1.

raw_value_unit_evidence: Table III, enzyme row Y241A, Xanthosine column group: Km = 487 uM; kcat = 0.19 s^-1; printed kcat/Km = 4.0 x 10^2 s^-1 M^-1.


sequence_source: UniProt A9TXA6 direct FASTA sequence

column_label: Table II: Kinetic parameters for PpNRH1, ZmNRH2a, ZmNRH2b, and ZmNRH3 (Plant Physiology 2013, 163(4):1568-1583); printed column heads Substrate, then per enzyme column group Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1). Table II, substrate row Xanthosine, enzyme column group PpNRH1; column Km (uM) = 116; column kcat (s^-1) = 7.0; column kcat/Km (s^-1 M^-1) = 6.1 x 10^4. captured primary segment: Table II | Xanthosine | PpNRH1 | Km 116 uM | kcat 7.0 s^-1 | kcat/Km 6.1 x 10^4 s^-1 M^-1 | 200 mM Tris-HCl buffer (pH 7.5), 30 C

normalized_value_unit_evidence: Km: printed Table II cell 116 uM; 1 uM is 1/1000 mM, so 116 / 1000 = 0.116 mM. kcat: printed Table II cell 7.0 s^-1; the printed unit is already the canonical unit and no unit conversion applies, so the value is 7.0 s^(-1). kcat/Km: printed Table II cell 6.1 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.1 x 10^4 / 1000 = 61.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Xanthosine, enzyme column group PpNRH1: Km = 116 uM; kcat = 7.0 s^-1; printed kcat/Km = 6.1 x 10^4 s^-1 M^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9TXA6 and applied mutation signature D250A to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic parameters for PpNRH1 and mutant proteins with the potential natural substrates inosine and xanthosine (Plant Physiology 2013, 163(4):1568-1583); printed column heads Enzyme, Relative Rate Inosine/Xanthosine (%), then per substrate column group Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1). Table III, enzyme row D250A, Inosine column group; column Km (uM) = 134; column kcat (s^-1) = 7.2; column kcat/Km (s^-1 M^-1) = 5.3 x 10^4. captured primary segment: Table III | Inosine | PpNRH1 D250A | Km 134 uM | kcat 7.2 s^-1 | kcat/Km 5.3 x 10^4 s^-1 M^-1 | 200 mM Tris-HCl buffer (pH 7.5), 30 C

normalized_value_unit_evidence: Km: printed Table III cell 134 uM; 1 uM is 1/1000 mM, so 134 / 1000 = 0.134 mM. kcat: printed Table III cell 7.2 s^-1; the printed unit is already the canonical unit and no unit conversion applies, so the value is 7.2 s^(-1). kcat/Km: printed Table III cell 5.3 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.3 x 10^4 / 1000 = 53.0 s^-1 mM^-1.

raw_value_unit_evidence: Table III, enzyme row D250A, Inosine column group: Km = 134 uM; kcat = 7.2 s^-1; printed kcat/Km = 5.3 x 10^4 s^-1 M^-1.


column_label: Table II: Kinetic parameters for PpNRH1, ZmNRH2a, ZmNRH2b, and ZmNRH3 (Plant Physiology 2013, 163(4):1568-1583); printed column heads Substrate, then per enzyme column group Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1). Table II, substrate row Inosine, enzyme column group PpNRH1; column Km (uM) = 78; column kcat (s^-1) = 6.0; column kcat/Km (s^-1 M^-1) = 7.7 x 10^4. captured primary segment: Table II | Inosine | PpNRH1 | Km 78 uM | kcat 6.0 s^-1 | kcat/Km 7.7 x 10^4 s^-1 M^-1 | 200 mM Tris-HCl buffer (pH 7.5), 30 C

normalized_value_unit_evidence: Km: printed Table II cell 78 uM; 1 uM is 1/1000 mM, so 78 / 1000 = 0.078 mM. kcat: printed Table II cell 6.0 s^-1; the printed unit is already the canonical unit and no unit conversion applies, so the value is 6.0 s^(-1). kcat/Km: printed Table II cell 7.7 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.7 x 10^4 / 1000 = 77.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Inosine, enzyme column group PpNRH1: Km = 78 uM; kcat = 6.0 s^-1; printed kcat/Km = 7.7 x 10^4 s^-1 M^-1.


