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


enzyme_display_name: beta-lactamase

organism: Acinetobacter baumannii

substrate_name: cephalothin

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

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

enzyme: beta-lactamase

substrate: cephalothin

source: brenda


organism: Acinetobacter baylyi

substrate_name: ampicillin

mutation_signature: Unknown

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

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

substrate: ampicillin


organism: Acinetobacter bereziniae

substrate_name: Imipenem

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

substrate: Imipenem


organism: Acinetobacter pittii

kcat_display: Not reported

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


organism: Aeromonas hydrophila

substrate_name: biapenem

substrate: biapenem


substrate_name: H2O; Imipenem

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

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_name: nitrocefin

substrate: nitrocefin


enzyme_display_name: Beta-lactamase OXA-9

organism: Enterobacter aerogenes

substrate_name: H2O; Nitrocefin

km_display: Not reported

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

enzyme: Beta-lactamase OXA-9

substrate: H2O; Nitrocefin


enzyme_display_name: Beta-lactamase

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

enzyme: Beta-lactamase

substrate: Cefotaxime; H2O


substrate_name: ceftazidime

substrate: ceftazidime


substrate_name: 7-aminocephalosporanic acid

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

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

source_databases_merged: brenda skid

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

ki_unit: mM

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

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

substrate: cefpirome


enzyme_display_name: Beta-lactamase TEM

substrate_name: Unknown

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

enzyme: Beta-lactamase TEM

substrate: Unknown


enzyme_display_name: Beta-lactamase CTX-M-25

substrate_name: H2O; Benzylpenicillin

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

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


substrate_name: cefotaxime

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.

substrate: cefotaxime


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.


verification_status: unverified

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

status: unverified


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


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

substrate: Imipenem


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


substrate_name: ceftazidime

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

substrate: ceftazidime


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


source_db: skid

source_license: CC BY-NC-ND 4.0

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

source: skid


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


substrate_name: H2O; Penicillin G

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

substrate: H2O; Penicillin G


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


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_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


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


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: nitrocefin

verification_status: corrected

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

status: corrected


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

substrate: H2O; Imipenem


substrate_name: Nitrocefin; H2O

sequence_source: UniProtKB REST direct accession lookup: C7C422

substrate: Nitrocefin; H2O


enzyme_display_name: deoxycytidine kinase

substrate_name: ATP; 2'-Deoxycytidine

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

assay_conditions_summary: cofactor ATP

enzyme: deoxycytidine kinase

substrate: ATP; 2'-Deoxycytidine


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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

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

source_db: oed

kcat_over_km_origin: calculated

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

data_origin: experimental

source: oed


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


enzyme_display_name: hydroxylysine kinase

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

enzyme: hydroxylysine kinase

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

substrate_name: H2O; Nitrocefin

unit: uM/s

substrate: H2O; Nitrocefin


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

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

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


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

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

proof_lines:
wild-type enzyme
wild-type 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


enzyme_display_name: pyruvate kinase

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

enzyme: pyruvate kinase

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.

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

assay_conditions_summary: cofactor ATP


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

source_db: uniprot

enzyme: thioredoxin-disulfide reductase (NADPH)

source: uniprot


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


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


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.

mutation_type: deletion

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

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

verification_status: verified

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

status: verified


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)


organism: Tetrahymena pyriformis

substrate_name: ATP

sequence_source: UniProtKB U3T2Y2 direct accession lookup on 2026-06-28

proof_lines: pH 8.0, 25°C, recombinant His6-tagged isozyme AK2

substrate: ATP


organism: Toxocara canis

substrate_name: L-Arg

sequence_source: UniProtKB A7YVI5 direct accession lookup on 2026-06-28

proof_lines: in 100 mM Tris-HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, 5 mM NADH, at 25°C

substrate: L-Arg


organism: Tribolium castaneum


substrate_name: Nomega-phospho-L-arginine

substrate: Nomega-phospho-L-arginine


organism: Trypanosoma brucei brucei

sequence_source: UniProtKB Q38EV2 direct accession lookup on 2026-06-28

assay_conditions_summary: pH 7.5; 301.15 K; cofactor ATP

proof_lines:
pH 7.5, 28°C, recombinant isozyme AK1
pH 7.5, 37°C, recombinant isozyme AK1


