sequence_source: UniProtKB accession Q84N28 direct lookup (UniProtKB reviewed (Swiss-Prot); Triticum aestivum; Flavone O-methyltransferase 1; EC 2.1.1.-; length 360)


organism: Triticum aestivum

substrate_name: tricetin

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

proof_lines: pH and temperature not specified in the publication, mutant W259A

substrate: tricetin

source: brenda


proof_lines: pH and temperature not specified in the publication, mutant E322I


proof_lines: pH and temperature not specified in the publication, mutant G305S


proof_lines: pH and temperature not specified in the publication, mutant D263N


proof_lines: pH and temperature not specified in the publication, mutant W259Y


mutation_signature: Unknown

sequence_source: UniProtKB accession Q38J50 direct lookup (UniProtKB reviewed (Swiss-Prot); Triticum aestivum; Tricetin 3',4',5'-O-trimethyltransferase; EC 2.1.1.169; length 356)

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

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


km_display: Not reported

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

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: (R,S)-reticuline 7-O-methyltransferase

organism: Papaver somniferum

substrate_name: guaiacol

sequence_source: UniProtKB accession Q6WUC2 direct lookup (UniProtKB reviewed (Swiss-Prot); Papaver somniferum; (R,S)-reticuline 7-O-methyltransferase; EC 2.1.1.291; length 355)

proof_lines: pH 8.0, 35°C, cosubstrate guaiacol or (R)-reticuline

proof_lines: pH 8.0, 35°C, cosubstrate isovanillic acid

enzyme: (R,S)-reticuline 7-O-methyltransferase

substrate: guaiacol


substrate_name: (R)-reticuline

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

data_origin: experimental

substrate: (R)-reticuline

status: unverified

source: oed


substrate_name: (S)-reticuline

sequence_source: UniProtKB reviewed accession Q6WUC2

substrate: (S)-reticuline


enzyme_display_name: hydroxyethylthiazole kinase

organism: Staphylococcus aureus

sequence_source: UniProtKB reviewed accession Q6GEY3

enzyme: hydroxyethylthiazole kinase


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

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

source_databases_merged: brenda skid


enzyme_display_name: alkylglycerone-phosphate synthase

organism: Cavia porcellus

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

sequence_source: UniProtKB exact accession P97275 direct check on 2026-06-28

enzyme: alkylglycerone-phosphate synthase


organism: Trypanosoma brucei

substrate_name: Palmitoyldihydroxyacetone phosphate

sequence_source: UniProtKB exact accession O97157 direct check on 2026-06-28

substrate: Palmitoyldihydroxyacetone phosphate


enzyme_display_name: S-methyl-5-thioribose kinase

organism: Bacillus subtilis

substrate_name: ATP; 5-Methylthio-D-ribose

sequence_source: UniProtKB exact accession O31663 direct check on 2026-06-28

assay_conditions_summary: cofactor ATP

enzyme: S-methyl-5-thioribose kinase

substrate: ATP; 5-Methylthio-D-ribose


organism: Oryza sativa

sequence_source: UniProtKB exact accession Q7XR61 direct check on 2026-06-28


enzyme_display_name: inositol-1,3,4-trisphosphate 5/6-kinase

organism: Arabidopsis thaliana

sequence_source: UniProtKB exact accession O80568 direct check on 2026-06-28

enzyme: inositol-1,3,4-trisphosphate 5/6-kinase


organism: Bos taurus

sequence_source: UniProtKB exact accession P0C0T1 direct check on 2026-06-28


organism: Homo sapiens

sequence_source: UniProtKB exact accession Q13572 direct check on 2026-06-28


enzyme_display_name: pyruvate kinase

substrate_name: Phosphoenolpyruvate; ADP

sequence_source: UniProtKB exact accession P14618 direct check on 2026-06-28

assay_conditions_summary: cofactor ADP

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Zea mays

substrate_name: ATP

source_db: uniprot

substrate: ATP

source: uniprot


enzyme_display_name: glucuronokinase

substrate_name: D-glucuronic acid

enzyme: glucuronokinase

substrate: D-glucuronic acid


enzyme_display_name: hydroxylysine kinase

substrate_name: (5R)-5-hydroxy-L-lysine (in the presence of 2 mM ATP)

enzyme: hydroxylysine kinase


organism: Unknown

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


organism: Aquifex aeolicus (strain VF5)

verification_status: corrected

status: corrected


organism: Escherichia coli (strain K12)


enzyme_display_name: chlorate reductase

organism: Stutzerimonas chloritidismutans

substrate_name: chlorate

sequence: LNMLEPVGETLASEYPYXK

wild_type_sequence: LNMLEPVGETLASEYPYXK

enzyme: chlorate reductase

substrate: chlorate


assay_conditions_summary: cofactor CoA


substrate_name: palmitoyl-dihydroxyacetonephosphate (in the presence of 0.5 mM of hexadecanol)


organism: Rattus norvegicus

substrate_name: hexadecanol

substrate: hexadecanol


organism: Glycine max


organism: Plasmodium falciparum (isolate 3D7)

proof_lines: kcat is 1.3 sec(-1) for (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP) (with methyl viologen as electron donor and at 30 degrees Celsius).


organism: Papaver somniferum

proof_lines: kcat is 0.1 sec(-1) with guaiacol as substrate. kcat is 0.07 sec(-1) with (S)-reticuline as substrate. kcat is 0.07 sec(-1) with (R)-reticuline as substrate. kcat is 0.03 sec(-1) with (R)-protosinomenine as substrate. kcat is 0.02 sec(-1) w


organism: Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73)

proof_lines: kcat is 15.4 sec(-1) with 5-deoxy-D-ribose as substrate. kcat is 6.2 sec(-1) with S-methyl-5-thio-D-ribose as substrate.


organism: Escherichia coli O45:K1 (strain S88 / ExPEC)

proof_lines: kcat is 10.6 sec(-1) with 5-methythioribose as substrate. kcat is 16.1 sec(-1) with 5-deoxyribose as substrate. kcat is 5.4 sec(-1) with S-ribosyl-L-homocysteine as substrate. kcat is 11.6 sec(-1) with ribose as substrate.


substrate_name: thiazole

proof_lines: kcat is 0.068 sec(-1) for thiazole. kcat is 0.069 sec(-1) for ATP.

substrate: thiazole


proof_lines: kcat is 1.79 sec(-1) for thiazole. kcat is 2.39 sec(-1) for ATP.


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: D-glycero-alpha-D-manno-heptose 1-phosphate (at pH 7.4 and 25 degrees Celsius)

proof_lines: kcat is 3.0 sec(-1) and 1.35 sec(-1) for D-glycero-alpha-D-manno-heptose 1-phosphate determined by 31P NMR and HPLC method, respectively.


organism: Aquifex aeolicus

substrate_name: Unknown

ki_unit: mM

sequence_source: UniProtKB:O67625 (ISPH_AQUAE); reviewed canonical accession

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

substrate: Unknown


organism: Burkholderia glumae

assay_conditions_summary: pH 8

proof_lines: pH 8, temperature not specified in the publication


organism: Escherichia coli

sequence_source: UniProtKB:P62623 (ISPH_ECOLI); reviewed canonical accession


organism: Azospira oryzae

substrate_name: Chlorate

substrate: Chlorate


substrate_name: reduced benzyl viologen

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

assay_conditions_summary: cofactor FMN

substrate: reduced benzyl viologen


organism: Cavia porcellus


substrate_name: octadecanol

sequence_source: UniProtKB:Q9EQR2 (ADAS_RAT); reviewed canonical accession

substrate: octadecanol


organism: Bacillus subtilis

sequence_source: UniProtKB:O31663 (MTNK_BACSU); reviewed canonical accession

proof_lines:
37°C, approx. value
pH 8.0, 25°C


organism: Klebsiella aerogenes

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP


organism: Klebsiella pneumoniae

sequence_source: UniProtKB:Q9F0P1 (MTNK_KLEPN); reviewed canonical accession


organism: Lupinus luteus

assay_conditions_summary: pH 9.7; 308.15 K; cofactor ATP


organism: Bos taurus

sequence_source: UniProtKB:P0C0T1 (ITPK1_BOVIN); reviewed canonical accession


organism: Saccharomyces cerevisiae


organism: Saccharomyces pastorianus


organism: Schistosoma mansoni


organism: Spinacia oleracea


organism: Streptococcus mutans


organism: Streptococcus sanguis


organism: Synechococcus elongatus


organism: Toxoplasma gondii


organism: Trachemys scripta


organism: Trypanosoma brucei


organism: Trypanosoma cruzi


organism: Zapus hudsonius


organism: Danio rerio

substrate_name: D-glucuronate

assay_conditions_summary: pH 7.5; 308.15 K; cofactor ATP

substrate: D-glucuronate


organism: Lilium longiflorum

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Rattus norvegicus

substrate_name: GTP; 5-Hydroxy-L-lysine

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

substrate: GTP; 5-Hydroxy-L-lysine


enzyme_display_name: beta-lactamase

organism: Serratia fonticola

substrate_name: ceftazidime

proof_lines: at 25°C in 50 mM sodium phosphate (pH 7.0)

enzyme: beta-lactamase

substrate: ceftazidime


enzyme_display_name: FAD diphosphatase

organism: Vigna radiata var. radiata

substrate_name: NADH

assay_conditions_summary: cofactor NAD+

enzyme: FAD diphosphatase

substrate: NADH


organism: Homo sapiens

proof_lines: pH 7.6, 37°C, in presence of CSN1, first order rate constant

proof_lines: pH 7.6, 37°C, in absence of CSN1, first order rate constant


proof_lines: pH 7.2, 37°C, versus 1D-myo-inositol-1,3,4-trisphosphate


organism: Bos taurus

substrate_name: Phosphoenolpyruvate; ADP


organism: Brassica napus


organism: Canis familiaris


organism: Columba livia


organism: Coprinopsis lagopus


organism: Cupriavidus necator


organism: Mus musculus


organism: Mustela vison


organism: Ricinus communis


organism: Unknown

substrate_name: H2O; Cephalothin

substrate: H2O; Cephalothin


organism: Escherichia coli

substrate_name: H2O; Nitrocefin

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.2
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: H2O; Nitrocefin


substrate_name: H2O; Cephaloridine

substrate: H2O; Cephaloridine


substrate_name: cefpirome

source_db: skid

source_license: CC BY-NC-ND 4.0

substrate: cefpirome

source: skid


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: nitrocefin

substrate: nitrocefin


organism: Pseudomonas putida

substrate_name: H2O; Ampicillin

sequence_source: UniProtKB exact accession Q8GCU7 canonical sequence, direct lookup on 2026-06-28

substrate: H2O; Ampicillin


substrate_name: moxalactam

sequence_source: UniProtKB exact accession Q9RMI1 canonical sequence, direct lookup on 2026-06-28

substrate: moxalactam


organism: Shewanella livingstonensis

substrate_name: H2O; Amoxicillin

sequence_source: UniProtKB exact accession Q53BU1 canonical sequence, direct lookup on 2026-06-28

substrate: H2O; Amoxicillin


organism: Stenotrophomonas maltophilia

sequence_source: UniProtKB exact accession P52700 canonical sequence, direct lookup on 2026-06-28

