sequence_variant_note: Resolved canonical sequence from UniProtKB P52788 direct accession sequence with row-specific D201N substitution reconstructed on 2026-06-15 and applied mutation signature D201N to reconstruct the assayed variant sequence.

proof_lines:
mutant D201N, pH 7.5, 37°C
mutant D201N


enzyme_display_name: spermine synthase

organism: Homo sapiens

substrate_name: spermidine

source_db: brenda

km_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

sequence_variant_note: Resolved canonical sequence from UniProtKB P52788 direct accession sequence with row-specific D276N substitution reconstructed on 2026-06-15 and applied mutation signature D276N to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines:
mutant D276N, pH 7.5, 37°C
mutant D276N

enzyme: spermine synthase

substrate: spermidine

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB P52788 direct accession sequence with row-specific D201A substitution reconstructed on 2026-06-15 and applied mutation signature D201A to reconstruct the assayed variant sequence.

proof_lines:
mutant D201A, pH 7.5, 37°C
mutant D201A


mutation_signature: Unknown

sequence_source: UniProtKB P52788 direct accession sequence, retrieved 2026-06-15

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

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


substrate_name: S-Adenosylmethioninamine; Spermidine

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

km_unit: mM

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

substrate: S-Adenosylmethioninamine; Spermidine


enzyme_display_name: inositol-tetrakisphosphate 1-kinase

organism: Arabidopsis thaliana

substrate_name: ATP

kcat_display: Not reported

sequence_source: UniProtKB Q9SBA5 direct accession sequence, retrieved 2026-06-15

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

enzyme: inositol-tetrakisphosphate 1-kinase

substrate: ATP


organism: Bos taurus

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

ki_unit: mM

sequence_source: UniProtKB P0C0T1 direct accession sequence, retrieved 2026-06-15

assay_conditions_summary: cofactor ATP


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

sequence_source: UniProtKB Q13572 direct accession sequence, retrieved 2026-06-15

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines:
pH 7.2, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.2

source_databases_merged: sabio_rk brenda skid


enzyme_display_name: mevalonate 3-kinase

organism: Thermoplasma acidophilum

substrate_name: (R)-mevalonate

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q9HIN1 on 2026-06-15 and applied mutation signature T275A to reconstruct the assayed variant sequence.

data_origin: experimental

enzyme: mevalonate 3-kinase

substrate: (R)-mevalonate

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q9HIN1 on 2026-06-15 and applied mutation signature R185K to reconstruct the assayed variant sequence.


enzyme_display_name: hydroxymethylpyrimidine kinase

organism: Bacillus subtilis

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

enzyme: hydroxymethylpyrimidine kinase


organism: Escherichia coli

sequence_source: UniProtKB REST direct accession lookup for P76422 on 2026-06-15

proof_lines: pH 7.5, temperature not specified in the publication, recombinant enzyme ThiD


organism: Salmonella enterica subsp. enterica serovar Typhimurium

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

sequence_source: UniProtKB REST direct accession lookup for P55882 on 2026-06-15

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
pH 8.0, 25°C
pH 7.0, 25°C, recombinant enzyme, MgATP
pH 7.0, 25°C, recombinant enzyme

source_databases_merged: brenda skid


organism: Staphylococcus aureus

substrate_name: pyridoxine

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

substrate: pyridoxine


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

proof_lines: mutant C110A, pH not specified in the publication, temperature not specified in the publication


substrate_name: pyridoxal

proof_lines: mutant C214D, pH not specified in the publication, temperature not specified in the publication

substrate: pyridoxal


organism: Thermus thermophilus

sequence_source: UniProtKB REST direct accession lookup for Q5SKG3 on 2026-06-15


organism: Zea mays

sequence_source: UniProtKB REST direct accession lookup for Q2UVH9 on 2026-06-15


enzyme_display_name: inositol-hexakisphosphate 5-kinase

substrate_name: myo-Inositol hexakisphosphate; ATP

sequence_source: UniProtKB REST direct accession lookup for Q9UHH9 on 2026-06-15

enzyme: inositol-hexakisphosphate 5-kinase

substrate: myo-Inositol hexakisphosphate; ATP


substrate_name: Inositol hexakisphosphate

sequence_source: UniProtKB REST direct accession lookup for Q96PC2 on 2026-06-15

substrate: Inositol hexakisphosphate


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

proof_lines: isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C

proof_lines: isoform PPIP5K2, using 1D-myo-inositol hexakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C

proof_lines: isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 m MKCl, at 37°C


substrate_name: myo-Inositol hexakisphosphate

sequence_source: UniProtKB reviewed accession Q6PFW1

substrate: myo-Inositol hexakisphosphate


substrate_name: ATP; myo-Inositol hexakisphosphate

substrate: ATP; myo-Inositol hexakisphosphate


substrate_name: 1D-myo-inositol hexakisphosphate

sequence_source: UniProtKB reviewed accession O43314

substrate: 1D-myo-inositol hexakisphosphate


sequence_source: UniProtKB reviewed accession Q92551

assay_conditions_summary: pH 6.95; 310.15 K; cofactor ATP


organism: Mus musculus

sequence_source: UniProtKB reviewed accession Q6PD10


sequence_source: UniProtKB reviewed accession Q6ZQB6


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB reviewed accession Q12494


organism: Haemophilus influenzae

substrate_name: D-Ribitol 5-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q48230 canonical sequence with source-documented K386A substitution reconstructed and applied mutation signature K386A to reconstruct the assayed variant sequence.

