enzyme_display_name: acetylornithine transaminase

organism: Burkholderia cepacia

substrate_name: L-ornithine

enzyme: acetylornithine transaminase

substrate: L-ornithine


organism: Escherichia coli

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: cosubstrate 2-oxoglutarate, arginine inducible and arginine repressible enzyme

source: brenda


organism: Klebsiella aerogenes


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Escherichia coli (strain K12)

substrate_name: N-acetylornithine

source_db: uniprot

protein_accession_database: UniProt

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

substrate: N-acetylornithine

source: uniprot


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: N(2)-succinyl-L-ornithine (at 15 mM 2-ketoglutarate and pH 9.0)

assay_conditions_summary: pH 9


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: acetylornithine

substrate: acetylornithine


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

substrate_name: N-acetylornithine (at pH 9.5 and 25 degrees Celsius)


enzyme_display_name: hydroxyisourate hydrolase

organism: Glycine max

proof_lines: pH 7.5, 37°C, recombinant enzyme lacking the signal peptide

enzyme: hydroxyisourate hydrolase


enzyme_display_name: 2-dehydro-3-deoxyglucarate aldolase

enzyme: 2-dehydro-3-deoxyglucarate aldolase


organism: Picrophilus oshimae

assay_conditions_summary: pH 6.2; 333.15 K; buffer 50 mM sodium phosphate

proof_lines: at 60°C in 50 mM sodium phosphate buffer (pH 6.2)


enzyme_display_name: 2-hydroxyethylphosphonate dioxygenase

organism: Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)

enzyme: 2-hydroxyethylphosphonate dioxygenase


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

proof_lines: kcat is 2.31 sec(-1) with N-acetylornithine as substrate. kcat is 0.16 sec(-1) with ornithine as substrate. kcat is 0.14 sec(-1) with gamma-aminobutyric acid as substrate. kcat is 2.50 sec(-1) with 2-oxoglutarate as substrate (in the presen


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: KDG (at 70 degrees Celsius and pH 7.2)

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: kcat is 3.8 sec(-1) for ATP, 5 sec(-1) for KDG and 5.4 sec(-1) for KDGal (at 60 degrees Celsius and pH 7.5).

substrate: KDG (at 70 degrees Celsius and pH 7.2)


substrate_name: 5-Hydroxyisourate; H2O

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

sequence_source: UniProt Q8S3J3 chain 32-560; signal peptide 1-31 removed

substrate: 5-Hydroxyisourate; H2O


organism: Klebsiella pneumoniae

sequence_variant_note: Resolved canonical sequence from UniProt A6T926 canonical sequence with R41K reconstructed after residue check and applied mutation signature R41K to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant R41K, pH 7.6, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt A6T926 canonical sequence with S108A reconstructed after residue check and applied mutation signature S108A to reconstruct the assayed variant sequence.

proof_lines: mutant S108A, pH 7.6, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt A6T926 canonical sequence with H7N reconstructed after residue check and applied mutation signature H7N to reconstruct the assayed variant sequence.

proof_lines: mutant H7N, pH 7.6, temperature not specified in the publication


sequence_source: UniProt A6T926 canonical sequence

proof_lines: wild-type, pH 7.6, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt A6T926 canonical sequence with H92N reconstructed after residue check and applied mutation signature H92N to reconstruct the assayed variant sequence.

proof_lines: mutant H92N, pH 7.6, temperature not specified in the publication


source_db: oed

verification_status: verified

sequence_source: UniProt P23522 canonical chain 1-256

assay_conditions_summary: pH 7.5; 295.15 K; buffer pH 7; cofactor NADH

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 KDGlucA; column kcat (s^-1) = 27.3; column Km (uM) = 65; column kcat/Km (M^-1 s^-1) = 4.2 x 10^5. captured primary segment: KDGlucA | kcat 27.3 ± 0.4 s^-1 | Km 65 ± 3 uM | kcat/Km 4.2 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 27.3 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 27.3 s^(-1); the exported value is 27.3 s^(-1). Km: printed Table 1 cell 65 uM; 1 uM is 1/1000 mM, so 65 / 1000 = 0.065 mM; the exported value is 0.065 mM. kcat/Km: printed Table 1 cell 4.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^5 / 1000 = 420.0 s^(-1)*mM^(-1); the exported value is 420.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row KDGlucA: kcat = 27.3 s^-1; Km = 65 uM; printed kcat/Km = 4.2 x 10^5 M^-1 s^-1.

row_label: Table 1, row KDGlucA

data_origin: experimental

status: verified

source: oed


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

proof_lines:
data for Mg2+-activated YfaU
data for Ni2+-activated YfaU
Raw SKiD Env: Temp=-----, pH=-----

source_databases_merged: sabio_rk brenda skid


organism: Streptomyces viridochromogenes

verification_status: corrected

sequence_source: UniProtKB:Q5IW40 direct accession check; reviewed 2026-06-15

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

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5IW40 direct accession check; reviewed 2026-06-15 and applied mutation signature R90K to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae

substrate_name: 2-Oxoglutarate; N2-Acetyl-L-ornithine

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

sequence_source: UniProtKB:P18544 direct accession check; reviewed 2026-06-15

substrate: 2-Oxoglutarate; N2-Acetyl-L-ornithine


organism: Salmonella typhimurium

sequence_source: UniProtKB:P40732 direct accession check; reviewed 2026-06-15


substrate_name: L-Ornithine

verification_status: unverified

substrate: L-Ornithine

status: unverified


organism: Saccharolobus solfataricus

substrate_name: ATP

kcat_over_km_origin: calculated

sequence_source: UniProtKB:Q97U29 direct accession check; reviewed 2026-06-15

assay_conditions_summary: pH 7.5; 333.15 K; cofactor ATP

substrate: ATP


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

proof_lines:
pH 7.5, 60°C
pH 7.2, 60°C
Raw SKiD Env: Temp=60°C, pH=7.5

source_databases_merged: brenda skid


sequence_source: UniProtKB:Q8S3J3 direct accession check; reviewed 2026-06-15


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

substrate_name: KDG

assay_conditions_summary: cofactor ATP

substrate: KDG


substrate_name: hydroxyisourate

substrate: hydroxyisourate


enzyme_display_name: 2-oxopent-4-enoate hydratase

organism: Burkholderia xenovorans LB400

smiles: O=C([O-])C(O)=CC=CCl

enzyme: 2-oxopent-4-enoate hydratase


substrate_name: H2O; 2-Hydroxy-2,4-pentadienoate

substrate: H2O; 2-Hydroxy-2,4-pentadienoate


organism: Escherichia coli

substrate_name: 2-Hydroxy-2,4-pentadienoate; H2O

sequence_source: UniProtKB REST P77608

substrate: 2-Hydroxy-2,4-pentadienoate; H2O


organism: Escherichia coli (strain K12)

substrate_name: 2-hydroxy-pentadienoic acid (at pH 6)

assay_conditions_summary: pH 6

substrate: 2-hydroxy-pentadienoic acid (at pH 6)


organism: Spinacia oleracea

substrate_name: But-2-enoyl-[acyl-carrier protein]; H2O

substrate: But-2-enoyl-[acyl-carrier protein]; H2O


substrate_name: 2-hydroxypentadienoic acid

substrate: 2-hydroxypentadienoic acid


organism: Paraburkholderia xenovorans

proof_lines:
activated by Mg2+
activated by Mn2+


organism: Pseudomonas putida

assay_conditions_summary: pH 7


organism: Arabidopsis thaliana


organism: Homo sapiens

substrate_name: acetyl-CoA

assay_conditions_summary: cofactor NADPH

substrate: acetyl-CoA


organism: Mus musculus

substrate_name: malonyl-CoA

assay_conditions_summary: cofactor CoA

substrate: malonyl-CoA


organism: Rattus norvegicus

substrate_name: Unknown

km_display: Not reported

substrate: Unknown


organism: Helianthus annuus

proof_lines: pH 6.8, temperature not specified in the publication, HaHAD1 wild-type protein

proof_lines: pH 6.8, temperature not specified in the publication, HaHAD2 wild-type protein


sequence_variant_note: Resolved canonical sequence from UniProtKB:F2VYC9 canonical sequence with direct F166V reconstruction and applied mutation signature F166V to reconstruct the assayed variant sequence.

proof_lines: pH 6.8, temperature not specified in the publication, HaHAD1 F166V mutant


substrate_name: crotonoyl-CoA

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

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

substrate: crotonoyl-CoA


substrate_name: H2O; Crotonoyl-CoA

proof_lines: SABIO-RK modifier species: 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase(Enzyme) mutant K1699Q DH

substrate: H2O; Crotonoyl-CoA


substrate_name: Crotonoyl-CoA; H2O

proof_lines: SABIO-RK modifier species: 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase(Enzyme) mutant K1699A DH

substrate: Crotonoyl-CoA; H2O


sequence_source: UniProtKB:P49327 canonical sequence

column_label: TABLE THREE beta-hydroxyacyl dehydratase block, enzyme row WT; columns kcat (min^-1), KCRT (uM) and kcat/KCRT (uM^-1 min^-1); kcat cell = 6 min^-1; KCRT cell = 7 uM; kcat/KCRT cell = 0.9; author manuscript page 15 (PDF page 15). captured primary segment: crotonyl-CoA | wild-type HFAS, recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE beta-hydroxyacyl dehydratase block, enzyme row WT: Km CRT 7 uM | kcat 6 min^-1 | kcat/Km CRT printed cell 0.9 under the column head kcat/KCRT (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE beta-hydroxyacyl dehydratase block, enzyme row WT: KCRT = 7 uM; kcat = 6 min^-1; printed kcat/KCRT = 0.9 uM^-1 min^-1.

table_label: TABLE THREE (kinetic evaluation of the wild-type and Lys-1699 mutant HFAS enzymes), beta-hydroxyacyl dehydratase block; printed column heads enzyme | kcat (min^-1) | KCRT (uM) | kcat/KCRT (uM^-1 min^-1)


organism: Streptomyces coelicolor


enzyme_display_name: tryptophan transaminase

substrate_name: L-tryptophan

enzyme: tryptophan transaminase

substrate: L-tryptophan


organism: Zea mays

sequence_source: UniProtKB:B4FJJ9; NCBI Protein:NP_001136624.1; PMID:24599492 gene anchor GRMZM5G840928

assay_conditions_summary: pH 8; 295.15 K; cofactor ATP


organism: Mycobacterium tuberculosis


assay_conditions_summary: cofactor FMN


smiles: O=O


proof_lines:
flavin: FMNH2, pH 7.4, 25°C
flavin: FADH2, pH 7.4, 25°C


substrate_name: L-Tryptophan

substrate: L-Tryptophan


substrate_name: L-Tryptophan; 2-Oxoglutarate

substrate: L-Tryptophan; 2-Oxoglutarate


organism: Thermococcus litoralis

substrate_name: 2-Oxoglutarate; L-Tryptophan

substrate: 2-Oxoglutarate; L-Tryptophan


enzyme_display_name: 1-carboxybiuret hydrolase

organism: Pseudomonas sp.