organism: Trypanosoma cruzi

sequence_source: UniProtKB O96507 direct accession lookup on 2026-06-28

assay_conditions_summary: pH 7.3; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 7.3
pH 7.3, 30°C
Raw SKiD Env: Temp=30°C, pH=7.3


organism: Abyssogena kaikoi

sequence_source: UniProtKB REST direct accession lookup Q4AEC4; primary=Q4AEC4; retrieved 2026-06-28

assay_conditions_summary: cofactor ATP


organism: Anthopleura japonica

sequence_source: UniProtKB REST direct accession lookup O15992; primary=O15992; retrieved 2026-06-28

proof_lines: recombinant wild-type enzyme with MBP tag. The intact 2D/wild-type enzyme has a higher catalytic constant than the isolated domains


organism: Ascaris suum

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup D5FLG2; primary=D5FLG2; retrieved 2026-06-28 and applied mutation signature A105S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup D5FLG2; primary=D5FLG2; retrieved 2026-06-28 and applied mutation signature A105S/S106G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct accession lookup D5FLG2; primary=D5FLG2; retrieved 2026-06-28

proof_lines: mutant enzyme A105S, in 4.76 mM Tris-HCl (pH 8.0), at 25°C


proof_lines: mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C


proof_lines: recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup D5FLG2; primary=D5FLG2; retrieved 2026-06-28 and applied mutation signature S106G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C


organism: Caenorhabditis elegans

sequence_source: UniProtKB REST direct accession lookup Q10454; primary=Q10454; retrieved 2026-06-28


sequence_source: UniProtKB REST direct accession lookup O45011; primary=O45011; retrieved 2026-06-28


sequence_source: UniProtKB REST direct accession lookup O45518; primary=O45518; retrieved 2026-06-28


sequence_source: UniProtKB REST direct accession lookup Q27535; primary=Q27535; retrieved 2026-06-28


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


enzyme_display_name: Arginine kinase

column_label: Table 3, construct row 'Wild type'; column 'kcat (s-1) (% wild type)' = 180; column 'KM (phospho-arginine), mM' = 0.17; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 180 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 180.0 s^(-1). Km: printed Table 3 cell 0.17 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.17 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 1058.8235294117646 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 180.0 / 0.17 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'Wild type': kcat = 180 s-1; KM (phospho-arginine) = 0.17 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'Wild type'

enzyme: Arginine kinase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature L61P to reconstruct the assayed variant sequence.

column_label: Table 3, construct row 'L61P'; column 'kcat (s-1) (% wild type)' = 78; column 'KM (ADP), mM' = 0.018; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 78 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 78.0 s^(-1). Km: printed Table 3 cell 0.018 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.018 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 4333.333333333334 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 78.0 / 0.018 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'L61P': kcat = 78 s-1; KM (ADP) = 0.018 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'L61P'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature K16G to reconstruct the assayed variant sequence.

column_label: Table 3, construct row 'K16G'; column 'kcat (s-1) (% wild type)' = 2.00; column 'KM (ADP), mM' = 0.084; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.00 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 2.0 s^(-1). Km: printed Table 3 cell 0.084 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.084 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 23.809523809523807 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.0 / 0.084 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'K16G': kcat = 2.00 s-1; KM (ADP) = 0.084 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'K16G'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature R312G/E314V/H315D/E317A/E319V to reconstruct the assayed variant sequence.

column_label: Table 3, construct row 'R312G/E314V/H315D/E317A/E319V'; column 'kcat (s-1) (% wild type)' = 116; column 'KM (ADP), mM' = 0.08; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 116 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 116.0 s^(-1). Km: printed Table 3 cell 0.08 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.08 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 1450.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 116.0 / 0.08 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'R312G/E314V/H315D/E317A/E319V': kcat = 116 s-1; KM (ADP) = 0.08 mM; Table 3 prints no kcat/Km cell for this row.


organism: Locusta migratoria manilensis

substrate_name: L-arginine

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

substrate: L-arginine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L113G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L113K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L113D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L113I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T273D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T273S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T273G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T273A to reconstruct the assayed variant sequence.


