sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B2AM55 and applied mutation signature S273A to reconstruct the assayed variant sequence.

column_label: Table 1 (Steady-state kinetic parameters for wild-type and mutant PODANSg2158 with nitroethane as substrate), S273A column: parameter row 'kcat (s-1)' = 5.0; parameter row 'KNE (mM)' = 24; parameter row 'kcat/KNE (mM-1s-1)' = 0.21.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.0 s^-1; the cell is already in s^-1, so no unit conversion applies and the normalized value is 5.0 s^(-1). Km: printed Table 1 cell 24 mM; the cell is already in mM, so no unit conversion applies and the normalized value is 24.0 mM. kcat/Km: printed Table 1 cell 0.21 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell converts to 0.21 s^(-1)*mM^(-1) with no numeric change.

raw_value_unit_evidence: Table 1, S273A column, nitroethane parameter rows: kcat (s-1) = 5.0; KNE (mM) = 24; kcat/KNE (mM-1s-1) = 0.21.


enzyme_display_name: Nitroalkane oxidase

organism: Podospora anserina

substrate_name: nitroethane

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB B2AM55 canonical sequence fetched by direct UniProt REST lookup; row-specific variant reconstructed from selected mutation_signature S273A after residue-coordinate check. and applied mutation signature S273A to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant enzyme S273A, in 50 mM HEPES, pH 8.0, 30°C

enzyme: Nitroalkane oxidase

substrate: nitroethane

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB B2AM55 canonical sequence fetched by direct UniProt REST lookup; row-specific variant reconstructed from selected mutation_signature D399N after residue-coordinate check. and applied mutation signature D399N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D399N, in 50 mM HEPES, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB B2AM55 canonical sequence fetched by direct UniProt REST lookup; row-specific variant reconstructed from selected mutation_signature R406K after residue-coordinate check. and applied mutation signature R406K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R406K, in 50 mM HEPES, pH 8.0, 30°C


substrate_name: nitroethane; O2

mutation_signature: Unknown

sequence_source: UniProtKB B2AM55 canonical wild-type sequence fetched by direct UniProt REST lookup.

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

proof_lines: wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C

substrate: nitroethane; O2


enzyme_display_name: nitroalkane oxidase

organism: Pseudomonas aeruginosa

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9HWH9 PA4202/nmoA canonical sequence; H183C reconstructed after direct residue check showed H at canonical position 183. and applied mutation signature H183C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H183C, at 30°C, pH not specified in the publication

enzyme: nitroalkane oxidase


source_db: oed

verification_status: corrected

sequence_source: UniProtKB:B2AM55 direct REST lookup on 2026-06-13

smiles: O=O

assay_conditions_summary: pH 8; 303.15 K; cofactor FAD

column_label: Table 1 (Steady-state kinetic parameters for wild-type and mutant PODANSg2158 with nitroethane as substrate), Wild-Type column: parameter row 'kcat (s-1)' = 15; parameter row 'KO2 (mM)' = 0.39; parameter row 'kcat/KO2 (mM-1s-1)' = 38.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15 s^-1; the cell is already in s^-1, so no unit conversion applies and the normalized value is 15.0 s^(-1). Km: printed Table 1 cell 0.39 mM; the cell is already in mM, so no unit conversion applies and the normalized value is 0.39 mM. kcat/Km: printed Table 1 cell 38 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell converts to 38.0 s^(-1)*mM^(-1) with no numeric change.

raw_value_unit_evidence: Table 1, Wild-Type column, oxygen parameter rows: kcat (s-1) = 15; KO2 (mM) = 0.39; kcat/KO2 (mM-1s-1) = 38.

table_label: Table 1: Steady-state kinetic parameters for wild-type and mutant PODANSg2158 with nitroethane as substrate (Biochemistry 2010, 49(24):5035-5041)

data_origin: experimental

status: corrected

source: oed


verification_status: unverified

kcat_over_km_origin: calculated

status: unverified


organism: Fusarium oxysporum

kcat_display: Not reported

sequence_source: UniProtKB Q8X1D8 direct EC+organism lookup

assay_conditions_summary: pH 8


sequence_source: Canonical context from UniProtKB Q8X1D8; variant sequence not reconstructed because selected mutation label conflicts

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


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8X1D8 plus selected/PMC-supported mutation R409K and applied mutation signature R409K to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, mutant enzyme R409K, substrate inhibition constant


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8X1D8 plus selected/PMC-supported mutation D402E and applied mutation signature D402E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8X1D8 plus selected/PMC-supported mutation C397S and applied mutation signature C397S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8X1D8 plus selected/PMC-supported mutation S171A and applied mutation signature S171A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


substrate_name: H2O; Nitroethane; O2 / 1-Nitrobutane; H2O; O2 / nitroethane

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

sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA lookup for Q8X1D8 on 2026-06-13 plus D402E reconstruction from the selected mutation label and applied mutation signature D402E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: nitroalkane oxidase(Enzyme) mutant D402E


sequence_source: UniProtKB REST/FASTA lookup for Q8X1D8 on 2026-06-13


sequence_source: UniProtKB REST/FASTA lookup for Q8X1D8 on 2026-06-13 plus D402E reconstruction from the selected mutation label


substrate_name: H2O2; Acetaldehyde; Nitrite / Nitroalkane reaction bundles

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

proof_lines:
cosubstrate D2O, 30°C, pH 8.5
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=°C, pH=8

source_databases_merged: sabio_rk brenda skid


substrate_name: 1-nitrohexane / 1-nitrooctane / nitroethane

sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA lookup for Q8X1D8 on 2026-06-13 plus S276A reconstruction from the selected mutation label and applied mutation signature S276A to reconstruct the assayed variant sequence.

proof_lines:
mutant S276A, pH 8.0, 30°C
mutant enzyme S276A, at pH 8.0 and 30°C


column_label: Table 2, substrate block 'nitroethane', enzyme-form column 'wild-type NAO'; column 'kcat(nitroethane) (s-1)' = 15; column 'K(nitroethane) (mM)' = 2.3; column 'kcat/K(nitroethane) (mM-1 s-1)' = 6.3

normalized_value_unit_evidence: kcat: printed Table 2 cell 15 s^-1; already in s^-1, so no unit conversion applies; the exported value is 15.0 s^(-1). Km: printed Table 2 cell 2.3 mM; already in mM, so no unit conversion applies; the exported value is 2.3 mM. kcat/Km: printed Table 2 cell 6.3 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell normalizes to 6.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, nitroethane block, wild-type NAO column: kcat = 15 s^-1; Km = 2.3 mM; printed kcat/Km = 6.3 mM^-1 s^-1.

table_label: Table 2: Kinetic parameters for wild-type nitroalkane oxidase, wild-type NAO column (Biochemistry 2009, 48(15):3407-3416)


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature S276A to reconstruct the assayed variant sequence.

column_label: Table 2, substrate block 'nitroethane', enzyme-form column 'S276A NAO'; column 'kcat(nitroethane) (s-1)' = 1.0; column 'K(nitroethane) (mM)' = 3.3; column 'kcat/K(nitroethane) (mM-1 s-1)' = 0.30

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.0 s^-1; already in s^-1, so no unit conversion applies; the exported value is 1.0 s^(-1). Km: printed Table 2 cell 3.3 mM; already in mM, so no unit conversion applies; the exported value is 3.3 mM. kcat/Km: printed Table 2 cell 0.30 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell normalizes to 0.3 s^(-1)*mM^(-1). The exact quotient of the same two printed cells is 1.0 / 3.3 = 0.30303030303030304 s^-1 mM^-1, which the paper prints rounded to its own two-decimal precision as 0.30; the exported ratio keeps the exact quotient and is corroborated by that printed cell.

raw_value_unit_evidence: Table 2, nitroethane block, S276A NAO column: kcat = 1.0 s^-1; Km = 3.3 mM; printed kcat/Km = 0.30 mM^-1 s^-1.

table_label: Table 2: Kinetic parameters for S276A nitroalkane oxidase, S276A NAO column (Biochemistry 2009, 48(15):3407-3416)

status: verified


substrate_name: nitroethane / 1-nitrohexane / 1-nitrooctane

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature R409K to reconstruct the assayed variant sequence.

column_label: Table 1 prints one enzyme-label column followed by four kinetic columns whose heads are kcat, s^-1 | kred, s^-1 | Km, mM | kcat/Km, mM^-1 s^-1. The cited cell set is Table 1, enzyme row R409K: kcat, s^-1 = 2.6; kred, s^-1 = 2.6; Km, mM = 26.3; kcat/Km, mM^-1 s^-1 = 0.098.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.6 under the column head kcat, s^-1; that column is already per second, so no unit conversion applies and the paper value is 2.6 s^(-1). Km: printed Table 1 cell 26.3 under the column head Km, mM; that column is already in millimolar, so no unit conversion applies and the paper value is 26.3 mM. kcat/Km: printed Table 1 cell 0.098 under the column head kcat/Km, mM^-1 s^-1; that head is already reciprocal millimolar per second, so no unit conversion applies and the paper value is 0.098 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R409K: kcat = 2.6 s^-1; kred = 2.6 s^-1; Km = 26.3 mM; printed kcat/Km = 0.098 mM^-1 s^-1.

row_label: Table 1, enzyme row R409K

table_label: Table 1: Kinetic Parameters for Active Site Variants of F. oxysporum NAO with Nitroethane (Arch Biochem Biophys 2017, 632:41-46)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature S171A to reconstruct the assayed variant sequence.

column_label: Table 1 prints one enzyme-label column followed by four kinetic columns whose heads are kcat, s^-1 | kred, s^-1 | Km, mM | kcat/Km, mM^-1 s^-1. The cited cell set is Table 1, enzyme row S171A: kcat, s^-1 = 5.4; kred, s^-1 = 49; Km, mM = 2.1; kcat/Km, mM^-1 s^-1 = 2.6.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.4 under the column head kcat, s^-1; that column is already per second, so no unit conversion applies and the paper value is 5.4 s^(-1). Km: printed Table 1 cell 2.1 under the column head Km, mM; that column is already in millimolar, so no unit conversion applies and the paper value is 2.1 mM. kcat/Km: printed Table 1 cell 2.6 under the column head kcat/Km, mM^-1 s^-1; that head is already reciprocal millimolar per second, so no unit conversion applies and the paper value is 2.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row S171A: kcat = 5.4 s^-1; kred = 49 s^-1; Km = 2.1 mM; printed kcat/Km = 2.6 mM^-1 s^-1.

row_label: Table 1, enzyme row S171A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature C397S to reconstruct the assayed variant sequence.

column_label: Table 1 prints one enzyme-label column followed by four kinetic columns whose heads are kcat, s^-1 | kred, s^-1 | Km, mM | kcat/Km, mM^-1 s^-1. The cited cell set is Table 1, enzyme row C397S: kcat, s^-1 = 5.4; kred, s^-1 = 42; Km, mM = 2.1; kcat/Km, mM^-1 s^-1 = 2.6.