substrate_name: 1-Carboxybiuret; H2O

enzyme: 1-carboxybiuret hydrolase

substrate: 1-Carboxybiuret; H2O


organism: Pseudomonas sp. ADP

assay_conditions_summary: pH 9; 295.15 K; cofactor ADP

proof_lines: pH 9, 22°C, recombinant enzyme expressed in Escherichia coli

proof_lines: pH 9.0, temperature not specified in the publication

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


smiles: N=C(O)CC(O)=NC(=O)O


enzyme_display_name: hydroquinone glucosyltransferase

organism: Rauvolfia serpentina

substrate_name: Vanillin

enzyme: hydroquinone glucosyltransferase

substrate: Vanillin


ki_unit: mM

sequence_source: UniProtKB reviewed canonical sequence Q9AR73 (HQGT_RAUSE), retrieved by direct EC 2.4.1.218 + Rauvolfia serpentina lookup


enzyme_display_name: 7-methylguanosine nucleotidase

substrate_name: m(7)GMP (at 37 degrees Celsius)

enzyme: 7-methylguanosine nucleotidase

substrate: m(7)GMP (at 37 degrees Celsius)


substrate_name: AMP

substrate: AMP


substrate_name: (S)-NADHX

substrate: (S)-NADHX


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

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


organism: Pseudomonas sp. (strain ADP)

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 15.5 sec(-1) with 1-carboxybiuret as substrate. kcat is 9.4 sec(-1) with 1-nitrobiuret as substrate. kcat is 7 sec(-1) with 1-carboxymalonamide as substrate. kcat is 19 sec(-1) with succinamate as substrate.


sequence_source: UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15

proof_lines: pH 7.5, 50°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15 and applied mutation signature A204V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15 and applied mutation signature E368D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15 and applied mutation signature E368A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15 and applied mutation signature L86I to reconstruct the assayed variant sequence.


substrate_name: hydroquinone

substrate: hydroquinone


organism: Drosophila melanogaster

substrate_name: 7-Methylguanosine 5'-phosphate

sequence_source: UniProtKB reviewed accession Q9W197; direct UniProt REST accession lookup on 2026-06-15

column_label: Table 2 (Steady-state kinetic parameters for CG3362), substrate row 'm7GMP'; column 'Km' unit uM = 13; column 'Vmax' unit umol/min/mg = 11; column 'kcat' unit 1/s = 6.3; column 'kcat/Km' = 0.46; the Ki cell of this row is empty.

normalized_value_unit_evidence: kcat: printed cell 6.3 1/s; the printed unit is already per second, so no unit conversion applies; 6.3 s^(-1). Km: printed cell 13 uM; 1 uM is 0.001 mM, so 13 / 1000 = 0.013 mM. kcat/Km: printed cell 0.46 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.46 x 1000 = 460.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row m7GMP: Km cell 13 uM; Vmax cell 11 umol/min/mg; kcat cell 6.3 1/s; kcat/Km cell 0.46 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 2, substrate row m7GMP

table_label: Table 2: Steady-state kinetic parameters for CG3362 (J. Biol. Chem. 2013, 288(4):2441-2451)

substrate: 7-Methylguanosine 5'-phosphate


substrate_name: UMP

column_label: Table 2 (Steady-state kinetic parameters for CG3362), substrate row 'UMP'; column 'Km' unit uM = 91; column 'Vmax' unit umol/min/mg = 4.0; column 'kcat' unit 1/s = 2.3; column 'kcat/Km' = 0.03; the Ki cell of this row is empty.

normalized_value_unit_evidence: kcat: printed cell 2.3 1/s; the printed unit is already per second, so no unit conversion applies; 2.3 s^(-1). Km: printed cell 91 uM; 1 uM is 0.001 mM, so 91 / 1000 = 0.091 mM. kcat/Km: printed cell 0.03 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.03 x 1000 = 30.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row UMP: Km cell 91 uM; Vmax cell 4.0 umol/min/mg; kcat cell 2.3 1/s; kcat/Km cell 0.03 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 2, substrate row UMP

substrate: UMP


substrate_name: CMP

column_label: Table 2 (Steady-state kinetic parameters for CG3362), substrate row 'CMP'; column 'Km' unit uM = 48; column 'Vmax' unit umol/min/mg = 21; column 'kcat' unit 1/s = 12.0; column 'kcat/Km' = 0.25; the Ki cell of this row is empty.

normalized_value_unit_evidence: kcat: printed cell 12.0 1/s; the printed unit is already per second, so no unit conversion applies; 12.0 s^(-1). Km: printed cell 48 uM; 1 uM is 0.001 mM, so 48 / 1000 = 0.048 mM. kcat/Km: printed cell 0.25 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.25 x 1000 = 250.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row CMP: Km cell 48 uM; Vmax cell 21 umol/min/mg; kcat cell 12.0 1/s; kcat/Km cell 0.25 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 2, substrate row CMP

substrate: CMP


substrate_name: 7-Methylguanosine 5'-phosphate; H2O

normalized_value_unit_evidence: kcat: printed cell 6.3 1/s; the printed unit is already per second, so no unit conversion applies; 6.3 s^(-1). Km: printed cell 13 uM; 1 uM is 0.001 mM, so 13 / 1000 = 0.013 mM. Vmax: printed cell 11 umol/min/mg; 1 umol/min/mg is 0.000001 mol per 60 s per 0.001 g, so 11 / 60 / 1000 = 0.0001833333333333333 mol s^(-1) g^(-1). kcat/Km: printed cell 0.46 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.46 x 1000 = 460.0 s^(-1)*mM^(-1).

substrate: 7-Methylguanosine 5'-phosphate; H2O


sequence_source: UniProtKB reviewed accession Q9H0P0; direct UniProt REST accession lookup on 2026-06-15

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


sequence_source: UniProtKB reviewed accession Q969T7; direct UniProt REST accession lookup on 2026-06-15

column_label: Table 3 (Steady-state kinetic parameters for human cNIII-like), substrate row 'CMP'; column 'Km' unit uM = 79; column 'Vmax' unit umol/min/mg = 12.0; column 'kcat' unit 1/s = 7; column 'kcat/Km' = 0.09; Table 3 prints no Ki column.

normalized_value_unit_evidence: kcat: printed cell 7 1/s; the printed unit is already per second, so no unit conversion applies; 7.0 s^(-1). Km: printed cell 79 uM; 1 uM is 0.001 mM, so 79 / 1000 = 0.079 mM. kcat/Km: printed cell 0.09 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.09 x 1000 = 90.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row CMP: Km cell 79 uM; Vmax cell 12.0 umol/min/mg; kcat cell 7 1/s; kcat/Km cell 0.09 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 3, substrate row CMP

table_label: Table 3: Steady-state kinetic parameters for human cNIII-like (J. Biol. Chem. 2013, 288(4):2441-2451)


column_label: Table 3 (Steady-state kinetic parameters for human cNIII-like), substrate row 'UMP'; column 'Km' unit uM = 439; column 'Vmax' unit umol/min/mg = 10.7; column 'kcat' unit 1/s = 6.2; column 'kcat/Km' = 0.01; Table 3 prints no Ki column.

normalized_value_unit_evidence: kcat: printed cell 6.2 1/s; the printed unit is already per second, so no unit conversion applies; 6.2 s^(-1). Km: printed cell 439 uM; 1 uM is 0.001 mM, so 439 / 1000 = 0.439 mM. kcat/Km: printed cell 0.01 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.01 x 1000 = 10.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row UMP: Km cell 439 uM; Vmax cell 10.7 umol/min/mg; kcat cell 6.2 1/s; kcat/Km cell 0.01 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 3, substrate row UMP


substrate_name: H2O; 7-Methylguanosine 5'-phosphate

column_label: Table 3 (Steady-state kinetic parameters for human cNIII-like), substrate row 'm7GMP'; column 'Km' unit uM = 7.8; column 'Vmax' unit umol/min/mg = 0.41; column 'kcat' unit 1/s = 0.24; column 'kcat/Km' = 0.03; Table 3 prints no Ki column.

normalized_value_unit_evidence: kcat: printed cell 0.24 1/s; the printed unit is already per second, so no unit conversion applies; 0.24 s^(-1). Km: printed cell 7.8 uM; 1 uM is 0.001 mM, so 7.8 / 1000 = 0.0078 mM. Vmax: printed cell 0.41 umol/min/mg; 1 umol/min/mg is 0.000001 mol per 60 s per 0.001 g, so 0.41 / 60 / 1000 = 0.000006833333333333333 mol s^(-1) g^(-1). kcat/Km: printed cell 0.03 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.03 x 1000 = 30.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row m7GMP: Km cell 7.8 uM; Vmax cell 0.41 umol/min/mg; kcat cell 0.24 1/s; kcat/Km cell 0.03 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 3, substrate row m7GMP

substrate: H2O; 7-Methylguanosine 5'-phosphate


sequence_source: UniProtKB reviewed Q936X3

smiles: N=C(O)N=C(O)NC(=O)O


sequence_source: UniProtKB reviewed Q94AF2

assay_conditions_summary: pH 8; 295.15 K; cofactor NADH

row_label: Arabidopsis / NADHX

table_label: Table I


assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH


row_label: Arabidopsis / NADPHX


sequence_source: UniProtKB reviewed Q8IW45 with PubMed 30576410 natural variant VAR_082224

sequence_variant_note: Mutation signature G63S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: ATP-dependent NAD(P)H-hydrate dehydratase(Enzyme) mutant G63S N-terminal His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8IW45 with PubMed 30576410 natural variant VAR_082225 and applied mutation signature R308C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ATP-dependent NAD(P)H-hydrate dehydratase(Enzyme) mutant R308C N-terminal His-tagged


sequence_source: UniProtKB reviewed Q8IW45


sequence_source: UniProtKB reviewed Q9CZ42 canonical sequence 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: SABIO-RK modifier species: ATP-dependent NAD(P)H-hydrate dehydratase(Enzyme) mutant Carkd (lacking mitochondrail propeptide), N-terminal His-tag


sequence_source: UniProtKB inactive/deleted accession A0A3L6F337


substrate_name: m(7)GMP (at 25 degrees Celsius)

proof_lines: kcat is 6.3 sec(-1) with m(7)GMP. kcat is 12 sec(-1) with CMP. kcat is 0.88 sec(-1) with GMP. kcat is 0.28 sec(-1) with AMP. kcat is 2.3 sec(-1) with UMP.

substrate: m(7)GMP (at 25 degrees Celsius)


proof_lines: kcat is 0.24 sec(-1) with m(7)GMP. kcat is 7 sec(-1) with CMP. kcat is 0.07 sec(-1) with GMP. kcat is 0.04 sec(-1) with AMP. kcat is 6.2 sec(-1) with UMP.