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


organism: Klebsiella pneumoniae

substrate_name: ceftaxidime

sequence_source: UniProtKB:Q09HD0 direct accession lookup (release 2026_02)

substrate: ceftaxidime


substrate_name: temocillin

sequence_source: UniProtKB:Q6XEC0 direct accession lookup (release 2026_02)

substrate: temocillin


organism: Aeromonas sobria

substrate_name: H2O; Imipenem

substrate: H2O; Imipenem


organism: Enterobacter cloacae


organism: Haemophilus ducreyi


substrate_name: H2O; Benzylpenicillin

substrate: H2O; Benzylpenicillin


organism: Mycobacterium tuberculosis


organism: Proteus vulgaris


organism: Pseudomonas aeruginosa

substrate_name: Cefdinir; H2O

substrate: Cefdinir; H2O


substrate_name: ceftazidime

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


organism: Pseudomonas fluorescens

substrate_name: carbenicillin

substrate: carbenicillin


enzyme_display_name: deoxycytidine kinase

organism: Homo sapiens

substrate_name: cytidine

sequence_source: UniProtKB:P27707 direct REST lookup on 2026-06-28

enzyme: deoxycytidine kinase

substrate: cytidine


substrate_name: gemcitabine

verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P27707 and applied mutation signature A100V/R104M/D133A to reconstruct the assayed variant sequence.

column_label: Table 1 Steady state kinetic data, A100V/R104M/D133A mutant dCK block, row 'gemcitabine'; column 'Km (µM)' = 50; column 'kcat (s–1)' = 3.52; column 'kcat / Km (M–1 s–1)' = 70.4 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.52 s-1; already in s-1, no conversion; the paper value is 3.52 s^(-1). Km: printed Table 1 cell 50 uM; 50 / 1000 = 0.05 mM. kcat/Km: printed Table 1 cell 70.4 x 10^3 M-1 s-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 70400 / 1000 = 70.4 s^(-1)*mM^(-1); the quotient of the printed component cells is 3.52 / 0.05 = 70.4 s-1 mM-1, identical to the printed cell.

raw_value_unit_evidence: Table 1, A100V/R104M/D133A mutant dCK block, row Gemcitabine: Km = 50 uM; kcat = 3.52 s-1; printed kcat/Km = 70.4 x 10^3 M-1 s-1.

row_label: Table 1, A100V/R104M/D133A mutant dCK, row gemcitabine

table_label: Table 1 Steady state kinetic data (Nature Structural Biology 2003, 10(7):513-519)

substrate: gemcitabine

status: verified


substrate_name: Zalcitabine

substrate: Zalcitabine


column_label: Table 1 Steady state kinetic data, A100V/R104M/D133A mutant dCK block, row '2'-Deoxycytidine'; column 'Km (µM)' = 4; column 'kcat (s–1)' = 0.93; column 'kcat / Km (M–1 s–1)' = 232.5 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.93 s-1; already in s-1, no conversion; the paper value is 0.93 s^(-1). Km: printed Table 1 cell 4 uM; 4 / 1000 = 0.004 mM. kcat/Km: printed Table 1 cell 232.5 x 10^3 M-1 s-1; 1 M-1 s-1 is 0.001 s-1 mM-1, so 232500 / 1000 = 232.5 s^(-1)*mM^(-1); the quotient of the printed component cells is 0.93 / 0.004 = 232.5 s-1 mM-1, identical to the printed cell.

raw_value_unit_evidence: Table 1, A100V/R104M/D133A mutant dCK block, row dC: Km = 4 uM; kcat = 0.93 s-1; printed kcat/Km = 232.5 x 10^3 M-1 s-1.

row_label: Table 1, A100V/R104M/D133A mutant dCK, row 2'-Deoxycytidine


substrate_name: Cytarabine

substrate: Cytarabine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature A100V/R104M/D133A to reconstruct the assayed variant sequence.


substrate_name: ATP

mutation_signature: residues 65-79 deletion mutant with 2-deoxycytidine as cosubstrate

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

mutation_type: deletion

substrate: ATP


mutation_signature: residues 65-79 deletion mutant with 1-beta-D-arabinofuranosylcytosine as cosubstrate


mutation_signature: residues 65-79 deletion mutant with ATP as cosubstrate


proof_lines: less than 0.001 mM, residues 65-79 deletion mutant with UTP as cosubstrate


proof_lines: wild type enzyme with ATP as cosubstrate

proof_lines: wild type enzyme with UTP as cosubstrate

proof_lines: wild type enzyme with 1-beta-D-arabinofuranosylcytosine as cosubstrate


substrate_name: UTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature C185A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: C185A mutant enzyme with 2-deoxyadenosine as phosphate acceptor, pH 7.6

proof_lines: C185A mutant enzyme with 2-deoxycytidine as phosphate acceptor, pH 7.6

substrate: UTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature C9S/C45S/C59S/C146S to reconstruct the assayed variant sequence.

proof_lines: cosubstrate L-2-deoxycytidine, mutant C9S/C45S/C59S/C146S, 37°C, pH 7.5

proof_lines: cosubstrate troxacitabine, mutant C9S/C45S/C59S/C146S, 37°C, pH 7.5

proof_lines: cosubstrate D-2-deoxycytidine, mutant C9S/C45S/C59S/C146S, 37°C, pH 7.5


sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature S74D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature S74Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 direct REST lookup on 2026-06-28 and applied mutation signature S74A to reconstruct the assayed variant sequence.


substrate_name: Phosphoenolpyruvate; ADP

substrate: Phosphoenolpyruvate; ADP


organism: Saccharomyces cerevisiae


organism: Trichomonas vaginalis


organism: Trypanosoma brucei


organism: Arabidopsis thaliana

substrate_name: ATP; D-Glucuronate

sequence_source: UniProtKB REST direct accession lookup Q93ZC9; checked 2026-06-28

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: allosteric interaction (Hill coefficient: 1.54)

substrate: ATP; D-Glucuronate


organism: Bacillus subtilis

substrate_name: GTP; 2'-Deoxycytidine

sequence_source: UniProtKB REST direct accession lookup P37529; checked 2026-06-28

substrate: GTP; 2'-Deoxycytidine


organism: Gallus gallus

substrate_name: deoxycytidine

sequence_source: UniProtKB REST direct accession lookup Q5ZMF3; checked 2026-06-28

proof_lines: at pH 8.0, temperature not specified in the publication

substrate: deoxycytidine


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines:
pH 7.6, 37°C, recombinant enzyme
cosubstrate ATP, 37°C, pH 7.6
pH 7.5, 37°C


organism: Unknown

substrate_name: deoxyguanosine

substrate: deoxyguanosine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P27707 and applied mutation signature R104L/D133A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer of 100 mM Tris pH 7; cofactor NADH

column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dG' under the R104L-D133A column group; column 'kcat (sec-1)' = 3.66; column 'Km (uM)' = 2266; column 'kcat/Km (x 10^-3)' = 1.6.

normalized_value_unit_evidence: Km: printed Table 4 cell 2266 in the column head unit micromolar; 2266 / 1000 = 2.266 mM, and the exported value is 2.266 mM. kcat: printed Table 4 cell 3.66 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 3.66 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 1.6 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 1.6 s^-1 mM^-1. The exported ratio carried on the same identity is 1.6151809355692852.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row D-dG: kcat = 3.66 sec-1; Km = 2266 micromolar; printed kcat/Km = 1.6 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dG', R104L-D133A column group

table_label: Table 4: Comparison of catalytic efficiencies of new mutants with wild type dCK (Biochemistry 2009, 48(6):1256-1263)


sequence_source: UniProtKB:P27707 reviewed human DCK sequence, checked by UniProt REST on 2026-06-28

column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'AraC' under the WT column group; column 'kcat (sec-1)' = 0.34; column 'Km (uM)' = 13.1; column 'kcat/Km (x 10^-3)' = 26.0.

normalized_value_unit_evidence: Km: printed Table 4 cell 13.1 in the column head unit micromolar; 13.1 / 1000 = 0.013099999999999999 mM, and the exported value is 0.0131 mM. kcat: printed Table 4 cell 0.34 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 0.34 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 26.0 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 26.0 s^-1 mM^-1. The exported ratio carried on the same identity is 25.954198473282442.

raw_value_unit_evidence: Table 4, WT column group, body row AraC: kcat = 0.34 sec-1; Km = 13.1 micromolar; printed kcat/Km = 26.0 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'AraC', WT column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'AraC' under the R104L-D133A column group; column 'kcat (sec-1)' = 0.79; column 'Km (uM)' = 50.6; column 'kcat/Km (x 10^-3)' = 15.6.

normalized_value_unit_evidence: Km: printed Table 4 cell 50.6 in the column head unit micromolar; 50.6 / 1000 = 0.0506 mM, and the exported value is 0.0506 mM. kcat: printed Table 4 cell 0.79 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 0.79 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 15.6 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 15.6 s^-1 mM^-1. The exported ratio carried on the same identity is 15.612648221343875.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row AraC: kcat = 0.79 sec-1; Km = 50.6 micromolar; printed kcat/Km = 15.6 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'AraC', R104L-D133A column group


substrate_name: L-thymidine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 reviewed human DCK sequence, checked by UniProt REST on 2026-06-28; mutation_signature=R104M/D133A from selected batch record and applied mutation signature R104M/D133A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R104M/D133A, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

substrate: L-thymidine


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'Gem' under the R104L-D133A column group; column 'kcat (sec-1)' = 2.01; column 'Km (uM)' = 33.8; column 'kcat/Km (x 10^-3)' = 59.5.

normalized_value_unit_evidence: Km: printed Table 4 cell 33.8 in the column head unit micromolar; 33.8 / 1000 = 0.0338 mM, and the exported value is 0.0338 mM. kcat: printed Table 4 cell 2.01 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 2.01 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 59.5 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 59.5 s^-1 mM^-1. The exported ratio carried on the same identity is 59.467455621301774.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row Gem: kcat = 2.01 sec-1; Km = 33.8 micromolar; printed kcat/Km = 59.5 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'Gem', R104L-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'L-dT' under the R104L-D133A column group; column 'kcat (sec-1)' = 1.33; column 'Km (uM)' = 17.8; column 'kcat/Km (x 10^-3)' = 74.7.