raw_value_unit_evidence: Table 1, enzyme row C397S: kcat = 5.4 s^-1; kred = 42 s^-1; Km = 2.1 mM; printed kcat/Km = 2.6 mM^-1 s^-1.

row_label: Table 1, enzyme row C397S


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature Y398F to reconstruct the assayed variant sequence.

column_label: Table 1 prints one enzyme-label column followed by four kinetic columns whose heads are kcat, s^-1 | kred, s^-1 | Km, mM | kcat/Km, mM^-1 s^-1. The cited cell set is Table 1, enzyme row Y398F: kcat, s^-1 = 11; kred, s^-1 = 96; Km, mM = 4.8; kcat/Km, mM^-1 s^-1 = 2.2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 11 under the column head kcat, s^-1; that column is already per second, so no unit conversion applies and the paper value is 11.0 s^(-1). Km: printed Table 1 cell 4.8 under the column head Km, mM; that column is already in millimolar, so no unit conversion applies and the paper value is 4.8 mM. kcat/Km: printed Table 1 cell 2.2 under the column head kcat/Km, mM^-1 s^-1; that head is already reciprocal millimolar per second, so no unit conversion applies and the paper value is 2.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Y398F: kcat = 11 s^-1; kred = 96 s^-1; Km = 4.8 mM; printed kcat/Km = 2.2 mM^-1 s^-1.

row_label: Table 1, enzyme row Y398F


sequence_variant_note: Resolved canonical sequence from UniProt Q8X1D8 canonical sequence; S171V reconstructed after confirming residue 171 is Ser in the canonical sequence. and applied mutation signature S171V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


sequence_source: UniProt Q8X1D8 reviewed F. oxysporum nitroalkane oxidase canonical sequence.

proof_lines: wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C

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


sequence_variant_note: Resolved canonical sequence from UniProt Q8X1D8 canonical sequence; Y398F reconstructed after confirming residue 398 is Tyr in the canonical sequence. and applied mutation signature Y398F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


sequence_variant_note: Resolved canonical sequence from UniProt Q8X1D8 canonical sequence; S171T reconstructed after confirming residue 171 is Ser in the canonical sequence. and applied mutation signature S171T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


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

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


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

proof_lines: mutant enzyme H183S, at 30°C, pH not specified in the publication


enzyme_display_name: glyoxylate reductase (NADP(+))

organism: Thermus thermophilus HB27

substrate_name: NADPH

assay_conditions_summary: pH 6.7; 318.15 K; cofactor NADPH

proof_lines: with glyoxylate as substrate, pH 6.7, 45°C

enzyme: glyoxylate reductase (NADP(+))

substrate: NADPH


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession F4I907; direct REST lookup on 2026-06-13

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

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH

proof_lines: with succinic semialdehyde as substrate, pH 7.6, 30°C

proof_lines: recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C

proof_lines: isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C


substrate_name: glyoxylate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature K170E to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E

substrate: glyoxylate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature F231A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; cofactor NADPH

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature T95A to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature S121A to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature N174A to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature D239A to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature K170R to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R


organism: Acetobacter aceti

substrate_name: glycolate

assay_conditions_summary: pH 9; 318.15 K; cofactor NADP+

proof_lines: with NADP+ as cosubstrate, at pH 9.0 and 45°C

proof_lines: with NAD+ as cosubstrate, at pH 9.0 and 45°C

proof_lines: with NADPH as cosubstrate, at pH 4.0 and 45°C

substrate: glycolate


organism: Chlamydomonas reinhardtii


organism: Euglena gracilis

assay_conditions_summary: cofactor NADPH


organism: Homo sapiens

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines: pH 7.5, 37°C, recombinant enzyme, with NADPH


organism: Neurospora crassa


organism: Oryza sativa

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25°C

proof_lines: isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25°C


mutation_signature: recombinant truncated 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

proof_lines: pH 7.8, temperature not specified in the publication, recombinant truncated enzyme


sequence_source: UniProtKB REST JSON primaryAccession Q9LSV0, accessed 2026-06-13

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme

proof_lines: pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer

proof_lines: pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a microplate reader


assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C

proof_lines: isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.8 and 25°C


organism: Malus domestica

sequence_source: UniProtKB REST JSON primaryAccession A0A1C8M582, accessed 2026-06-13

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.5 and 25°C

proof_lines: isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.5 and 25°C


sequence_source: UniProtKB REST JSON primaryAccession A0A1C8M593, accessed 2026-06-13

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25°C

proof_lines: isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.3 and 25°C


organism: Paecilomyces sp. 'thermophila'

sequence_source: UniProtKB REST JSON primaryAccession A0A0H3U0Y7, accessed 2026-06-13

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NADPH

proof_lines: pH 7.5, 50°C, recombinant enzyme, with NADPH


organism: Oryza sativa Japonica Group

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH

proof_lines: isoform GR2, with NADPH as cosubstrate, at pH 7.4 and 30°C


organism: Populus gelrica


organism: Pyrococcus horikoshii OT3

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: with hydroxypyruvate as substrate, pH 7.5


organism: Sinorhizobium meliloti

substrate_name: pyruvate

substrate: pyruvate


organism: Spinacia oleracea

substrate_name: NADH

proof_lines:
cofactor NADPH
cofactor NADH

substrate: NADH


organism: Thermus thermophilus

proof_lines: pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme

proof_lines: pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme

proof_lines: pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme


organism: Saccharomyces cerevisiae


organism: Branchiostoma floridae

substrate_name: all-trans-retinal

assay_conditions_summary: pH 6; 310.15 K; cofactor NADH

proof_lines:
isoform 2, pH 6.0, 37°C
isoform 1, pH 6.0, 37°C

substrate: all-trans-retinal


substrate_name: NAD+

assay_conditions_summary: pH 7.3; 310.15 K; cofactor NAD+

proof_lines: pH and temperature not specified in the publication

substrate: NAD+


organism: Kangiella koreensis


organism: Rattus norvegicus

substrate_name: retinol

substrate: retinol


substrate_name: all-trans-retinol

sequence_source: UniProtKB REST direct lookup for O75452 on 2026-06-13

column_label: Table 1: Kinetic constants of purified AKR, MDR and SDR enzymes with retinoids (Biochem. J. 2006, 399:101-109); substrate block 'All-trans-Retinol'; enzyme column head 'RoDH-4'; parameter rows 'K m (uM)' = 1.1, 'k cat (min^-1)' = 1.20 and 'k cat /K m (mM^-1 min^-1)' = 1100. The six enzyme column heads read, left to right, AKR1B1, AKR1B10, ADH4, ADH1B2, RDH11* and RoDH-4.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.1 uM; 1.1 / 1000 = 0.0011 mM. kcat: printed Table 1 cell 1.20 min^-1; 1.20 / 60 = 0.02 s^-1. kcat/Km: printed Table 1 cell 1100 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 of 1 s^-1 mM^-1, so 1100 / 60 = 18.333333333333332 s^-1 mM^-1. Each of these converted quantities reproduces the exported value for this row: kcat 0.02 s^(-1), km 0.0011 mM.

raw_value_unit_evidence: Table 1, substrate block 'All-trans-Retinol', enzyme column 'RoDH-4': K m (uM) = 1.1; k cat (min^-1) = 1.20; printed k cat /K m (mM^-1 min^-1) = 1100.

substrate: all-trans-retinol


sequence_source: UniProtKB REST direct lookup for Q8IZV5 on 2026-06-13

assay_conditions_summary: pH 7.4; cofactor NADP+

proof_lines: wild type enzyme, in 100 mM sodium phosphate, pH 7.4


substrate_name: all-trans retinal

assay_conditions_summary: cofactor NADH

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

substrate: all-trans retinal


organism: Mus musculus

sequence_source: UniProtKB REST direct lookup for Q8VIJ7 on 2026-06-13


sequence_source: UniProtKB REST direct lookup for Q05A13 on 2026-06-13

assay_conditions_summary: cofactor NAD+

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


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WPR5 REST lookup on 2026-06-13


organism: Nostoc sp. PCC 7120 = FACHB-418


organism: Synechocystis sp. PCC 6803

sequence_source: UniProtKB reviewed accession P74334 REST lookup on 2026-06-13

proof_lines: recombinant enzyme, pH 7.0, 28°C, in presence of 0.1 CMC C8E6


enzyme_display_name: 22alpha-hydroxysteroid 23-monooxygenase

organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed canonical sequence for accession Q9M066 (C90C1_ARATH), retrieved through UniProt REST on 2026-06-13.

enzyme: 22alpha-hydroxysteroid 23-monooxygenase


organism: Salvia splendens

substrate_name: Malonyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8W1W9 direct REST/FASTA check, 2026-06-13; variant_status=reconstructed_variant_sequence and applied mutation signature N315A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

substrate: Malonyl-CoA


sequence_source: UniProtKB reviewed Q8W1W9 direct REST/FASTA check, 2026-06-13; variant_status=canonical_wild_type_sequence

column_label: Table 2 (Kinetic Parameters of Selected Ss5MaT1 Mutants), enzyme line wild type, shisonin column group; the shared column kcat (s-1) = 8.7; column Km (uM) of the shisonin group = 35; column kcat/Km (s-1 uM-1) of the shisonin group = 0.25.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8.7 in the shared column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 8.7 s^(-1). Km: printed Table 2 cell 35 in the shisonin column headed Km (uM); 1 uM is 0.001 mM, so 35 / 1000 = 0.035 mM. kcat/Km: printed Table 2 cell 0.25 in the shisonin column headed kcat/Km (s-1 uM-1); 1 s-1 uM-1 is 1000 s^(-1)*mM^(-1), so 0.25 x 1000 = 250.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 8.7 / 0.035 = 248.57142857142853 s^(-1)*mM^(-1), which written to the precision the table prints is the printed cell 0.25 s-1 uM-1.

raw_value_unit_evidence: Table 2, enzyme line wild type, shisonin column group: kcat = 8.7 s-1; Km = 35 uM; printed kcat/Km = 0.25 s-1 uM-1.