organism: Streptomyces viridochromogenes


sequence_source: UniProt REST direct accession lookup, Q5IW40, 2026-06-15


enzyme_display_name: valine N-monooxygenase

organism: Lotus japonicus

substrate_name: L-Valine

enzyme: valine N-monooxygenase

substrate: L-Valine


organism: Manihot esculenta

substrate_name: L-Isoleucine

substrate: L-Isoleucine


sequence_source: UniProt REST direct accession lookup, Q9M7B8, 2026-06-15


organism: Escherichia coli

substrate_name: Glyceraldehyde

smiles: O=CC(O)CO

substrate: Glyceraldehyde


substrate_name: isoleucine

proof_lines: kcat is 120 min(-1) with isoleucine as substrate (PubMed:15122013). kcat is 44 min(-1) with valine as substrate (PubMed:15122013).

substrate: isoleucine


proof_lines: kcat is 220 min(-1) with isoleucine as substrate (PubMed:15122013). kcat is 50 min(-1) with valine as substrate (PubMed:15122013).


substrate_name: valine

proof_lines: kcat is 2.3 min(-1) with isoleucine as substrate (PubMed:10636899). kcat is 4.3 min(-1) with valine as substrate (PubMed:10636899).

substrate: valine


organism: Escherichia coli (strain K12)

substrate_name: dihydroxyacetone

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

proof_lines: kcat is 2.8 sec(-1). Values measured with the DhaKLM complex.

substrate: dihydroxyacetone


proof_lines: kcat is 2.8 sec(-1) with dihydroxyacetone as substrate. Values measured with the DhaKLM complex (PubMed:11350937). kcat is 290 min(-1) with dihydroxyacetone as substrate. kcat is 12.5 min(-1) with D,L-glyceraldehyde as substrate (PubMed:154


organism: Arabidopsis thaliana

proof_lines: kcat is 140 min(-1) with indole-3-acetaldoxime as substrate. kcat is 26 min(-1) with p-hydroxyphenylacetaldoxime as substrate. kcat is 25 min(-1) with phenylacetaldoxime as substrate.


enzyme_display_name: gluconate dehydratase

organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)

substrate_name: D-xylonate

proof_lines: kcat is 1406 min(-1) with D-xylonate as substrate. kcat is 2626 min(-1) with D-gluconate as substrate. kcat is 46 min(-1) with L-arabinonate as substrate. kcat is 218 min(-1) with D-galactonate as substrate. kcat is 196 min(-1) with D-fucon

enzyme: gluconate dehydratase

substrate: D-xylonate


organism: Chromohalobacter israelensis (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)

substrate_name: Unknown

proof_lines: kcat is 0.02 sec(-1) with D-mannonate. kcat is 0.04 sec(-1) with D-gluconate.

substrate: Unknown


organism: Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)

proof_lines: kcat is 0.03 sec(-1) with D-mannonate. kcat is 0.05 sec(-1) with D-gluconate.


organism: Musicola paradisiaca (strain Ech703)

proof_lines: kcat is 0.04 sec(-1) with D-mannonate. kcat is 0.03 sec(-1) with D-gluconate.


organism: Pantoea ananatis (strain LMG 20103)


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

proof_lines: kcat is 10.4 sec(-1) for gluconate and 1.08 sec(-1) for galactonate (at 70 degrees Celsius and pH 6). kcat is 12.6 sec(-1) for gluconate (at 78 degrees Celsius and pH 7).


organism: Salmonella enteritidis PT4 (strain P125109)


organism: Salmonella virchow (strain SL491)


organism: Streptomyces bingchenggensis (strain BCW-1)


enzyme_display_name: L-fuconate dehydratase

organism: Homo sapiens

substrate_name: L-fuconate

proof_lines: kcat is 0.5 sec(-1) for L-fuconate. kcat is 0.3 sec(-1) for L-galactonate. kcat is 0.3 sec(-1) for L-arabinonate. kcat is 0.04 sec(-1) for D-arabinonate. kcat is 0.002 sec(-1) for D-ribonate.

enzyme: L-fuconate dehydratase

substrate: L-fuconate


enzyme_display_name: pseudouridylate synthase

substrate_name: pseudouridine 5'-phosphate

proof_lines: kcat is 1.41 sec(-1) with pseudouridine 5'-phosphate as substrate.

enzyme: pseudouridylate synthase

substrate: pseudouridine 5'-phosphate


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

substrate_name: galactonate (at 60 degrees Celsius and pH 6.2)

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


organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)


organism: Mus musculus

substrate_name: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one (using iron as cofactor)

sequence_source: source_record; direct UniProt Q99JT9 check matched the selected canonical sequence

smiles: CSCCC(=O)/C(=C/O)/O

proof_lines: kcat is 114.3 sec(-1) with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using iron as cofactor) (PubMed:26858196). kcat is 7.55 sec(-1) with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using cobalt as cofa


substrate_name: pseudouridine 5'-phosphate (in the presence of 0.5 mM Mn(2+))

sequence_source: source_record; direct UniProt P33025 check matched the selected canonical sequence

proof_lines: kcat is 3.74 sec(-1) for the synthesis of PsiMP.


organism: Klebsiella oxytoca

substrate_name: 1,2-Dihydroxyhex-1-en-3-one; O2

substrate: 1,2-Dihydroxyhex-1-en-3-one; O2


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


proof_lines:
Fe2+ bound enzyme, pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7


organism: Oryza sativa

substrate_name: 1,2-Dihydroxy-3-ketopent-1-ene; O2

substrate: 1,2-Dihydroxy-3-ketopent-1-ene; O2


enzyme_display_name: psoralen synthase

organism: Ammi majus

substrate_name: O2; Marmesin; NADPH; H+

proof_lines: SABIO-RK modifier species: psoralen synthas(Enzyme) mutant M120V, N-terminal 37 residues replaced by corresponding 33-residue membrane anchor region of CYP73A1

enzyme: psoralen synthase

substrate: O2; Marmesin; NADPH; H+


substrate_name: Marmesin; NADPH; O2; H+

assay_conditions_summary: pH 7; 300.15 K; cofactor NADPH

proof_lines: pH 7.0, 27°C, recombinant enzyme in microsomes

substrate: Marmesin; NADPH; O2; H+


organism: Apium graveolens

substrate_name: Marmesin; H+; NADPH; O2

substrate: Marmesin; H+; NADPH; O2


organism: Pastinaca sativa

substrate_name: O2; NADPH; Marmesin; H+

substrate: O2; NADPH; Marmesin; H+


organism: Arabidopsis thaliana

substrate_name: 3-Indoleacetaldoxime; O2; H+; NADPH; L-Cysteine

assay_conditions_summary: pH 8.1; 302.15 K; cofactor NADPH

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


organism: Oryza sativa subsp. indica

substrate_name: 1,2-dihydroxy-3-ketopent-1-ene (DHKP) (using iron as cofactor)


organism: Dictyostelium discoideum

substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: cis-zeatin O-beta-D-glucosyltransferase

organism: Zea mays

substrate_name: cis-zeatin

enzyme: cis-zeatin O-beta-D-glucosyltransferase

substrate: cis-zeatin


enzyme_display_name: phosphonopyruvate hydrolase

organism: Variovorax sp. (strain Pal2)

substrate_name: phosphonopyruvate (at 37 degrees Celsius, pH 7.0, with 5 umol CoCl(2))

enzyme: phosphonopyruvate hydrolase


enzyme_display_name: ADP-ribose 1''-phosphate phosphatase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ADP-ribose 1''-phosphate

enzyme: ADP-ribose 1''-phosphate phosphatase

substrate: ADP-ribose 1''-phosphate


organism: Sulfolobus solfataricus

substrate_name: D-Gluconate

sequence_source: UniProt REST accession lookup Q97U27

substrate: D-Gluconate


organism: Aspergillus niger

substrate_name: L-fuconate

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

proof_lines: recombinant enzyme, pH 7.0, temperature not specified in the publication


organism: Xanthomonas campestris

substrate_name: D-Arabinonate

sequence_source: UniProt REST accession lookup Q8P3K2

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

substrate: D-Arabinonate


substrate_name: L-Fuconate

substrate: L-Fuconate


substrate_name: L-Galactonate

substrate: L-Galactonate


organism: Escherichia coli

substrate_name: H2O; Pseudouridine 5'-phosphate

sequence_source: UniProt REST accession lookup P33025

proof_lines:
pH 7.1, 30°C
Raw SKiD Env: Temp=30°C, pH=7.1

substrate: H2O; Pseudouridine 5'-phosphate


substrate_name: Uracil; D-Ribose 5-phosphate

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt P33025 canonical sequence and applied mutation signature E31A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pseudouridylate synthase(Enzyme) mutant E31A

substrate: Uracil; D-Ribose 5-phosphate


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt P33025 canonical sequence and applied mutation signature K166A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pseudouridylate synthase(Enzyme) mutant K166A


substrate_name: D-Ribose 5-phosphate; Uracil

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt P33025 canonical sequence and applied mutation signature N289A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pseudouridylate synthase(Enzyme) mutant N289A

substrate: D-Ribose 5-phosphate; Uracil


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt P33025 canonical sequence and applied mutation signature K93A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pseudouridylate synthase(Enzyme) mutant K93A


substrate_name: (E)-phenylacetaldoxime

sequence_source: UniProtKB:P48421 direct accession lookup

substrate: (E)-phenylacetaldoxime


enzyme_display_name: glutathione amide reductase

organism: Chromatium gracile

substrate_name: Glutathione amide disulfide

sequence_source: UniProtKB:D0VWY5 direct accession lookup

enzyme: glutathione amide reductase

substrate: Glutathione amide disulfide


substrate_name: NADH; Glutathione amide disulfide; H+

assay_conditions_summary: cofactor NADH

substrate: NADH; Glutathione amide disulfide; H+


substrate_name: NADH

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: Oxidized glutathione

substrate: Oxidized glutathione


organism: Thermus thermophilus

substrate_name: S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GBB2 direct accession lookup plus Y194A reconstruction and applied mutation signature Y194A to reconstruct the assayed variant sequence.

substrate: S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GBB2 direct accession lookup plus D170A reconstruction and applied mutation signature D170A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GBB2 direct accession lookup plus Y78A reconstruction and applied mutation signature Y78A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q8GBB2 direct accession lookup


organism: Oryza sativa Japonica Group

substrate_name: cis-zeatin


sequence_source: UniProtKB accession Q7XU02


sequence_source: UniProtKB accession Q7XU03


substrate_name: UDP-D-glucose; cis-Zeatin

sequence_source: UniProtKB accession Q8RXA5

substrate: UDP-D-glucose; cis-Zeatin


sequence_source: UniProtKB accession Q93XP7


substrate_name: Unknown

sequence_source: UniProtKB accession Q9S7N2

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Malassezia furfur

substrate_name: L-tryptophan

sequence_source: UniProtKB accession S4UF58

substrate: L-tryptophan


organism: Variovorax sp.