substrate: D-Ribitol 5-phosphate


substrate_name: CTP

verification_status: verified

sequence_source: UniProtKB reviewed accession Q48230

column_label: Table label: Table 1: Steady State Kinetic Parameters Describing Substrate Specificity of Reductase and Cytidylyltransferase Activities of Bcs1. Row: CTP. Section: (2) cytidylyltransferase. Columns read: K m (uM) cell 99, k cat (s^-1) cell 13, k cat / K m (x10^-5 M^-1 s^-1) cell 1.3. metric: kcat; raw value: 13; raw unit: s^-1; normalized value: 13.0 s^(-1); metric: Km; raw value: 99; raw unit: uM; normalized value: 0.099 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 131.3131313131313 s^-1 mM^-1; assay condition: C-terminally His-tagged Bcs1 (CDP-ribitol synthase, cytidylyltransferase activity); all assays were carried out at 25 degrees C and were performed in triplicate; cytidylyltransferase activity was monitored in a continuous coupled assay for the detection of inorganic pyrophosphate in a mixture containing 25 mM HEPES (pH 7.2), 1 mM DTT, 0.01% Triton X-100, 10 mM MgCl2, and 200 uM MESG; steady state parameters were determined in the presence of saturating cosubstrate. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: Table 1 section (2) cytidylyltransferase, row CTP: kcat 13 s^-1 = 13.0 s^(-1); Km 99 uM = 0.099 mM (1 uM = 0.001 mM); kcat/Km 131.3131313131313 s^-1 mM^-1 as the exact quotient of this row's own printed kcat and Km cells (13 s^-1 divided by 0.099 mM). The row's printed kcat/Km cell reads 1.3 in a column headed (x10-5 M-1 s-1), i.e. 1.3 x 10^5 M^-1 s^-1 = 130.0 s^-1 mM^-1; the exact quotient 131.3131313131313 rounds to 1.3 x 10^5 at the printed cell's own two-significant-figure precision, so the printed cell and the exported quotient agree and the difference is printed precision only. In the PDF text the plus-minus sign renders as ( and the header multiplication sign as x.

raw_value_unit_evidence: Table 1: Steady State Kinetic Parameters Describing Substrate Specificity of Reductase and Cytidylyltransferase Activities of Bcs1 | metric header row of Table 1: Kma (µM) kcata (s-1) kcat/Km (x10-5 M-1 s-1); section header: (2) cytidylyltransferase | row: CTP 99 ( 9.1 13 ( 0.5 1.3 | cells read: K m = 99 uM; k cat = 13 s^-1; k cat / K m = 1.3 x 10^5 M^-1 s^-1

row_label: (2) cytidylyltransferase | CTP

substrate: CTP

status: verified


sequence_source: UniProtKB reviewed accession Q48230 canonical sequence with source-documented K386A substitution reconstructed


enzyme_display_name: apo-salmochelin esterase

substrate_name: triglucosyl-enterobactin

sequence_source: UniProtKB:A0A0H2V871 direct lookup on 2026-06-15; reviewed Swiss-Prot entry IROE_ECOL6, 318 aa.

enzyme: apo-salmochelin esterase

substrate: triglucosyl-enterobactin


substrate_name: monoglucosyl-enterobactin

substrate: monoglucosyl-enterobactin


substrate_name: diglucosyl-enterobactin

substrate: diglucosyl-enterobactin


organism: Mycobacterium tuberculosis

substrate_name: 4-nitrophenyl phosphate

sequence_source: UniProtKB:O33194 direct lookup on 2026-06-15; reviewed Swiss-Prot entry G3PP_MYCTU, 353 aa.

substrate: 4-nitrophenyl phosphate


substrate_name: DL-glycerol 3-phosphate

verification_status: corrected

smiles: O=P(O)(O)OCC(O)CO

column_label: Table 1 (Binding and steady-state kinetic parameters for Rv1692), substrate row 'D,L-glycerol 3-phosphate'; column 'kcat, s^-1' = 0.77; column 'Km, mM' = 0.89; column 'kcat/Km, s^-1 M^-1 (x10^3)' = 0.86; column 'Kd, uM' = 165.3; column 'Hill no.' = 2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.77 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.77 s^(-1). Km: printed Table 1 cell 0.89 mM; the column head prints mM, so no unit conversion applies and the exported value is 0.89 mM. kcat/Km: printed Table 1 cell 0.86 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 860 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 0.86 s^-1 mM^-1. Quotient disclosure for this row: 0.77 / 0.89 = 0.8651685393258427 s^-1 mM^-1, which is the value the export currently carries; this pass puts the printed efficiency cell in its place.

raw_value_unit_evidence: Table 1, substrate row 'D,L-glycerol 3-phosphate': kcat = 0.77 s^-1; Km = 0.89 mM; printed kcat/Km = 0.86 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 0.86 x 10^3 s^-1 M^-1.

table_label: Table 1: Binding and steady-state kinetic parameters for Rv1692 (PNAS 2013, 110(28):11320-11325); printed columns Kd (uM), kcat (s^-1), Km (mM), Hill no., and kcat/Km (s^-1 M^-1) under a (x10^3) multiplier

substrate: DL-glycerol 3-phosphate

status: corrected


substrate_name: L-glycerol 3-phosphate

column_label: Table 1 (Binding and steady-state kinetic parameters for Rv1692), substrate row 'L-glycerol 3-phosphate'; column 'kcat, s^-1' = 0.02; column 'Km, mM' = 1.10; column 'kcat/Km, s^-1 M^-1 (x10^3)' = 0.02; column 'Kd, uM' = 158.2; column 'Hill no.' = 1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.02 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.02 s^(-1). Km: printed Table 1 cell 1.10 mM; the column head prints mM, so no unit conversion applies and the exported value is 1.1 mM. kcat/Km: printed Table 1 cell 0.02 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 20 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 0.02 s^-1 mM^-1. Quotient disclosure for this row: 0.02 / 1.1 = 0.01818181818181818 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the two decimal places Table 1 uses.

raw_value_unit_evidence: Table 1, substrate row 'L-glycerol 3-phosphate': kcat = 0.02 s^-1; Km = 1.10 mM; printed kcat/Km = 0.02 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 0.02 x 10^3 s^-1 M^-1.

substrate: L-glycerol 3-phosphate


substrate_name: D-ribulose 5-phosphate

column_label: Table 1 (Binding and steady-state kinetic parameters for Rv1692), substrate row 'D-ribulose 5-phosphate'; column 'kcat, s^-1' = 0.18; column 'Km, mM' = 1.30; column 'kcat/Km, s^-1 M^-1 (x10^3)' = 0.14; column 'Kd, uM' = 201.8; column 'Hill no.' = 2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.18 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.18 s^(-1). Km: printed Table 1 cell 1.30 mM; the column head prints mM, so no unit conversion applies and the exported value is 1.3 mM. kcat/Km: printed Table 1 cell 0.14 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 140 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 0.14 s^-1 mM^-1. Quotient disclosure for this row: 0.18 / 1.3 = 0.13846153846153844 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the two decimal places Table 1 uses.

raw_value_unit_evidence: Table 1, substrate row 'D-ribulose 5-phosphate': kcat = 0.18 s^-1; Km = 1.30 mM; printed kcat/Km = 0.14 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 0.14 x 10^3 s^-1 M^-1.