normalized_value_unit_evidence: Km: printed Table 4 cell 17.8 in the column head unit micromolar; 17.8 / 1000 = 0.0178 mM, and the exported value is 0.0178 mM. kcat: printed Table 4 cell 1.33 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 1.33 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 74.7 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 74.7 s^-1 mM^-1. The exported ratio carried on the same identity is 74.71910112359551.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row L-dT: kcat = 1.33 sec-1; Km = 17.8 micromolar; printed kcat/Km = 74.7 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'L-dT', R104L-D133A column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P27707 and applied mutation signature R104M/D133A to reconstruct the assayed variant sequence.

column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'L-dT' under the R104M-D133A column group; column 'kcat (sec-1)' = 3.13; column 'Km (uM)' = 138.0; column 'kcat/Km (x 10^-3)' = 22.7.

normalized_value_unit_evidence: Km: printed Table 4 cell 138.0 in the column head unit micromolar; 138.0 / 1000 = 0.138 mM, and the exported value is 0.138 mM. kcat: printed Table 4 cell 3.13 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 3.13 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 22.7 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 22.7 s^-1 mM^-1. The exported ratio carried on the same identity is 22.681159420289852.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row L-dT: kcat = 3.13 sec-1; Km = 138.0 micromolar; printed kcat/Km = 22.7 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'L-dT', R104M-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dA' under the R104L-D133A column group; column 'kcat (sec-1)' = 5.72; column 'Km (uM)' = 162.3; column 'kcat/Km (x 10^-3)' = 35.2.

normalized_value_unit_evidence: Km: printed Table 4 cell 162.3 in the column head unit micromolar; 162.3 / 1000 = 0.1623 mM, and the exported value is 0.1623 mM. kcat: printed Table 4 cell 5.72 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 5.72 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 35.2 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 35.2 s^-1 mM^-1. The exported ratio carried on the same identity is 35.243376463339494.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row D-dA: kcat = 5.72 sec-1; Km = 162.3 micromolar; printed kcat/Km = 35.2 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dA', R104L-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'AraC' under the R104M-D133A column group; column 'kcat (sec-1)' = 1.43; column 'Km (uM)' = 136.5; column 'kcat/Km (x 10^-3)' = 10.5.

normalized_value_unit_evidence: Km: printed Table 4 cell 136.5 in the column head unit micromolar; 136.5 / 1000 = 0.1365 mM, and the exported value is 0.1365 mM. kcat: printed Table 4 cell 1.43 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 1.43 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 10.5 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 10.5 s^-1 mM^-1. The exported ratio carried on the same identity is 10.476190476190474.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row AraC: kcat = 1.43 sec-1; Km = 136.5 micromolar; printed kcat/Km = 10.5 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'AraC', R104M-D133A column group


substrate_name: D-thymidine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P27707 reviewed human DCK sequence, checked by UniProt REST on 2026-06-28; mutation_signature=R104L/D133A from selected batch record and applied mutation signature R104L/D133A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R104L/D133A, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

substrate: D-thymidine


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'Gem' under the R104M-D133A column group; column 'kcat (sec-1)' = 2.68; column 'Km (uM)' = 56.2; column 'kcat/Km (x 10^-3)' = 47.7.

normalized_value_unit_evidence: Km: printed Table 4 cell 56.2 in the column head unit micromolar; 56.2 / 1000 = 0.0562 mM, and the exported value is 0.0562 mM. kcat: printed Table 4 cell 2.68 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 2.68 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 47.7 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 47.7 s^-1 mM^-1. The exported ratio carried on the same identity is 47.686832740213525.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row Gem: kcat = 2.68 sec-1; Km = 56.2 micromolar; printed kcat/Km = 47.7 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'Gem', R104M-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dT' under the R104M-D133A column group; column 'kcat (sec-1)' = 1.74; column 'Km (uM)' = 144.0; column 'kcat/Km (x 10^-3)' = 12.1.

normalized_value_unit_evidence: Km: printed Table 4 cell 144.0 in the column head unit micromolar; 144.0 / 1000 = 0.144 mM, and the exported value is 0.144 mM. kcat: printed Table 4 cell 1.74 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 1.74 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 12.1 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 12.1 s^-1 mM^-1. The exported ratio carried on the same identity is 12.083333333333334.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row D-dT: kcat = 1.74 sec-1; Km = 144.0 micromolar; printed kcat/Km = 12.1 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dT', R104M-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dC' under the R104L-D133A column group; column 'kcat (sec-1)' = 0.25; column 'Km (uM)' = 8.0; column 'kcat/Km (x 10^-3)' = 31.3.

normalized_value_unit_evidence: Km: printed Table 4 cell 8.0 in the column head unit micromolar; 8.0 / 1000 = 0.008 mM, and the exported value is 0.008 mM. kcat: printed Table 4 cell 0.25 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 0.25 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 31.3 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 31.3 s^-1 mM^-1. The exported ratio carried on the same identity is 31.25.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row D-dC: kcat = 0.25 sec-1; Km = 8.0 micromolar; printed kcat/Km = 31.3 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dC', R104L-D133A column group


substrate_name: 2'-Deoxycytidine; ATP

substrate: 2'-Deoxycytidine; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature S74E to reconstruct the assayed variant sequence.


substrate_name: thymidine

sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104M/D133N to reconstruct the assayed variant sequence.

substrate: thymidine


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature A100V/R104M/D133S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104M/D133S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104M/D133T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104Q/D133N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104Q/D133G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature R104M/D133A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P27707 direct lookup plus row-specific mutation reconstruction


sequence_source: UniProtKB P27707 direct lookup; canonical Homo sapiens deoxycytidine kinase sequence

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


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature A100V/R104M/D133A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature D47E/R104Q/D133G/N163I/F242L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27707 direct lookup plus row-specific mutation reconstruction and applied mutation signature A100V/R104M/D133T to reconstruct the assayed variant sequence.


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dT' under the R104L-D133A column group; column 'kcat (sec-1)' = 3.20; column 'Km (uM)' = 24.3; column 'kcat/Km (x 10^-3)' = 131.7.

normalized_value_unit_evidence: Km: printed Table 4 cell 24.3 in the column head unit micromolar; 24.3 / 1000 = 0.024300000000000002 mM, and the exported value is 0.0243 mM. kcat: printed Table 4 cell 3.20 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 3.2 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 131.7 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 131.7 s^-1 mM^-1. The exported ratio carried on the same identity is 131.68724279835394.

raw_value_unit_evidence: Table 4, R104L-D133A column group, body row D-dT: kcat = 3.20 sec-1; Km = 24.3 micromolar; printed kcat/Km = 131.7 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dT', R104L-D133A column group


column_label: Table 4 (Comparison of catalytic efficiencies of new mutants with wild type dCK), body row 'D-dC' under the R104M-D133A column group; column 'kcat (sec-1)' = 1.80; column 'Km (uM)' = 5.70; column 'kcat/Km (x 10^-3)' = 315.8.

normalized_value_unit_evidence: Km: printed Table 4 cell 5.70 in the column head unit micromolar; 5.70 / 1000 = 0.0057 mM, and the exported value is 0.0057 mM. kcat: printed Table 4 cell 1.80 in the column head unit sec-1; reciprocal seconds is already the canonical unit, so no unit conversion applies and the exported value is 1.8 s^(-1). kcat/Km: Printed Table 4 kcat/Km cell 315.8 under the column head kcat/Km (x 10^-3); with kcat printed in sec-1 and Km printed in micromolar the tabulated figure is the efficiency in units of 10^3 M^-1 s^-1, which is numerically the same as mM^-1 s^-1, so the printed cell converts unchanged to 315.8 s^-1 mM^-1. The exported ratio carried on the same identity is 315.7894736842105.

raw_value_unit_evidence: Table 4, R104M-D133A column group, body row D-dC: kcat = 1.80 sec-1; Km = 5.70 micromolar; printed kcat/Km = 315.8 under the column head kcat/Km (x 10^-3).

row_label: Table 4, body row 'D-dC', R104M-D133A column group


enzyme_display_name: Beta-lactamase

organism: Acinetobacter baumannii

substrate_name: Imipenem

sequence_source: UniProtKB:Q5QT35 direct accession lookup (primary=Q5QT35)

enzyme: Beta-lactamase

substrate: Imipenem


substrate_name: Cefotaxime; H2O

sequence_source: UniProtKB:P05364 direct accession lookup (primary=P05364)

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: Cefotaxime; H2O


substrate_name: 7-aminocephalosporanic acid

sequence_source: UniProtKB:Q59401 direct accession lookup (primary=Q59401)

substrate: 7-aminocephalosporanic acid


organism: Bacillus subtilis (strain 168)

substrate_name: deoxyadenosine (with GTP at pH 8.5 and at 37 degrees Celsius)


substrate_name: deoxycytidine (dC)

substrate: deoxycytidine (dC)


organism: Mus musculus


organism: Bos taurus

substrate_name: cytosine arabinoside

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

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

substrate: cytosine arabinoside


substrate_name: troxacitabine

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

proof_lines: C9S/C45S/C59S/C146Smutant enzyme with UTP as phosphate donor, 37°C, pH 7.5

substrate: troxacitabine


proof_lines: C9S/C45S/C59S/C146S mutant enzyme with ATP as phosphate donor, 37°C, pH 7.5

proof_lines: C9S/C45S/C59S/C146S mutant enzyme with UTP as phosphate donor, 37°C, pH 7.5


proof_lines: pH 7.6, 37°C, enzyme mutant S74E, with co-substrate UTP

proof_lines: pH 7.6, 37°C, enzyme mutant S74E, with co-substrate ATP

proof_lines: pH 7.6, 37°C, enzyme mutant S74E, with substrates deoxycytidine and ATP, mixed inhibition


substrate_name: gemcitabine

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

proof_lines: pH 7.6, 37°C, wild-type enzyme, with co-substrate UTP

proof_lines: wild type enzyme with ATP as phosphate donor, 37°C, pH 7.5

substrate: gemcitabine


proof_lines:
cytosine arabinoside-induced cells
cosubstrate ATP, 37°C, pH 7.6
cosubstrate UTP, 37°C, pH 7.6


organism: Aeromonas hydrophila

substrate_name: benzylpenicillin

assay_conditions_summary: pH 6.5; 303.15 K; buffer 20 mM sodium cacodylate

proof_lines: mutant enzyme N116H/N220G, in 20 mM sodium cacodylate buffer, pH 6.5