row_label: Table 2, enzyme row wild type, shisonin column group

table_label: Table 2: Kinetic Parameters of Selected Ss5MaT1 Mutants (Biochemistry 2003, 42(6):1764-1771). The printed table has one line per enzyme form and, left to right, a single shared kcat (s-1) column, then a Km (uM) and a kcat/Km (s-1 uM-1) column for shisonin, then a Km (uM) and a kcat/Km (s-1 uM-1) column for malonyl-CoA.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8W1W9 direct REST/FASTA check, 2026-06-13; variant_status=reconstructed_variant_sequence and applied mutation signature Y45A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: anthocyanin 5-O-glucoside 6'''-O-malonyltransferase(Enzyme) mutant Y45A His6-tagged

proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, Y45A mutant Ss5MaT1

proof_lines: pH 7, 30°C, shisonin as cosubstrate, Y45A mutant Ss5MaT1


column_label: Table 2 (Kinetic Parameters of Selected Ss5MaT1 Mutants), enzyme line wild type, malonyl-CoA column group; the shared column kcat (s-1) = 8.7; column Km (uM) of the malonyl-CoA group = 22; column kcat/Km (s-1 uM-1) of the malonyl-CoA group = 0.40.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8.7 in the shared column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 8.7 s^(-1). Km: printed Table 2 cell 22 in the malonyl-CoA column headed Km (uM); 1 uM is 0.001 mM, so 22 / 1000 = 0.022 mM. kcat/Km: printed Table 2 cell 0.40 in the malonyl-CoA column headed kcat/Km (s-1 uM-1); 1 s-1 uM-1 is 1000 s^(-1)*mM^(-1), so 0.40 x 1000 = 400.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 8.7 / 0.022 = 395.45454545454544 s^(-1)*mM^(-1), which written to the precision the table prints is the printed cell 0.40 s-1 uM-1.

raw_value_unit_evidence: Table 2, enzyme line wild type, malonyl-CoA column group: kcat = 8.7 s-1; Km = 22 uM; printed kcat/Km = 0.40 s-1 uM-1.

row_label: Table 2, enzyme row wild type, malonyl-CoA column group


sequence_source: UniProtKB reviewed Q8W1W9 direct REST/FASTA check, 2026-06-13; variant_status=reconstructed_variant_sequence


enzyme_display_name: inulosucrase

organism: Lactobacillus johnsonii

substrate_name: Sucrose; (2,1-beta-D-Fructosyl)n

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

sequence_source: UniProtKB reviewed Q74K42 direct REST/FASTA check, 2026-06-13; variant_status=sequence_identity_only

enzyme: inulosucrase

substrate: Sucrose; (2,1-beta-D-Fructosyl)n


substrate_name: Sucrose

sequence_source: UniProtKB reviewed Q74K42 direct REST/FASTA check, 2026-06-13; variant_status=canonical_wild_type_sequence

substrate: Sucrose


organism: Lactobacillus reuteri

substrate_name: (2,1-beta-D-Fructosyl)n; Sucrose

km_display: Not reported

sequence_source: UniProtKB Q8GP32 FASTA direct lookup on 2026-06-13

substrate: (2,1-beta-D-Fructosyl)n; Sucrose


organism: Leuconostoc citreum

substrate_name: sucrose

sequence_source: UniProtKB Q7X481 FASTA direct lookup on 2026-06-13

proof_lines: pH 6.0, 30°C, recombinant wild-type enzyme

substrate: sucrose


mutation_signature: truncated version IslA4

sequence_source: UniProtKB Q7X481 FASTA direct lookup on 2026-06-13; truncation construct not reconstructed


mutation_signature: truncated version IslA2


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7X481 FASTA direct lookup on 2026-06-13; Y676W reconstructed after residue check and applied mutation signature Y676W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7X481 FASTA direct lookup on 2026-06-13; F619V reconstructed after residue check and applied mutation signature F619V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7X481 FASTA direct lookup on 2026-06-13; R618K reconstructed after residue check and applied mutation signature R618K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7X481 FASTA direct lookup on 2026-06-13; A602P reconstructed after residue check and applied mutation signature A602P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8W1W9 direct REST FASTA/JSON lookup; variant sequence reconstructed from UniProt mutagenesis feature where applicable and applied mutation signature R301A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: anthocyanin 5-O-glucoside 6'''-O-malonyltransferase(Enzyme) mutant R301A His6-tagged

proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, R301A mutant Ss5MaT1

proof_lines: pH 7, 30°C, shisonin as cosubstrate, R301A mutant Ss5MaT1


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8W1W9 direct REST FASTA/JSON lookup; variant sequence reconstructed from UniProt mutagenesis feature where applicable and applied mutation signature N315A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: anthocyanin 5-O-glucoside 6'''-O-malonyltransferase(Enzyme) mutant N315A His6-tagged

proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, N315A mutant Ss5MaT1

proof_lines: pH 7, 30°C, shisonin as cosubstrate, N315A mutant Ss5MaT1


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8W1W9 direct REST FASTA/JSON lookup; variant sequence reconstructed from UniProt mutagenesis feature where applicable and applied mutation signature Q150A to reconstruct the assayed variant sequence.


substrate_name: shisonin

sequence_source: UniProtKB:Q8W1W9 direct REST FASTA/JSON lookup; variant sequence reconstructed from UniProt mutagenesis feature where applicable

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

proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, wild-type Ss5MaT1

proof_lines: pH 7, 30°C, shisonin as cosubstrate, wild-type Ss5MaT1

substrate: shisonin


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8W1W9 direct REST FASTA/JSON lookup; variant sequence reconstructed from UniProt mutagenesis feature where applicable and applied mutation signature D171A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: anthocyanin 5-O-glucoside 6'''-O-malonyltransferase(Enzyme) mutant Q150A His6-tagged

proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, Q150A mutant Ss5MaT1

proof_lines: pH 7, 30°C, shisonin as cosubstrate, Q150A mutant Ss5MaT1


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8W1W9 direct REST FASTA/JSON lookup; variant sequence reconstructed from UniProt mutagenesis feature where applicable and applied mutation signature K258A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: anthocyanin 5-O-glucoside 6'''-O-malonyltransferase(Enzyme) mutant K258A His6-tagged

proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, K258A mutant Ss5MaT1

proof_lines: pH 7, 30°C, shisonin as cosubstrate, K258A mutant Ss5MaT1


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8W1W9 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature K258A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8W1W9 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature D390A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: anthocyanin 5-O-glucoside 6'''-O-malonyltransferase(Enzyme) mutant D390A His6-tagged

proof_lines: below, pH 7, 30°C, malonyl-CoA as cosubstrate, D390A mutant Ss5MaT1


sequence_source: UniProtKB Q8W1W9 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8W1W9 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature H167A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: anthocyanin 5-O-glucoside 6'''-O-malonyltransferase(Enzyme) mutant H167A His6-tagged

proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, H167A mutant Ss5MaT1

proof_lines: pH 7, 30°C, shisonin as cosubstrate, H167A mutant Ss5MaT1


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8W1W9 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature Q150A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8W1W9 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature R301A to reconstruct the assayed variant sequence.


proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, recombinant Ss5MaT1

proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, native Ss5MaT1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8W1W9 and applied mutation signature H167A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters of Selected Ss5MaT1 Mutants), enzyme line H167A, shisonin column group; the shared column kcat (s-1) = 0.002; column Km (uM) of the shisonin group = 5.4; column kcat/Km (s-1 uM-1) of the shisonin group = 0.00037.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.002 in the shared column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.002 s^(-1). Km: printed Table 2 cell 5.4 in the shisonin column headed Km (uM); 1 uM is 0.001 mM, so 5.4 / 1000 = 0.0054 mM. kcat/Km: printed Table 2 cell 0.00037 in the shisonin column headed kcat/Km (s-1 uM-1); 1 s-1 uM-1 is 1000 s^(-1)*mM^(-1), so 0.00037 x 1000 = 0.37 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme line H167A, shisonin column group: kcat = 0.002 s-1; Km = 5.4 uM; printed kcat/Km = 0.00037 s-1 uM-1.

row_label: Table 2, enzyme row H167A, shisonin column group


enzyme_display_name: O-acetyl-ADP-ribose deacetylase

organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A8D6 FASTA fetched 2026-06-13; D35A reconstructed after residue check. and applied mutation signature D35A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

enzyme: O-acetyl-ADP-ribose deacetylase


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB reviewed accession P0A8D6 FASTA fetched 2026-06-13.

source: skid


organism: Homo sapiens

substrate_name: O-acetyl-ADP-D-ribose

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9BQ69 FASTA fetched 2026-06-13; G270E reconstructed after residue check. and applied mutation signature G270E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 296.15 K; cofactor ADP

proof_lines: mutant G270E of isoform MacroD1, at pH 7.3 and 23°C

substrate: O-acetyl-ADP-D-ribose


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9BQ69 FASTA fetched 2026-06-13; D160A reconstructed after residue check. and applied mutation signature D160A to reconstruct the assayed variant sequence.

proof_lines: mutant D160A of isoform MacroD1, at pH 7.3 and 23°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9BQ69 FASTA fetched 2026-06-13; N174A/D184A reconstructed after residue check. and applied mutation signature N174A/D184A to reconstruct the assayed variant sequence.

proof_lines: mutant N174A/D184A of isoform MacroD1, at pH 7.3 and 23°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9BQ69 FASTA fetched 2026-06-13; H188A reconstructed after residue check. and applied mutation signature H188A to reconstruct the assayed variant sequence.

proof_lines: mutant H188A of isoform MacroD1, at pH 7.3 and 23°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9BQ69 FASTA fetched 2026-06-13; C199A reconstructed after residue check. and applied mutation signature C199A to reconstruct the assayed variant sequence.

proof_lines: mutant C199A of isoform MacroD1, at pH 7.3 and 23°C


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


sequence_source: UniProtKB:Q9BQ69 canonical sequence (UniProtKB reviewed (Swiss-Prot)), checked 2026-06-13

assay_conditions_summary: pH 6.8; 298.15 K; cofactor ADP


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

assay_conditions_summary: pH 7.3; 298.15 K; cofactor ADP

proof_lines:
at pH 7.3 and 25°C
at pH 6.8 and 25°C
isoform MacroD1, at pH 7.3 and 23°C

source_databases_merged: brenda skid


enzyme_display_name: phosphoglycolate phosphatase

sequence_source: UniProtKB:P32662 canonical sequence (UniProtKB reviewed (Swiss-Prot)), checked 2026-06-13

smiles: O=C(O)COP(=O)(O)O

enzyme: phosphoglycolate phosphatase


enzyme_display_name: glycerone kinase

sequence_source: UniProtKB:P54838 REST FASTA/API direct accession lookup

assay_conditions_summary: cofactor ATP

enzyme: glycerone kinase


substrate_name: dihydroxyacetone

sequence_source: UniProtKB:P43550 REST FASTA/API direct accession lookup

substrate: dihydroxyacetone


organism: Schizosaccharomyces pombe

sequence_source: UniProtKB:O13902 REST FASTA/API direct accession lookup

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A8D6 REST FASTA/API direct accession lookup and applied mutation signature D35A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A8D6 REST FASTA/API direct accession lookup and applied mutation signature N25A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0A8D6 REST FASTA/API direct accession lookup