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

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


organism: Lucilia cuprina

proof_lines: recombinant enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C

proof_lines: native enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C


enzyme_display_name: Arginine kinase Met e 2

substrate_name: ATP; L-Arginine

enzyme: Arginine kinase Met e 2

substrate: ATP; L-Arginine


organism: Nautilus pompilius


organism: Neocaridina denticulata

proof_lines:
pH 8.0, 25°C, recombinant enzyme
pH 8.0, 20°C, recombinant enzyme
pH 8.0, 15°C, recombinant enzyme


assay_conditions_summary: pH 8; 290.65 K; cofactor ATP

proof_lines:
pH 8.0, 17.5°C, recombinant enzyme
pH 8.0, 25°C, recombinant enzyme
pH 8.0, 30°C, recombinant enzyme


organism: Octopus vulgaris


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


organism: Polybetes pythagoricus

proof_lines:
pH 8.6, 30°C
Raw SKiD Env: Temp=30°C, pH=8.6


organism: Sabellastarte spectabilis


organism: Sepioteuthis lessoniana


organism: Teladorsagia circumcincta

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


organism: Tetrahymena pyriformis

proof_lines: pH 8.0, 25°C, recombinant His6-tagged isozyme AK1


organism: Bos taurus

substrate_name: thioredoxin

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

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 1200 sec(-1) with thioredoxin as substrate.

substrate: thioredoxin


organism: Drosophila melanogaster

substrate_name: NADPH (at pH 7.4)

proof_lines: Measurements were conducted with isoform A unless noted otherwise.

substrate: NADPH (at pH 7.4)


organism: Homo sapiens

proof_lines: kcat is 100 min(-1) with H2O2 as substrate.


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: TRX1 (at pH 7.4)

assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines: kcat is 1725 min(-1) with TRX1 as substrate (at pH 7.4) (PubMed:23845423). kcat is 51.7 sec(-1) with TRX1 as substrate (at 25 degrees Celsius and at pH 7.4) (PubMed:23845423). kcat is 275.2 min(-1) with NADPH and DTNB as substrates (at pH 7

substrate: TRX1 (at pH 7.4)


organism: Rattus norvegicus

proof_lines: kcat is 2500 min(-1) with thioredoxin as substrate.


organism: Gallus gallus

substrate_name: deoxyguanosine

proof_lines: kcat is 0.67 sec(-1) with deoxyguanosine as substrate. kcat is 0.52 sec(-1) with deoxycytidine as substrate. kcat is 2.56 sec(-1) with deoxyadenosine as substrate. kcat is 0.53 sec(-1) with deoxyuridine as substrate. kcat is 0.26 sec(-1) wi

substrate: deoxyguanosine


substrate_name: deoxycytidine

proof_lines: kcat is 0.05 sec(-1) with deoxycytodine as substrate. kcat is 4.07 sec(-1) with deoxyadenosine as substrate. kcat is 1.23 sec(-1) with deoxyguanosine as substrate. kcat is 1.05 sec(-1) with deoxyuridine as substrate. kcat is 1.08 sec(-1) wi

substrate: deoxycytidine


organism: Xenopus laevis

proof_lines: kcat is 1.26 sec(-1) with deoxyguanosine as substrate. kcat is 4.87 sec(-1) with deoxyadenosine as substrate. kcat is 0.42 sec(-1) with deoxycytidine as substrate. kcat is 0.36 sec(-1) with deoxyuridine as substrate. kcat is 0.14 sec(-1) wi


proof_lines: kcat is 0.09 sec(-1) with deoxycytodine as substrate. kcat is 3.40 sec(-1) with deoxyguanosine as substrate. kcat is 2.73 sec(-1) with deoxyadenosine as substrate. kcat is 0.29 sec(-1) with deoxythymidine as substrate. kcat is 1.27 sec(-1)


enzyme_display_name: peptide deformylase

organism: Arabidopsis thaliana

substrate_name: N-Formyl-Met-Ala-Ser

sequence_source: UniProtKB reviewed accession Q9FV53; direct REST lookup 2026-06-28