substrate: benzylpenicillin


substrate_name: biapenem

proof_lines:
above, V67I mutant, 30°C, pH 6.5
V67I mutant, 30°C, pH 6.5

substrate: biapenem


proof_lines:
above, V67D mutant, 30°C, pH 6.5
V67D mutant, 30°C, pH 6.5


proof_lines:
T157A mutant, 30°C, pH 6.5
above, T157A mutant, 30°C, pH 6.5


substrate_name: nitrocefin

substrate: nitrocefin


proof_lines:
above, K224Q mutant, 30°C, pH 6.5
K224Q mutant, 30°C, pH 6.5


proof_lines:
above, H263A mutant, 30°C, pH 6.5
H263A mutant, 30°C, pH 6.5


proof_lines:
above, H196A mutant, 30°C, pH 6.5
H196A mutant, 30°C, pH 6.5


proof_lines:
H118A mutant, 30°C, pH 6.5
above, H118A mutant, 30°C, pH 6.5


substrate_name: H2O; Ampicillin

substrate: H2O; Ampicillin


organism: Aeromonas veronii

substrate_name: Unknown

sequence_source: UniProtKB:O31272 direct REST lookup 2026-06-28

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Aeromonas veronii bv. sobria


organism: Achromobacter sp. sallbros1

substrate_name: piperacillin

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for E7BCS7

proof_lines:
pH 7.2, 25°C
or below, pH 7.2, 25°C

substrate: piperacillin


organism: Achromobacter xylosoxidans

substrate_name: cephalothin

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for B3FIE3

proof_lines: Km above 2 mM, in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C

substrate: cephalothin


substrate_name: ampicillin

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for Q5QT35

proof_lines:
37°C, pH 7.0
Raw SKiD Env: Temp=37°C, pH=7

substrate: ampicillin


substrate_name: ticarcillin

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for Q5I2N2

substrate: ticarcillin


proof_lines: pH 7.2, temperature not specified in the publication, recombinant enzyme


substrate_name: Imipenem

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for Q9L4P2

proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, wild-type enzyme

proof_lines: 25°C, pH not specified in the publication, without sodium bicarbonate, wild-type enzyme

proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, wild-type 0.85 enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); reconstructed from Q9L4P2 canonical sequence by applying W165A at 1-based canonical residue 165 and applied mutation signature W165A to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, mutant enzyme W165A


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

proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, mutant enzyme W166A

proof_lines: 25°C, pH not specified in the publication, without sodium bicarbonate, mutant enzyme W166A


organism: Acinetobacter baylyi

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for Q0VJU2


organism: Acinetobacter bereziniae

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for I6S7G0

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


organism: Acinetobacter pittii

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for Q7WZ37


organism: Aeromonas enteropelogenes

substrate_name: cefotaxime

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for B2BSN6

substrate: cefotaxime


substrate_name: H2O; Imipenem

sequence_source: UniProtKB REST release 2026_02 (API deployment 2026-06-12; checked 2026-06-28); direct exact accession lookup for P26918

proof_lines:
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=-----, pH=9
Raw SKiD Env: Temp=30°C, pH=6.5

substrate: H2O; Imipenem


assay_conditions_summary: pH 8; 303.15 K; buffer 20 mM sodium cacodylate

proof_lines:
wild type enzyme, at pH 8.0
wild type enzyme, at pH 9.0
wild-type, 30°C, pH 6.5

substrate: Imipenem


enzyme_display_name: Beta-lactamase OXA-9

organism: Enterobacter aerogenes

substrate_name: H2O; Nitrocefin

enzyme: Beta-lactamase OXA-9

substrate: H2O; Nitrocefin


organism: Enterobacter cloacae

substrate_name: Cefotaxime; H2O

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

assay_conditions_summary: pH 7; 303.15 K; buffer 50mM sodium phosphate

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

proof_lines: at 30°C in 50mM sodium phosphate buffer (pH 7.0)

source_databases_merged: sabio_rk brenda skid

substrate: Cefotaxime; H2O


substrate_name: ceftazidime

substrate: ceftazidime


substrate_name: 7-aminocephalosporanic acid

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

substrate: 7-aminocephalosporanic acid


enzyme_display_name: Imipenem-hydrolyzing beta-lactamase

substrate_name: Penicillin G; H2O

enzyme: Imipenem-hydrolyzing beta-lactamase

substrate: Penicillin G; H2O


organism: Escherichia coli

substrate_name: H2O; Cephaloridine

substrate: H2O; Cephaloridine


enzyme_display_name: Beta-lactamase Toho-1

substrate_name: Benzylpenicillin; H2O

enzyme: Beta-lactamase Toho-1

substrate: Benzylpenicillin; H2O


substrate_name: cefpirome

substrate: cefpirome


enzyme_display_name: Beta-lactamase TEM

proof_lines: wild-type inhibitor protein, pH 7.5, 25°C

enzyme: Beta-lactamase TEM


enzyme_display_name: Beta-lactamase CTX-M-25

substrate_name: H2O; Benzylpenicillin

enzyme: Beta-lactamase CTX-M-25

substrate: H2O; Benzylpenicillin


substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


enzyme_display_name: Beta-lactamase OXA-1

enzyme: Beta-lactamase OXA-1


substrate_name: cefepime

substrate: cefepime


sequence_source: UniProt direct accession check P13661


proof_lines: His6-tagged wild type OXA-1, pH 7.4, room temperature


substrate_name: cefalotin

sequence_source: UniProt direct accession check P28585

substrate: cefalotin


sequence_variant_note: Resolved canonical sequence from UniProt direct accession check P28585 plus mutation R276W and applied mutation signature R276W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt direct accession check P28585 plus mutation R276C and applied mutation signature R276C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt direct accession check P28585 plus mutation R276G and applied mutation signature R276G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt direct accession check P28585 plus mutation R276N and applied mutation signature R276N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt direct accession check P28585 plus mutation R276S and applied mutation signature R276S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt direct accession check P28585 plus mutation R276H and applied mutation signature R276H to reconstruct the assayed variant sequence.


substrate_name: CENTA; H2O

sequence_source: UniProt direct accession check Q9S169

substrate: CENTA; H2O


substrate_name: cephalothin

sequence_source: UniProt direct accession check A3RIY0

proof_lines: 30°C, pH 7.0. The affinity of MIR-4 beta-lactamase for ceftazidime is quite low

substrate: cephalothin


substrate_name: Imipenem

sequence_source: UniProt direct accession check P00811

proof_lines:
mutant AmpC-A-S287N
mutant AmpC-B2-S287N


proof_lines:
wild-type AmpC-A
wild-type AmpC-B2


sequence_source: UniProtKB direct accession lookup J7I0S9 on 2026-06-28; J7I0S9_ECOLX; unreviewed


sequence_source: UniProtKB direct accession lookup M1VE66 on 2026-06-28; M1VE66_ECOLX; unreviewed

proof_lines:
pH 7.2, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=7.2


substrate_name: cefoxitin

sequence_source: UniProtKB direct accession lookup H6WET3 on 2026-06-28; H6WET3_ECOLX; unreviewed

substrate: cefoxitin


substrate_name: nitrocefin

sequence_source: UniProtKB direct accession lookup I3VKD5 on 2026-06-28; I3VKD5_ECOLX; unreviewed

substrate: nitrocefin


sequence_source: UniProtKB direct accession lookup H6WZS9 on 2026-06-28; H6WZS9_ECOLX; unreviewed


sequence_source: UniProtKB direct accession lookup P00811 on 2026-06-28; AMPC_ECOLI; reviewed

proof_lines:
pH 6.5, 22°C
Raw SKiD Env: Temp=-----, pH=-----


substrate_name: H2O; Cefuroxime

sequence_source: UniProtKB direct accession lookup Q6SJ61 on 2026-06-28; Q6SJ61_ECOLX; unreviewed

substrate: H2O; Cefuroxime


substrate_name: H2O; Ampicillin

sequence_source: UniProtKB direct accession lookup P62593 on 2026-06-28; BLAT_ECOLX; reviewed

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

substrate: H2O; Ampicillin


sequence_source: UniProtKB direct accession lookup P28585 on 2026-06-28; BLC1_ECOLX; reviewed


organism: Fluoribacter gormanii

sequence_source: UniProtKB direct accession lookup Q9K578 on 2026-06-28; Q9K578_9GAMM; unreviewed


organism: Fusobacterium nucleatum

substrate_name: ampicillin

sequence_source: UniProtKB direct accession lookup Q6XL56 on 2026-06-28; Q6XL56_FUSNU; unreviewed

substrate: ampicillin


organism: Homo sapiens

substrate_name: H2O; Cefotaxime

substrate: H2O; Cefotaxime


substrate_name: H2O; Imipenem

sequence_source: UniProtKB direct accession lookup P16444 on 2026-06-28; DPEP1_HUMAN; reviewed

substrate: H2O; Imipenem


organism: Klebsiella aerogenes

substrate_name: Unknown

substrate: Unknown


substrate_name: benzylpenicillin

sequence_source: UniProtKB direct accession lookup Q1KY81 on 2026-06-28; Q1KY81_KLEAE; unreviewed

proof_lines: 100 microM nitrocefin as the reporter substrate, TEM-149 wild-type, pH 7.0, 25°C

substrate: benzylpenicillin


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB REST exact accession lookup: Q79MP6 (Q79MP6_PSEAI); retrieved 2026-06-28


substrate_name: ertapenem

sequence_source: UniProtKB REST exact accession lookup: Q840P9 (BLBV7_PSEAI); retrieved 2026-06-28

substrate: ertapenem


sequence_source: UniProtKB REST exact accession lookup: Q9XAY4 (Q9XAY4_PSEAI); retrieved 2026-06-28


sequence_source: UniProtKB REST exact accession lookup: Q2HY42 (Q2HY42_PSEAI); retrieved 2026-06-28


substrate_name: ceftazidime

sequence_source: UniProtKB REST exact accession lookup: Q7WYA8 (BLAB_PSEAI); retrieved 2026-06-28

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

substrate: ceftazidime


substrate_name: cephalotin

sequence_source: UniProtKB REST exact accession lookup: Q5U807 (Q5U807_PSEAI); retrieved 2026-06-28

substrate: cephalotin


sequence_source: UniProtKB REST exact accession lookup: Q8KRJ3 (Q8KRJ3_PSEAI); retrieved 2026-06-28


substrate_name: H2O; Nitrocefin

sequence_source: UniProtKB REST exact accession lookup: P24735 (AMPC_PSEAE); retrieved 2026-06-28

substrate: H2O; Nitrocefin


substrate_name: H2O; Penicillin G

sequence_source: UniProtKB REST exact accession lookup: P37321 (BLE1_PSEAI); retrieved 2026-06-28

substrate: H2O; Penicillin G


organism: Pseudomonas fluorescens

substrate_name: carbenicillin

sequence_source: UniProtKB REST exact accession lookup: P85302 (AMPC_PSEFL); retrieved 2026-06-28

substrate: carbenicillin


organism: Pseudomonas luteola

substrate_name: ticarcillin

sequence_source: UniProtKB REST exact accession lookup: Q670S6 (Q670S6_PSELU); retrieved 2026-06-28

proof_lines: pH and temperature not specified in the publication

substrate: ticarcillin


organism: Pseudomonas putida

substrate_name: cefepime

sequence_source: UniProtKB REST exact accession lookup: Q8GIW8 (Q8GIW8_PSEPU); retrieved 2026-06-28

substrate: cefepime


sequence_source: UniProtKB REST exact accession lookup: Q8GCU7 (Q8GCU7_PSEPU); retrieved 2026-06-28

proof_lines: enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin

proof_lines: inhibitor binding constant (Ki) using 10 microM nitrocefin as indicator substrate


organism: Riemerella anatipestifer

sequence_source: UniProtKB REST exact accession lookup: J9QX37 (J9QX37_RIEAN); retrieved 2026-06-28


organism: Serratia fonticola

substrate_name: moxalactam

sequence_source: UniProtKB REST exact accession lookup: Q9RMI1 (Q9RMI1_SERFO); retrieved 2026-06-28

proof_lines:
pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7

substrate: moxalactam


substrate_name: H2O; Benzylpenicillin

sequence_source: UniProtKB REST exact accession lookup: P80545 (BLAC_SERFO); retrieved 2026-06-28

substrate: H2O; Benzylpenicillin


sequence_source: UniProtKB REST direct accession lookup: Q1KY81

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +2, so it is treated as a source-provided variant sequence.