substrate: D-ribulose 5-phosphate


substrate_name: Glycerol 2-phosphate

smiles: O=P(O)(O)OC(CO)CO

column_label: Table 1 (Binding and steady-state kinetic parameters for Rv1692), substrate row 'Glycerol 2-phosphate'; column 'kcat, s^-1' = 0.18; column 'Km, mM' = 2.01; column 'kcat/Km, s^-1 M^-1 (x10^3)' = 0.09; column 'Kd, uM' = 328.7; column 'Hill no.' = 2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.18 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.18 s^(-1). Km: printed Table 1 cell 2.01 mM; the column head prints mM, so no unit conversion applies and the exported value is 2.01 mM. kcat/Km: printed Table 1 cell 0.09 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 90 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 0.09 s^-1 mM^-1. Quotient disclosure for this row: 0.18 / 2.01 = 0.08955223880597016 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the two decimal places Table 1 uses.

raw_value_unit_evidence: Table 1, substrate row 'Glycerol 2-phosphate': kcat = 0.18 s^-1; Km = 2.01 mM; printed kcat/Km = 0.09 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 0.09 x 10^3 s^-1 M^-1.

substrate: Glycerol 2-phosphate


column_label: Table 1 (Binding and steady-state kinetic parameters for Rv1692), substrate row 'Para-nitrophenyl phosphate'; column 'kcat, s^-1' = 1.00; column 'Km, mM' = 19.30; column 'kcat/Km, s^-1 M^-1 (x10^3)' = 0.05; column 'Kd, uM' = 60.8; column 'Hill no.' = 1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.00 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 1.0 s^(-1). Km: printed Table 1 cell 19.30 mM; the column head prints mM, so no unit conversion applies and the exported value is 19.3 mM. kcat/Km: printed Table 1 cell 0.05 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 50 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 0.05 s^-1 mM^-1. Quotient disclosure for this row: 1.0 / 19.3 = 0.05181347150259067 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the two decimal places Table 1 uses.

raw_value_unit_evidence: Table 1, substrate row 'Para-nitrophenyl phosphate': kcat = 1.00 s^-1; Km = 19.30 mM; printed kcat/Km = 0.05 under the column head kcat/Km, s^-1 M^-1 (x10^3), i.e. 0.05 x 10^3 s^-1 M^-1.


organism: Aspergillus saitoi

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E411D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E124D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature D269E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E414D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E414D


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E474D to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E411D


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E273D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q48230 direct REST lookup on 2026-06-15 by applying R18A. and applied mutation signature R18A to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB Q48230 direct REST lookup on 2026-06-15 by applying R18A.


enzyme_display_name: [protein-PII] uridylyltransferase

substrate_name: UTP; [Protein-PII]

sequence_source: UniProtKB P27249 direct REST lookup on 2026-06-15

enzyme: [protein-PII] uridylyltransferase

substrate: UTP; [Protein-PII]


substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: ATP


substrate_name: UTP

substrate: UTP


substrate_name: GTP

substrate: GTP


substrate_name: ferric monoglucosyl-enterobactin

sequence_source: UniProtKB A0A0H2V871 direct REST lookup on 2026-06-15

substrate: ferric monoglucosyl-enterobactin


substrate_name: enterobactin

substrate: enterobactin


substrate_name: ferric enterobactin

substrate: ferric enterobactin


substrate_name: ferric diglucosyl-enterobactin

substrate: ferric diglucosyl-enterobactin


proof_lines: turnover number above 0.13 1/sec, at pH 7.5 and 23°C


substrate_name: ferric triglucosyl-enterobactin

substrate: ferric triglucosyl-enterobactin


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

substrate_name: L-methionine (R)-S-oxide

sequence_variant_note: Resolved canonical sequence from UniProt REST Q9HJW5 canonical sequence with validated C60S substitution reconstruction and applied mutation signature C60S to reconstruct the assayed variant sequence.

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

substrate: L-methionine (R)-S-oxide


sequence_source: UniProt REST Q9HJW5 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9HJW5 canonical sequence with validated C15S substitution reconstruction and applied mutation signature C15S to reconstruct the assayed variant sequence.


enzyme_display_name: methionine synthase

organism: Sus scrofa

sequence_source: UniProt REST Q9MYZ4 canonical sequence

enzyme: methionine synthase


substrate_name: L-Homocysteine

substrate: L-Homocysteine


organism: Streptomyces fradiae

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProt REST P95748 canonical sequence

substrate: S-adenosyl-L-methionine


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

proof_lines: pH 7.5, 24°C, cosubstrate: 0.89 mM dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose

proof_lines: pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt REST P95748 canonical sequence with validated H123N substitution reconstruction and applied mutation signature H123N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P95748 canonical sequence with validated H123A substitution reconstruction and applied mutation signature H123A to reconstruct the assayed variant sequence.


enzyme_display_name: UDP-sugar diphosphatase

substrate_name: NADH

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

enzyme: UDP-sugar diphosphatase

substrate: NADH


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NMN

substrate: NMN


substrate_name: AMP

substrate: AMP


substrate_name: UDP-D-glucose

proof_lines: chimera UshA catalytic domain/CpdB specificity domain, pH not specified in the publication, temperature not specified in the publication

proof_lines: chimera CpdB catalytic domain/UshA specificity domain, pH not specified in the publication, temperature not specified in the publication

substrate: UDP-D-glucose


substrate_name: ADP-D-ribose

sequence_source: UniProtKB direct lookup Q9D142 on 2026-06-15

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

assay_conditions_summary: pH 8; 310.15 K; cofactor ADP

proof_lines: in 50 mM Tris-HCl, pH 8.0, 10 mM Mg2+, at 37°C

proof_lines: in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 37°C

substrate: ADP-D-ribose


substrate_name: UDPglucose; H2O

sequence_source: UniProtKB direct lookup Q865Y9 on 2026-06-15

assay_conditions_summary: cofactor ADP

substrate: UDPglucose; H2O


organism: Yersinia intermedia

substrate_name: UDP-glucose

sequence_source: UniProtKB direct lookup A4URQ8 on 2026-06-15

substrate: UDP-glucose


enzyme_display_name: gamma-resorcylate decarboxylase

organism: Agrobacterium tumefaciens

sequence_source: UniProtKB direct lookup Q60FX6 on 2026-06-15

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

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

enzyme: gamma-resorcylate decarboxylase


organism: Polaromonas sp. JS666

sequence_source: UniProtKB direct lookup Q12BV1 on 2026-06-15

proof_lines:
pH 7.0, 30°C
Raw SKiD Env: Temp=30°C, pH=7


organism: Rhizobium sp.