sequence_source: UniProtKB accession Q84G06

proof_lines:
37°C
25°C, pH 7.5
Raw SKiD Env: Temp=25°C, pH=7.5


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB accession Q84G06 by applying R188A and applied mutation signature R188A to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae

substrate_name: ADP-ribose 1''-phosphate

sequence_source: UniProtKB accession P38218

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

substrate: ADP-ribose 1''-phosphate


proof_lines: Ki above 10 mM, in 20 mM Tris-HCl, pH 7.5, 5 mM MgCl2, 2.5 mM spermidine, 100 mM dithiothreitol, 0.4% (v/v) Triton X-100, at 30°C


organism: Haloferax volcanii

substrate_name: D-gluconate

sequence_source: UniProtKB accession D4GYD4

substrate: D-gluconate


organism: Picrophilus oshimae

substrate_name: D-galactonate

substrate: D-galactonate


substrate_name: D-Gluconate

sequence_source: UniProtKB accession Q97U27

substrate: D-Gluconate


organism: Oryza sativa


organism: Petroselinum crispum

assay_conditions_summary: pH 7; 293.15 K; cofactor NADPH


organism: Zea mays

substrate: cis-zeatin


organism: Bacteria


organism: Clostridium sporogenes

proof_lines: cosubstrate phenylalanine , pH 8.4, 22°C approximately

proof_lines: cosubstrate tryptophan, pH 8.4, 22°C approximately


organism: Sus scrofa

proof_lines:
pH 8.0, 37°C
cosubstrate phenylalanine, pH 8.0, 37°C


organism: Burkholderia cepacia


substrate_name: 3-Phosphonopyruvate; H2O

substrate: 3-Phosphonopyruvate; H2O


organism: Severe acute respiratory syndrome-related coronavirus

assay_conditions_summary: pH 7.5; cofactor ADP

proof_lines: in 50 mM Tris (pH 7.5), 1 mM MgCl2, 0.1 mM sodium azide, temperature not specified in the publication


organism: Alcaligenes sp.


organism: Clostridium pasteurianum


organism: Penicillium citrinum


organism: Saccharolobus solfataricus

sequence_source: UniProtKB reviewed accession Q97U27, FASTA direct check


organism: Sulfolobus solfataricus


organism: Thermoplasma acidophilum


organism: Aureobasidium pullulans

substrate_name: L-fuconate

substrate: L-fuconate


substrate_name: L-arabonate

substrate: L-arabonate


organism: Xanthomonas campestris


organism: Agrobacterium tumefaciens

substrate_name: Uracil

substrate: Uracil


organism: Saccharomyces cerevisiae

substrate_name: tRNAVal

proof_lines: substrate from yeast, in absence of Mg2+

proof_lines: substrate from yeast, intronless, limiting

substrate: tRNAVal


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Tetrahymena pyriformis

substrate_name: ribose 5-phosphate

substrate: ribose 5-phosphate


organism: Escherichia coli (strain K12)

substrate_name: succinyl-CoA (at pH 7.4)

assay_conditions_summary: pH 7.4; cofactor CoA

substrate: succinyl-CoA (at pH 7.4)


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: ppGpp (at 30 degrees Celsius and pH 8)

assay_conditions_summary: pH 8

substrate: ppGpp (at 30 degrees Celsius and pH 8)


organism: Streptococcus dysgalactiae subsp. equisimilis

substrate_name: GTP

assay_conditions_summary: cofactor ATP

substrate: GTP


organism: Escherichia coli

sequence_source: UniProt REST direct lookup P0A9D8

assay_conditions_summary: cofactor CoA


organism: Pseudomonas amygdali pv. tabaci

substrate_name: succinyl-CoA

sequence_source: UniProt REST direct lookup P31852

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: succinyl-CoA


substrate_name: DhaK; Dihydroxyacetone

sequence_source: UniProt REST direct lookup P76015

substrate: DhaK; Dihydroxyacetone


substrate_name: Phosphoenolpyruvate; Dihydroxyacetone

substrate: Phosphoenolpyruvate; Dihydroxyacetone


substrate_name: Dihydroxyacetone; Phosphoenolpyruvate

substrate: Dihydroxyacetone; Phosphoenolpyruvate


substrate_name: Glycerone

sequence_source: UniProt REST direct lookup P76014

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

substrate: Glycerone


organism: Mycobacterium tuberculosis

substrate_name: Guanosine 3',5'-bis(diphosphate)

sequence_source: UniProt REST direct lookup P9WHG9

substrate: Guanosine 3',5'-bis(diphosphate)


enzyme_display_name: yapsin 1

substrate_name: amidorphin

sequence_source: UniProt REST direct lookup P32329

enzyme: yapsin 1

substrate: amidorphin


substrate_name: Adrenocorticotropic hormone 1-39; H2O

substrate: Adrenocorticotropic hormone 1-39; H2O


substrate_name: Dynorphin B (1-13)

substrate: Dynorphin B (1-13)


substrate_name: Dynorphin A (1-11)

substrate: Dynorphin A (1-11)


proof_lines:
vs. L-2-aminopimelate
vs. tetrahydropicolinate


organism: Pseudomonas aeruginosa


substrate_name: dihydroxyacetone

substrate: dihydroxyacetone


substrate_name: Proinsulin

substrate: Proinsulin


enzyme_display_name: Anthranilate O-methyltransferase 1

organism: Zea mays

substrate_name: anthranilate

sequence_source: UniProtKB reviewed accession D9J0Z7; matching NCBI protein ADI87449.1 translated from GenBank HM242244.1

proof_lines: 25°C, pH not specified in the publication, isoenzyme AAMT1

enzyme: Anthranilate O-methyltransferase 1

substrate: anthranilate


enzyme_display_name: cyanamide hydratase

organism: Albifimbria verrucaria

substrate_name: cyanamide

sequence_source: UniProtKB P22143 / CYAH_ALBVE exact EC+organism lookup; UniProt release 2026_02 reported X-Total-Results: 1 for organism_name:"Albifimbria verrucaria" AND ec:4.2.1.69.

smiles: C(#N)N

enzyme: cyanamide hydratase

substrate: cyanamide


enzyme_display_name: anthranilate O-methyltransferase

substrate_name: S-adenosyl-L-methionine

enzyme: anthranilate O-methyltransferase

substrate: S-adenosyl-L-methionine


organism: Homo sapiens


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: (S)-ureidoglycine aminohydrolase

organism: Arabidopsis thaliana

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProt direct lookup Q8GXV5

enzyme: (S)-ureidoglycine aminohydrolase

source: skid


organism: Myrothecium verrucaria

substrate_name: Cyanamide

sequence_source: UniProt direct lookup P22143

smiles: N=C=N

substrate: Cyanamide


substrate_name: H2O; Cyanamide

substrate: H2O; Cyanamide


organism: Saccharomyces cerevisiae

sequence_source: UniProt direct lookup P0CH63


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P0CH63 canonical sequence and H137N mutation signature and applied mutation signature H137N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P0CH63 canonical sequence and T157V mutation signature and applied mutation signature T157V to reconstruct the assayed variant sequence.


enzyme_display_name: L-arginine hydroxylase

organism: Streptomyces vinaceus

substrate_name: L-arginine

sequence_source: UniProtKB Q6WZB0 direct REST lookup; sequence matched

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

enzyme: L-arginine hydroxylase

substrate: L-arginine


substrate_name: L-homoarginine

substrate: L-homoarginine


substrate_name: L-Arginine

substrate: L-Arginine


substrate_name: L-canavanine

substrate: L-canavanine


substrate_name: Anthranilate; S-Adenosyl-L-methionine

sequence_source: UniProtKB D9J0Z7 direct REST lookup; sequence matched

substrate: Anthranilate; S-Adenosyl-L-methionine


substrate_name: Anthranilate

substrate: Anthranilate


substrate_name: S-Adenosyl-L-methionine; Anthranilate

sequence_source: UniProtKB B6SU46 direct REST lookup; sequence matched

proof_lines: 25°C, pH not specified in the publication, isoenzyme AAMT2

substrate: S-Adenosyl-L-methionine; Anthranilate


sequence_source: UniProtKB D9J100 direct REST lookup; sequence matched

proof_lines: 25°C, pH not specified in the publication, isoenzyme AAMT3


substrate_name: benzoate

substrate: benzoate


sequence_source: UniProtKB Q8GXV5 direct REST lookup; sequence matched


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8GXV5 direct REST lookup; sequence matched and applied mutation signature K291R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8GXV5 direct REST lookup; sequence matched and applied mutation signature Y252F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P46959, sequenceVersion 1, direct REST FASTA/JSON lookup

proof_lines: pH 8.0, 30°C, purified FlagGcd10pyGcd14p complex


organism: Thermus thermophilus

substrate_name: S-Adenosyl-L-methionine; tRNA

sequence_source: UniProtKB reviewed accession Q8GBB2, sequenceVersion 2, direct REST FASTA/JSON lookup

substrate: S-Adenosyl-L-methionine; tRNA


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GBB2 canonical sequence with D170A reconstructed after direct residue check and applied mutation signature D170A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (adenine58-N1)-methyltransferase(Enzyme) mutant D170A N-terminal His6-tag


substrate_name: tRNA; S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GBB2 canonical sequence with Y78A reconstructed after direct residue check and applied mutation signature Y78A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (adenine58-N1)-methyltransferase(Enzyme) mutant Y78A N-terminal His6-tag

substrate: tRNA; S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GBB2 canonical sequence with Y194A reconstructed after direct residue check and applied mutation signature Y194A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (adenine58-N1)-methyltransferase(Enzyme) mutant Y194A N-terminal His6-tag


substrate_name: adenine58 in tRNAPhe

proof_lines: pH 7.5-8.0, 55°C, wild-type Thermus thermophilus tRNAPhe as substrate

substrate: adenine58 in tRNAPhe


substrate_name: L-canavanine (at pH 8 and 30 degrees Celsius)

proof_lines: kcat is 2611 min(-1), 831 min(-1) and 73.2 min(-1) for L-arginine, L-homoarginine and L-canavanine, respectively (at pH 8 and 30 degrees Celsius).


substrate_name: anthranilic acid

proof_lines: kcat is 0.37 sec(-1) with anthranilic acid as substrate.

substrate: anthranilic acid


proof_lines: kcat is 0.45 sec(-1) with anthranilic acid as substrate. kcat is 0.04 sec(-1) with benzoic acid as substrate.


proof_lines: kcat is 761 sec(-1) for (S)-2-ureidoglycine.


enzyme_display_name: carotenoid-9',10'-cleaving dioxygenase

organism: Mustela putorius furo

substrate_name: all-trans-beta-carotene

enzyme: carotenoid-9',10'-cleaving dioxygenase

substrate: all-trans-beta-carotene


organism: Streptomyces galilaeus

substrate_name: rhodosaminyl aklavinone (with TDP-L-daunosamine as sugar donor)

proof_lines: kcat is 2.1 sec(-1) for transferase activity with rhodosaminyl aklavinone as sugar acceptor and TDP-L-daunosamine as sugar donor. kcat is 5.4 sec(-1) for transferase activity with idarubicin as sugar acceptor and TDP-L-2-deoxyfucose as suga


enzyme_display_name: acylpyruvate hydrolase

substrate_name: enol-oxaloacetate

proof_lines: kcat is 31.1 sec(-1) with enol-oxaloacetate as substrate.