enzyme: peptide deformylase

substrate: N-Formyl-Met-Ala-Ser


sequence_source: UniProtKB reviewed accession Q9FUZ2; direct REST lookup 2026-06-28


substrate_name: H2O; Formyl-L-methionyl peptide

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

substrate: H2O; Formyl-L-methionyl peptide


substrate_name: N-Formyl-Met-Ser-Asn-Glu

substrate: N-Formyl-Met-Ser-Asn-Glu


substrate_name: N-Formyl-Nle-Ala-Ser

substrate: N-Formyl-Nle-Ala-Ser


substrate_name: N-Formyl-Nva-Ala-Ser

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

substrate: N-Formyl-Nva-Ala-Ser


substrate_name: N-Formyl-Met-Leu-Phe

substrate: N-Formyl-Met-Leu-Phe


substrate_name: N-Formyl-Met-Leu-Glu

substrate: N-Formyl-Met-Leu-Glu


substrate_name: Formyl-L-methionyl peptide

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

substrate: Formyl-L-methionyl peptide


substrate_name: N-Formyl-Phe-Ala-Ser

substrate: N-Formyl-Phe-Ala-Ser


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


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


sequence_source: UniProtKB:Q9FV53 canonical sequence retrieved by direct accession lookup on 2026-06-28


substrate_name: Formyl-L-methionyl peptide; H2O

substrate: Formyl-L-methionyl peptide; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FV53 canonical sequence retrieved by direct accession lookup on 2026-06-28 and applied mutation signature L91E to reconstruct the assayed variant sequence.


substrate_name: H2O; N-Formyl-Met-Leu-p-nitroanilide

sequence_source: UniProtKB:Q9FUZ2 canonical sequence retrieved by direct accession lookup on 2026-06-28

substrate: H2O; N-Formyl-Met-Leu-p-nitroanilide


organism: Escherichia coli

sequence_source: UniProtKB:P0A6K3 canonical sequence retrieved by direct accession lookup on 2026-06-28


substrate_name: formyl-Met-Ala-Ser

substrate: formyl-Met-Ala-Ser


substrate_name: N-Formyl-Met-Leu

substrate: N-Formyl-Met-Leu


substrate_name: N-Formyl-L-methionine

substrate: N-Formyl-L-methionine


substrate_name: H2O; N-Formyl-L-methionine

assay_conditions_summary: pH 4.5; 310.15 K; buffer 50 mM potassium phosphate

proof_lines: pH 4.5, 37°C, recombinant enzyme with bound Ni2+

proof_lines: pH 4.5, 37°C, recombinant enzyme with bound Zn2+

proof_lines: in 50 mM potassium phosphate buffer, pH 7.0, temperature not specified in the publication

substrate: H2O; N-Formyl-L-methionine


organism: Helicobacter pylori

sequence_source: UniProtKB:Q672W7 canonical sequence retrieved by direct accession lookup on 2026-06-28


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 canonical sequence retrieved by direct accession lookup on 2026-06-28 and applied mutation signature E91M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9HBH1 canonical sequence retrieved by direct accession lookup on 2026-06-28

proof_lines: pH and temperature not specified in the publication


substrate_name: N-formyl-Met-Leu-rho-nitroanilide

substrate: N-formyl-Met-Leu-rho-nitroanilide


sequence_source: UniProtKB:Q9HBH1 direct accession check

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 direct accession check and applied mutation signature E91A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 direct accession check and applied mutation signature S47A/E91L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9HBH1 canonical context only; row-specific variant unresolved


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 direct accession check and applied mutation signature E91L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 direct accession check and applied mutation signature S47A to reconstruct the assayed variant sequence.


organism: Leptospira interrogans

substrate_name: N-formyl-Met-Ala-Ser

sequence_source: UniProtKB:Q93LE9 direct accession check

substrate: N-formyl-Met-Ala-Ser


organism: Mycobacterium tuberculosis

substrate_name: N-formyl-Met-Ala

sequence_source: UniProtKB:P9WIJ3 direct accession check

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WIJ3 direct accession check and applied mutation signature M145C to reconstruct the assayed variant sequence.