sequence_source: UniProtKB direct lookup Q60GU1 on 2026-06-15


organism: Clostridioides difficile

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

proof_lines: isozyme toxin A, with MgCl2 and 150 mM KCl


enzyme_display_name: methylglutaconyl-CoA hydratase

organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession F4JML5 direct REST check, 2026-06-15

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

enzyme: methylglutaconyl-CoA hydratase


organism: Homo sapiens

substrate_name: trans-3-Methylglutaconyl-CoA; H2O

sequence_source: UniProtKB reviewed accession Q13825 direct REST check, 2026-06-15

assay_conditions_summary: cofactor CoA

substrate: trans-3-Methylglutaconyl-CoA; H2O


enzyme_display_name: galactarate dehydratase

organism: Escherichia coli

substrate_name: D-Galactarate

sequence_source: UniProtKB reviewed accession P39829 direct REST check, 2026-06-15

column_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1). Table 1, row GalcD; column kcat (s^-1) = 22.0; column Km (uM) = 800; column kcat/Km (M^-1 s^-1) = 2.7 x 10^4. captured primary segment: GalcD | kcat 22.0 ± 0.7 s^-1 | Km 800 ± 9 uM | kcat/Km 2.7 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 22.0 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 22.0 s^(-1); the exported value is 22.0 s^(-1). Km: printed Table 1 cell 800 uM; 1 uM is 1/1000 mM, so 800 / 1000 = 0.8 mM; the exported value is 0.8 mM. kcat/Km: printed Table 1 cell 2.7 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.7 x 10^4 / 1000 = 27.0 s^(-1)*mM^(-1); the exported value is 27.5 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, row GalcD: kcat = 22.0 s^-1; Km = 800 uM; printed kcat/Km = 2.7 x 10^4 M^-1 s^-1.

row_label: Table 1, row GalcD

enzyme: galactarate dehydratase

substrate: D-Galactarate


table_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1)


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: galactarate

sequence_source: UniProtKB reviewed accession Q8ZL58 direct REST check, 2026-06-15

proof_lines: pH 8.0, 25°C, His6-tagged recombinant enzyme

substrate: galactarate


organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2


sequence_source: UniProtKB:Q12563 direct accession lookup; checked 2026-06-15


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E414D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E124D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E124D


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E124Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E124Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E273D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E273D


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature D269E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant D269E


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E474D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E474D


organism: Candida albicans

sequence_source: UniProtKB:Q8J0Q0 direct accession lookup; checked 2026-06-15


substrate_name: H2O; Man9GlcNAc; H2O

sequence_source: UniProtKB:Q9UKM7 direct accession lookup; checked 2026-06-15

substrate: H2O; Man9GlcNAc; H2O


organism: Neobacillus novalis

sequence_source: UniProtKB:A0A7R9KAR8 direct accession lookup; checked 2026-06-15

assay_conditions_summary: pH 6


organism: Streptococcus pneumoniae

substrate_name: Unknown

assay_conditions_summary: pH 9

proof_lines: in the coupled assay of SpGH92 and CfMan2A, with substrate 4-methylumbelliferyl alpha-D-mannopyranosyl-(1->2)-beta-D-mannopyranoside, pH 9.0-9.5, 22Â°C

substrate: Unknown


enzyme_display_name: beta-agarase

organism: Agarivorans albus

substrate_name: Agarose; H2O; Agarose

sequence: ASLVTSFEEA

wild_type_sequence: ASLVTSFEEA

sequence_source: UniProtKB:P85974 direct accession lookup; checked 2026-06-15

enzyme: beta-agarase

substrate: Agarose; H2O; Agarose


substrate_name: agarose

substrate: agarose


substrate_name: Neoagarotetraose

substrate: Neoagarotetraose


sequence_source: UniProtKB:A8W969 FASTA checked 2026-06-15


organism: Catenovulum agarivorans


organism: Cellvibrio sp. KY-GH-1


organism: Pseudoalteromonas sp. CY24

substrate_name: neoagarodecaose

sequence_source: UniProtKB:A1A3Y9 FASTA checked 2026-06-15

substrate: neoagarodecaose


organism: Wenyingzhuangia aestuarii

sequence_source: UniProtKB:A0A516RTC5 FASTA checked 2026-06-15


organism: Zobellia galactanivorans

sequence_source: UniProtKB:Q9RGX8 FASTA checked 2026-06-15


substrate_name: H2O; Agarose

sequence_source: UniProtKB:G0L322 FASTA checked 2026-06-15

substrate: H2O; Agarose


substrate_name: Agarose; H2O

sequence_source: UniProtKB:D7GXG4 FASTA checked 2026-06-15

substrate: Agarose; H2O


enzyme_display_name: creatininase

organism: Pseudomonas putida

substrate_name: creatinine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P83772 FASTA checked 2026-06-15; reconstructed W174F from selected BRENDA mutation note and applied mutation signature W174F to reconstruct the assayed variant sequence.

proof_lines: mutant W174F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication

enzyme: creatininase

substrate: creatinine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P83772 FASTA checked 2026-06-15; reconstructed E122Q from selected BRENDA mutation note and applied mutation signature E122Q to reconstruct the assayed variant sequence.

proof_lines: mutant E122Q, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant E122Q, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication


sequence_source: UniProtKB:P83772 FASTA checked 2026-06-15

proof_lines: wild-type, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication

proof_lines: wild-type, presence of EDTA, semi-apo-enzyme, pH not specified in the publication, temperature not specified in the publication

proof_lines: wild-type, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P83772 FASTA checked 2026-06-15; reconstructed Y121A from selected BRENDA mutation note and applied mutation signature Y121A to reconstruct the assayed variant sequence.

proof_lines: mutant Y121A, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P83772 FASTA checked 2026-06-15; reconstructed W154F from selected BRENDA mutation note and applied mutation signature W154F to reconstruct the assayed variant sequence.