enzyme: acylpyruvate hydrolase

substrate: enol-oxaloacetate


organism: Mus musculus

substrate_name: oxaloacetate

proof_lines: kcat is 210 nmol/min/mg for the decarboxylation of oxaloacetate. kcat is 140 nmol/min/mg for the hydrolysis of acetylpyruvate.

substrate: oxaloacetate


enzyme_display_name: ethylmalonyl-CoA decarboxylase

substrate_name: (S)-ethylmalonyl-CoA (in absence of ATP)

proof_lines: kcat is 10 sec(-1) with (S)-ethylmalonyl-CoA as substrate (in presence of 5 mM ATP). kcat is 1.68 sec(-1) with (S)-methylmalonyl-CoA as substrate (in presence of 5 mM ATP).

enzyme: ethylmalonyl-CoA decarboxylase


substrate_name: beta-Carotene; O2

sequence_source: UniProtKB direct accession lookup: Q7XJM2

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication

substrate: beta-Carotene; O2


substrate_name: beta-carotene

sequence_source: UniProtKB direct accession lookup: Q9BYV7

substrate: beta-carotene


substrate_name: dTDP-beta-L-daunosamine

sequence_source: UniProtKB direct accession lookup: Q9L555

substrate: dTDP-beta-L-daunosamine


substrate_name: H2O; Guanosine 3'-diphosphate 5'-triphosphate

sequence_source: UniProtKB direct accession lookup: P9WHG9


substrate_name: ppGpp

sequence_source: UniProtKB direct accession lookup: Q9I686

proof_lines: presence of Mn2+, 37°C, pH not specified in the publication

substrate: ppGpp


substrate_name: Acetylpyruvate; H2O

sequence_source: UniProtKB direct accession lookup: Q6P587

proof_lines:
at pH 7.4 and 25°C
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=25°C, pH=7.4

substrate: Acetylpyruvate; H2O


substrate_name: (S)-Ethylmalonyl-CoA

sequence_source: UniProtKB direct accession lookup: Q9D9V3

assay_conditions_summary: pH 7.1; 303.15 K; cofactor CoA

substrate: (S)-Ethylmalonyl-CoA


substrate_name: lutein

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

substrate: lutein


substrate_name: rhodosaminyl aklavinone

sequence_source: UniProtKB reviewed accession Q9L555 (AKNK_STRGJ), queried by EC 2.4.1.327 and Streptomyces galilaeus

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

proof_lines: with TDP-L-2-deoxyfucose as cosubstrate, in 75 mM Tris (pH 7.5), 12 mM MgCl2, at 25°C

proof_lines: with TDP-L-daunosamine as cosubstrate, in 75 mM Tris (pH 7.5), 12 mM MgCl2, at 25°C

substrate: rhodosaminyl aklavinone


organism: Drosophila melanogaster

sequence_source: UniProtKB reviewed accession Q9VAM9 (MESH1_DROME), queried by EC 3.1.7.2 and Drosophila melanogaster

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


proof_lines: pH 8.0, 30°C, kcat is reduced 2fold in the presence of the complex containing tRNA, ribosomes, and mRNA

proof_lines: pH 8.0, 30°C, KM is increased 3fold in the presence of the complex containing tRNA, ribosomes, and mRNA


substrate_name: (S)-ethylmalonyl-CoA

sequence_source: UniProtKB reviewed accession Q9D9V3 (ECHD1_MOUSE), queried by EC 4.1.1.94 and Mus musculus

assay_conditions_summary: pH 7.1; 303.15 K; cofactor ATP

proof_lines: pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-

proof_lines: pH 7.1, 30°C, recombinant enzyme in absence of ATP-Mg2-

substrate: (S)-ethylmalonyl-CoA


enzyme_display_name: tyrosine N-monooxygenase

organism: Sorghum bicolor

substrate_name: L-tyrosine (in the presence of 15 mM NaCl)

proof_lines: kcat is 198 min(-1) in the presence of 15 mM NaCl. kcat is 228 min(-1) in the absence of added salt.

enzyme: tyrosine N-monooxygenase


substrate_name: L-tyrosine

sequence_source: UniProtKB reviewed accession Q43135 (C79A1_SORBI)

assay_conditions_summary: pH 7.9; 303.15 K; cofactor NADPH

proof_lines: in reconstitution experiments using Sorghum bicolor

proof_lines: purified recombinant enzyme, in 50 mM Tricine, pH 7.9, a 30°C

substrate: L-tyrosine


substrate_name: L-Tyrosine

sequence_source: UniProtKB reviewed accession Q43135 direct REST lookup

substrate: L-Tyrosine


substrate_name: NADPH; H+; L-Tyrosine; O2

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADP+

proof_lines:
pH 7.9, 25°C
presence of 0.15 mM NaCl, pH 7.9, 25°C
pH 7.9, 30°C

substrate: NADPH; H+; L-Tyrosine; O2


enzyme_display_name: geranyl diphosphate diphosphatase

organism: Ocimum basilicum

substrate_name: geranyl diphosphate

smiles: CC(=CCC/C(=C/COP(=O)(O)OP(=O)(O)O)/C)C

proof_lines: kcat is 0.8 sec(-1) with geranyl diphosphate as substrate.

enzyme: geranyl diphosphate diphosphatase

substrate: geranyl diphosphate


organism: Cinnamomum tenuipile


organism: Camptotheca acuminata

sequence_source: UniProtKB REST direct lookup for A0A109P1X1


organism: Catharanthus roseus


sequence_source: UniProtKB reviewed accession Q8GUE4 direct lookup and identity reuse cache source_record sequence


substrate_name: Geranyl diphosphate; H2O

sequence_source: Reconstructed from UniProtKB reviewed accession Q6USK1 and SABIO-RK modifier label starts with Met-44

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

mutation_type: truncation

proof_lines: SABIO-RK modifier species: geranyl diphosphate diphosphatase(Enzyme) mutant truncated starts with Met-44

substrate: Geranyl diphosphate; H2O


substrate_name: H2O; Geranyl diphosphate

sequence_source: Reconstructed from UniProtKB reviewed accession Q6USK1 and SABIO-RK modifier label starts with Ser-35

proof_lines: SABIO-RK modifier species: geranyl diphosphate diphosphatase(Enzyme) mutant truncated starts with Ser-35

substrate: H2O; Geranyl diphosphate


substrate_name: Geranyl diphosphate

sequence_source: UniProtKB reviewed accession Q6USK1 direct lookup and identity reuse cache source_record sequence

smiles: CC(C)=CCC/C(C)=C/COP(=O)(O)OP(=O)(O)O

substrate: Geranyl diphosphate


substrate_name: Acetylpyruvate

sequence_source: UniProtKB reviewed accession Q6P587 direct lookup plus Expasy EC 3.7.1.5 cross-reference

proof_lines: pH 7.4, 22°C, recombinant wild-type FAHD1

substrate: Acetylpyruvate


sequence_source: Canonical accession context from UniProtKB Q6P587; row-specific H30A variant sequence unresolved

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


sequence_source: Canonical accession context from UniProtKB Q6P587; row-specific E33A variant sequence unresolved


substrate_name: oxaloacetate

substrate: oxaloacetate


sequence_source: UniProtKB reviewed accession Q8R0F8 direct lookup plus Expasy EC 3.7.1.5 cross-reference


enzyme_display_name: 2-oxoglutarate decarboxylase

organism: Mycobacterium smegmatis

sequence_source: UniProtKB reviewed accession A0R2B1

enzyme: 2-oxoglutarate decarboxylase


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


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WIS5


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


enzyme_display_name: allantoate deiminase

organism: Oryza sativa subsp. japonica

substrate_name: allantoate

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

enzyme: allantoate deiminase

substrate: allantoate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


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

substrate_name: alpha-ketoglutarate

substrate: alpha-ketoglutarate


mutation_signature: Met44-truncated mutant

sequence_source: UniProtKB:Q6USK1 plus PMID:14657409 PMC full-text Met-44 truncation mapping


mutation_signature: Ser35 truncated mutant

sequence_source: UniProtKB:Q6USK1 plus PMID:14657409 PMC full-text Ser-35 truncation mapping


sequence_source: UniProtKB:Q6USK1 reviewed entry linked to PMID:14657409


organism: Agrobacterium sp.


enzyme_display_name: pseudouridine kinase

organism: Arabidopsis thaliana

substrate_name: pseudouridine

enzyme: pseudouridine kinase

substrate: pseudouridine


organism: Escherichia coli

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Glycine max

substrate_name: Allantoate

substrate: Allantoate


organism: Metabacillus fastidiosus


organism: Phaseolus vulgaris


organism: Euglena gracilis


organism: Oenococcus oeni


organism: Picosynechococcus sp. PCC 7002

proof_lines:
pH 7.0, 25°C
at pH 7.0 and 25°C


organism: Homo sapiens

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB Q15047 REST lookup 2026-06-16

substrate: S-adenosyl-L-methionine


organism: Pseudomonas putida

substrate_name: N-acetyl-D-muramate 6-phosphate

sequence_source: UniProtKB Q88M11 REST lookup 2026-06-16

proof_lines:
pH 7.6, 22°C
at pH 7.6 and 22°C

substrate: N-acetyl-D-muramate 6-phosphate


sequence_source: UniProtKB I1L153 REST lookup 2026-06-16

column_label: Table I: Kinetic constants (Plant Physiol. 163:672-681, 2013), row 'GmAAH2': column 'Km' = 102; column 'kcat (s^-1)' = 34; column 'Catalytic Efficiency (s^-1 M^-1)' = 0.33 x 10^6; column 'Specific Activity (units mg^-1)' is printed but is not one of the export schema's kinetic metrics.

normalized_value_unit_evidence: Km: printed cell 102 uM; 102 uM / 1000 = 0.10200000000000001 mM. kcat: printed cell 34 s^-1; no unit conversion needed. Catalytic Efficiency: printed cell 0.33 x 10^6 s^-1 M^-1; 0.33 x 10^6 s^-1 M^-1 / 1000 = 330.0 s^-1 mM^-1. This paper prints its own Catalytic Efficiency cell for this row; it is an independently reported primary value and it does not equal the quotient computed from the row's own kcat and Km (34.0 / 0.10200000000000001 = 333.3333333333333). The catalog carries the quotient; this record proposes the paper's own printed value (330.0) as the catalytic-efficiency correction, per the ratio policy for an independently reported primary catalytic-efficiency cell.

raw_value_unit_evidence: Table I, row 'GmAAH2' (Plant Physiol. 163:672-681, 2013): Km = 102 uM; kcat = 34 s^-1; printed Catalytic Efficiency = 0.33 x 10^6 s^-1 M^-1.