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

substrate: N-formyl-Met-Ala


proof_lines: pH 7.0, 30°C, recombinant enzyme mutant M145C


proof_lines: pH 7.0, 30°C, recombinant wild-type enzyme


organism: Salmonella enterica subsp. enterica serovar Typhimurium

sequence_source: UniProtKB:Q8ZLM7 direct accession check


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8ZLM7 direct accession check and applied mutation signature C130M/V63C to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant enzyme mutant C130M/V63C


organism: Solanum lycopersicum

sequence_source: UniProtKB:Q9FUZ0 direct accession check


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

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

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


substrate_name: Lipoamide

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

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

proof_lines: isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C

proof_lines: TrxR-16, TrxR lacking the last 16 C-terminal amino acids

substrate: Lipoamide


organism: Hordeum vulgare

substrate_name: Hordeum vulgare thioredoxin disulfide h2

proof_lines:
pH 5.7, HvNTR2
pH 7.4, HvNTR1
pH 5.7, HvNTR1


organism: Medicago truncatula


organism: Meleagris gallopavo

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NADPH

substrate: NADPH


organism: Methanosarcina acetivorans

proof_lines: cosubstrate: 5,5-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication

proof_lines: Methanosarcina acetivorans thioredoxin 7, cosubstrate: NADPH, pH and temperature not specified in the publication


organism: Mus musculus

substrate_name: thioredoxin

proof_lines: Escherichia coli thioredoxin as substrate

substrate: thioredoxin


assay_conditions_summary: pH 7

proof_lines: truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0


proof_lines: wild type enzyme, in 50 mM potassium phosphate at pH 7.0


organism: Plasmodium berghei

substrate_name: dithionitrobenzene

substrate: dithionitrobenzene


organism: Plasmodium falciparum

substrate_name: methylseleninate

substrate: methylseleninate


substrate_name: DTNB

substrate: DTNB


substrate_name: H2O; Formyl-L-methionyl peptide

sequence_source: UniProtKB reviewed accession Q9FUZ0 FASTA

substrate: H2O; Formyl-L-methionyl peptide


substrate_name: Formyl-L-methionyl peptide; H2O

sequence_source: UniProtKB reviewed accession Q9FV54 FASTA

substrate: Formyl-L-methionyl peptide; H2O


organism: Staphylococcus epidermidis

substrate_name: N-formyl-L-Met-L-Ala-L-Ser

sequence_source: UniProtKB reviewed accession Q5HQ78 FASTA

proof_lines: Co2+-substituted PDF-1, in 50 mM HEPES, pH 7.5, at 37°C

substrate: N-formyl-L-Met-L-Ala-L-Ser


organism: Streptococcus agalactiae

substrate_name: Unknown

sequence_source: UniProtKB reviewed accession Q8E378 FASTA

substrate: Unknown


organism: Vibrio phage VP16T

substrate_name: formyl-Met-Ala-Ser

substrate: formyl-Met-Ala-Ser


proof_lines: pH 7.5, 37°C, recombinant enzyme with bound Zn2+, Zn-Vp16 PDF1B

proof_lines: pH 7.5, 37°C, recombinant enzyme with bound Ni2+, Ni-Vp16 PDF1B


organism: Drosophila melanogaster


organism: Entamoeba histolytica

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

proof_lines: with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C

proof_lines: with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C


organism: Escherichia coli

substrate_name: glutaredoxin 4

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: pH 7.5, temperature not specified in the publication

substrate: glutaredoxin 4


substrate_name: thioredoxin-R

assay_conditions_summary: pH 8

proof_lines: chimeric enzyme mutant, partly from Salmonella typhimurium AhpF protein

proof_lines: substrate mutant, thioredoxin-CAC, pH 8.0

substrate: thioredoxin-R


proof_lines: substrate wild-type, thioredoxin P34S, pH 8.0


organism: Haemonchus contortus

assay_conditions_summary: pH 7.8; 310.15 K; cofactor NADPH


organism: Homo sapiens


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: wild type enzyme, 10 mM potassium phosphate buffer (pH 7.0) containing 10 mM EDTA, at 25°C