proof_lines: mutant W154F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication


substrate_name: Creatinine; H2O

substrate: Creatinine; H2O


enzyme_display_name: sulfinoalanine decarboxylase

sequence_source: UniProtKB:Q6ZQY3 canonical sequence, REST release 2026_02

enzyme: sulfinoalanine decarboxylase


organism: Tribolium castaneum

substrate_name: cysteine sulfinic acid

substrate: cysteine sulfinic acid


organism: unidentified prokaryotic organism

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

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

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


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


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

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


enzyme_display_name: sphinganine-1-phosphate aldolase

organism: Burkholderia pseudomallei

substrate_name: sphinganine 1-phosphate

enzyme: sphinganine-1-phosphate aldolase

substrate: sphinganine 1-phosphate


organism: Homo sapiens

substrate_name: Sphingosine 1-phosphate

mutation_signature: Δ1

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

mutation_type: deletion

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

substrate: Sphingosine 1-phosphate


enzyme_display_name: chorismate lyase

organism: Escherichia coli

substrate_name: Chorismate

sequence_source: UniProtKB:P26602 canonical sequence, REST release 2026_02

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

enzyme: chorismate lyase

substrate: Chorismate


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


organism: Stenotrophomonas panacihumi

substrate_name: chorismate

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

substrate: chorismate


organism: Xylella fastidiosa


organism: Acinetobacter sp.

substrate_name: (E)-glutaconyl-CoA

proof_lines: dehydration hydration

substrate: (E)-glutaconyl-CoA


organism: Arabidopsis thaliana


organism: Glycine max

source_db: uniprot

source: uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Zea mays

substrate_name: ATP

substrate: ATP


organism: Haemophilus influenzae

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

assay_conditions_summary: cofactor NADPH


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

substrate_name: CTP

substrate: CTP


organism: Rattus norvegicus

substrate_name: Unknown

substrate: Unknown


substrate_name: (DL)-glycerol 3-phosphate

substrate: (DL)-glycerol 3-phosphate


organism: Agarivorans albus

substrate_name: agarose

substrate: agarose


organism: Pseudomonas putida


organism: Agrobacterium radiobacter

substrate_name: gamma-resorcylate (for decarboxylation)

substrate: gamma-resorcylate (for decarboxylation)


organism: Rhizobium sp. (strain MTP-10005)


substrate_name: L-aspartate

substrate: L-aspartate


substrate_name: sphingosine 1-phosphate

substrate: sphingosine 1-phosphate


substrate_name: dihydrosphingosin 1-phosphate

substrate: dihydrosphingosin 1-phosphate


organism: Escherichia coli (strain K12)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Homo sapiens


enzyme_display_name: pentachlorophenol monooxygenase

organism: Sphingobium chlorophenolicum

substrate_name: pentachlorophenol

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

enzyme: pentachlorophenol monooxygenase

substrate: pentachlorophenol


enzyme_display_name: cholestanetriol 26-monooxygenase

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

enzyme: cholestanetriol 26-monooxygenase


enzyme_display_name: pentalenolactone synthase

organism: Streptomyces arenae

substrate_name: pentalenolactone F

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

enzyme: pentalenolactone synthase

substrate: pentalenolactone F


organism: Streptomyces exfoliatus

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


organism: Streptomyces fradiae

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


enzyme_display_name: salicylate carboxymethyltransferase

organism: Arabidopsis thaliana

substrate_name: S-adenosyl-L-methionine

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

enzyme: salicylate carboxymethyltransferase

substrate: S-adenosyl-L-methionine


organism: Petunia hybrida

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


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


substrate_name: acetyl-CoA

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

substrate: acetyl-CoA


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

assay_conditions_summary: pH 6; cofactor CoA

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


enzyme_display_name: anthocyanidin 3-O-glucosyltransferase

organism: Fragaria ananassa

substrate_name: pelargonidin

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

enzyme: anthocyanidin 3-O-glucosyltransferase

substrate: pelargonidin


organism: Zea mays

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


organism: Humulus lupulus

substrate_name: phlorisovalerophenone

substrate: phlorisovalerophenone


substrate_name: naringenin chalcone

substrate: naringenin chalcone


enzyme_display_name: spermine synthase

substrate_name: S-adenosylmethionine

enzyme: spermine synthase

substrate: S-adenosylmethionine


enzyme_display_name: inositol-tetrakisphosphate 1-kinase

organism: Bos taurus

enzyme: inositol-tetrakisphosphate 1-kinase


organism: Glycine max


substrate_name: ATP

substrate: ATP


enzyme_display_name: hydroxymethylpyrimidine kinase

enzyme: hydroxymethylpyrimidine kinase


enzyme_display_name: inositol-hexakisphosphate 5-kinase

enzyme: inositol-hexakisphosphate 5-kinase


organism: Sus scrofa

substrate_name: prostamide H(2)

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

substrate: prostamide H(2)


enzyme_display_name: vitamin D 25-hydroxylase

substrate_name: vitamin D(2)

enzyme: vitamin D 25-hydroxylase

substrate: vitamin D(2)


organism: Pseudonocardia autotrophica

substrate_name: vitamin D(3)

substrate: vitamin D(3)


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

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: free methionine-R-sulfoxide

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

substrate: free methionine-R-sulfoxide


organism: Clarkia breweri

substrate_name: benzylalcohol

substrate: benzylalcohol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


organism: Vitis vinifera

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

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


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

substrate_name: agarose

substrate: agarose


enzyme_display_name: gamma-resorcylate decarboxylase

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

substrate_name: gamma-resorcylate

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

enzyme: gamma-resorcylate decarboxylase

substrate: gamma-resorcylate


organism: Mus musculus

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


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


organism: Unknown prokaryotic organism

substrate_name: L-cysteine

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

substrate: L-cysteine


enzyme_display_name: galactarate dehydratase

organism: Escherichia coli (strain K12)

substrate_name: galactarate

enzyme: galactarate dehydratase

substrate: galactarate


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

substrate_name: L-talarate

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

substrate: L-talarate


enzyme_display_name: quercetin 2,3-dioxygenase

organism: Aspergillus flavus

substrate_name: quercetin

enzyme: quercetin 2,3-dioxygenase

substrate: quercetin


organism: Aspergillus niger


organism: Bacillus subtilis

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

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

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


organism: Streptomyces sp.

assay_conditions_summary: pH 8; buffer pH 8

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

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


organism: Bacillus tropicus

substrate_name: Pentachlorophenol

substrate: Pentachlorophenol


organism: Flavobacterium sp.