sequence_source: UniProtKB C0M0V4 REST lookup 2026-06-16

column_label: Table I: Kinetic constants (Plant Physiol. 163:672-681, 2013), row 'GmAAH1': column 'Km' = 72; column 'kcat (s^-1)' = 37; column 'Catalytic Efficiency (s^-1 M^-1)' = 0.52 x 10^6; column 'Specific Activity (units mg^-1)' is printed but is not one of the export schema's kinetic metrics.

normalized_value_unit_evidence: Km: printed cell 72 uM; 72 uM / 1000 = 0.07200000000000001 mM. kcat: printed cell 37 s^-1; no unit conversion needed. Catalytic Efficiency: printed cell 0.52 x 10^6 s^-1 M^-1; 0.52 x 10^6 s^-1 M^-1 / 1000 = 520.0 s^-1 mM^-1. This paper prints its own Catalytic Efficiency cell for this row; it is an independently reported primary value and it does not equal the quotient computed from the row's own kcat and Km (37.0 / 0.07200000000000001 = 513.8888888888888). The catalog carries the quotient; this record proposes the paper's own printed value (520.0) as the catalytic-efficiency correction, per the ratio policy for an independently reported primary catalytic-efficiency cell.

raw_value_unit_evidence: Table I, row 'GmAAH1' (Plant Physiol. 163:672-681, 2013): Km = 72 uM; kcat = 37 s^-1; printed Catalytic Efficiency = 0.52 x 10^6 s^-1 M^-1.


organism: Oryza sativa

sequence_source: UniProtKB Q655X8 REST lookup 2026-06-16

column_label: Table I: Kinetic constants (Plant Physiol. 163:672-681, 2013), row 'OsAAH': column 'Km' = 83; column 'kcat (s^-1)' = 78; column 'Catalytic Efficiency (s^-1 M^-1)' = 0.94 x 10^6; column 'Specific Activity (units mg^-1)' is printed but is not one of the export schema's kinetic metrics.

normalized_value_unit_evidence: Km: printed cell 83 uM; 83 uM / 1000 = 0.083 mM. kcat: printed cell 78 s^-1; no unit conversion needed. Catalytic Efficiency: printed cell 0.94 x 10^6 s^-1 M^-1; 0.94 x 10^6 s^-1 M^-1 / 1000 = 940.0 s^-1 mM^-1. This paper prints its own Catalytic Efficiency cell for this row; it is an independently reported primary value and it does not equal the quotient computed from the row's own kcat and Km (78.0 / 0.083 = 939.7590361445783). The catalog carries the quotient; this record proposes the paper's own printed value (940.0) as the catalytic-efficiency correction, per the ratio policy for an independently reported primary catalytic-efficiency cell.

raw_value_unit_evidence: Table I, row 'OsAAH' (Plant Physiol. 163:672-681, 2013): Km = 83 uM; kcat = 78 s^-1; printed Catalytic Efficiency = 0.94 x 10^6 s^-1 M^-1.


sequence_source: UniProtKB A6YS26 REST lookup 2026-06-16


proof_lines: kcat is 0.23 sec(-1) with pseudouridine as substrate (PubMed:31907295). kcat is 5.28 sec(-1) with pseudouridine as substrate (PubMed:33290549). kcat is 5.80 sec(-1) with ATP as substrate (PubMed:33290549).


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: N-acetylmuramate 6-phosphate (at pH 7.6 and 22 degrees Celsius)

proof_lines: kcat is 0.88 sec(-1) (at pH 7.6 and 22 degrees Celsius).


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: rubredoxin--NAD(+) reductase

organism: Clostridium acetobutylicum

substrate_name: NADH

sequence_source: UniProtKB reviewed canonical sequence Q9AL95 retrieved 2026-06-16

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

enzyme: rubredoxin--NAD(+) reductase

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: ATP; Pseudouridine

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

sequence_source: UniProtKB reviewed canonical sequence P30235 retrieved 2026-06-16

substrate: ATP; Pseudouridine


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

substrate_name: rubredoxin

assay_conditions_summary: cofactor NADPH

substrate: rubredoxin


organism: Escherichia coli (strain K12)

substrate_name: pseudouridine (in the presence of 0.5 mM ATP)


organism: Bos taurus

sequence_source: UniProtKB reviewed accession Q2TBQ8 REST/FASTA lookup on 2026-06-16


organism: Mus musculus

substrate_name: D-glucose (at pH 7.1 in the presence of NADP)


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: glucose-6-phosphate (at 25 degrees Celsius)


organism: Methanothermobacter thermautotrophicus

substrate_name: sn-glycerol 1-phosphate

substrate: sn-glycerol 1-phosphate


organism: Thermoplasma acidophilum

substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


enzyme_display_name: small monomeric GTPase

substrate_name: GTP

proof_lines: quite low, increased GTP hydrolysis by action of guanine nucleotide release proteins, promoting replacement of bound GDP by GTP

enzyme: small monomeric GTPase

substrate: GTP


enzyme_display_name: maleate hydratase

organism: Arthrobacter sp.

substrate_name: Maleate

enzyme: maleate hydratase

substrate: Maleate


organism: Ectopseudomonas oleovorans

substrate_name: citraconate

substrate: citraconate


enzyme_display_name: carbonyl sulfide hydrolase

organism: Thiobacillus thioparus

substrate_name: carbonyl sulfide

enzyme: carbonyl sulfide hydrolase

substrate: carbonyl sulfide


proof_lines: kcat is 5.4 sec(-1) with GTP as substrate.


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

substrate_name: G1P (at 55 degrees Celsius and pH 8)

substrate: G1P (at 55 degrees Celsius and pH 8)


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

substrate_name: G-1,3-P (at 55 degrees Celsius and pH 7)


organism: Homo sapiens


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


enzyme_display_name: loganate O-methyltransferase

organism: Catharanthus roseus

substrate_name: loganic acid (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 0.31 sec(-1) with loganic acid as substrate (at pH 7.5 and 30 degrees Celsius).

enzyme: loganate O-methyltransferase


substrate_name: 23S rRNA within 50S ribosomal subunits

substrate: 23S rRNA within 50S ribosomal subunits


enzyme_display_name: 3-isopropylmalate dehydratase

enzyme: 3-isopropylmalate dehydratase


substrate_name: loganic acid

substrate: loganic acid


organism: Ophiorrhiza pumila

substrate_name: loganate

proof_lines: pH and temperature not specified in the publication

substrate: loganate


organism: Acidithiobacillus thiooxidans


organism: Candida maltosa

substrate_name: beta-carboxy-beta-hydroxyisocaproate

substrate: beta-carboxy-beta-hydroxyisocaproate


organism: Neurospora crassa

substrate_name: dimethylcitraconate

substrate: dimethylcitraconate


organism: Saccharomyces cerevisiae

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


organism: Escherichia coli

substrate_name: S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0C0R7 direct REST/FASTA check on 2026-06-16 plus D83A substitution from selected source mutation_signature and applied mutation signature D83A to reconstruct the assayed variant sequence.

substrate: S-Adenosyl-L-methionine


sequence_source: UniProtKB:P0C0R7 direct REST/FASTA check on 2026-06-16


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


sequence_source: UniProtKB:Q15047 direct REST/FASTA check on 2026-06-16

proof_lines: substrate [histone H3 peptide 1-15]-N6,N6-dimethyl-L-lysine9, pH 7.6, 23°C

proof_lines: substrate [histone H3 peptide 1-15]-N6,N6-dimethyl-L-lysine9, SETDB1:ATF7IP complex, pH 7.6, 23°C


sequence_source: UniProtKB:B2KPR3 direct REST/FASTA check on 2026-06-16

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


organism: Methanothermobacter marburgensis

substrate_name: Geranylgeranyl diphosphate

sequence_source: UniProtKB:P0C882 direct REST/FASTA check on 2026-06-16

substrate: Geranylgeranyl diphosphate


substrate_name: sn-Glyceryl phosphate

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

substrate: sn-Glyceryl phosphate


sequence_source: UniProtKB:Q9HJH3 direct REST/FASTA check on 2026-06-16


sequence_source: UniProtKB:H1AAP2 direct REST/FASTA check on 2026-06-16

smiles: O=C=S


proof_lines:
at pH 8.5 and 30°C
Raw SKiD Env: Temp=30°C, pH=8.5


organism: Streptococcus pneumoniae

sequence_source: UniProtKB:P0A3C4 direct REST/FASTA check on 2026-06-16


organism: Methanocaldococcus jannaschii


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


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


organism: Acinetobacter calcoaceticus

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines: reaction with 2,6-dichloroindophenol or Fe(CN)63-

substrate: NADH


organism: Streptomyces venezuelae

proof_lines: kcat is 92 min(-1) with dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose as substrate. kcat is 4.2 min(-1) with dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose as substrate.


organism: Bos taurus

proof_lines: synthetic 6-phosphogluconolactone, pH 6.5

proof_lines: synthetic 6-phosphogluconolactone, pH 7.4


organism: Dicentrarchus labrax


organism: Rattus norvegicus


organism: Alcanivorax borkumensis

sequence_source: UniProtKB REST lookup accession Q0VTB0 on 2026-06-16

assay_conditions_summary: pH 8; 318.15 K; cofactor NADH


sequence_source: UniProtKB REST lookup accession Q9ZGH6 on 2026-06-16


proof_lines: pH 7.5, 24°C, cosubstrate: 3.0 mM S-adenosyl-L-methionine


substrate_name: H2O; 6-Phospho-D-glucono-1,5-lactone

sequence_source: UniProtKB REST lookup accession Q2TBQ8 on 2026-06-16

substrate: H2O; 6-Phospho-D-glucono-1,5-lactone


organism: Giardia duodenalis


enzyme_display_name: L-threo-3-deoxy-hexylosonate aldolase

organism: Trichoderma reesei

enzyme: L-threo-3-deoxy-hexylosonate aldolase


enzyme_display_name: deaminated glutathione amidase

organism: Arabidopsis thaliana

proof_lines: kcat is 4.2 sec(-1) with N-(4-oxoglutarate)-L-cysteinylglycine as substrate (PubMed:30692244). kcat is 3.0 sec(-1) with ophthalmate as substrate (PubMed:30692244).

enzyme: deaminated glutathione amidase


organism: Mus musculus

substrate_name: N-(4-oxoglutarate)-L-cysteinylglycine (at pH 8.5)

proof_lines: kcat is 1.6 sec(-1) with N-(4-oxoglutarate)-L-cysteinylglycine as substrate.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 3.6 sec(-1) with N-(4-oxoglutarate)-L-cysteinylglycine as substrate.

substrate: N-(4-oxoglutarate)-L-cysteinylglycine (at pH 8.5)


enzyme_display_name: thermospermine synthase

organism: Thermus thermophilus

substrate_name: S-Adenosylmethioninamine

sequence_source: UniProtKB:Q5SK28 direct lookup, release 2026_02, checked 2026-06-16

enzyme: thermospermine synthase

substrate: S-Adenosylmethioninamine


sequence_source: UniProtKB:P27833 direct lookup, release 2026_02, checked 2026-06-16