organism: Bos taurus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

proof_lines:
M-type isozyme, 25°C, pH 7.0
L-type isozyme, 25°C, pH 7.0

substrate: Phosphoenolpyruvate; ADP


organism: Ricinus communis

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ADP

proof_lines: 2 isozymes with different kinetic mechanisms


organism: Spinacia oleracea

assay_conditions_summary: pH 7.1; 298.15 K; cofactor ADP

proof_lines:
isozyme PKII, pH 7.1, 25°C
isozyme PKI, pH 7.1, 25°C
pH 7.1, 25°C


organism: Unknown

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: N-formylmethionyl-Leu-p-nitroanilide

substrate: N-formylmethionyl-Leu-p-nitroanilide


substrate_name: H2O; Cephalothin

substrate: H2O; Cephalothin


organism: Apostichopus japonicus

substrate_name: L-Arg

substrate: L-Arg


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C


assay_conditions_summary: 298.15 K; cofactor ATP


proof_lines: mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C


organism: Cissites cephalotes

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


organism: Corbicula japonica

proof_lines:
25°C, D197G mutant of domain 2
37°C, D197G mutant enzyme of domain 2


proof_lines:
25°C, H60R mutant of domain 2
37°C, H60R mutant of domain 2


organism: Triticum aestivum

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 6.2; 303.15 K; cofactor ADP


organism: Streptococcus mutans

assay_conditions_summary: pH 7.5; cofactor ADP

proof_lines: in the presence of glucose 6-phosphate, at pH 7.5


organism: Toxoplasma gondii

proof_lines: PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ADP


organism: Abyssogena kaikoi

proof_lines: isolated domain 2, in 100 mM Tris-HCl (pH 8.0), at 10°C

proof_lines: two-domain enzyme, in 100 mM Tris-HCl (pH 8.0), at 25°C

proof_lines: isolated domain 2, in 100 mM Tris-HCl (pH 8.0), at 25°C


organism: Anthopleura japonica

proof_lines: mutant two-domain-enzyme D1-Lys6-D2, in 100 mM Tris/HCl, pH 8.0 at 25°C


proof_lines: mutant two-domain-enzyme D1(Y68G)-D2, in 100 mM Tris/HCl, pH 8.0 at 25°C

proof_lines: mutant two-domain-enzyme D1-D2(Y68G), in 100 mM Tris/HCl, pH 8.0 at 25°C


proof_lines: wild type one-domain-enzyme D1, in 100 mM Tris/HCl, pH 8.0 at 25°C

proof_lines: wild type one-domain-enzyme D2, in 100 mM Tris/HCl, pH 8.0 at 25°C

proof_lines: wild type two-domain-enzyme D1-D2, in 100 mM Tris/HCl, pH 8.0 at 25°C


mutation_type: delins


substrate_name: L-arginine

assay_conditions_summary: pH 8.1; cofactor ATP

substrate: L-arginine


organism: Anopheles gambiae

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

proof_lines: thioredoxin-2 from Drosophila melanogaster, pH 7.4

proof_lines: thioredoxin-1 from Anopheles gambiae, pH 7.4

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


organism: Arabidopsis thaliana

substrate_name: thioredoxin

substrate: thioredoxin


proof_lines:
thioredoxin from E. coli
human thioredoxin
E. coli thioredoxin


organism: Caenorhabditis elegans

assay_conditions_summary: pH 7

proof_lines: thioredoxin from Escherichia coli, wild type enzyme

proof_lines: wild type enzyme, in 50 mM potassium phosphate at pH 7.0


proof_lines: thioredoxin from Escherichia coli, mutant TR-GCCS

proof_lines: thioredoxin from Escherichia coli, mutant TR-SCCS


proof_lines: truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0


organism: Cereibacter sphaeroides

substrate_name: reductase

substrate: reductase


organism: Corynebacterium nephridii

substrate_name: thioredoxin C-2

substrate: thioredoxin C-2


organism: Drosophila melanogaster

substrate_name: methylseleninate

proof_lines:
recombinant protein
pH 7, 25°C
mitochondrial TrxR1 isoform

substrate: methylseleninate


mutation_signature: truncated thioredoxin reductase missing its final eight amino acids