sequence_variant_note: Resolved canonical sequence from UniProt A9TXA6 canonical sequence plus validated Y255A reconstruction and applied mutation signature Y255A to reconstruct the assayed variant sequence.


sequence_source: UniProt A9TXA6 canonical sequence plus validated E247A reconstruction


organism: Trypanosoma vivax

sequence_source: UniProtKB Q9GPQ4 REST lookup on 2026-06-24


substrate_name: Guanosine; H2O

assay_conditions_summary: pH 7.2; 308.15 K; buffer 50 mM phosphate

proof_lines:
pH 7.2, 35°C, His-tagged enzyme form
pH 7.2, 35°C, wiithout His-tag
pH 7.2, 35°C, without His-tag

substrate: Guanosine; H2O


organism: Zea mays

sequence_source: UniProtKB B6T563 REST lookup on 2026-06-24

column_label: Table II: Kinetic parameters for PpNRH1, ZmNRH2a, ZmNRH2b, and ZmNRH3 (Plant Physiology 2013, 163(4):1568-1583); printed column heads Substrate, then per enzyme column group Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1). Table II, substrate row Xanthosine, enzyme column group ZmNRH3; column Km (uM) = 396; column kcat (s^-1) = 6.2; column kcat/Km (s^-1 M^-1) = 1.6 x 10^4. captured primary segment: Table II | Xanthosine | ZmNRH3 | Km 396 uM | kcat 6.2 s^-1 | kcat/Km 1.6 x 10^4 s^-1 M^-1 | 200 mM Tris-HCl buffer (pH 7.5), 30 C

normalized_value_unit_evidence: Km: printed Table II cell 396 uM; 1 uM is 1/1000 mM, so 396 / 1000 = 0.396 mM. kcat: printed Table II cell 6.2 s^-1; the printed unit is already the canonical unit and no unit conversion applies, so the value is 6.2 s^(-1). kcat/Km: printed Table II cell 1.6 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^4 / 1000 = 16.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Xanthosine, enzyme column group ZmNRH3: Km = 396 uM; kcat = 6.2 s^-1; printed kcat/Km = 1.6 x 10^4 s^-1 M^-1.


column_label: Table II: Kinetic parameters for PpNRH1, ZmNRH2a, ZmNRH2b, and ZmNRH3 (Plant Physiology 2013, 163(4):1568-1583); printed column heads Substrate, then per enzyme column group Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1). Table II, substrate row Inosine, enzyme column group ZmNRH3; column Km (uM) = 201; column kcat (s^-1) = 7.2; column kcat/Km (s^-1 M^-1) = 3.6 x 10^4. captured primary segment: Table II | Inosine | ZmNRH3 | Km 201 uM | kcat 7.2 s^-1 | kcat/Km 3.6 x 10^4 s^-1 M^-1 | 200 mM Tris-HCl buffer (pH 7.5), 30 C

normalized_value_unit_evidence: Km: printed Table II cell 201 uM; 1 uM is 1/1000 mM, so 201 / 1000 = 0.201 mM. kcat: printed Table II cell 7.2 s^-1; the printed unit is already the canonical unit and no unit conversion applies, so the value is 7.2 s^(-1). kcat/Km: printed Table II cell 3.6 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.6 x 10^4 / 1000 = 36.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, substrate row Inosine, enzyme column group ZmNRH3: Km = 201 uM; kcat = 7.2 s^-1; printed kcat/Km = 3.6 x 10^4 s^-1 M^-1.


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9I0Q0 canonical sequence, direct REST lookup 2026-06-24


substrate_name: NADPH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone

substrate: NADPH


enzyme_display_name: cholesterol 24-hydroxylase

organism: Homo sapiens

substrate_name: O2; Cholesterol; NADPH; H+

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

sequence_source: UniProtKB:Q9Y6A2 canonical sequence, direct REST lookup 2026-06-24

assay_conditions_summary: cofactor NADP+

enzyme: cholesterol 24-hydroxylase

substrate: O2; Cholesterol; NADPH; H+


substrate_name: cholesterol 3-sulfate

mutation_signature: recombinant truncation mutant enzyme

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

mutation_type: truncation

substrate: cholesterol 3-sulfate


substrate_name: cholesterol

substrate: cholesterol


enzyme_display_name: (+)-pinoresinol reductase

substrate_name: (+)-pinoresinol

sequence_source: UniProtKB:Q9FVQ6 canonical sequence, direct REST lookup 2026-06-24