proof_lines: 100 microM nitrocefin as the reporter substrate, TEM-149 mutant T182M, pH 7.0, 25°C


organism: Klebsiella oxytoca

sequence_source: UniProtKB REST direct accession lookup: Q9S534


organism: Klebsiella pneumoniae

sequence_source: UniProtKB REST direct accession lookup: P0AD64


sequence_source: UniProtKB REST direct accession lookup: Q8GD10


substrate_name: ceftaxidime

sequence_source: UniProtKB REST direct accession lookup: Q09HD0

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM sodium phosphate

proof_lines: at 30°C in 100 mM sodium phosphate buffer, pH 7.0

substrate: ceftaxidime


substrate_name: aztreonam

sequence_source: UniProtKB REST direct accession lookup: Q4TVR4

substrate: aztreonam


substrate_name: cefalothin

sequence_source: UniProtKB REST direct accession lookup: A1EGT8

substrate: cefalothin


substrate_name: temocillin

sequence_source: UniProtKB REST direct accession lookup: Q6XEC0

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

substrate: temocillin


substrate_name: ampicillin

sequence_source: UniProtKB REST direct accession lookup: Q8KQ59

substrate: ampicillin


substrate_name: Unknown

substrate: Unknown


substrate_name: nitrocefin

sequence_source: UniProtKB REST direct accession lookup: Q9F918

column_label: Retained official OUP PDF Table 3, Nitrocefin row, wild-type SHV-14 column: Km 45 +/- 1.7; kcat 5.85 +/- 0.2; kcat/Km 0.13.

normalized_value_unit_evidence: Km 45 uM normalizes to 0.045 mM; kcat is 5.85 s^-1; independently printed kcat/Km 0.13 s^-1 uM^-1 normalizes to 130 s^-1 mM^-1.

raw_value_unit_evidence: Table 3 Nitrocefin wild-type SHV-14 column: Km 45 +/- 1.7 uM; kcat 5.85 +/- 0.2 s^-1; independently printed kcat/Km 0.13 s^-1 uM^-1.

row_label: Nitrocefin / SHV-14

table_label: Table 3. Kinetics analysis of SHV-14 and its mutated proteins

substrate: nitrocefin


substrate_name: piperacillin

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup: Q9F918 and applied mutation signature E164A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant His-tagged mutant E164A

substrate: piperacillin


substrate_name: cefoperazone

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup: Q9F918 and applied mutation signature E162A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant His-tagged mutant E162A

substrate: cefoperazone


substrate_name: H2O; Imipenem

sequence_source: UniProtKB REST direct accession lookup: E9NWK5

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

substrate: H2O; Imipenem


substrate_name: Nitrocefin; H2O

sequence_source: UniProtKB REST direct accession lookup: C7C422

substrate: Nitrocefin; H2O


substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


substrate_name: ATP; 2'-Deoxycytidine

sequence_source: UniProtKB:O00142; direct REST lookup on 2026-06-28

assay_conditions_summary: cofactor ATP

substrate: ATP; 2'-Deoxycytidine


sequence_source: UniProtKB:P27707; direct REST lookup on 2026-06-28

proof_lines:
cosubstrate ATP, pH 7.5, 37°C
cosubstrate UTP, pH 7.5, 37°C
with ATP as cosubstrate


organism: Lactobacillus acidophilus

substrate_name: ATP; Deoxycytidine

substrate: ATP; Deoxycytidine


organism: Macaca fascicularis

sequence_source: UniProtKB:Q4R5R5; direct REST lookup on 2026-06-28


organism: Mus musculus

sequence_source: UniProtKB:P43346; direct REST lookup on 2026-06-28


organism: Mycoplasma mycoides

sequence_source: UniProtKB:Q93IG4; direct REST lookup on 2026-06-28


organism: Rattus norvegicus

sequence_source: UniProtKB:P48769; direct REST lookup on 2026-06-28


organism: Xenopus laevis

substrate_name: deoxyguanosine

sequence_source: UniProtKB:A0A1L8HV70; direct REST lookup on 2026-06-28

assay_conditions_summary: pH 8

proof_lines: at pH 8.0, temperature not specified in the publication

substrate: deoxyguanosine


substrate_name: ATP; 5-Hydroxy-L-lysine

sequence_source: UniProtKB:A2RU49; direct REST lookup on 2026-06-28

assay_conditions_summary: pH 7.1; 303.15 K; cofactor ATP

proof_lines:
cosubstrate ATP, pH 7.1, 30°C
pH 7.1, 30°C
cosubstrate GTP, pH 7.1, 30°C

substrate: ATP; 5-Hydroxy-L-lysine


organism: Burkholderia pseudomallei

substrate_name: D-glucose 1-phosphate

sequence_source: UniProtKB:Q63R79; direct REST lookup on 2026-06-28

substrate: D-glucose 1-phosphate


substrate_name: GTP

substrate: GTP


organism: Yersinia pseudotuberculosis

sequence_source: UniProtKB:Q8GJ90; direct REST lookup on 2026-06-28

proof_lines: recombinant His6-tagged enzyme, pH 7.5, 22°C, with alpha-D-mannose 1-phosphate


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


organism: Mycolicibacterium smegmatis

substrate_name: Bocillin-FL

sequence_variant_note: Resolved canonical sequence from UniProtKB:A0R0P0 plus E193A reconstruction and applied mutation signature E193A to reconstruct the assayed variant sequence.

substrate: Bocillin-FL


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0R0P0 plus Y194F reconstruction and applied mutation signature Y194F to reconstruct the assayed variant sequence.


organism: Nocardia asteroides

substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


organism: Nocardia farcinica

unit: uM/s


organism: Ochrobactrum anthropi


organism: Pectobacterium carotovorum

substrate_name: cefoxitin

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

substrate: cefoxitin


organism: Proteus mirabilis


organism: Providencia stuartii


organism: Pseudomonas aeruginosa

substrate_name: carbenicillin

substrate: carbenicillin


substrate_name: cephalotin

substrate: cephalotin


substrate_name: cefotaxime

substrate: cefotaxime


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


organism: Klebsiella pneumoniae

sequence_source: UniProtKB direct accession lookup P0A3M1 (BLA5_KLEPN); retrieved 2026-06-28


substrate_name: Imipenem

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

substrate: Imipenem


organism: Klebsiella pneumoniae subsp. ozaenae

sequence_source: UniProtKB direct accession lookup P0A9Z9 (BLA2_KLEPO); retrieved 2026-06-28


organism: Kluyvera ascorbata


organism: Laribacter hongkongensis

substrate_name: cephalothin

sequence_source: UniProtKB direct accession lookup Q6GVZ4 (Q6GVZ4_9NEIS); retrieved 2026-06-28

substrate: cephalothin


organism: Metapseudomonas otitidis

sequence_source: UniProtKB direct accession lookup E6Y3G9 (E6Y3G9_9GAMM); retrieved 2026-06-28

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


organism: Moraxella catarrhalis

substrate_name: Amoxicillin; H2O

sequence_source: UniProtKB direct accession lookup Q49095 (Q49095_MORCA); retrieved 2026-06-28

substrate: Amoxicillin; H2O


sequence_source: UniProtKB direct accession lookup Q59514 (BLA1_MORCA); retrieved 2026-06-28


organism: Morganella morganii

substrate_name: H2O; Ampicillin

sequence_source: UniProtKB direct accession lookup Q704Y9 (Q704Y9_MORMO); retrieved 2026-06-28

substrate: H2O; Ampicillin


sequence_source: UniProtKB direct accession lookup Q705J0 (Q705J0_MORMO); retrieved 2026-06-28


substrate_name: Benzylpenicillin; H2O

sequence_source: UniProtKB direct accession lookup Q704Z0 (Q704Z0_MORMO); retrieved 2026-06-28

substrate: Benzylpenicillin; H2O


organism: Morganella morganii subsp. morganii

assay_conditions_summary: pH 7; 303.15 K; buffer 20 mM phosphate

proof_lines: in 20 mM phosphate buffer, (pH 7.0) at 30°C


substrate_name: piperacillin

substrate: piperacillin


organism: Mycobacterium tuberculosis

substrate_name: H2O; Nitrocefin

sequence_source: UniProtKB direct accession lookup P9WKD3 (BLAC_MYCTU); retrieved 2026-06-28

substrate: H2O; Nitrocefin


sequence_source: UniProtKB direct accession lookup A5U493 (BLAC_MYCTA); retrieved 2026-06-28


organism: Serratia marcescens

substrate_name: nitrocefin

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P52699 canonical sequence using PMID 15788415 Asp-120(81) plus UniProt chain 19-246 mapping and applied mutation signature D120E with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D120E, 1 mM Zn(NO3)2 added

substrate: nitrocefin


substrate_name: benzylpenicillin

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P52699 canonical sequence using PMID 15788415 Asp-120(81) plus UniProt chain 19-246 mapping and applied mutation signature D120A with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D120A, 1 mM Zn(NO3)2 added

substrate: benzylpenicillin


substrate_name: H2O; Cephaloridine

sequence_source: UniProt exact accession Q7DHD4 canonical sequence, REST lookup 2026-06-28