organism: Sphingobium chlorophenolicum

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


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

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

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


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


organism: Homo sapiens

substrate_name: vitamin D2

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

substrate: vitamin D2


organism: Citrus sinensis

substrate_name: salicylate

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

substrate: salicylate


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


organism: Glycine max


organism: Solanum lycopersicum

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


enzyme_display_name: selenocysteine Se-methyltransferase

organism: Astragalus bisulcatus

substrate_name: L-selenocysteine

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

enzyme: selenocysteine Se-methyltransferase

substrate: L-selenocysteine


organism: Clarkia breweri

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

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

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

substrate: acetyl-CoA


organism: Rattus norvegicus

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


organism: Sus scrofa

substrate_name: bufuralol

substrate: bufuralol


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


organism: Streptomyces arenae

substrate_name: pentalenolactone F

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

substrate: pentalenolactone F


organism: Streptomyces exfoliatus


enzyme_display_name: methionine synthase

organism: Bos taurus

enzyme: methionine synthase


organism: Candida albicans

substrate_name: L-homocysteine

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

substrate: L-homocysteine


organism: Phaseolus vulgaris


organism: Zea mays

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


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

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

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


enzyme_display_name: mevalonate 3-kinase

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

substrate_name: ATP

assay_conditions_summary: cofactor ATP

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

enzyme: mevalonate 3-kinase

substrate: ATP


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

substrate_name: (R)-mevalonate

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

substrate: (R)-mevalonate


organism: Acinetobacter baumannii (strain IS-123)

substrate_name: HMP

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

substrate: HMP


organism: Haemophilus influenzae

substrate_name: D-ribulose 5-phosphate

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

substrate: D-ribulose 5-phosphate


enzyme_display_name: [protein-PII] uridylyltransferase

organism: Escherichia coli (strain K12)

substrate_name: GlnB protein

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

enzyme: [protein-PII] uridylyltransferase

substrate: GlnB protein


enzyme_display_name: apo-salmochelin esterase

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

substrate_name: Ent

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

enzyme: apo-salmochelin esterase

substrate: Ent


organism: Mus musculus

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


enzyme_display_name: beta-agarase

organism: Microbulbifer thermotolerans

substrate_name: agar

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

enzyme: beta-agarase

substrate: agar


organism: Wenyingzhuangia aestuarii

substrate_name: funoran

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

substrate: funoran


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

substrate_name: agarose

substrate: agarose


substrate_name: S-adenosylmethioninamine; spermidine

substrate: S-adenosylmethioninamine; spermidine


organism: Homo sapiens


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


organism: Mammalia

substrate_name: S-Adenosylmethioninamine; Spermidine

substrate: S-Adenosylmethioninamine; Spermidine


substrate_name: Unknown

substrate: Unknown


organism: Rattus norvegicus

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


organism: Glycine max

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

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

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


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Escherichia coli

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

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


organism: Plasmodium falciparum

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

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


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

assay_conditions_summary: pH 6.8; 310.15 K; cofactor ATP

proof_lines: pH and temperature not specified in the publication


organism: Clarkia concinna

substrate_name: benzyl alcohol

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

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

substrate: benzyl alcohol


organism: Jasminum sambac

substrate_name: acetyl-CoA

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

substrate: acetyl-CoA


organism: Brassica oleracea

substrate_name: cyanidin

substrate: cyanidin


organism: Daucus carota


organism: Pericallis hybrida

substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Silene dioica

substrate_name: UDPglucose

substrate: UDPglucose


organism: Vitis vinifera


organism: Xanthisma gracile


organism: Zea mays

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


enzyme_display_name: kaempferol 3-O-galactosyltransferase

organism: Eriobotrya japonica

substrate_name: quercetin

enzyme: kaempferol 3-O-galactosyltransferase

substrate: quercetin


organism: Petunia sp.

substrate_name: UDP

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

substrate: UDP


organism: Vigna mungo

substrate_name: kaempferol

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

substrate: kaempferol


organism: Saccharomyces cerevisiae

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


organism: Trypanosoma cruzi

substrate_name: p-nitrophenyl-alpha-D-mannoside

substrate: p-nitrophenyl-alpha-D-mannoside


organism: Alteromonas sp.

substrate_name: neoagarohexaose

substrate: neoagarohexaose


organism: Microbulbifer elongatus

substrate_name: beta-4-nitrophenyl galactopyranoside

substrate: beta-4-nitrophenyl galactopyranoside


organism: Saccharophagus degradans

substrate_name: agarose

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

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


organism: Streptomyces coelicolor

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

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


organism: Zobellia galactanivorans

substrate_name: liquid-phase agarose

proof_lines: AgaB AgaAc

substrate: liquid-phase agarose


enzyme_display_name: bacillolysin

organism: Geobacillus stearothermophilus

substrate_name: Unknown

enzyme: bacillolysin


organism: Priestia megaterium

substrate_name: plasminogen

substrate: plasminogen


enzyme_display_name: creatininase

organism: Homo sapiens

substrate_name: creatinine

enzyme: creatininase

substrate: creatinine


organism: Paenarthrobacter ureafaciens


organism: Pseudomonas putida


organism: Phycomyces blakesleeanus

substrate_name: dihydroxyacetone phosphate

substrate: dihydroxyacetone phosphate


substrate_name: NADH; Glycerone phosphate

assay_conditions_summary: cofactor NADH

substrate: NADH; Glycerone phosphate


substrate_name: H2O; Glycerol 3-phosphate

proof_lines:
for Gpp1p
for Gpp2p

substrate: H2O; Glycerol 3-phosphate


organism: Aspergillus phoenicis

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


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


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


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


substrate_name: mannobiose

assay_conditions_summary: pH 5

substrate: mannobiose


organism: Candida albicans


organism: Penicillium citrinum

substrate: Unknown


organism: Rattus norvegicus


organism: Ricinus communis


organism: Pseudomonas sp.


enzyme_display_name: UDP-sugar diphosphatase

organism: Escherichia coli

substrate_name: UDP-glucose

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

enzyme: UDP-sugar diphosphatase


organism: Saccharomyces cerevisiae


organism: Agrobacterium tumefaciens


enzyme_display_name: sulfinoalanine decarboxylase

organism: Aedes aegypti

substrate_name: L-cysteine sulfinate

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

enzyme: sulfinoalanine decarboxylase

substrate: L-cysteine sulfinate


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


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


organism: Bos taurus

substrate_name: cysteine sulfinic acids

substrate: cysteine sulfinic acids


substrate_name: cysteine sulfinate

proof_lines:
minor enzyme form
liver enzyme
brain enzyme

substrate: cysteine sulfinate


organism: Sus scrofa

proof_lines: CSADII fusion protein with beta-galactosidase

proof_lines: CSADI fusion protein with beta-galactosidase


enzyme_display_name: sphinganine-1-phosphate aldolase

assay_conditions_summary: pH 10.6; 310.15 K; buffer conditions

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

enzyme: sphinganine-1-phosphate aldolase


organism: Mus musculus

substrate_name: sphingosine 1-phosphate

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

substrate: sphingosine 1-phosphate


enzyme_display_name: inositol-hexakisphosphate 5-kinase

organism: Xenopus sp.