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


sequence_source: UniProtKB:P76015 direct lookup on 2026-06-13

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines:
pH 7.5, 30°C, DhaK-DhaL-DhaM complex
Raw SKiD Env: Temp=22°C, pH=7.5


substrate_name: glycerone phosphate

sequence_source: UniProtKB:P37349 direct lookup on 2026-06-13

substrate: glycerone phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P76015 direct lookup plus H56N reconstruction on 2026-06-13 and applied mutation signature H56N to reconstruct the assayed variant sequence.

smiles: O=C(CO)CO

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


proof_lines: apparent value, Km above 0.008 mM, wild type enzyme, in 50 mM potassium phosphate pH 7.5, at 22°C


sequence_source: UniProtKB:P76015 direct lookup plus H56N reconstruction on 2026-06-13

proof_lines: apparent value, mutant enzyme H56N, in 50 mM potassium phosphate pH 7.5, at 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P76015 direct lookup plus H56A reconstruction on 2026-06-13 and applied mutation signature H56A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P76015 direct lookup plus H56A reconstruction on 2026-06-13

proof_lines: apparent value, mutant enzyme H56A, in 50 mM potassium phosphate pH 7.5, at 22°C


organism: Limosilactobacillus reuteri

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

proof_lines: recombinant enzyme, hydrolytic reaction, pH 5.4, 20°C

proof_lines: recombinant enzyme, transferase reaction, pH 5.4, 20°C

proof_lines: recombinant Lev-(GGS)6-D272NInu fusion enzyme, pH 5.0, 50°C


proof_lines: recombinant wild-type enzyme Inu, pH 5.0, 50°C

proof_lines: recombinant wild-type enzyme, pH 5.5, 50°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GP32 plus source mutation note G237P and applied mutation signature G237P to reconstruct the assayed variant sequence.

proof_lines: recombinant enzyme mutant G237P, pH 5.5, 50°C


organism: Citrobacter freundii

substrate_name: ATP

substrate: ATP


substrate_name: Glyceraldehyde

smiles: O=CC(O)CO

substrate: Glyceraldehyde


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


substrate_name: ATP; Dihydroxyacetone

substrate: ATP; Dihydroxyacetone


sequence_variant_note: Resolved canonical sequence from UniProt Q9BQ69 canonical FASTA; reconstructed D184A after one-based residue check and applied mutation signature D184A to reconstruct the assayed variant sequence.

proof_lines: mutant D184A of isoform MacroD1, at pH 7.3 and 23°C


sequence_source: UniProt A1Z1Q3 canonical FASTA

proof_lines:
isoform MacroD2, at pH 7.3 and 23°C
Raw SKiD Env: Temp=23°C, pH=7.3


sequence_variant_note: Resolved canonical sequence from UniProt Q9BQ69 canonical FASTA; reconstructed N171A after one-based residue check and applied mutation signature N171A to reconstruct the assayed variant sequence.

proof_lines: mutant N171A of isoform MacroD1, at pH 7.3 and 23°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9BQ69 canonical FASTA; reconstructed D167A after one-based residue check and applied mutation signature D167A to reconstruct the assayed variant sequence.

proof_lines: mutant D167A of isoform MacroD1, at pH 7.3 and 23°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9BQ69 canonical FASTA; reconstructed N174A after one-based residue check and applied mutation signature N174A to reconstruct the assayed variant sequence.

proof_lines: mutant N174A of isoform MacroD1, at pH 7.3 and 23°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9BQ69 canonical FASTA; reconstructed T226A after one-based residue check and applied mutation signature T226A to reconstruct the assayed variant sequence.

proof_lines: mutant T226A of isoform MacroD1, at pH 7.3 and 23°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9BQ69 canonical FASTA; reconstructed S268A after one-based residue check and applied mutation signature S268A to reconstruct the assayed variant sequence.

proof_lines: mutant S268A of isoform MacroD1, at pH 7.3 and 23°C


sequence_variant_note: Resolved canonical sequence from UniProt Q9BQ69 canonical FASTA; reconstructed S176A after one-based residue check and applied mutation signature S176A to reconstruct the assayed variant sequence.

proof_lines: mutant S176A of isoform MacroD1, at pH 7.3 and 23°C


enzyme_display_name: lipid-phosphate phosphatase

substrate_name: 4-Nitrophenyl phosphate

sequence_source: UniProtKB:P34913 direct accession lookup on 2026-06-13

enzyme: lipid-phosphate phosphatase

substrate: 4-Nitrophenyl phosphate


substrate_name: H2O; 4-Nitrophenyl phosphate

substrate: H2O; 4-Nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P34913 direct lookup plus one-based R103C reconstruction on 2026-06-13 and applied mutation signature R103C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species:  lipid-phosphate phosphatase(Enzyme) mutant R103C His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P34913 direct lookup plus one-based R103C/R287Q reconstruction on 2026-06-13 and applied mutation signature R103C/R287Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species:  lipid-phosphate phosphatase(Enzyme) mutant R103C/R287Q His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P34913 direct lookup plus one-based R287Q reconstruction on 2026-06-13 and applied mutation signature R287Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species:  lipid-phosphate phosphatase(Enzyme) mutant R287Q His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P34913 direct lookup plus one-based K55R reconstruction on 2026-06-13 and applied mutation signature K55R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species:  lipid-phosphate phosphatase(Enzyme) mutant K55R His6-tagged


substrate_name: 4-Nitrophenyl phosphate; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P34913 direct lookup plus one-based C154Y reconstruction on 2026-06-13 and applied mutation signature C154Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species:  lipid-phosphate phosphatase(Enzyme) mutant C154Y His6-tagged

substrate: 4-Nitrophenyl phosphate; H2O


enzyme_display_name: IMP cyclohydrolase

sequence_variant_note: Resolved canonical sequence from UniProt P31939 canonical sequence checked via UniProt REST on 2026-06-13 and applied mutation signature Y104A/D125A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: IMP cyclohydrolase(Enzyme) mutant Y104A/D125A double

enzyme: IMP cyclohydrolase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31939 and applied mutation signature Y104F to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Results for ATIC Mutants), printed enzyme line 'Y104F'; column 'Km (uM)' = 3.6; column 'kcat (s-1)' = 0.036; column 'kcat/Km (M-1 s-1)' = 1 x 10^4.

normalized_value_unit_evidence: Km: printed Table 2 cell 3.6 in a column headed Km (uM); 1 uM is 0.001 mM, so 3.6 / 1000 = 0.0036 mM. kcat: printed Table 2 cell 0.036 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.036 s^(-1). kcat/Km: printed Table 2 cell 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 1 x 10^4 / 1000 = 10.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.036 s^(-1), Km 0.004 mM and kcat_over_km 9.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed enzyme line 'Y104F': Km (uM) = 3.6; kcat (s-1) = 0.036; kcat/Km (M-1 s-1) = 1 x 10^4.

row_label: Table 2, printed enzyme line 'Y104F'

table_label: Table 2: Steady-State Results for ATIC Mutants (Biochemistry 2004, 43(5):1184-1192). Printed column heads, in printed order: (enzyme, unlabelled first column); Km (uM); kcat (s-1); kcat/Km (M-1 s-1). Footnote a reads that the Km, kcat and catalytic efficiency values for all site-directed mutants are summarized in the table and that the errors were calculated from the errors from fitting the raw data to the Michaelis-Menten equation.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31939 and applied mutation signature K137R to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Results for ATIC Mutants), printed enzyme line 'K137R'; column 'Km (uM)' = 2.7; column 'kcat (s-1)' = 0.507; column 'kcat/Km (M-1 s-1)' = 2 x 10^5.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.7 in a column headed Km (uM); 1 uM is 0.001 mM, so 2.7 / 1000 = 0.0027 mM. kcat: printed Table 2 cell 0.507 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.507 s^(-1). kcat/Km: printed Table 2 cell 2 x 10^5 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2 x 10^5 / 1000 = 200.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.507 s^(-1) and Km 0.0027 mM.

raw_value_unit_evidence: Table 2, printed enzyme line 'K137R': Km (uM) = 2.7; kcat (s-1) = 0.507; kcat/Km (M-1 s-1) = 2 x 10^5.

row_label: Table 2, printed enzyme line 'K137R'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31939 and applied mutation signature K137A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Results for ATIC Mutants), printed enzyme line 'K137A'; column 'Km (uM)' = 31.0; column 'kcat (s-1)' = 0.276; column 'kcat/Km (M-1 s-1)' = 9 x 10^3.

normalized_value_unit_evidence: Km: printed Table 2 cell 31.0 in a column headed Km (uM); 1 uM is 0.001 mM, so 31.0 / 1000 = 0.031 mM. kcat: printed Table 2 cell 0.276 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.276 s^(-1). kcat/Km: printed Table 2 cell 9 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 9 x 10^3 / 1000 = 9.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.276 s^(-1), Km 0.031 mM and kcat_over_km 8.903225806451614 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed enzyme line 'K137A': Km (uM) = 31.0; kcat (s-1) = 0.276; kcat/Km (M-1 s-1) = 9 x 10^3.

row_label: Table 2, printed enzyme line 'K137A'


normalized_value_unit_evidence: Km: printed Table 2 cell 3.6 in a column headed Km (uM); 1 uM is 0.001 mM, so 3.6 / 1000 = 0.0036 mM. kcat: printed Table 2 cell 0.036 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.036 s^(-1). kcat/Km: printed Table 2 cell 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 1 x 10^4 / 1000 = 10.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.036 s^(-1) and Km 0.0036 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31939 and applied mutation signature D125A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Results for ATIC Mutants), printed enzyme line 'D125A'; column 'Km (uM)' = 9.1; column 'kcat (s-1)' = 0.014; column 'kcat/Km (M-1 s-1)' = 2 x 10^3.

normalized_value_unit_evidence: Km: printed Table 2 cell 9.1 in a column headed Km (uM); 1 uM is 0.001 mM, so 9.1 / 1000 = 0.0091 mM. kcat: printed Table 2 cell 0.014 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.014 s^(-1). kcat/Km: printed Table 2 cell 2 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 2 x 10^3 / 1000 = 2.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.014 s^(-1) and Km 0.009099999999999999 mM.

raw_value_unit_evidence: Table 2, printed enzyme line 'D125A': Km (uM) = 9.1; kcat (s-1) = 0.014; kcat/Km (M-1 s-1) = 2 x 10^3.

row_label: Table 2, printed enzyme line 'D125A'


sequence_variant_note: Resolved canonical sequence from UniProt P31939 canonical sequence checked via UniProt REST on 2026-06-13 and applied mutation signature Y104F/D125A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: IMP cyclohydrolase(Enzyme) mutant Y104F/D125A double


sequence_source: UniProt P31939 canonical sequence checked via UniProt REST on 2026-06-13

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

column_label: Table 2 (Steady-State Results for ATIC Mutants), printed enzyme line 'wt'; column 'Km (uM)' = 0.9; column 'kcat (s-1)' = 8.6; column 'kcat/Km (M-1 s-1)' = 1 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.9 in a column headed Km (uM); 1 uM is 0.001 mM, so 0.9 / 1000 = 0.0009 mM. kcat: printed Table 2 cell 8.6 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 8.6 s^(-1). kcat/Km: printed Table 2 cell 1 x 10^7 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1 x 10^7 / 1000 = 10000.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 8.6 s^(-1), Km 0.0009 mM and kcat_over_km 9555.555555555555 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed enzyme line 'wt': Km (uM) = 0.9; kcat (s-1) = 8.6; kcat/Km (M-1 s-1) = 1 x 10^7.

row_label: Table 2, printed enzyme line 'wt'


enzyme_display_name: beta-Ala-His dipeptidase

substrate_name: Homocarnosine

sequence_source: UniProtKB REST lookup for Q96KN2 on 2026-06-13; reviewed entry CNDP1_HUMAN.

enzyme: beta-Ala-His dipeptidase

substrate: Homocarnosine


substrate_name: carnosine

substrate: carnosine


substrate_name: Carnosine; H2O

proof_lines:
presence of CD2+, pH 7.5, 30°C
pH 7.5, 30°C
pH 8.0, 37°C

substrate: Carnosine; H2O


sequence_source: UniProtKB REST lookup for Q8BUG2 on 2026-06-13; reviewed entry CNDP1_MOUSE.