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

substrate: H2O; Cephaloridine


sequence_source: UniProt exact accession P52699 canonical sequence, REST lookup 2026-06-28

proof_lines:
wild-type enzyme
wild-type value


sequence_source: UniProt exact accession P52682 canonical sequence, REST lookup 2026-06-28


sequence_source: UniProt exact accession P18539 canonical sequence, REST lookup 2026-06-28


proof_lines:
pH 7.5, 25°C
at 30°C
Raw SKiD Env: Temp=25°C, pH=7.5


organism: Shewanella algae

sequence_source: UniProt exact accession Q6VCW0 canonical sequence, REST lookup 2026-06-28


organism: Shewanella frigidimarina

substrate_name: H2O; Amoxicillin

sequence_source: UniProt exact accession Q53BU0 canonical sequence, REST lookup 2026-06-28

substrate: H2O; Amoxicillin


organism: Shewanella livingstonensis

sequence_source: UniProt exact accession Q53BU1 canonical sequence, REST lookup 2026-06-28


organism: Shigella sonnei

sequence_source: UniProt exact accession A5LH21 canonical sequence, REST lookup 2026-06-28


organism: Shouchella clausii

substrate_name: ceftazidime

sequence_source: UniProt exact accession A8RR46 canonical sequence, REST lookup 2026-06-28

proof_lines: kcat above than 3.3/sec at 30°C in 100 mM sodium phosphate (pH 7)

proof_lines: kcat less than 0.3/sec at 30°C in 100 mM sodium phosphate (pH 7)

substrate: ceftazidime


organism: Shouchella lehensis

substrate_name: ampicilin

substrate: ampicilin


organism: Staphylococcus aureus

sequence_source: UniProt exact accession P00807 canonical sequence, REST lookup 2026-06-28


organism: Stenotrophomonas maltophilia

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


substrate_name: ampicillin

sequence_source: UniProt exact accession P52700 canonical sequence, REST lookup 2026-06-28

proof_lines:
wild-type enzyme, pH 7.0, 25°C
wild-typewith 1.90 equiv of Zn(2+)

substrate: ampicillin


organism: Arabidopsis thaliana

substrate_name: ADP

sequence_source: UniProtKB:Q9FFP6 REST lookup 2026-06-28

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

substrate: ADP


sequence_source: UniProtKB:Q9FM97 REST lookup 2026-06-28


sequence_source: UniProtKB:Q94KE3 REST lookup 2026-06-28


sequence_source: UniProtKB:Q9SJQ0 REST lookup 2026-06-28


sequence_source: UniProtKB:Q9FNN1 REST lookup 2026-06-28


organism: Corynebacterium glutamicum

sequence_source: UniProtKB:Q46078 REST lookup 2026-06-28

assay_conditions_summary: pH 7; 308.15 K; cofactor ADP


sequence_source: UniProtKB:Q8NLN1 REST lookup 2026-06-28


organism: Entamoeba histolytica

substrate_name: phosphoenolpyruvate

sequence_source: UniProtKB:C4LXC4 REST lookup 2026-06-28

substrate: phosphoenolpyruvate


sequence_source: UniProtKB:P52700 REST lookup on 2026-06-28

proof_lines: lactamase ZnFe-L1, 1.0 Zn(2+), 1.0 Fe(3+)


substrate_name: Unknown

sequence_source: UniProtKB:E9RIT0 REST lookup on 2026-06-28 returned inactive/deleted record without replacement sequence

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


sequence_source: UniProtKB:O51899 REST lookup on 2026-06-28; source token was (O51899)*4


organism: Treponema pallidum

substrate_name: Penicillin G; H2O

sequence_source: UniProtKB:P29723 REST lookup on 2026-06-28 found a live accession, but its EC/name contradict EC 3.5.2.6 beta-lactamase

substrate: Penicillin G; H2O


organism: Yersinia enterocolitica

substrate_name: cefalotin

sequence_source: UniProtKB:Q01166 REST lookup on 2026-06-28

substrate: cefalotin


organism: Yersinia ruckeri

substrate_name: cefuroxime

sequence_source: UniProtKB:Q20I87 REST lookup on 2026-06-28

substrate: cefuroxime


organism: Homo sapiens

substrate_name: Phosphoenolpyruvate; ADP

sequence_source: UniProtKB:P14618 direct accession lookup

assay_conditions_summary: pH 8; 305.15 K; cofactor ATP

proof_lines: pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate

proof_lines: Zn2+ bound to the ADP-binding site of the free enzyme, pH 7.4, 37°C

substrate: Phosphoenolpyruvate; ADP


proof_lines: Y235F mutant, Vmax = 0.6 micromol/min/mg


proof_lines: Y235S mutant, Vmax = 1.2 micromol/min/mg


proof_lines: wild type enzyme, in the presence of 2.5 mM D-fructose 1,6-bisphosphate

proof_lines: wild type enzyme, in the absence of D-fructose 1,6-bisphosphate


proof_lines: Y235A mutant, Vmax = 1.1 micromol/min/mg


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14618 reconstructed substitution H391Y and applied mutation signature H391Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H391Y, in the presence of 2.5 mM D-fructose 1,6-bisphosphate

proof_lines: mutant enzyme H391Y, in the absence of D-fructose 1,6-bisphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14618 reconstructed substitution K422R and applied mutation signature K422R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K422R, in the absence of D-fructose 1,6-bisphosphate

proof_lines: mutant enzyme K422R, in the presence of 2.5 mM D-fructose 1,6-bisphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30613-2 reconstructed substitution C436M and applied mutation signature C436M to reconstruct the assayed variant sequence.

proof_lines: mutant C436M, pH not specified in the publication, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30613-2 reconstructed substitution C436H and applied mutation signature C436H to reconstruct the assayed variant sequence.

proof_lines: mutant C436H, pH not specified in the publication, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30613-2 reconstructed substitution C436S and applied mutation signature C436S to reconstruct the assayed variant sequence.

proof_lines: mutant C436S, pH not specified in the publication, 30°C


sequence_source: UniProtKB:P30613 direct accession lookup

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30613-2 reconstructed substitution S12D and applied mutation signature S12D to reconstruct the assayed variant sequence.

proof_lines: mutant S12D, pH not specified in the publication, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30613-2 reconstructed substitution C436D and applied mutation signature C436D to reconstruct the assayed variant sequence.

proof_lines: mutant C436D, pH not specified in the publication, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30613-2 reconstructed substitution C436N and applied mutation signature C436N to reconstruct the assayed variant sequence.

proof_lines: mutant C436N, pH not specified in the publication, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30613-2 reconstructed substitution C436A and applied mutation signature C436A to reconstruct the assayed variant sequence.

proof_lines: mutant C436A, pH not specified in the publication, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30613-2 reconstructed substitution C436T and applied mutation signature C436T to reconstruct the assayed variant sequence.

proof_lines: mutant C436T, pH not specified in the publication, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST https://rest.uniprot.org/uniprotkb/P14618.json; primaryAccession=P14618; entryType=UniProtKB reviewed (Swiss-Prot); organism=Homo sapiens; protein=Pyruvate kinase PKM; EC=2.7.1.40; sequence_length=531 aa. Variant sequence reconstructed by changing canonical residue 415 from G to R from the selected paper/source note PKM2G415R. and applied mutation signature G415R to reconstruct the assayed variant sequence.


substrate_name: ADP; Phosphoenolpyruvate

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/P30613.json; primaryAccession=P30613; entryType=UniProtKB reviewed (Swiss-Prot); organism=Homo sapiens; protein=Pyruvate kinase PKLR; EC=2.7.1.40; sequence_length=574 aa.

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

assay_conditions_summary: cofactor ADP

substrate: ADP; Phosphoenolpyruvate


sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/P14618.json; primaryAccession=P14618; entryType=UniProtKB reviewed (Swiss-Prot); organism=Homo sapiens; protein=Pyruvate kinase PKM; EC=2.7.1.40; sequence_length=531 aa.


organism: Lactococcus lactis subsp. cremoris

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/A2RKA3.json; primaryAccession=A2RKA3; entryType=UniProtKB unreviewed (TrEMBL); organism=Lactococcus lactis subsp. cremoris (strain MG1363); protein=Pyruvate kinase; EC=2.7.1.40; sequence_length=502 aa.


organism: Lactococcus lactis subsp. lactis

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/Q07637.json; primaryAccession=Q07637; entryType=UniProtKB reviewed (Swiss-Prot); organism=Lactococcus lactis subsp. lactis (strain IL1403); protein=Pyruvate kinase; EC=2.7.1.40; sequence_length=502 aa.


organism: Leishmania mexicana

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/Q27686.json; primaryAccession=Q27686; entryType=UniProtKB reviewed (Swiss-Prot); organism=Leishmania mexicana; protein=Pyruvate kinase; EC=2.7.1.40; sequence_length=499 aa.

assay_conditions_summary: pH 7.5; cofactor ADP


sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/Q27686.json; primaryAccession=Q27686; entryType=UniProtKB reviewed (Swiss-Prot); organism=Leishmania mexicana; protein=Pyruvate kinase; EC=2.7.1.40; sequence_length=499 aa. Sequence retained as context only; row-specific full/variant sequence remains unresolved.


organism: Mus musculus

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/P53657.json; primaryAccession=P53657; entryType=UniProtKB reviewed (Swiss-Prot); organism=Mus musculus; protein=Pyruvate kinase PKLR; EC=2.7.1.40; sequence_length=574 aa.


sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/P52480.json; primaryAccession=P52480; entryType=UniProtKB reviewed (Swiss-Prot); organism=Mus musculus; protein=Pyruvate kinase PKM; EC=2.7.1.40; sequence_length=531 aa.


organism: Oncorhynchus mykiss

substrate_name: Phosphoenolpyruvate; Phosphate; AMP

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/Q98TA0.json; primaryAccession=Q98TA0; entryType=UniProtKB unreviewed (TrEMBL); organism=Oncorhynchus mykiss; protein=pyruvate kinase; EC=2.7.1.40; sequence_length=122 aa. Sequence retained as context only; row-specific full/variant sequence remains unresolved.