proof_lines: isoform PrR1, pH and temperature not specified in the publication

enzyme: (+)-pinoresinol reductase

substrate: (+)-pinoresinol


organism: Camellia sinensis var. sinensis

sequence_source: UniProtKB:A0A3G5BK00 canonical sequence, direct REST lookup 2026-06-24


sequence_source: UniProtKB:A0A3G5BJU1 canonical sequence, direct REST lookup 2026-06-24


organism: Forsythia x intermedia

sequence_source: UniProtKB:P93143 canonical sequence, direct REST lookup 2026-06-24

proof_lines: isoform PLR1, pH and temperature not specified in the publication


organism: Isatis tinctoria

substrate_name: (+/-)-lariciresinol

sequence_source: UniProtKB:I6LRS1 canonical sequence, direct REST lookup 2026-06-24

substrate: (+/-)-lariciresinol


substrate_name: (+/-)-pinoresinol

sequence_variant_note: Resolved canonical sequence from UniProtKB:I6LRS1 canonical sequence plus reconstructed V46A from selected source note and applied mutation signature V46A to reconstruct the assayed variant sequence.

substrate: (+/-)-pinoresinol


organism: Catharanthus roseus

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

proof_lines: recombinant enzyme lacking transit peptide, artificial reductant dithiothreitol

proof_lines: recombinant enzyme lacking transit peptide, artificial reductant glutathione


substrate_name: 5'-adenylyl sulfate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8L5D0 canonical sequence plus reconstructed D122G from selected source note and applied mutation signature D122G to reconstruct the assayed variant sequence.

proof_lines: mutant D122G, pH not specified in the publication, temperature not specified in the publication

substrate: 5'-adenylyl sulfate


sequence_source: UniProtKB:Q8L5D0 canonical sequence, direct REST lookup 2026-06-24

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


substrate_name: p-nitrophenyl-alpha-L-fucose

substrate: p-nitrophenyl-alpha-L-fucose


substrate_name: UDP-beta-D-GlcNAc

substrate: UDP-beta-D-GlcNAc


sequence_source: UniProtKB O09008 direct lookup; reviewed MFNG_MOUSE canonical sequence, Mus musculus, EC 2.4.1.222.


enzyme_display_name: glycine transaminase

substrate_name: Glyoxylate; L-Glutamate

sequence_source: UniProtKB Q9LR30 direct lookup; reviewed GGT1_ARATH canonical sequence, Arabidopsis thaliana, EC 2.6.1.4, PubMed 12529529 evidence.

enzyme: glycine transaminase

substrate: Glyoxylate; L-Glutamate


substrate_name: L-Glutamate; Glyoxylate

sequence_source: UniProtKB REST exact accession lookup for Q9S7E9

substrate: L-Glutamate; Glyoxylate


substrate_name: glyoxylate

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

substrate: glyoxylate


organism: Hydrogenobacter thermophilus

substrate_name: L-glutamate

sequence_source: UniProtKB REST exact accession lookup for D2Z0H9

proof_lines: pH and temperature not specified in the publication

substrate: L-glutamate


organism: Oryza sativa Japonica Group

sequence_source: UniProtKB REST exact accession lookup for A0A0P0X1V6

proof_lines: cosubstrate 2-oxoglutarate, pH 7.6, 30°C


enzyme_display_name: serine--pyruvate transaminase

substrate_name: L-Serine; Pyruvate

sequence_source: UniProtKB REST exact accession lookup for Q56YA5

enzyme: serine--pyruvate transaminase

substrate: L-Serine; Pyruvate


organism: Drosophila melanogaster

substrate_name: alanine

substrate: alanine


organism: Felis silvestris catus

sequence_source: UniProtKB REST exact accession lookup for P41689


organism: Mus musculus

sequence_source: UniProtKB REST exact accession lookup for O35423


organism: Rattus norvegicus

sequence_source: UniProtKB REST exact accession lookup for P09139


enzyme_display_name: mitogen-activated protein kinase kinase kinase

substrate_name: MKK4; ATP

sequence_source: UniProtKB REST exact accession lookup for Q16584

assay_conditions_summary: cofactor ATP

substrate: MKK4; ATP


substrate_name: ATP; Myelin basic protein

sequence_source: UniProtKB REST exact accession lookup for Q02779

enzyme: mitogen-activated protein kinase kinase kinase

substrate: ATP; Myelin basic protein


sequence_source: UniProtKB REST exact accession lookup for P80192


substrate_name: Myelin basic protein; ATP

substrate: Myelin basic protein; ATP


organism: Bombus ignitus

substrate_name: phosphatidylcholine hydroperoxide

substrate: phosphatidylcholine hydroperoxide


substrate_name: (beta-(13-Hydroperoxy-cis-9, trans-11-octadecadienoyl)-gamma-palmitoyl)-L-alpha-phosphatidylcholine; Reduced glutathione