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication, presence of 1 mM cysteine

proof_lines: pH 7.0, temperature not specified in the publication, presence of 1 mM glutathione

proof_lines: pH 7.0, temperature not specified in the publication, presence of 1 mM reduced glutathione


organism: Pseudomonas putida

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


organism: Archaeoglobus fulgidus

sequence_source: UniProtKB REST lookup for O28464 on 2026-06-13; unreviewed entry O28464_ARCFU.


sequence_source: UniProtKB REST lookup for P15639 on 2026-06-13; reviewed entry PUR9_ECOLI.

proof_lines: pH 7.5, temperature not specified in the publication


organism: Gallus gallus

substrate_name: Unknown

ki_unit: mM

proof_lines:
pH 7.4
about, pH 7.4

substrate: Unknown


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


proof_lines: SABIO-RK modifier species: IMP cyclohydrolase(Enzyme) mutant Y104A


proof_lines: SABIO-RK modifier species: IMP cyclohydrolase(Enzyme) mutant D125N


proof_lines: SABIO-RK modifier species: IMP cyclohydrolase(Enzyme) mutant K137A


proof_lines: SABIO-RK modifier species: IMP cyclohydrolase(Enzyme) mutant D125E


sequence_source: UniProtKB REST direct lookup P31939 on 2026-06-13

normalized_value_unit_evidence: Km: printed Table 2 cell 0.9 in a column headed Km (uM); 1 uM is 0.001 mM, so 0.9 / 1000 = 0.0009 mM. kcat: printed Table 2 cell 8.6 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 8.6 s^(-1). kcat/Km: printed Table 2 cell 1 x 10^7 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1 x 10^7 / 1000 = 10000.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 8.6 s^(-1) and Km 0.0009 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31939 and applied mutation signature D125N to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Results for ATIC Mutants), printed enzyme line 'D125N'; column 'Km (uM)' = 2.7; column 'kcat (s-1)' = 0.603; column 'kcat/Km (M-1 s-1)' = 2 x 10^5.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.7 in a column headed Km (uM); 1 uM is 0.001 mM, so 2.7 / 1000 = 0.0027 mM. kcat: printed Table 2 cell 0.603 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.603 s^(-1). kcat/Km: printed Table 2 cell 2 x 10^5 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2 x 10^5 / 1000 = 200.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.603 s^(-1), Km 0.003 mM and kcat_over_km 201.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed enzyme line 'D125N': Km (uM) = 2.7; kcat (s-1) = 0.603; kcat/Km (M-1 s-1) = 2 x 10^5.

row_label: Table 2, printed enzyme line 'D125N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31939 and applied mutation signature Y104A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Results for ATIC Mutants), printed enzyme line 'Y104A'; column 'Km (uM)' = 3.0; column 'kcat (s-1)' = 0.136; column 'kcat/Km (M-1 s-1)' = 5 x 10^4.

normalized_value_unit_evidence: Km: printed Table 2 cell 3.0 in a column headed Km (uM); 1 uM is 0.001 mM, so 3.0 / 1000 = 0.003 mM. kcat: printed Table 2 cell 0.136 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.136 s^(-1). kcat/Km: printed Table 2 cell 5 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 5 x 10^4 / 1000 = 50.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.136 s^(-1), Km 0.003 mM and kcat_over_km 45.333333333333336 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, printed enzyme line 'Y104A': Km (uM) = 3.0; kcat (s-1) = 0.136; kcat/Km (M-1 s-1) = 5 x 10^4.

row_label: Table 2, printed enzyme line 'Y104A'


normalized_value_unit_evidence: Km: printed Table 2 cell 9.1 in a column headed Km (uM); 1 uM is 0.001 mM, so 9.1 / 1000 = 0.0091 mM. kcat: printed Table 2 cell 0.014 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.014 s^(-1). kcat/Km: printed Table 2 cell 2 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 2 x 10^3 / 1000 = 2.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.014 s^(-1), Km 0.009 mM and kcat_over_km 1.5555555555555558 s^(-1)*mM^(-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31939 and applied mutation signature K66A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Results for ATIC Mutants), printed enzyme line 'K66A'; column 'Km (uM)' = 115; column 'kcat (s-1)' = 0.062; column 'kcat/Km (M-1 s-1)' = 5 x 10^2.

normalized_value_unit_evidence: Km: printed Table 2 cell 115 in a column headed Km (uM); 1 uM is 0.001 mM, so 115 / 1000 = 0.115 mM. kcat: printed Table 2 cell 0.062 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.062 s^(-1). kcat/Km: printed Table 2 cell 5 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 5 x 10^2 / 1000 = 0.5 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.062 s^(-1) and Km 0.115 mM.

raw_value_unit_evidence: Table 2, printed enzyme line 'K66A': Km (uM) = 115; kcat (s-1) = 0.062; kcat/Km (M-1 s-1) = 5 x 10^2.

row_label: Table 2, printed enzyme line 'K66A'


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB REST direct lookup Q58043 on 2026-06-13


organism: Staphylococcus lugdunensis

mutation_signature: IMP cyclohydrolase of the domain truncation pET- -IMPCH

proof_lines: IMP cyclohydrolase of the domain truncation mutant pET-28c-IMPCH, pH 7.4, temperature not specified in the publication


proof_lines: full length bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC), pH 7.4, temperature not specified in the publication


substrate_name: 1-Stearoylglycerol 3-phosphate

sequence_source: UniProtKB:P34913 direct accession lookup (UniProtKB reviewed Swiss-Prot; fetched 2026-06-13)

assay_conditions_summary: pH 7; 303.15 K; buffer A = BisTris/HCl buffer

column_label: Table 2 Kinetic constants of recombinant purified human sEH for lipid phosphates. Compound row 18; column 'K M (uM)' = 4.2; column 'k cat (10^-3 . s^-1)' = 125; column 'k cat /K M (10^-3 . s^-1 . uM^-1)' = 33.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.2 uM; 4.2 / 1000 = 0.0042 mM; the exported value is 0.004 mM. kcat: printed Table 2 cell 125 in the column unit 10^-3 s^-1; 125 x 10^-3 = 0.125 s^-1; the exported value is 0.125 s^(-1). kcat/Km: printed Table 2 cell 33 in the column unit 10^-3 s^-1 uM^-1; 33 x 10^-3 s^-1 uM^-1 = 33 s^-1 mM^-1 because 1 s^-1 uM^-1 = 1000 s^-1 mM^-1; the exported value is 31.25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, compound row 18: K M = 4.2 uM; k cat = 125 in the printed column unit 10^-3 s^-1; k cat /K M = 33 in the printed column unit 10^-3 s^-1 uM^-1.

row_label: Table 2, compound row 18 (1-stearyl-2-hydroxy-3-glycerophosphate, the Table 1 name for compound 18)

substrate: 1-Stearoylglycerol 3-phosphate


substrate_name: N-Acetylsphingosine 1-phosphate

substrate: N-Acetylsphingosine 1-phosphate


substrate_name: 1-Palmitoylglycerol 3-phosphate

substrate: 1-Palmitoylglycerol 3-phosphate


substrate_name: 1-Myristoylglycerol 3-phosphate

column_label: Table 2 Kinetic constants of recombinant purified human sEH for lipid phosphates. Compound row 16; column 'K M (uM)' = 5.1; column 'k cat (10^-3 . s^-1)' = 354; column 'k cat /K M (10^-3 . s^-1 . uM^-1)' = 76.

normalized_value_unit_evidence: Km: printed Table 2 cell 5.1 uM; 5.1 / 1000 = 0.0051 mM; the exported value is 0.005 mM. kcat: printed Table 2 cell 354 in the column unit 10^-3 s^-1; 354 x 10^-3 = 0.354 s^-1; the exported value is 0.354 s^(-1). kcat/Km: printed Table 2 cell 76 in the column unit 10^-3 s^-1 uM^-1; 76 x 10^-3 s^-1 uM^-1 = 76 s^-1 mM^-1 because 1 s^-1 uM^-1 = 1000 s^-1 mM^-1; the exported value is 70.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, compound row 16: K M = 5.1 uM; k cat = 354 in the printed column unit 10^-3 s^-1; k cat /K M = 76 in the printed column unit 10^-3 s^-1 uM^-1.

row_label: Table 2, compound row 16 (1-myristoyl-2-hydroxy-3-glycerophosphate, the Table 1 name for compound 16)

substrate: 1-Myristoylglycerol 3-phosphate


substrate_name: 1-Arachidonoyl-sn-glycerol 3-phosphate

assay_conditions_summary: pH 7; 303.15 K; buffer Buffer A (BisTris/HCl

column_label: Table label: Table 2 Kinetic constants of recombinant purified human sEH for lipid phosphates. Row label: compound 20 * (1-arachidonoyl-2-hydroxy-3-glycerophosphate); Column label: kcat, Km, and kcat/Km primary cells; raw value: 250, 13, and 20; raw unit: 10^-3 s^-1, μM, and 10^-3 s^-1 μM^-1; normalized value: 0.25 s^-1, 0.013 mM, and 20.0 s^-1 mM^-1; assay condition: purified recombinant human sEH in Buffer A at pH 7.0 and 30 °C; Table 2 marks substrate inhibition at high substrate concentrations; captured primary segment: 20 * | 13 ± 2 | 250 ± 16 | 20 ± 2 | 1 | 0.96–0.99.