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

substrate: Phosphoenolpyruvate; Phosphate; AMP


organism: Oryctolagus cuniculus

substrate_name: Phosphoenolpyruvate; dADP

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/P11974.json; primaryAccession=P11974; entryType=UniProtKB reviewed (Swiss-Prot); organism=Oryctolagus cuniculus; protein=Pyruvate kinase PKM; EC=2.7.1.40; sequence_length=531 aa.

substrate: Phosphoenolpyruvate; dADP


organism: Plasmodium falciparum

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/C6KTA4.json; primaryAccession=C6KTA4; entryType=UniProtKB unreviewed (TrEMBL); organism=Plasmodium falciparum (isolate 3D7); protein=Pyruvate kinase; EC=2.7.1.40; sequence_length=511 aa.

proof_lines: in presence of inhibitor suramin, pH and temperature not specified in the publication


organism: Rattus norvegicus

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/P11980.json; primaryAccession=P11980; entryType=UniProtKB reviewed (Swiss-Prot); organism=Rattus norvegicus; protein=Pyruvate kinase PKM; EC=2.7.1.40; sequence_length=531 aa.


sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/P12928.json; primaryAccession=P12928; entryType=UniProtKB reviewed (Swiss-Prot); organism=Rattus norvegicus; protein=Pyruvate kinase PKLR; EC=2.7.1.40; sequence_length=574 aa.


sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/B1WBN9.json; primaryAccession=B1WBN9; entryType=UniProtKB unreviewed (TrEMBL); organism=Rattus norvegicus; protein=Pyruvate kinase; EC=2.7.1.40; sequence_length=543 aa.


organism: Bacillus licheniformis

substrate_name: H2O; Phenoxymethylpenicillin

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----

substrate: H2O; Phenoxymethylpenicillin


substrate_name: penicillin G

proof_lines: mutant E166C, carrying 6-bromoacetyl-2-dimethylaminonaphthalene label, pH 7.0, 22°C

substrate: penicillin G


organism: Bacteroides fragilis

proof_lines: pH and temperature not specified in the publication


organism: Brachyspira pilosicoli

substrate_name: carbenicillin

proof_lines: at 25°C in 100 mM sodium phosphate (pH 7.0)

substrate: carbenicillin


organism: Burkholderia cenocepacia

substrate_name: ticarcillin

substrate: ticarcillin


organism: Burkholderia pseudomallei

substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


organism: Chryseobacterium indologenes

substrate_name: Sulbactam

assay_conditions_summary: pH 6.5; buffer 30 mM sodium cacodylate

proof_lines: in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4

substrate: Sulbactam


organism: Citrobacter diversus

substrate_name: H2O; Benzylpenicillin

substrate: H2O; Benzylpenicillin


organism: Citrobacter freundii

substrate_name: Imipenem

substrate: Imipenem


organism: Stenotrophomonas maltophilia

substrate_name: biapenem

proof_lines:
mutant D120C, pH 7.0, 25°C
below, mutant D120C, pH 7.0, 25°C

substrate: biapenem


proof_lines:
mutant D120S, pH 7.0, 25°C
below, mutant D120S, pH 7.0, 25°C


substrate_name: Nitrocefin; H2O

substrate: Nitrocefin; H2O


substrate_name: nitrocefin

proof_lines:
H116C, not applicable Zn(2+) content
H116C with 0.85 equiv of Zn(2+)

substrate: nitrocefin


proof_lines:
H121C with 0.98 equiv of Zn(2+)
H121C, not applicable Zn(2+) content


organism: Saccharolobus solfataricus

substrate_name: phosphoenolpyruvate

sequence_source: UniProtKB:Q97ZD7 direct accession check (2026-06-28)

assay_conditions_summary: 343.15 K; cofactor ADP

proof_lines: 70°C, pH not specified in the publication

proof_lines: 50°C, pH not specified in the publication

proof_lines: 65°C, pH not specified in the publication

substrate: phosphoenolpyruvate


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P52489 direct accession check (2026-06-28)


organism: Selenomonas ruminantium

sequence_source: UniProtKB:Q9LBS6 direct accession check (2026-06-28)

assay_conditions_summary: pH 7; cofactor ATP


organism: Thermofilum pendens

substrate_name: ADP

sequence_source: UniProtKB:A1RX09 direct accession check (2026-06-28)

assay_conditions_summary: pH 6; 318.15 K; cofactor ADP

proof_lines: pH 6.0, 45°C, recombinant enzyme with His6 tag

substrate: ADP


organism: Toxoplasma gondii

substrate_name: Unknown

sequence_source: UniProtKB exact accession Q969A2 canonical sequence via rest.uniprot.org, checked 2026-06-28

substrate: Unknown


organism: Trachemys scripta elegans

sequence_source: UniProtKB exact accession Q9I8C5 canonical sequence via rest.uniprot.org, checked 2026-06-28

assay_conditions_summary: pH 6.6; 295.15 K; cofactor ADP

proof_lines:
anoxic muscle enzyme, pH 6.6, 22°C
muscle enzyme, pH 7.2, 22°C
muscle enzyme, pH 6.6, 22°C


sequence_source: UniProtKB exact accession Q9PU23 canonical sequence via rest.uniprot.org, checked 2026-06-28

assay_conditions_summary: pH 7.2; 295.15 K; cofactor ADP

proof_lines:
liver enzyme, pH 7.2, 22°C
anoxic liver enzyme, pH 7.2, 22°C
liver enzyme, pH 6.6, 22°C


organism: Trichomonas vaginalis

substrate_name: Phosphoenolpyruvate; ADP

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

substrate: Phosphoenolpyruvate; ADP


organism: Trypanosoma brucei


organism: Trypanosoma brucei brucei

sequence_source: UniProtKB exact accession P30615 canonical sequence via rest.uniprot.org, checked 2026-06-28

proof_lines: recombinant enzyme, pH 7.2, 25°C, in presence of fructose 1,6-bisphosphate

proof_lines: recombinant enzyme, pH 7.2, 25°C, in presence of fructose 2,6-bisphosphate


organism: Trypanosoma congolense

sequence_source: UniProtKB exact accession G0UYF4 canonical sequence via rest.uniprot.org, checked 2026-06-28


organism: Ustilago maydis

sequence_source: UniProtKB exact accession A0A0D1E735 canonical sequence via rest.uniprot.org, checked 2026-06-28


organism: Vibrio cholerae serotype O1

sequence_source: UniProtKB exact accession Q9KUN0 canonical sequence via rest.uniprot.org, checked 2026-06-28

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

proof_lines: pH 7.0, 25°C, recombinant non-His-tagged enzyme

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme, in presence of fructose 1,6-bisphosphate


sequence_source: UniProtKB exact accession Q9KQJ0 canonical sequence via rest.uniprot.org, checked 2026-06-28

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme, in presence of glucose 6-phosphate


organism: Zymomonas mobilis

sequence_source: UniProtKB exact accession Q5NR78 canonical sequence via rest.uniprot.org, checked 2026-06-28


organism: Aeromonas veronii bv. sobria

sequence_source: UniProtKB exact accession O31272 canonical sequence via rest.uniprot.org, checked 2026-06-28


organism: Aliivibrio salmonicida

sequence_source: UniProtKB exact accession B6EPH0 canonical sequence via rest.uniprot.org, checked 2026-06-28

proof_lines: pH 7.2, 37°C, recombinant enzyme, in presence of NaCl


organism: Bacillus cereus

substrate_name: H2O; Cefotaxime

sequence_source: UniProtKB exact accession P04190 canonical sequence via rest.uniprot.org, checked 2026-06-28

substrate: H2O; Cefotaxime


substrate_name: 6-Aminopenicillanate; H2O

sequence_source: UniProtKB exact accession P00809 canonical sequence via rest.uniprot.org, checked 2026-06-28

substrate: 6-Aminopenicillanate; H2O


substrate_name: H2O; Ampicillin

sequence_source: UniProtKB exact accession P14488 canonical sequence via rest.uniprot.org, checked 2026-06-28

substrate: H2O; Ampicillin


enzyme_display_name: thioredoxin-disulfide reductase (NADPH)

organism: Drosophila melanogaster

enzyme: thioredoxin-disulfide reductase (NADPH)


organism: Mus musculus

substrate_name: 5,5'-dithiobis(2-nitrobenzoic acid)

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

assay_conditions_summary: cofactor NADPH

substrate: 5,5'-dithiobis(2-nitrobenzoic acid)


substrate_name: 5,5'-Dithiobis(2-nitrobenzoic acid)

sequence_source: UniProtKB:Q99MD6; exact accession lookup; TRXR3_MOUSE; UniProtKB reviewed (Swiss-Prot); length 652; CRC64 AC6342C64DDEC1BC

substrate: 5,5'-Dithiobis(2-nitrobenzoic acid)


substrate_name: H+; NADPH; 5,5'-Dithiobis(2-nitrobenzoic acid)

sequence_source: UniProtKB:Q9JMH6; exact accession lookup; TRXR1_MOUSE; UniProtKB reviewed (Swiss-Prot); length 613; CRC64 C9FD2E2E8C55118C

assay_conditions_summary: cofactor NADP+


substrate: H+; NADPH; 5,5'-Dithiobis(2-nitrobenzoic acid)


substrate_name: Hydroxyethyl disulfide

smiles: OCCSSCCO

substrate: Hydroxyethyl disulfide


substrate_name: hydrogen peroxide

sequence_source: UniProtKB:Q9JLT4; exact accession lookup; TRXR2_MOUSE; UniProtKB reviewed (Swiss-Prot); length 524; CRC64 74D4713DC8EF6A80

proof_lines: semisynthetic enzyme with 91% content of selenium

proof_lines: semisynthetic enzyme with 63% content of selenium

substrate: hydrogen peroxide


substrate_name: thioredoxin

substrate: thioredoxin


substrate_name: thioredoxin disulfide

proof_lines: full-length mouse enzyme with C-terminal sequence GCCG

proof_lines: full-length mouse enzyme with C-terminal sequence SCCS

proof_lines: full-length mouse enzyme with C-terminal sequence GCUG

substrate: thioredoxin disulfide


mutation_signature: truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid

mutation_type: truncation


organism: Plasmodium falciparum

substrate_name: H+; NADPH; Methyl methanethiolsulfonate

sequence_source: UniProtKB:Q25861; exact accession lookup; TRXR_PLAF5; UniProtKB reviewed (Swiss-Prot); length 541; CRC64 5449D50D7BA5BD9D

substrate: H+; NADPH; Methyl methanethiolsulfonate


substrate_name: Methyl methanethiolsulfonate

smiles: CSS(C)(=O)=O

substrate: Methyl methanethiolsulfonate


organism: Pseudomonas fluorescens

substrate_name: H+; NADPH; Oxidized thioredoxin

substrate: H+; NADPH; Oxidized thioredoxin


organism: Rattus norvegicus

substrate_name: Dithionitrobenzoic acid; NADPH; H+

sequence_source: UniProtKB:O89049; exact accession lookup; TRXR1_RAT; UniProtKB reviewed (Swiss-Prot); length 499; CRC64 B23E5B5E661B174E

substrate: Dithionitrobenzoic acid; NADPH; H+


substrate_name: Lipoamide

sequence_variant_note: Resolved canonical sequence from UniProtKB:O89049 canonical sequence with selected source mutation Y116T applied; exact accession lookup; TRXR1_RAT; canonical length 499; CRC64 B23E5B5E661B174E and applied mutation signature Y116T to reconstruct the assayed variant sequence.