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


enzyme_display_name: sedoheptulokinase

substrate_name: Sedoheptulose

sequence_source: UniProtKB:Q9D5J6 direct lookup, release 2026_02, checked 2026-06-16

enzyme: sedoheptulokinase

substrate: Sedoheptulose


substrate_name: sedoheptulose

substrate: sedoheptulose


enzyme_display_name: CTP-dependent riboflavin kinase

organism: Metallosphaera yellowstonensis

substrate_name: riboflavin

sequence_source: UniProtKB:H2C8H2 direct lookup, release 2026_02, checked 2026-06-16

enzyme: CTP-dependent riboflavin kinase

substrate: riboflavin


substrate_name: CTP

sequence_source: UniProtKB:Q60365 direct lookup, release 2026_02, checked 2026-06-16

proof_lines:
pH 7.2, 70°C
Raw SKiD Env: Temp=70°C, pH=7.2

substrate: CTP


organism: Pyrobaculum sp. WP30


enzyme_display_name: anhydro-N-acetylmuramic acid kinase

organism: Escherichia coli

sequence_source: UniProtKB:P77570 direct lookup, release 2026_02, checked 2026-06-16

enzyme: anhydro-N-acetylmuramic acid kinase


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9I5Q5 direct lookup, release 2026_02, checked 2026-06-16

proof_lines: in 50 mM HEPES, pH 7.5, 10 mM MgCl2, and 50 mM KCl, at 37°C


enzyme_display_name: glycoprotein-mannosyl O(6)-kinase

substrate_name: ATP

sequence_source: UniProtKB:Q3TUA9 direct lookup, release 2026_02, checked 2026-06-16

proof_lines: pH and temperature not specified in the publication, recombinant murine POMK catalytic domain

enzyme: glycoprotein-mannosyl O(6)-kinase

substrate: ATP


enzyme_display_name: alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase

sequence_source: UniProtKB:P16687 direct lookup, release 2026_02, checked 2026-06-16

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


substrate_name: GTP

enzyme: alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase

substrate: GTP


enzyme_display_name: tRNA uracil 4-sulfurtransferase

sequence_source: UniProtKB:P77718 direct lookup, release 2026_02, checked 2026-06-16

enzyme: tRNA uracil 4-sulfurtransferase


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


enzyme_display_name: L-asparagine oxygenase

organism: Streptomyces coelicolor

substrate_name: L-asparagine

enzyme: L-asparagine oxygenase

substrate: L-asparagine


organism: Zea mays

substrate_name: DIBOA glucoside

substrate: DIBOA glucoside


enzyme_display_name: phenylalanine N-monooxygenase

substrate_name: L-phenylalanine

enzyme: phenylalanine N-monooxygenase

substrate: L-phenylalanine


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


enzyme_display_name: geraniol 8-hydroxylase

organism: Catharanthus roseus

substrate_name: geraniol

smiles: CC(C)=CCC/C(C)=C/CO

enzyme: geraniol 8-hydroxylase

substrate: geraniol


proof_lines:
pH 7.4, 27°C
pH 8.0, 30°C, recombinant enzyme


enzyme_display_name: 4-aminobenzoate N-oxygenase

organism: Streptomyces thioluteus

proof_lines:
pH 7.4, 20°C
Raw SKiD Env: Temp=20°C, pH=7.4

enzyme: 4-aminobenzoate N-oxygenase


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

substrate_name: L-Methionine S-oxide

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

substrate: L-Methionine S-oxide


enzyme_display_name: mitomycin 6-O-methyltransferase

organism: Streptomyces lavendulae

substrate_name: 7-demethylmitomycin A

enzyme: mitomycin 6-O-methyltransferase

substrate: 7-demethylmitomycin A


enzyme_display_name: 1-deoxy-D-xylulose-5-phosphate synthase

organism: Agrobacterium tumefaciens

substrate_name: pyruvate

enzyme: 1-deoxy-D-xylulose-5-phosphate synthase

substrate: pyruvate


organism: Botryococcus braunii

substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


organism: Deinococcus radiodurans

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H304A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'D-glyceraldehyde 3-phosphate', enzyme-form row 'H304A': column 'KM (mM)' = 0.08; column 'kcat/KM (s-1 M-1)' = 1.1 x 10^4; column 'kcat (s-1)' = 0.90. captured primary segment: Table 2 | substrate D-glyceraldehyde 3-phosphate | Deinococcus radiodurans DXS H304A | KM 0.08 mM | kcat 0.90 s-1 | kcat/KM 1.1 x 10^4 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.08 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.08 mM. kcat: printed Table 2 cell 0.90 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 0.9 s^(-1). kcat/KM: printed Table 2 cell 1.1 x 10^4 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 11000 / 1000 = 11.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.9 / 0.08 = 11.25 s-1 mM-1, against the printed catalytic-efficiency cell 1.1 x 10^4 s-1 M-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 2, substrate block 'D-glyceraldehyde 3-phosphate', printed enzyme-form row 'H304A': kcat = 0.90 s-1; KM = 0.08 mM; printed kcat/KM = 1.1 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature D430A to reconstruct the assayed variant sequence.

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

column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'D430A': column 'KM (mM)' = 0.52; column 'kcat/KM (s-1 M-1)' = 1.4 x 10^4; column 'kcat (s-1)' = 7.2. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS D430A | KM 0.52 mM | kcat 7.2 s-1 | kcat/KM 1.4 x 10^4 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.52 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.52 mM. kcat: printed Table 2 cell 7.2 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 7.2 s^(-1). kcat/KM: printed Table 2 cell 1.4 x 10^4 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 14000 / 1000 = 14.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.2 / 0.52 = 13.846153846153847 s-1 mM-1, against the printed catalytic-efficiency cell 1.4 x 10^4 s-1 M-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'D430A': kcat = 7.2 s-1; KM = 0.52 mM; printed kcat/KM = 1.4 x 10^4 s-1 M-1.


organism: Methanococcus maripaludis

substrate_name: Sulfide

substrate: Sulfide


enzyme_display_name: keratan sulfotransferase

organism: Homo sapiens

substrate_name: 3'-Phosphoadenylyl sulfate

enzyme: keratan sulfotransferase

substrate: 3'-Phosphoadenylyl sulfate


enzyme_display_name: (3S)-malyl-CoA thioesterase

organism: Cereibacter sphaeroides

substrate_name: (S)-malyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

column_label: Table 1, Mcl2 thioester cleavage: kcat 110 s^-1; target-substrate Km 0.09 mM; printed kcat/Km 1.2 × 10^6 M^-1 s^-1 = 1200 s^-1 mM^-1. Current 1222.2222222222222 lies in the printed-efficiency rounding interval [1150, 1250) s^-1 mM^-1.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=110 s^-1 and target-substrate Km=0.09 mM. Their stored-precision quotient is 110 / 0.09 = 1222.2222222222222 s^-1 mM^-1. Printed efficiency normalizes separately to 1200 s^-1 mM^-1.

raw_value_unit_evidence: kcat raw_value=110 raw_unit=s^-1; Km raw_value=0.09 raw_unit=mM; printed kcat/Km raw_value=1.2 × 10^6 raw_unit=M^-1 s^-1

row_label: Mcl2 / thioester cleavage

table_label: Table 1: Molecular and catalytic properties of recombinant (3S)-malyl-CoA/β-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase from R. sphaeroides

enzyme: (3S)-malyl-CoA thioesterase

substrate: (S)-malyl-CoA


proof_lines: pH 7.5, 30°C, in the presence of divalent cations (Mg2+ or Mn2+)


organism: Rhodobacter sphaeroides

substrate_name: L-Malyl-CoA

substrate: L-Malyl-CoA


enzyme_display_name: hydroxyacylglutathione hydrolase

organism: Arabidopsis thaliana

substrate_name: S-D-lactoylglutathione

enzyme: hydroxyacylglutathione hydrolase

substrate: S-D-lactoylglutathione


substrate_name: (R)-S-Lactoylglutathione

sequence_variant_note: Resolved canonical sequence from uniprot_accession_mutation_reconstruction and applied mutation signature D58C to reconstruct the assayed variant sequence.

substrate: (R)-S-Lactoylglutathione


sequence_variant_note: Resolved canonical sequence from uniprot_accession_mutation_reconstruction and applied mutation signature H54N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H82A to reconstruct the assayed variant sequence.

column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'H82A': column 'KM (mM)' = 0.23; column 'kcat/KM (s-1 M-1)' = 1.7 x 10^3; column 'kcat (s-1)' = 0.38. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS H82A | KM 0.23 mM | kcat 0.38 s-1 | kcat/KM 1.7 x 10^3 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.23 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.23 mM. kcat: printed Table 2 cell 0.38 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 0.38 s^(-1). kcat/KM: printed Table 2 cell 1.7 x 10^3 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 1700 / 1000 = 1.7 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.38 / 0.23 = 1.6521739130434783 s-1 mM-1, against the printed catalytic-efficiency cell 1.7 x 10^3 s-1 M-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'H82A': kcat = 0.38 s-1; KM = 0.23 mM; printed kcat/KM = 1.7 x 10^3 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature H434A to reconstruct the assayed variant sequence.


column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'D-glyceraldehyde 3-phosphate', enzyme-form row 'H82A': column 'KM (mM)' = 0.03; column 'kcat/KM (s-1 M-1)' = 1.3 x 10^4; column 'kcat (s-1)' = 0.37. captured primary segment: Table 2 | substrate D-glyceraldehyde 3-phosphate | Deinococcus radiodurans DXS H82A | KM 0.03 mM | kcat 0.37 s-1 | kcat/KM 1.3 x 10^4 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.03 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.03 mM. kcat: printed Table 2 cell 0.37 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 0.37 s^(-1). kcat/KM: printed Table 2 cell 1.3 x 10^4 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 13000 / 1000 = 13.0 s^(-1)*mM^(-1). The quotient of the two printed component cells is 0.37 / 0.03 = 12.333333333333334 s-1 mM-1, which falls outside the rounding interval of the printed cell 1.3 x 10^4 at the place value that printed literal carries, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 2, substrate block 'D-glyceraldehyde 3-phosphate', printed enzyme-form row 'H82A': kcat = 0.37 s-1; KM = 0.03 mM; printed kcat/KM = 1.3 x 10^4 s-1 M-1.


column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'H304A': column 'KM (mM)' = 1.7; column 'kcat/KM (s-1 M-1)' = 5.8 x 10^2; column 'kcat (s-1)' = 0.90. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS H304A | KM 1.7 mM | kcat 0.90 s-1 | kcat/KM 5.8 x 10^2 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 1.7 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 1.7 mM. kcat: printed Table 2 cell 0.90 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 0.9 s^(-1). kcat/KM: printed Table 2 cell 5.8 x 10^2 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 580 / 1000 = 0.58 s^(-1)*mM^(-1). The quotient of the two printed component cells is 0.9 / 1.7 = 0.5294117647058824 s-1 mM-1, which falls outside the rounding interval of the printed cell 5.8 x 10^2 at the place value that printed literal carries, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'H304A': kcat = 0.90 s-1; KM = 1.7 mM; printed kcat/KM = 5.8 x 10^2 s-1 M-1.