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


organism: Momordica charantia


enzyme_display_name: 3-hydroxyanthranilate 3,4-dioxygenase

organism: Cupriavidus metallidurans

substrate_name: O2; 3-Hydroxyanthranilate

sequence_variant_note: Resolved canonical sequence from direct_uniprotkb_fasta_reconstructed_variant and applied mutation signature R47A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-hydroxyanthranilate 3,4-dioxygenase(Enzyme) mutant R47A

enzyme: 3-hydroxyanthranilate 3,4-dioxygenase

substrate: O2; 3-Hydroxyanthranilate


sequence_variant_note: Resolved canonical sequence from direct_uniprotkb_fasta_reconstructed_variant and applied mutation signature E110A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-hydroxyanthranilate 3,4-dioxygenase(Enzyme) mutant E110A


substrate_name: 3-Hydroxyanthranilate; O2

sequence_variant_note: Resolved canonical sequence from direct_uniprotkb_fasta_reconstructed_variant and applied mutation signature R99A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-hydroxyanthranilate 3,4-dioxygenase(Enzyme) mutant R99A

substrate: 3-Hydroxyanthranilate; O2


organism: Saccharomyces cerevisiae

substrate_name: 3-hydroxyanthranilic acid

substrate: 3-hydroxyanthranilic acid


organism: uncultured bacterium HF130_AEPn_1

sequence_variant_note: Resolved canonical sequence from direct_uniprotkb_fasta_reconstructed_variant and applied mutation signature Y24E to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from direct_uniprotkb_fasta_reconstructed_variant and applied mutation signature E27A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from direct_uniprotkb_fasta_reconstructed_variant and applied mutation signature H80A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprotkb_fasta_reconstructed_variant and applied mutation signature Y24F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprotkb_fasta_reconstructed_variant and applied mutation signature H62A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB D0E8I5 canonical sequence with E27A substitution reconstructed after residue 27 matched E. and applied mutation signature E27A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB D0E8I5 canonical sequence with H80A substitution reconstructed after residue 80 matched H. and applied mutation signature H80A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB D0E8I5 canonical sequence with Y24E substitution reconstructed after residue 24 matched Y. and applied mutation signature Y24E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB D0E8I5 canonical sequence.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB D0E8I5 canonical sequence with Y24F substitution reconstructed after residue 24 matched Y. and applied mutation signature Y24F to reconstruct the assayed variant sequence.


enzyme_display_name: Renilla-type luciferase

organism: Gaussia princeps (in: crustaceans)

substrate_name: coelenterazine

sequence_source: UniProtKB Q9BLZ2 canonical sequence.

proof_lines: K0.5 value, Hill coefficient 1.8, pH 7.5, temperature not specified in the publication

enzyme: Renilla-type luciferase

substrate: coelenterazine


organism: Renilla reniformis

sequence_source: UniProtKB P27652 canonical sequence.

proof_lines: pH 7.8, 25°C, recombinant His-tagged wild-type enzyme

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


sequence_source: UniProtKB P27652 canonical context only; selected row names modified FcUni-RLuc/C-SRLuc8 constructs without construct sequence.

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

proof_lines: modified enzyme FcUni-RLuc, pH 7.2, 25°C

proof_lines: pH 7.8, 25°C, recombinant His-tagged enzyme

proof_lines: pH 7.2, 37°C, recombinant modified enzyme C-SRLuc8


sequence_source: UniProtKB P27652 canonical context only; selected row names engineered mutant super RLuc8 without row-specific sequence.

proof_lines: pH 7.2, 37°C, recombinant engineered mutant super RLuc 8


organism: Pseudomonas putida

sequence_source: UniProtKB H3JQW0 canonical sequence.

proof_lines: pH 9.0, temperature not specified in the publication


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB Q9I0Q0 canonical sequence.