assay_conditions_summary: 293.15 K; buffer TE

proof_lines: mutant enzyme Y116T, in TE buffer, at 20°C

substrate: Lipoamide


sequence_variant_note: Resolved canonical sequence from UniProtKB:O89049 canonical sequence with selected source mutation Y116I applied; exact accession lookup; TRXR1_RAT; canonical length 499; CRC64 B23E5B5E661B174E and applied mutation signature Y116I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y116I, in TE buffer, at 20°C


organism: Hordeum vulgare subsp. vulgare

substrate_name: Hordeum vulgare thioredoxin 2 mutant E86A

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

proof_lines: mutant R140A, pH 7.5, temperature not specified in the publication


substrate_name: Hordeum vulgare thioredoxin 2

proof_lines: mutant M43A, pH 7.5, temperature not specified in the publication

substrate: Hordeum vulgare thioredoxin 2


proof_lines: mutant G225R/G226D, pH 7.5, temperature not specified in the publication


substrate_name: Arabidopsis thaliana thioredoxin 3

proof_lines: mutant G225R/G226D/P227V, pH 7.5, temperature not specified in the publication

substrate: Arabidopsis thaliana thioredoxin 3


proof_lines: mutant W42A/M43A, pH 7.5, temperature not specified in the publication


proof_lines: mutant W42A, pH 7.5, temperature not specified in the publication


substrate_name: Hordeum vulgare thioredoxin 2 mutant I51G

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


proof_lines: mutant N45A/D46A, pH 7.5, temperature not specified in the publication


organism: Leptospira biflexa serovar Patoc

substrate_name: NADPH

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

substrate: NADPH


organism: Medicago truncatula

substrate_name: 5,5'-dithiobis(2-nitrobenzoic acid)

assay_conditions_summary: pH 7.5; cofactor NADPH


organism: Methanosarcina acetivorans

substrate_name: H+; NADH; 5,5'-Dithiobis(2-nitrobenzoic acid)


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q39243 direct REST lookup; live TRXB1_ARATH; organism Arabidopsis thaliana; EC 1.8.1.9

proof_lines: pH 7.5, temperature not specified in the publication


organism: Arthrospira platensis

substrate_name: H+; NADPH; 5,5'-Dithiobis(2-nitrobenzoic acid)


organism: Babesia bovis

substrate_name: 5,5'-dithio-bis(2-nitrobenzoic acid)

sequence_source: UniProtKB:A7AW73 direct REST lookup; live A7AW73_BABBO; organism Babesia bovis

substrate: 5,5'-dithio-bis(2-nitrobenzoic acid)


assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH


organism: Bos taurus

substrate_name: Oxidized glutaredoxin; NADPH; H+

sequence_source: UniProtKB:O62768 direct REST lookup; live TRXR1_BOVIN; organism Bos taurus; EC 1.8.1.9

substrate: Oxidized glutaredoxin; NADPH; H+


sequence_source: UniProtKB:P91938 direct REST lookup; live TRXR1_DROME; organism Drosophila melanogaster; EC 1.8.1.9

proof_lines: full-length Drosophila enzyme with C-terminal sequence SCCS

substrate: 5,5'-dithiobis(2-nitrobenzoic acid)


mutation_signature: truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid truncated enzyme (missing residues CCS from the C-termin


organism: Escherichia coli

sequence_source: UniProtKB:P0A9P4 direct REST lookup; live TRXB_ECOLI; organism Escherichia coli (strain K12); EC 1.8.1.9


organism: Euglena gracilis

sequence_source: UniProtKB:W8VNN5 direct REST lookup; live W8VNN5_EUGGR; organism Euglena gracilis; EC 1.8.1.9

assay_conditions_summary: pH 7.2; cofactor NADPH

proof_lines: pH 7.2, temperature not specified in the publication


sequence_source: UniProtKB:W8VZ54 direct REST lookup; live W8VZ54_EUGGR; organism Euglena gracilis; EC 1.8.1.9


sequence_source: UniProtKB:W8VVL6 direct REST lookup; live W8VVL6_EUGGR; organism Euglena gracilis; EC 1.8.1.9


substrate_name: NADH

mutation_signature: truncated mutant

assay_conditions_summary: pH 7.2; cofactor NADH

proof_lines: truncated mutant, pH 7.2, temperature not specified in the publication

substrate: NADH


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:A9LN30 direct REST lookup; live A9LN30_HORVV; organism Hordeum vulgare subsp. vulgare; EC 1.8.1.9 using selected mutation evidence and applied mutation signature Δ42 to reconstruct the assayed variant sequence.

proof_lines: mutant Delta42-47, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:A9LN30 direct REST lookup; live A9LN30_HORVV; organism Hordeum vulgare subsp. vulgare; EC 1.8.1.9 using selected mutation evidence and applied mutation signature G222D/A223G/G224E to reconstruct the assayed variant sequence.

proof_lines: mutant G222D/A223G/G224E, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:A9LN30 direct REST lookup; live A9LN30_HORVV; organism Hordeum vulgare subsp. vulgare; EC 1.8.1.9 using selected mutation evidence and applied mutation signature N139A to reconstruct the assayed variant sequence.

proof_lines: mutant N139A, pH 7.5, temperature not specified in the publication


sequence_source: UniProtKB O89049 (TRXR1_RAT), reviewed Swiss-Prot, REST checked 2026-06-28

proof_lines: purified, recombinant, tetrameric enzyme


sequence_source: UniProtKB Q9Z0J5 (TRXR2_RAT), reviewed Swiss-Prot, REST checked 2026-06-28

substrate: H+; NADPH; 5,5'-Dithiobis(2-nitrobenzoic acid)


organism: Saccharolobus solfataricus

substrate_name: thioredoxin

sequence_source: UniProtKB Q97W27 (Q97W27_SACS2), unreviewed TrEMBL, REST checked 2026-06-28

assay_conditions_summary: pH 5.5; 333.15 K; cofactor NADPH


organism: Triticum aestivum

sequence_source: UniProtKB Q8VX47 (Q8VX47_WHEAT), unreviewed TrEMBL, REST checked 2026-06-28

proof_lines:
wild-type
wild-type, thioredoxin from E. coli


enzyme_display_name: arginine kinase

organism: Cissites cephalotes

substrate_name: L-Arg; ATP

sequence_source: UniProtKB:A4F2K7 canonical sequence

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines: in 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, at 25°C

enzyme: arginine kinase

substrate: L-Arg; ATP


organism: Daphnia magna

substrate_name: ATP; L-arginine

sequence_source: UniProtKB:A0A0A7CK57 canonical sequence

assay_conditions_summary: cofactor ATP

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

substrate: ATP; L-arginine


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0A7CK57 canonical sequence with reviewer-reconstructed variant and applied mutation signature H284A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H284A, pH and temperature not specified in the publication


organism: Euphausia superba

substrate_name: L-arginine; ATP

sequence_source: UniProtKB:W8GJF4 canonical sequence

assay_conditions_summary: pH 8; 293.15 K; cofactor ATP

substrate: L-arginine; ATP


substrate_name: L-Arginine

substrate: L-Arginine


organism: Fenneropenaeus chinensis

substrate_name: L-Arginine; ATP; L-Arginine; ATP; L-Arginine phosphate; ADP

sequence_source: UniProtKB:Q4KY22 canonical sequence


organism: Frankliniella occidentalis

substrate_name: L-Arginine; ATP; L-Arginine; ATP; L-Arginine phosphate; ADP; L-arginine

source_db: sabio_rk; brenda

sequence_source: UniProtKB:A0A3G5HLZ2 canonical sequence

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

source: sabio_rk; brenda


organism: Haemonchus contortus

sequence_source: UniProtKB:K0DG62 canonical sequence

proof_lines: pH 7.5, 30°C, recombinant His-tagged enzyme


organism: Limulus polyphemus

substrate_name: L-Arginine phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature E59N to reconstruct the assayed variant sequence.

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

column_label: Table 3, construct row 'E59N'; column 'kcat (s-1) (% wild type)' = 12.5; column 'KM (phospho-arginine), mM' = 0.78; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 12.5 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 12.5 s^(-1). Km: printed Table 3 cell 0.78 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.78 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 16.025641025641026 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 12.5 / 0.78 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'E59N': kcat = 12.5 s-1; KM (phospho-arginine) = 0.78 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'E59N'

table_label: Table 3: Kinetic analysis of site directed mutants of Limulus arginine kinase in the specificity loops (Protein Science 2004, 13:575-585)

substrate: L-Arginine phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature D62G to reconstruct the assayed variant sequence.

column_label: Table 3, construct row 'D62G'; column 'kcat (s-1) (% wild type)' = 41; column 'KM (phospho-arginine), mM' = 0.99; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 41 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 41.0 s^(-1). Km: printed Table 3 cell 0.99 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.99 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 41.41414141414141 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 41.0 / 0.99 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'D62G': kcat = 41 s-1; KM (phospho-arginine) = 0.99 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'D62G'


substrate_name: ADP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature Y68S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor ADP

column_label: Table 3, construct row 'Y68S'; column 'kcat (s-1) (% wild type)' = 18; column 'KM (ADP), mM' = 0.135; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 18 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 18.0 s^(-1). Km: printed Table 3 cell 0.135 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.135 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 133.33333333333331 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 18.0 / 0.135 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'Y68S': kcat = 18 s-1; KM (ADP) = 0.135 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'Y68S'

substrate: ADP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature E59D to reconstruct the assayed variant sequence.

column_label: Table 3, construct row 'E59D'; column 'kcat (s-1) (% wild type)' = 32; column 'KM (phospho-arginine), mM' = 0.20; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 32 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 32.0 s^(-1). Km: printed Table 3 cell 0.20 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.2 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 160.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 32.0 / 0.2 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'E59D': kcat = 32 s-1; KM (phospho-arginine) = 0.20 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'E59D'


substrate_name: L-Arginine phosphate; ADP; L-Arginine phosphate; ADP; L-Arginine; ATP; ADP; L-Arginine phosphate

sequence_source: UniProtKB:P51541 canonical sequence


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature S63H/G64P to reconstruct the assayed variant sequence.

column_label: Table 2, mutant row '#4' with substitutions S63H/G64P; column 'kcat (s-1) (% wild type)' = 28.0; column 'KM (phospho-arginine) mM' = 8.66; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 28.0 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 28.0 s^(-1). Km: printed Table 2 cell 8.66 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 8.66 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 3.233256351039261 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 28.0 / 8.66 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, mutant row '#4' with substitutions S63H/G64P: kcat = 28.0 s-1; KM (phospho-arginine) = 8.66 mM; Table 2 prints no kcat/Km cell for this row.

table_label: Table 2: Kinetic analysis of chimeric insertional mutants of Limulus arginine kinase in the N-terminal domain specificity loop (Protein Science 2004, 13:575-585)


organism: Metapenaeus ensis

substrate_name: ATP (at pH 8.5 and 30 degrees Celsius)

assay_conditions_summary: pH 8.5; cofactor ATP

substrate: ATP (at pH 8.5 and 30 degrees Celsius)


organism: Penaeus vannamei

substrate_name: ATP (at pH 8.6 and 30 degrees Celsius)

assay_conditions_summary: pH 8.6; cofactor ATP

substrate: ATP (at pH 8.6 and 30 degrees Celsius)