normalized_value_unit_evidence: metric: kcat; raw value: 250; raw unit: 10^-3 s^-1; normalized value: 0.25; normalized unit: s^(-1); metric: Km; raw value: 13; raw unit: μM; normalized value: 0.013; normalized unit: mM; metric: kcat/Km; raw value: 20; raw unit: s^(-1)*mM^(-1); normalized value: 20.0; normalized unit: s^(-1)*mM^(-1);

raw_value_unit_evidence: Table 2 Kinetic constants of recombinant purified human sEH for lipid phosphates. Header columns: K M (μM); k cat (10^-3 s^-1); kcat/K M (10^-3 s^-1 microM^-1). Compound 20 * row: 20 * | 13 ± 2 | 250 ± 16 | 20 ± 2 | 1 | 0.96–0.99. Table 1 substrate name: 1-arachidonoyl-2-hydroxy-3-glycerophosphate.

row_label: Table 2 | compound 20 * (1-arachidonoyl-2-hydroxy-3-glycerophosphate)

substrate: 1-Arachidonoyl-sn-glycerol 3-phosphate


substrate_name: sphingosine 1-phosphate

column_label: Table label: Table 2 Kinetic constants of recombinant purified human sEH for lipid phosphates. Row: compound 27 (shingosine-1-phosphate). Columns read: K M (μM) cell 31, k cat (10 −3 .s −1 ) cell 18, k cat /K M (10 −3 .s −1 .μM −1 ) cell 0.58. metric: kcat; raw value: 18; raw unit: 10^-3 s^-1; normalized value: 0.018 s^(-1); metric: Km; raw value: 31; raw unit: uM; normalized value: 0.031 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.5806451612903225 s^-1 mM^-1; assay condition: Recombinant purified human sEH (soluble epoxide hydrolase) N-terminal phosphatase activity; kinetic parameters for a series of lisophoshatidic acids and sphingosine phosphates were determined under steady-state conditions using the purified recombinant human sEH; enzyme solution at 2.6 ug/mL ([E] = 40 nM) in Buffer A (BisTris/HCl buffer, pH 7.0, 25 mM, containing 1 mM MgCl2 and 0.1 mg/mL BSA); the reaction mixtures were incubated at 30 degrees C for 5 to 30 minutes; results are means +/- SD (n = 3). Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: Table 2 row 27 normalized into export units. k cat: the column header is `k cat (10 −3 .s −1 )`, so the printed cell 18 is 18 x 10^-3 s^-1 = 0.018 s^(-1). K M: the column header is `K M (μM)`, so the printed cell 31 is 31 μM = 0.031 mM (1 μM = 0.001 mM). k cat / K M: the column header is `k cat /K M (10 −3 .s −1 .μM −1 )`; because 1 μM^-1 = 1000 mM^-1, the column unit 10^-3 s^-1 μM^-1 equals 1 s^-1 mM^-1 exactly, so the printed cell 0.58 is 0.58 s^-1 mM^-1. Rendering quirks of the flattened JATS text: the superscript minus one renders as −1, the micro sign as μ, the plus-minus as ±, the en dash in the r 2 range as –, and superscripts/subscripts are flattened to spaces, so `k cat (10 −3 .s −1 )` is the paper's k_cat column in units of 10^-3 s^-1 and `r 2` is the paper's r^2 column.

raw_value_unit_evidence: Table 2 Kinetic constants of recombinant purified human sEH for lipid phosphates. | header row of Table 2: # | K M (μM) | k cat (10 −3 .s −1 ) | k cat /K M (10 −3 .s −1 .μM −1 ) | n | r 2 | data row: 27 | 31 ± 4 | 18 ± 1 | 0.58 ± 0.04 | 1 | 0.95–0.99 | compound 27 is named in Table 1 as `27 shingosine-1-phosphate`. The cells of Table 2 row 27 read: K M = 31 μM (average +/- SD 31 ± 4); k cat = 18 in units of 10^-3 s^-1 (average +/- SD 18 ± 1); k cat / K M = 0.58 in units of 10^-3 s^-1 μM^-1 (average +/- SD 0.58 ± 0.04).

row_label: Table 2 | compound 27 (shingosine-1-phosphate)

substrate: sphingosine 1-phosphate


organism: Rattus norvegicus

sequence_source: UniProtKB:P80299 direct accession lookup (UniProtKB reviewed Swiss-Prot; fetched 2026-06-13)


organism: Brucella anthropi

sequence_source: UniProtKB REST accession Q59632 direct lookup on 2026-06-13


proof_lines: 100 mM Tris/HCl or 50 mM potassium phosphate, pH 8.0, 30°C


organism: Arabidopsis thaliana

substrate_name: malonyl-CoA

sequence_source: UniProtKB reviewed entry Q9LJB4 direct REST lookup; sequence version 1; PubMed:17292360 functional support; BRENDA EC 2.3.1.172 cross-reference.

assay_conditions_summary: pH 7.1; 298.15 K; cofactor CoA

substrate: malonyl-CoA


substrate_name: malvin

substrate: malvin


substrate_name: cyanin

substrate: cyanin


proof_lines: cyanidin 3-O-[[2-O-beta-D-xylosyl]-6-O-(6-O-(4-coumaroyl)-beta-D-glucoside)] 5-O-beta-D-glucoside as co-substrate, pH 7.1, 25°C

proof_lines: cyanidin 3-O-[[2-O-(2-O-sinapoyl)-beta-D-xylosyl]-6-O-(6-O-(4-coumaroyl)-beta-D-glucoside)] 5-O-beta-D-glucoside as co-substrate, pH 7.1, 25°C


organism: Salvia splendens

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8W1W9 direct REST lookup plus PubMed:12578391 mutagenesis feature D171A; variant sequence reconstructed during review. and applied mutation signature D171A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: anthocyanin 5-O-glucoside 6'''-O-malonyltransferase(Enzyme) mutant D171A His6-tagged

proof_lines: pH 7, 30°C, malonyl-CoA as cosubstrate, D171A mutant Ss5MaT1

proof_lines: pH 7, 30°C, shisonin as cosubstrate, D171A mutant Ss5MaT1


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8W1W9 direct REST lookup plus PubMed:12578391 mutagenesis feature Y45A; variant sequence reconstructed during review. and applied mutation signature Y45A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed entry Q8W1W9 direct REST lookup plus PubMed:12578391 mutagenesis feature D171A; variant sequence reconstructed during review.


organism: Thermococcus kodakarensis

sequence_source: UniProtKB:Q5JD29 FASTA direct lookup 2026-06-13


organism: Escherichia coli (strain K12)

substrate_name: O-acetyl-ADP-ribose

source_db: uniprot

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

assay_conditions_summary: cofactor ADP

substrate: O-acetyl-ADP-ribose

source: uniprot


organism: Mus musculus

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


proof_lines: kcat are 14 sec(-1), 354 sec(-1), 167 sec(-1), 125 sec(-1), 177 sec(-1), 250 sec(-1), 18 sec(-1) and 136 sec(-1) for farnesyl pyro-phosphate, 1-myristoyl-2-hydroxy-3-glycerophosphate, 1-palmityl-2-hydroxy-3-glycerophosphate, 1-stearyl-2-hyd


substrate_name: carnosine (at 30 degrees Celsius and in the absence of cadmium ions)

proof_lines: 1 hour incubation in 50 mM Tris-HCl, pH 7.5.


organism: Cryptococcus neoformans (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)

substrate_name: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 7.5 sec(-1) with AICAR formyltransferase activity with (6S)-10-formyltetrahydrofolate as substrate (PubMed:36063996). kcat is 7.7 sec(-1) for FAICAR cyclization activity (at pH 7.5 and 37 degrees Celsius) (PubMed:36063996).


organism: Homo sapiens

substrate_name: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate)

proof_lines: kcat is 3.7 sec(-1) for AICAR formyltransferase activity with (6S)-10-formyltetrahydrofolate as substrate (PubMed:10985775). kcat is 4.1 sec(-1) for AICAR formyltransferase activity with 10-formyldihydrofolate as substrate (PubMed:10985775)


substrate_name: bisdemalonylsalvianin (with malonyl-CoA as cosubstrate)

assay_conditions_summary: cofactor CoA


substrate_name: dihydroxyacetone

smiles: C(C(=O)CO)O

substrate: dihydroxyacetone


substrate_name: FAD with manganese

assay_conditions_summary: cofactor FAD

substrate: FAD with manganese


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Sus scrofa

substrate_name: D-glyceraldehyde

substrate: D-glyceraldehyde


organism: Limosilactobacillus reuteri

substrate_name: sucrose

substrate: sucrose


proof_lines: transferase activity, measurement of alpha-D-glucose minus beta-D-fructose, pH 6.5, 30°C

proof_lines: hydrolytic activity, measurement of beta-D-fructose, pH 6.5, 30°C

proof_lines: overall activity, measurement of alpha-D-glucose, pH 6.5, 30°C


organism: Streptomyces viridochromogenes


organism: [Candida] boidinii

substrate_name: ATP

proof_lines:
pH 8.0, 30-37°C
ATP in form of MgATP2-

substrate: ATP


organism: [Candida] methylica


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


assay_conditions_summary: pH 9


organism: Plasmodium berghei (strain Anka)


substrate_name: Unknown


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


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


organism: Rattus norvegicus

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


substrate_name: carnosine

substrate: carnosine


substrate_name: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.4)


substrate: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.4)


organism: Citrobacter freundii

substrate_name: D,L-glyceraldehyde

proof_lines: pH and temperature not specified in the publication

substrate: D,L-glyceraldehyde


organism: Enterococcus faecalis

substrate_name: ATP; Dihydroxyacetone

substrate: ATP; Dihydroxyacetone


organism: Klebsiella pneumoniae

substrate_name: Dihydroxyacetone; ATP

substrate: Dihydroxyacetone; ATP


organism: Escherichia coli

substrate_name: O-acetyl-ADP-D-ribose

substrate: O-acetyl-ADP-D-ribose


assay_conditions_summary: pH 7; 303.15 K; cofactor ADP


organism: Staphylococcus aureus

assay_conditions_summary: pH 7.3; 296.15 K; cofactor ADP


organism: Leuconostoc citreum

sequence_variant_note: Resolved canonical sequence from UniProt Q7X481 plus one-residue reconstruction from selected BRENDA mutation note and applied mutation signature L499F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q7X481 plus one-residue reconstruction from selected BRENDA mutation note and applied mutation signature R618K to reconstruct the assayed variant sequence.


sequence_source: UniProt Q7X481 Leuconostoc citreum inulosucrase


sequence_variant_note: Resolved canonical sequence from UniProt Q7X481 plus one-residue reconstruction from selected BRENDA mutation note and applied mutation signature S425A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q8GP32 Limosilactobacillus reuteri inu inulosucrase; selected PMID 16899050 names Lactobacillus reuteri 121 inulosucrase


organism: Homo sapiens

substrate_name: 4-nitrophenyl phosphate

sequence_source: UniProtKB P34913 reviewed canonical sequence for Homo sapiens EPHX2/HYES_HUMAN, EC 3.1.3.76.

proof_lines: pH 7.8, 37°C, recombinant wild-type N-terminal domain

proof_lines: pH 7.8, 37°C, recombinant wild-type enzyme

proof_lines: pH 7.4, 37°C, recombinant wild-type allele MFA enzyme and mutant R103C

substrate: 4-nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P34913 reviewed canonical Homo sapiens EPHX2 sequence by applying R103C and R287Q. and applied mutation signature R103C/R287Q to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, recombinant mutant R103C/R287Q


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P34913 reviewed canonical Homo sapiens EPHX2 sequence by applying R287Q. and applied mutation signature R287Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P34913 reviewed canonical Homo sapiens EPHX2 sequence used only as context; variant sequence not reconstructed because the selected evidence does not prove a double K55R/C154Y mutant.