substrate_name: Inositol hexakisphosphate

enzyme: inositol-hexakisphosphate 5-kinase

substrate: Inositol hexakisphosphate


organism: Arabidopsis thaliana

substrate_name: DL-glycerol 3-phosphate

assay_conditions_summary: pH 7

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

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

substrate: DL-glycerol 3-phosphate


organism: Corynebacterium glutamicum

substrate_name: L-glycerol 3-phosphate

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

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

substrate: L-glycerol 3-phosphate


organism: Dunaliella salina


organism: Dunaliella tertiolecta


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


organism: Osmerus mordax

substrate_name: glycerol 3-phosphate

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

substrate: glycerol 3-phosphate


organism: Tetrahymena pyriformis

substrate_name: sphinganine 1-phosphate

substrate: sphinganine 1-phosphate


enzyme_display_name: chorismate lyase

substrate_name: chorismate

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

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

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

enzyme: chorismate lyase

substrate: chorismate


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

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


organism: Mycobacterium tuberculosis

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

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

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


organism: Stenotrophomonas maltophilia

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


enzyme_display_name: methylglutaconyl-CoA hydratase

organism: Homo sapiens

assay_conditions_summary: cofactor CoA

proof_lines:
lymphocyte enzyme
fibroblast enzyme

enzyme: methylglutaconyl-CoA hydratase


organism: Pseudomonas putida

assay_conditions_summary: pH 7.9; 298.15 K; cofactor CoA

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


enzyme_display_name: galactarate dehydratase

substrate_name: meso-galactarate

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

enzyme: galactarate dehydratase

substrate: meso-galactarate


organism: Escherichia coli

substrate_name: galactarate

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

substrate: galactarate


organism: Oceanobacillus iheyensis

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

assay_conditions_summary: pH 8

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


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

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


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

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


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

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


enzyme_display_name: ferric-chelate reductase (NADH)

organism: Paracoccus denitrificans

substrate_name: Fe(3+)EGTA and NADH

sequence: MVKTVAVMVGSLRKDSLAHKLMKVLQK

wild_type_sequence: MVKTVAVMVGSLRKDSLAHKLMKVLQK

enzyme: ferric-chelate reductase (NADH)

substrate: Fe(3+)EGTA and NADH


organism: Vibrio vulnificus

substrate_name: Unknown


organism: Beta vulgaris

substrate_name: Fe3+; NADH; H+

substrate: Fe3+; NADH; H+


substrate_name: NADH

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH

substrate: NADH


substrate_name: NADH; Fe3+; H+

sequence: SRLPPATRDKLADEITFFPA

wild_type_sequence: SRLPPATRDKLADEITFFPA

substrate: NADH; Fe3+; H+


organism: Solanum lycopersicum

substrate_name: NADH; H+; Fe3+

substrate: NADH; H+; Fe3+


substrate_name: glutaredoxin 1

substrate: glutaredoxin 1


organism: Myxococcus xanthus

substrate_name: arsenate

assay_conditions_summary: pH 9

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

substrate: arsenate


organism: Pteris vittata


organism: Saccharomyces cerevisiae

substrate_name: glutaredoxin

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

substrate: glutaredoxin


enzyme_display_name: cyanuric acid amidohydrolase

organism: Neomoorella thermoacetica

substrate_name: cyanuric acid

enzyme: cyanuric acid amidohydrolase

substrate: cyanuric acid


organism: Paracidovorax citrulli


organism: Pseudomonas sp.

assay_conditions_summary: pH 8; cofactor ADP


enzyme_display_name: L-lysine 6-transaminase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

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

enzyme: L-lysine 6-transaminase


enzyme_display_name: sedoheptulose-bisphosphatase

organism: Spinacia oleracea

substrate_name: Fructose 1,6-bisphosphate

enzyme: sedoheptulose-bisphosphatase

substrate: Fructose 1,6-bisphosphate


substrate_name: sedoheptulose 1,7-bisphosphate

substrate: sedoheptulose 1,7-bisphosphate


organism: Synechocystis sp.


organism: Acidovorax citrulli

substrate_name: Cyanuric acid; H2O

substrate: Cyanuric acid; H2O


organism: Azorhizobium caulinodans

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

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

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

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


organism: Bradyrhizobium diazoefficiens

substrate_name: H2O; Cyanuric acid

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

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

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

substrate: H2O; Cyanuric acid


organism: Bradyrhizobium sp.


organism: Methylobacterium sp.

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

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

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


organism: Moorella thermoacetica


organism: Nocardioides sp.


organism: Pseudomonas pseudoalcaligenes


assay_conditions_summary: pH 8; 295.15 K; cofactor ADP


organism: Homo sapiens

substrate_name: GPC

substrate: GPC


organism: Oryza sativa

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

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

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


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

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


sequence_source: direct UniProt lookup Q336V5

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

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


sequence_source: direct UniProt lookup Q10SX6


organism: Pteris vittata

sequence_source: direct UniProt lookup Q1A5X4


organism: Saccharomyces cerevisiae

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

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

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


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

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

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


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

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

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


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

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

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


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

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

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


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

sequence_source: direct UniProt lookup Q06597

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


organism: Staphylococcus aureus

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


substrate_name: Arsenate; Reduced thioredoxin

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

proof_lines: SABIO-RK modifier species: arsenate reductase (glutaredoxin)(Enzyme) mutant D105A

substrate: Arsenate; Reduced thioredoxin


sequence_source: direct UniProt lookup P74313

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


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

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


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

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


organism: Arabidopsis thaliana

substrate_name: para-nitrophenyl phosphate

substrate: para-nitrophenyl phosphate


organism: Oryza sativa subsp. japonica

substrate_name: arsenate


organism: Rhizobium meliloti (strain 1021)


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

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: sedoheptulose 1,7-bisphosphate (SBP)

substrate: sedoheptulose 1,7-bisphosphate (SBP)