smiles: O=O


substrate_name: NADH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: NADPH

substrate: NADPH


organism: Salmonella typhi

substrate_name: CTP; D-Glucose 1-phosphate

sequence_source: UniProtKB:Q8Z5I4 direct REST lookup on 2026-06-24

substrate: CTP; D-Glucose 1-phosphate


organism: Streptomyces sp. 139

substrate_name: CTP

sequence_source: UniProtKB:Q8KN04 direct REST lookup on 2026-06-24

substrate: CTP


organism: Yersinia pseudotuberculosis

sequence_source: UniProtKB:Q57430 direct REST lookup on 2026-06-24


organism: Escherichia coli

substrate_name: H+; CTP; Mo-Molybdopterin

sequence_source: UniProtKB:Q46810 direct REST lookup on 2026-06-24

substrate: H+; CTP; Mo-Molybdopterin


substrate_name: CTP; Mo-Molybdopterin

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

proof_lines: SABIO-RK modifier species: molybdenum cofactor cytidylyltransferase(Enzyme) mutant MocA with M1 motif of MobA

proof_lines: SABIO-RK modifier species: molybdenum cofactor cytidylyltransferase(Enzyme) mutant MocA with M2 motif of MobA

proof_lines: SABIO-RK modifier species: molybdenum cofactor cytidylyltransferase(Enzyme) mutant MocA with M1 and M2 motifs of MobA

substrate: CTP; Mo-Molybdopterin


substrate_name: PaoD; MocA-M2

substrate: PaoD; MocA-M2


substrate_name: PaoD; MocA

substrate: PaoD; MocA


substrate_name: apoTorA; N-MocA-C-MobA

substrate: apoTorA; N-MocA-C-MobA


proof_lines: SABIO-RK modifier species: molybdenum cofactor cytidylyltransferase(Enzyme) mutant fusion of N-terminal MocA domain and C-terminal MobA domain


substrate_name: TorD; N-MocA-C-MobA

substrate: TorD; N-MocA-C-MobA


substrate_name: N-MocA-C-MobA; CTP

substrate: N-MocA-C-MobA; CTP


sequence_source: UniProtKB:P0AC78 direct REST lookup on 2026-06-24

proof_lines:
pH 8.5, 37°C, in presence of Mn2+
pH 8.5, 37°C, in presence of Mg2+
pH 8.0, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AC78 canonical sequence reconstructed with selected mutation D91N on 2026-06-24 and applied mutation signature D91N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase(Enzyme) mutant D91N FLAG-His5-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AC78 canonical sequence reconstructed with selected mutation D90N on 2026-06-24 and applied mutation signature D90N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase(Enzyme) mutant D90N FLAG-His5-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AC78 canonical sequence reconstructed with selected mutation D159E on 2026-06-24 and applied mutation signature D159E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase(Enzyme) mutant D159E FLAG-His5-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AC78 canonical sequence reconstructed with selected mutation D90E on 2026-06-24 and applied mutation signature D90E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase(Enzyme) mutant D90E FLAG-His5-tagged


organism: Curcuma longa

substrate_name: feruloyl-CoA

sequence_source: Direct UniProtKB accession lookup performed; sequence not accepted because kinetic evidence contract remains unresolved

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

substrate: feruloyl-CoA


substrate_name: cinnamoyl-diketide-N-acetylcysteamine

substrate: cinnamoyl-diketide-N-acetylcysteamine


substrate_name: 3-oxo-5-phenyl-4-pentenoic acid

substrate: 3-oxo-5-phenyl-4-pentenoic acid


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


enzyme_display_name: sphingosine N-acyltransferase

organism: Arabidopsis thaliana

substrate_name: sphinganine

sequence_source: Direct UniProtKB accession lookup performed; sequence not accepted due to unresolved blocker

enzyme: sphingosine N-acyltransferase

substrate: sphinganine


organism: Bos taurus

substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


organism: Mus musculus

substrate_name: sphingosine

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: presence of lambda protein phosphatase, pH 7.4, 37°C

proof_lines: absence of lambda protein phosphatase, pH 7.4, 37°C

substrate: sphingosine


organism: Trypanosoma cruzi

substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 7.5; 301.15 K; cofactor CoA

substrate: palmitoyl-CoA


organism: Rattus norvegicus

substrate_name: H+; Acetyl-CoA; 2n 2n 2n NADPH; n n n Malonyl-CoA

assay_conditions_summary: cofactor NADPH