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

proof_lines: pH 7.4, 37°C, recombinant mutants K55R and C154Y


substrate_name: geranylgeranyl diphosphate

proof_lines:
recombinant enzyme
pH 7.0, 30°C, recombinant enzyme
pH 7.8, 37°C, recombinant enzyme

substrate: geranylgeranyl diphosphate


proof_lines:
pH 7.8, 37°C, native enzyme
pH 7.8, 37°C, recombinant enzyme


substrate_name: Carnosine; H2O

proof_lines: Vmax: 356 pmol/min/microgram after addition of 0.08 mM homocarnosine

substrate: Carnosine; H2O


substrate_name: H2O; Carnosine

substrate: H2O; Carnosine


proof_lines:
pH 7.5, mutant K66A
pH 7.5, 22°C, mutant K66A


proof_lines:
pH 7.5, mutant D125N
pH 7.5, 22°C, mutant D125N


proof_lines:
pH 7.5, mutant D125A
pH 7.5, 22°C, mutant D125A


proof_lines:
pH 7.5, mutant Y104F
pH 7.5, 22°C, mutant Y104F


proof_lines:
pH 7.5, mutant D125E
pH 7.5, 22°C, mutant D125E


proof_lines:
pH 7.5, mutant K137A
pH 7.5, 22°C, mutant K137A


proof_lines:
pH 7.5, wild type
pH 7.5, 22°C, wild-type


proof_lines:
pH 7.5, mutant K137R
pH 7.5, 22°C, mutant K137R


proof_lines:
pH 7.5, mutant Y104A
pH 7.5, 22°C, mutant Y104A


proof_lines:
pH 7.5, 22°C, mutantY104F
pH 7.5, 22°C, mutantD125A
pH 7.5, 22°C, mutantK137A


organism: Mus musculus


enzyme_display_name: sucrose 6(F)-phosphate phosphorylase

organism: Ilumatobacter coccineus (strain NBRC 103263 / KCTC 29153 / YM16-304)

proof_lines: kcat is 126 sec(-1) for the phosphorolysis of sucrose 6(F)-phosphate (at 35 degrees Celsius and pH 7). kcat is 45 sec(-1) for the synthetic direction with alpha-D-glucose 1-phosphate and D-fructose 6-phosphate as substrates (at 35 degrees C

enzyme: sucrose 6(F)-phosphate phosphorylase


organism: Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032)

proof_lines: kcat is 82.6 sec(-1) for the phosphorolysis of sucrose 6(F)-phosphate (at 55 degrees Celsius and pH 6.5). kcat is 66.2 sec(-1) for the phosphorolysis of sucrose (at 55 degrees Celsius and pH 6.5). kcat is 24.2 sec(-1) for the synthetic dire


substrate_name: beta-D-fructofuranose

substrate: beta-D-fructofuranose


enzyme_display_name: succinyl-diaminopimelate desuccinylase

organism: Salmonella typhimurium

sequence_source: UniProtKB reviewed accession Q8ZN75

enzyme: succinyl-diaminopimelate desuccinylase


organism: Vibrio cholerae

sequence_source: UniProtKB reviewed accession Q9KQ52

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


substrate_name: Phosphate; Sucrose / related merged source substrates

sequence_source: UniProtKB:D9TT09 direct accession lookup

proof_lines: pH and temperature not specified in the publication


substrate_name: alpha-D-glucopyranose 1-phosphate

assay_conditions_summary: pH 6; 328.15 K; buffer 50 mM MES

column_label: Table 2: Apparent kinetic parameters for sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum (Appl Microbiol Biotechnol 2014, 98:7027-7037); printed column heads Reaction | Substrate | KM (mM) | kcat (s^-1) | kcat/KM (mM^-1 s^-1). The cited cell set is Table 2, Synthesis, substrate row alpha-D-Glucose 1-phosphate (footnote c): column KM (mM) = 15.6; column kcat (s^-1) = 14.4; column kcat/KM (mM^-1 s^-1) = 0.9. The printed uncertainties of the two component cells are shown in the table beside the central values, and only the central values are transcribed here. captured primary segment: Table 2, Synthesis, substrate row alpha-D-Glucose 1-phosphate (footnote c) | construct sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum | substrate alpha-D-Glucose 1-phosphate | condition 55 C in 50 mM MES buffer pH 6.0 in the presence of 200 mM D-fructose | KM 15.6 mM | kcat 14.4 s^-1 | kcat/KM 0.9 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 15.6 mM; the printed affinity column of this paper is already in millimolar, so no unit conversion applies and the paper value is 15.6 mM. kcat: printed Table 2 kcat cell 14.4 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 14.4 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 0.9 mM^-1 s^-1; the printed efficiency column of this paper is already per second per millimolar, so no unit conversion applies and the printed cell is 0.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 14.4 / 15.6 = 0.9230769230769231 s^-1 mM^-1, which written to the one decimal the paper's efficiency column uses is 0.9 mM^-1 s^-1, the printed cell.

raw_value_unit_evidence: Table 2, Synthesis, substrate row alpha-D-Glucose 1-phosphate (footnote c): KM = 15.6 mM; kcat = 14.4 s^-1; printed kcat/KM = 0.9 mM^-1 s^-1.

substrate: alpha-D-glucopyranose 1-phosphate


substrate_name: beta-D-Fructose 6-phosphate

column_label: Table 2: Apparent kinetic parameters for sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum (Appl Microbiol Biotechnol 2014, 98:7027-7037); printed column heads Reaction | Substrate | KM (mM) | kcat (s^-1) | kcat/KM (mM^-1 s^-1). The cited cell set is Table 2, Synthesis, substrate row D-Fructose 6-phosphate (footnote d): column KM (mM) = 15.1; column kcat (s^-1) = 24.2; column kcat/KM (mM^-1 s^-1) = 1.6. The printed uncertainties of the two component cells are shown in the table beside the central values, and only the central values are transcribed here. captured primary segment: Table 2, Synthesis, substrate row D-Fructose 6-phosphate (footnote d) | construct sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum | substrate D-Fructose 6-phosphate | condition 55 C in 50 mM MES buffer pH 6.0 in the presence of 100 mM alpha-D-glucose 1-phosphate (synthesis) | KM 15.1 mM | kcat 24.2 s^-1 | kcat/KM 1.6 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 15.1 mM; the printed affinity column of this paper is already in millimolar, so no unit conversion applies and the paper value is 15.1 mM. kcat: printed Table 2 kcat cell 24.2 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 24.2 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 1.6 mM^-1 s^-1; the printed efficiency column of this paper is already per second per millimolar, so no unit conversion applies and the printed cell is 1.6 s^(-1)*mM^(-1). Quotient disclosure for this row: 24.2 / 15.1 = 1.6026490066225165 s^-1 mM^-1, which written to the one decimal the paper's efficiency column uses is 1.6 mM^-1 s^-1, the printed cell.

raw_value_unit_evidence: Table 2, Synthesis, substrate row D-Fructose 6-phosphate (footnote d): KM = 15.1 mM; kcat = 24.2 s^-1; printed kcat/KM = 1.6 mM^-1 s^-1.

substrate: beta-D-Fructose 6-phosphate


substrate_name: Sucrose 6-phosphate

assay_conditions_summary: pH 6.5; 328.15 K; buffer 50 mM MES

column_label: Table 2: Apparent kinetic parameters for sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum (Appl Microbiol Biotechnol 2014, 98:7027-7037); printed column heads Reaction | Substrate | KM (mM) | kcat (s^-1) | kcat/KM (mM^-1 s^-1). The cited cell set is Table 2, Phosphorolysis, substrate row Sucrose 6'-phosphate (footnote a): column KM (mM) = 12.7; column kcat (s^-1) = 82.6; column kcat/KM (mM^-1 s^-1) = 6.5. The printed uncertainties of the two component cells are shown in the table beside the central values, and only the central values are transcribed here. captured primary segment: Table 2, Phosphorolysis, substrate row Sucrose 6'-phosphate (footnote a) | construct sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum | substrate Sucrose 6'-phosphate | condition 55 C in 50 mM MES buffer pH 6.5 in the presence of 100 mM of inorganic phosphate | KM 12.7 mM | kcat 82.6 s^-1 | kcat/KM 6.5 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 12.7 mM; the printed affinity column of this paper is already in millimolar, so no unit conversion applies and the paper value is 12.7 mM. kcat: printed Table 2 kcat cell 82.6 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 82.6 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 6.5 mM^-1 s^-1; the printed efficiency column of this paper is already per second per millimolar, so no unit conversion applies and the printed cell is 6.5 s^(-1)*mM^(-1). Quotient disclosure for this row: 82.6 / 12.7 = 6.503937007874016 s^-1 mM^-1, which written to the one decimal the paper's efficiency column uses is 6.5 mM^-1 s^-1, the printed cell.

raw_value_unit_evidence: Table 2, Phosphorolysis, substrate row Sucrose 6'-phosphate (footnote a): KM = 12.7 mM; kcat = 82.6 s^-1; printed kcat/KM = 6.5 mM^-1 s^-1.