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

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

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


organism: Bos taurus

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


organism: Pseudomonas sp.

substrate_name: cyanuric acid

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

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

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

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


organism: Pseudomonas sp. ADP

assay_conditions_summary: pH 9; 295.15 K; cofactor ADP


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


organism: Pseudonocardia dioxanivorans

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


organism: Rhizobium leguminosarum

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

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

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

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


sequence_source: direct UniProt REST accession lookup


enzyme_display_name: linoleate 11-lipoxygenase

organism: Fusarium oxysporum

substrate_name: linolenate

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

enzyme: linoleate 11-lipoxygenase

substrate: linolenate


organism: Gaeumannomyces graminis

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

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


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


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


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


substrate_name: linoleic acid

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

substrate: linoleic acid


organism: Cyberlindnera jadinii

substrate_name: L-lysine

substrate: L-lysine


organism: [Flavobacterium] lutescens

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


organism: Haemophilus influenzae

substrate_name: D-ribitol 5-phosphate

substrate: D-ribitol 5-phosphate


substrate_name: D-Ribitol 5-phosphate; CTP

substrate: D-Ribitol 5-phosphate; CTP


sequence_source: UniProtKB reviewed accession Q8X150


substrate_name: (13R)-hydroperoxylinolenic acid

sequence_source: UniProtKB reviewed accession Q8X151

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

substrate: (13R)-hydroperoxylinolenic acid


substrate_name: linoleate

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

substrate: linoleate


substrate_name: O2; alpha-Linolenate

substrate: O2; alpha-Linolenate


smiles: O=O


substrate_name: alpha-Linolenate

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

substrate: alpha-Linolenate


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

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

assay_conditions_summary: pH 8; 310.15 K; buffer an assay

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

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

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

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


substrate_name: L-Lysine

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

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

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

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

substrate: L-Lysine


sequence_source: UniProtKB reviewed accession Q9ZQI7

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

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

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

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


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

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

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

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


substrate_name: 2-Oxoglutarate; L-Lysine

sequence_source: UniProtKB reviewed accession Q93ZN9

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

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

substrate: 2-Oxoglutarate; L-Lysine


substrate_name: L-Lysine; 2-Oxoglutarate

substrate: L-Lysine; 2-Oxoglutarate


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

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

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

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


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

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

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

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


organism: Fusarium oxysporum (strain Fo5176)


organism: Gaeumannomyces avenae

substrate_name: alpha-linoleate

substrate: alpha-linoleate


organism: Gaeumannomyces tritici


organism: Streptomyces clavuligerus

substrate_name: lysine

substrate: lysine


substrate_name: lysophosphatidylcholine

substrate: lysophosphatidylcholine


organism: Escherichia coli

substrate_name: arsenate

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

substrate: arsenate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

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


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

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

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


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

substrate_name: cyanuric acid

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

substrate: cyanuric acid


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

row_label: Table 2, enzyme row Bradyrhizobium japonicum USDA 110


organism: Bradyrhizobium sp. (strain ORS 375)

substrate_name: Unknown

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

substrate: Unknown


organism: Ectopseudomonas oleovorans (strain CECT 5344)

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


organism: Methylobacterium sp. (strain 4-46)

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


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

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


organism: Pseudomonas sp

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

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

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

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


organism: Pseudomonas sp. (strain ADP)

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


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

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


organism: Staphylococcus aureus


organism: Mus musculus

substrate_name: p-nitrophenylphosphocholine

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

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

substrate: p-nitrophenylphosphocholine


organism: Rattus norvegicus

substrate_name: p-nitrophenylphosphorylthymidine

substrate: p-nitrophenylphosphorylthymidine


organism: Mycobacterium tuberculosis

substrate_name: L-lysine

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

substrate: L-lysine


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

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


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


organism: Haemophilus influenzae

substrate_name: CTP; D-Ribitol 5-phosphate

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

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

substrate: CTP; D-Ribitol 5-phosphate


substrate_name: D-Ribitol 5-phosphate; CTP

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

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

substrate: D-Ribitol 5-phosphate; CTP


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


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


organism: Bos taurus

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


substrate_name: Sphingosyl-phosphocholine

substrate: Sphingosyl-phosphocholine


substrate_name: H2O; sn-Glycero-3-phosphocholine

substrate: H2O; sn-Glycero-3-phosphocholine


substrate_name: 4-Nitrophenyl phosphocholine

substrate: 4-Nitrophenyl phosphocholine


organism: Streptomyces sanglieri


enzyme_display_name: propionate kinase

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

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

assay_conditions_summary: cofactor ATP

enzyme: propionate kinase

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


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: propionate

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: propionate


enzyme_display_name: kojibiose hydrolase

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

substrate_name: kojibiose

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

enzyme: kojibiose hydrolase

substrate: kojibiose


organism: Mucilaginibacter mallensis

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

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


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

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


organism: Sarocladium sp

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


organism: Weissella viridescens

substrate_name: tRNA(Ala)

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

substrate: tRNA(Ala)


enzyme_display_name: 2'-5' oligoadenylate synthase

organism: Homo sapiens

substrate_name: ATP

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

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

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

enzyme: 2'-5' oligoadenylate synthase

substrate: ATP


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

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

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


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

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


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


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


organism: Sus scrofa

substrate_name: NAD+

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

assay_conditions_summary: cofactor NAD+

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

substrate: NAD+


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

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


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

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

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

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


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

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


organism: Flavobacterium johnsoniae

substrate_name: kojitriose

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

substrate: kojitriose


substrate_name: alpha-D-glucopyranosyl fluoride

substrate: alpha-D-glucopyranosyl fluoride


substrate_name: kojitetraose

substrate: kojitetraose


substrate_name: kojipentaose

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

substrate: kojipentaose


substrate_name: L-alanyl-tRNAAla

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

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

substrate: L-alanyl-tRNAAla


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


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

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


substrate_name: L-alanyl-tRNA

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

substrate: L-alanyl-tRNA


enzyme_display_name: inositol 3-kinase

organism: Zea mays

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

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

enzyme: inositol 3-kinase


organism: Lactobacillus viridescens

substrate_name: L-Alanyl-tRNA(Ala)

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

substrate: L-Alanyl-tRNA(Ala)


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


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

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


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


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

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


enzyme_display_name: dimethylallylcistransferase

organism: Solanum habrochaites

substrate_name: neryl diphosphate

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

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

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

enzyme: dimethylallylcistransferase

substrate: neryl diphosphate