sequence_source: UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present

proof_lines: apparent value, wild type enzyme, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H434A to reconstruct the assayed variant sequence.

column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'H434A': column 'KM (mM)' = 1.7; column 'kcat/KM (s-1 M-1)' = 5.9 x 10^3; column 'kcat (s-1)' = 9.9. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS H434A | KM 1.7 mM | kcat 9.9 s-1 | kcat/KM 5.9 x 10^3 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 1.7 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 1.7 mM. kcat: printed Table 2 cell 9.9 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 9.9 s^(-1). kcat/KM: printed Table 2 cell 5.9 x 10^3 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 5900 / 1000 = 5.9 s^(-1)*mM^(-1). The quotient of the two printed component cells is 9.9 / 1.7 = 5.8235294117647065 s-1 mM-1, which falls outside the rounding interval of the printed cell 5.9 x 10^3 at the place value that printed literal carries, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'H434A': kcat = 9.9 s-1; KM = 1.7 mM; printed kcat/KM = 5.9 x 10^3 s-1 M-1.


column_label: Table 2: DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and D-glyceraldehyde 3-phosphate (J Phys Chem B 2016, 120(37):9922-9934); the table prints two substrate blocks, each with the column heads 'KM (mM)', 'kcat/KM (s-1 M-1)', 'kcat (s-1)' and '% WT' and one line per enzyme form. Substrate block 'Pyruvate', enzyme-form row 'wild-type': column 'KM (mM)' = 0.28; column 'kcat/KM (s-1 M-1)' = 2.6 x 10^4; column 'kcat (s-1)' = 7.4. captured primary segment: Table 2 | substrate pyruvate | Deinococcus radiodurans DXS wild-type | KM 0.28 mM | kcat 7.4 s-1 | kcat/KM 2.6 x 10^4 s-1 M-1 | DXS-DXR coupled assay at pH 8.0

normalized_value_unit_evidence: KM: printed Table 2 cell 0.28 mM; the printed column head is 'KM (mM)', so no unit conversion applies and the paper value is 0.28 mM. kcat: printed Table 2 cell 7.4 s-1; the printed column head is 'kcat (s-1)', already per second, so no unit conversion applies and the paper value is 7.4 s^(-1). kcat/KM: printed Table 2 cell 2.6 x 10^4 s-1 M-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 26000 / 1000 = 26.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.4 / 0.28 = 26.428571428571427 s-1 mM-1, against the printed catalytic-efficiency cell 2.6 x 10^4 s-1 M-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 2, substrate block 'Pyruvate', printed enzyme-form row 'wild-type': kcat = 7.4 s-1; KM = 0.28 mM; printed kcat/KM = 2.6 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature D430A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature N181A to reconstruct the assayed variant sequence.

column_label: Table 1: Domain I mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 23), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'N181A': column 'KM,app (mM)' = 0.03 ± 0.01; column 'kcat,app (s-1)' = 0.43 ± 0.02; column '(kcat/KM)app (s-1 M-1)' = 1.4 x 10^4; unheaded relative-efficiency column = 0.09.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.43 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.43 s^(-1); the exported value is 0.43 s^(-1). Km: printed Table 1 cell 0.03 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.03 mM; the exported value is 0.03 mM. kcat/KM: printed Table 1 cell 1.4 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.4 x 10^4 / 1000 = 14.0 s^-1 mM^-1; the paper value is 14.0 s^(-1)*mM^(-1); the exported value is 14.333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Protein row 'N181A', GAP as the variable substrate: KM,app = 0.03 mM; kcat,app = 0.43 s-1; printed (kcat/KM)app = 1.4 x 10^4 s-1 M-1.

row_label: Table 1, Protein row 'N181A', with GAP as the variable substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature Y395A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme Y395A, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature R423A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme R423A, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature N181A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme N181A, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H434K to reconstruct the assayed variant sequence.

column_label: Table 4: Domain II mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 26), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'H434K': column 'KM,app (mM)' = 1.7 ± 0.1; column 'kcat,app (s-1)' = 9.9 ± 0.2; column '(kcat/KM)app (s-1 M-1)' = 5.9 x 10^3; unheaded relative-efficiency column = 0.2+.

normalized_value_unit_evidence: kcat: printed Table 4 cell 9.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 9.9 s^(-1); the exported value is 9.9 s^(-1). Km: printed Table 4 cell 1.7 mM; the printed unit is already mM, no unit conversion applies; the paper value is 1.7 mM; the exported value is 0.05 mM. kcat/KM: printed Table 4 cell 5.9 x 10^3 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 5.9 x 10^3 / 1000 = 5.9 s^-1 mM^-1; the paper value is 5.9 s^(-1)*mM^(-1); the exported value is 198.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Protein row 'H434K', pyruvate as the variable substrate: KM,app = 1.7 mM; kcat,app = 9.9 s-1; printed (kcat/KM)app = 5.9 x 10^3 s-1 M-1.

row_label: Table 4, Protein row 'H434K', with pyruvate as the variable substrate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature Y395A to reconstruct the assayed variant sequence.

column_label: Table 4: Domain II mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 26), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'Y395A': column 'KM,app (mM)' = 0.16 ± 0.01; column 'kcat,app (s-1)' = 3.6 ± 0.1; column '(kcat/KM)app (s-1 M-1)' = 2.2 x 10^4; unheaded relative-efficiency column = 0.8.

normalized_value_unit_evidence: kcat: printed Table 4 cell 3.6 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 3.6 s^(-1); the exported value is 3.6 s^(-1). Km: printed Table 4 cell 0.16 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.16 mM; the exported value is 0.16 mM. kcat/KM: printed Table 4 cell 2.2 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 2.2 x 10^4 / 1000 = 22.0 s^-1 mM^-1; the paper value is 22.0 s^(-1)*mM^(-1); the exported value is 22.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Protein row 'Y395A', pyruvate as the variable substrate: KM,app = 0.16 mM; kcat,app = 3.6 s-1; printed (kcat/KM)app = 2.2 x 10^4 s-1 M-1.

row_label: Table 4, Protein row 'Y395A', with pyruvate as the variable substrate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature R423A to reconstruct the assayed variant sequence.

column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'R423A': column 'KM,app (mM)' = 12 ± 3.2; column 'kcat,app (s-1)' = 1.7 ± 0.3; column '(kcat/KM)app (s-1 M-1)' = 1.4 x 10^2; unheaded relative-efficiency column = 9 x 10^-4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.7 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 1.7 s^(-1); the exported value is 1.7 s^(-1). Km: printed Table 3 cell 12 mM; the printed unit is already mM, no unit conversion applies; the paper value is 12.0 mM; the exported value is 12.0 mM. kcat/KM: printed Table 3 cell 1.4 x 10^2 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.4 x 10^2 / 1000 = 0.14 s^-1 mM^-1; the paper value is 0.14 s^(-1)*mM^(-1); the exported value is 0.14166666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Protein row 'R423A', GAP as the variable substrate: KM,app = 12 mM; kcat,app = 1.7 s-1; printed (kcat/KM)app = 1.4 x 10^2 s-1 M-1.

row_label: Table 3, Protein row 'R423A', with GAP as the variable substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUB5 direct accession lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature H304A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme H304A, at pH 8.0 and 37°C


substrate_name: Unknown

sequence_source: UniProtKB reviewed accession Q9RUB5 REST lookup on 2026-06-16

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

proof_lines: inhibition with respect to pyruvate, at pH 8.0 and 37°C

proof_lines: inhibition with respect to D-glyceraldehyde 3-phosphate, at pH 8.0 and 37°C

substrate: Unknown


column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'H434A': column 'KM,app (mM)' = 0.23 ± 0.01; column 'kcat,app (s-1)' = 9.6 ± 0.3; column '(kcat/KM)app (s-1 M-1)' = 4.2 x 10^4; unheaded relative-efficiency column = 0.3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 9.6 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 9.6 s^(-1); the exported value is 9.9 s^(-1). Km: printed Table 3 cell 0.23 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.23 mM; the exported value is 0.23 mM. kcat/KM: printed Table 3 cell 4.2 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^4 / 1000 = 42.0 s^-1 mM^-1; the paper value is 42.0 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

raw_value_unit_evidence: Table 3, Protein row 'H434A', GAP as the variable substrate: KM,app = 0.23 mM; kcat,app = 9.6 s-1; printed (kcat/KM)app = 4.2 x 10^4 s-1 M-1.

row_label: Table 3, Protein row 'H434A', with GAP as the variable substrate


column_label: Table 2: Domain I mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 24), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'H82A': column 'KM,app (mM)' = 0.23 ± 0.02; column 'kcat,app (s-1)' = 0.38 ± 0.01; column '(kcat/KM)app (s-1 M-1)' = 1.7 x 10^3; unheaded relative-efficiency column = 0.07.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.38 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.38 s^(-1); the exported value is 0.38 s^(-1). Km: printed Table 2 cell 0.23 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.23 mM; the exported value is 0.03 mM. kcat/KM: printed Table 2 cell 1.7 x 10^3 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.7 x 10^3 / 1000 = 1.7 s^-1 mM^-1; the paper value is 1.7 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

raw_value_unit_evidence: Table 2, Protein row 'H82A', pyruvate as the variable substrate: KM,app = 0.23 mM; kcat,app = 0.38 s-1; printed (kcat/KM)app = 1.7 x 10^3 s-1 M-1.

row_label: Table 2, Protein row 'H82A', with pyruvate as the variable substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RUB5 REST lookup plus selected-row mutation_signature D430A and applied mutation signature D430A to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme D430A, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature Y395F to reconstruct the assayed variant sequence.

column_label: Table 4: Domain II mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 26), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'Y395F': column 'KM,app (mM)' = 0.19 ± 0.01; column 'kcat,app (s-1)' = 2.9 ± 0.02; column '(kcat/KM)app (s-1 M-1)' = 1.6 x 10^4; unheaded relative-efficiency column = 0.6.

normalized_value_unit_evidence: kcat: printed Table 4 cell 2.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 2.9 s^(-1); the exported value is 5.9 s^(-1). Km: printed Table 4 cell 0.19 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.19 mM; the exported value is 0.19 mM. kcat/KM: printed Table 4 cell 1.6 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^4 / 1000 = 16.0 s^-1 mM^-1; the paper value is 16.0 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

raw_value_unit_evidence: Table 4, Protein row 'Y395F', pyruvate as the variable substrate: KM,app = 0.19 mM; kcat,app = 2.9 s-1; printed (kcat/KM)app = 1.6 x 10^4 s-1 M-1.

row_label: Table 4, Protein row 'Y395F', with pyruvate as the variable substrate