substrate: Sucrose 6-phosphate


substrate_name: sucrose 6F-phosphate

row_label: Table 2, Phosphorolysis, substrate row Sucrose 6'-phosphate (footnote a)

table_label: Table 2: Apparent kinetic parameters for sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum (Appl Microbiol Biotechnol 2014, 98:7027-7037); printed column heads Reaction | Substrate | KM (mM) | kcat (s^-1) | kcat/KM (mM^-1 s^-1)

substrate: sucrose 6F-phosphate


substrate_name: D-Fructose

column_label: Table 2: Apparent kinetic parameters for sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum (Appl Microbiol Biotechnol 2014, 98:7027-7037); printed column heads Reaction | Substrate | KM (mM) | kcat (s^-1) | kcat/KM (mM^-1 s^-1). The cited cell set is Table 2, Synthesis, substrate row D-Fructose (footnote d): column KM (mM) = 41.6; column kcat (s^-1) = 16.9; column kcat/KM (mM^-1 s^-1) = 0.4. The printed uncertainties of the two component cells are shown in the table beside the central values, and only the central values are transcribed here. captured primary segment: Table 2, Synthesis, substrate row D-Fructose (footnote d) | construct sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum | substrate D-Fructose | condition 55 C in 50 mM MES buffer pH 6.0 in the presence of 100 mM alpha-D-glucose 1-phosphate (synthesis) | KM 41.6 mM | kcat 16.9 s^-1 | kcat/KM 0.4 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 41.6 mM; the printed affinity column of this paper is already in millimolar, so no unit conversion applies and the paper value is 41.6 mM. kcat: printed Table 2 kcat cell 16.9 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 16.9 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 0.4 mM^-1 s^-1; the printed efficiency column of this paper is already per second per millimolar, so no unit conversion applies and the printed cell is 0.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 16.9 / 41.6 = 0.40624999999999994 s^-1 mM^-1, which written to the one decimal the paper's efficiency column uses is 0.4 mM^-1 s^-1, the printed cell.

raw_value_unit_evidence: Table 2, Synthesis, substrate row D-Fructose (footnote d): KM = 41.6 mM; kcat = 16.9 s^-1; printed kcat/KM = 0.4 mM^-1 s^-1.

substrate: D-Fructose


organism: Ilumatobacter coccineus

substrate_name: D-Fructose 6-phosphate

sequence_source: UniProt REST exact accession lookup for A0A6C7EEG6

substrate: D-Fructose 6-phosphate


substrate_name: S-Adenosyl-L-methionine

sequence_source: UniProtKB direct lookup, P0A9H7 and P0A9H8 identical canonical sequences, checked 2026-06-13

substrate: S-Adenosyl-L-methionine


substrate_name: Se-Adenosyl-L-selenomethionine

substrate: Se-Adenosyl-L-selenomethionine


sequence_source: UniProtKB direct lookup, P0A9H8 and P0A9H7 identical canonical sequences, checked 2026-06-13


substrate_name: Te-Adenosyl-L-telluromethionine

substrate: Te-Adenosyl-L-telluromethionine


organism: Lactobacillus acidophilus

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB direct lookup, Q5FJM0 canonical sequence, checked 2026-06-13

proof_lines:
with Tris, at pH 8.0 and 37°C
with Tris/NaHCO3, at pH 8.0 and 37°C
Raw SKiD Env: Temp=37°C, pH=8

substrate: S-adenosyl-L-methionine


enzyme_display_name: diguanylate cyclase

organism: Caulobacter vibrioides

substrate_name: Unknown

enzyme: diguanylate cyclase

substrate: Unknown


sequence_source: UniProtKB:Q9A3B9 canonical sequence checked 2026-06-13


substrate_name: cyclic di-3',5'-guanylate

sequence_source: UniProtKB:Q9A5I5 canonical sequence checked 2026-06-13

substrate: cyclic di-3',5'-guanylate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A5I5 canonical sequence checked 2026-06-13; variant reconstructed from selected BRENDA mutation note and applied mutation signature R313A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A5I5 canonical sequence checked 2026-06-13; variant reconstructed from selected BRENDA mutation note and applied mutation signature R148A/R178A/R313A to reconstruct the assayed variant sequence.

proof_lines: triple mutant R148A/R178A/R313A, inhibited


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A5I5 canonical sequence checked 2026-06-13; variant reconstructed from selected BRENDA mutation note and applied mutation signature R148A/R178A to reconstruct the assayed variant sequence.


substrate_name: GTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AA89 direct lookup; row-specific variant reconstructed by residue substitution where mutation_signature is present and applied mutation signature L65G to reconstruct the assayed variant sequence.

substrate: GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AA89 direct lookup; row-specific variant reconstructed by residue substitution where mutation_signature is present and applied mutation signature L65Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AA89 direct lookup; row-specific variant reconstructed by residue substitution where mutation_signature is present and applied mutation signature L65T to reconstruct the assayed variant sequence.

proof_lines: enzyme with 5-coordinate Fe(III) heme mutant L65T, pH 8.0, 24°C


sequence_source: UniProtKB:P0AA89 direct lookup; row-specific variant reconstructed by residue substitution where mutation_signature is present

proof_lines: enzyme with 5-coordinate Fe(III) heme mutant L65G, pH 8.0, 24°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AA89 direct lookup; row-specific variant reconstructed by residue substitution where mutation_signature is present and applied mutation signature Y43F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AA89 direct lookup; row-specific variant reconstructed by residue substitution where mutation_signature is present and applied mutation signature Y43A 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.

proof_lines: enzyme with 5-coordinate Fe(III) heme, pH 8.0, 24°C


proof_lines: enzyme with 5-coordinate Fe(III) heme mutant Y43F, pH 8.0, 24°C


substrate_name: alpha-D-glucose 1-phosphate

sequence_source: UniProtKB reviewed accession A0A6C7EEG6 checked via UniProt REST on 2026-06-13.

substrate: alpha-D-glucose 1-phosphate


substrate_name: phosphate

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

substrate: phosphate


organism: [Ruminococcus] gnavus

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


substrate_name: Phosphate

sequence_source: UniProtKB reviewed accession D9TT09 checked via UniProt REST on 2026-06-13.

column_label: Table 2: Apparent kinetic parameters for sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum (Appl Microbiol Biotechnol 2014, 98:7027-7037); printed column heads Reaction | Substrate | KM (mM) | kcat (s^-1) | kcat/KM (mM^-1 s^-1). The cited cell set is Table 2, Phosphorolysis, substrate row Phosphate (footnote b): column KM (mM) = 6.9; column kcat (s^-1) = 59.3; column kcat/KM (mM^-1 s^-1) = 8.6. The printed uncertainties of the two component cells are shown in the table beside the central values, and only the central values are transcribed here. captured primary segment: Table 2, Phosphorolysis, substrate row Phosphate (footnote b) | construct sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum | substrate Phosphate | condition 55 C in 50 mM MES buffer pH 6.5 in the presence of 350 mM sucrose (phosphorolysis) | KM 6.9 mM | kcat 59.3 s^-1 | kcat/KM 8.6 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 6.9 mM; the printed affinity column of this paper is already in millimolar, so no unit conversion applies and the paper value is 6.9 mM. kcat: printed Table 2 kcat cell 59.3 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 59.3 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 8.6 mM^-1 s^-1; the printed efficiency column of this paper is already per second per millimolar, so no unit conversion applies and the printed cell is 8.6 s^(-1)*mM^(-1). Quotient disclosure for this row: 59.3 / 6.9 = 8.594202898550725 s^-1 mM^-1, which written to the one decimal the paper's efficiency column uses is 8.6 mM^-1 s^-1, the printed cell.

raw_value_unit_evidence: Table 2, Phosphorolysis, substrate row Phosphate (footnote b): KM = 6.9 mM; kcat = 59.3 s^-1; printed kcat/KM = 8.6 mM^-1 s^-1.

substrate: Phosphate


substrate_name: Sucrose

column_label: Table 2: Apparent kinetic parameters for sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum (Appl Microbiol Biotechnol 2014, 98:7027-7037); printed column heads Reaction | Substrate | KM (mM) | kcat (s^-1) | kcat/KM (mM^-1 s^-1). The cited cell set is Table 2, Phosphorolysis, substrate row Sucrose (footnote a): column KM (mM) = 76.5; column kcat (s^-1) = 66.2; column kcat/KM (mM^-1 s^-1) = 0.9. The printed uncertainties of the two component cells are shown in the table beside the central values, and only the central values are transcribed here. captured primary segment: Table 2, Phosphorolysis, substrate row Sucrose (footnote a) | construct sucrose 6'-phosphate phosphorylase from T. thermosaccharolyticum | substrate Sucrose | condition 55 C in 50 mM MES buffer pH 6.5 in the presence of 100 mM of inorganic phosphate | KM 76.5 mM | kcat 66.2 s^-1 | kcat/KM 0.9 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 76.5 mM; the printed affinity column of this paper is already in millimolar, so no unit conversion applies and the paper value is 76.5 mM. kcat: printed Table 2 kcat cell 66.2 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 66.2 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 0.9 mM^-1 s^-1; the printed efficiency column of this paper is already per second per millimolar, so no unit conversion applies and the printed cell is 0.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 66.2 / 76.5 = 0.865359477124183 s^-1 mM^-1, which written to the one decimal the paper's efficiency column uses is 0.9 mM^-1 s^-1, the printed cell.

raw_value_unit_evidence: Table 2, Phosphorolysis, substrate row Sucrose (footnote a): KM = 76.5 mM; kcat = 66.2 s^-1; printed kcat/KM = 0.9 mM^-1 s^-1.

substrate: Sucrose


substrate_name: beta-D-fructofuranose

row_label: Table 2, Synthesis, substrate row D-Fructose (footnote d)

substrate: beta-D-fructofuranose


substrate_name: D-Glucose 1-phosphate

row_label: Table 2, Synthesis, substrate row alpha-D-Glucose 1-phosphate (footnote c)

substrate: D-Glucose 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AA89 canonical sequence retrieved through UniProt REST on 2026-06-13; L65T reconstructed after confirming residue 65 is L. and applied mutation signature L65T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AA89 canonical sequence retrieved through UniProt REST on 2026-06-13; Y43A reconstructed after confirming residue 43 is Y. and applied mutation signature Y43A to reconstruct the assayed variant sequence.

proof_lines: enzyme with 5-coordinate Fe(III) heme mutant Y43A, pH 8.0, 24°C


sequence_source: UniProtKB P0AA89 canonical sequence retrieved through UniProt REST on 2026-06-13.


organism: Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130

sequence_source: UniProtKB Q72MQ6 canonical sequence retrieved through UniProt REST on 2026-06-13.


organism: Thermotoga maritima

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9X2A8 canonical sequence retrieved through UniProt REST on 2026-06-13; R158A reconstructed after confirming residue 158 is R. and applied mutation signature R158A to reconstruct the assayed variant sequence.


organism: Xanthomonas citri pv. citri

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

proof_lines: mutant K759A, Michaelis-Menten model, pH 8.0, 30°C


proof_lines: wild-type, Michaelis-Menten model, pH 8.0, 30°C


enzyme_display_name: Porphobilinogen deaminase

substrate_name: H2O; Porphobilinogen

sequence_variant_note: Resolved canonical sequence from UniProtKB:P06983 canonical sequence plus selected SABIO-RK mutation annotation and applied mutation signature R131L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hydroxymethylbilane synthase(Enzyme) mutant R131L

enzyme: Porphobilinogen deaminase

substrate: H2O; Porphobilinogen


substrate_name: Porphobilinogen; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P06983 canonical sequence plus selected SABIO-RK mutation annotation and applied mutation signature R11L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hydroxymethylbilane synthase(Enzyme) mutant R11L

substrate: Porphobilinogen; H2O