organism: Plasmodium falciparum

substrate_name: DTNB

substrate: DTNB


organism: Rattus norvegicus

proof_lines: SeC498C mutant enzyme, human thioredoxin


proof_lines: wild-type enzyme, Km-value can be reduced by addition of selenocysteine


proof_lines: substrate: thioredoxin from calf and rat


substrate_name: thioredoxin 3

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

substrate: thioredoxin 3


substrate_name: thioredoxin 2

proof_lines: mutant enzyme K137A, pH and temperature not specified in the publication

substrate: thioredoxin 2


organism: Schistosoma mansoni

assay_conditions_summary: pH 7; 298.15 K; buffer conditions

proof_lines: truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 100 mM potassium phosphate pH 7.0, at 25°C


proof_lines: full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C

proof_lines: full length enzyme, in 50 mM potassium phosphate pH 7.0, at 25°C


organism: Solanum lycopersicum

substrate_name: Insulin; Reduced thioredoxin

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication

substrate: Insulin; Reduced thioredoxin


organism: Spinacia oleracea


organism: Limulus polyphemus

substrate_name: ADP

sequence_source: NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context.

assay_conditions_summary: cofactor ADP

substrate: ADP


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E225D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E225Q/E314Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E314S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E225Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E314Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E314D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature R312G/E314V/H315D/E317A/E319V to reconstruct the assayed variant sequence.


organism: Locusta migratoria

substrate_name: Unknown

substrate: Unknown


organism: Locusta migratoria manilensis

substrate_name: ATP

assay_conditions_summary: pH 8.6; 303.15 K; cofactor ATP

substrate: ATP


proof_lines: pH 8.6, 30°C, recombinant arginine kinase


organism: Corbicula japonica

proof_lines:
25°C, domain 2
25°C, two-domain enzyme
37°C, domain 2


proof_lines:
25°C, H60G mutant of domain 2
37°C, H60G mutant of domain 2


organism: Crassostrea sp.

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ATP


organism: Ctenocephalides felis

proof_lines:
isoform arginine kinase 2
isoform arginine kinase 1


organism: Desulfotalea psychrophila

assay_conditions_summary: pH 8; 298.15 K; cofactor ADP


enzyme_display_name: peroxidase

organism: Aggregatibacter actinomycetemcomitans

sequence_source: UniProtKB exact accession A2A1C5

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

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: peroxidase


organism: Amphitrite ornata

sequence_source: UniProtKB exact accession Q9NAV8

proof_lines: 2,4,6-trichlorophenol, pH 7.0, temperature not specified in the publication

proof_lines: cosubstrate 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid), pH 7.0, temperature not specified in the publication


organism: Amycolatopsis sp.

sequence_source: UniProtKB exact accession K7N5M8

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


organism: Armoracia rusticana

substrate_name: H2O2; 2,4-Dichlorophenol

substrate: H2O2; 2,4-Dichlorophenol


smiles: OO


substrate_name: N-Acetyl-L-tryptophanamide

substrate: N-Acetyl-L-tryptophanamide


substrate_name: 2-Chloro-4-methoxyphenol; H2O2

substrate: 2-Chloro-4-methoxyphenol; H2O2


substrate_name: L-Dopa; H2O2

substrate: L-Dopa; H2O2


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


sequence_source: UniProtKB exact accession K7ZW57


sequence_source: UniProtKB exact accession K7ZWW6


sequence_source: UniProtKB exact accession K7ZW28


substrate_name: guaiacol

assay_conditions_summary: pH 5

proof_lines: mutant F143A, pH 5, temperature not specified in the publication

substrate: guaiacol


proof_lines: mutant F130A, pH 5, temperature not specified in the publication


proof_lines: mutant F130A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication


proof_lines: mutant F68A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication


proof_lines: mutant F179A, pH 5, temperature not specified in the publication


proof_lines: mutant F68A, pH 5, temperature not specified in the publication


proof_lines: mutant F142A, pH 5, temperature not specified in the publication


proof_lines: wild-type isoform C, pH 5, temperature not specified in the publication


substrate_name: H2O2 / 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)

sequence_source: UniProtKB exact accession P00433


sequence_variant_note: Resolved canonical sequence from UniProtKB exact accession P00433 with reconstructed mature-chain substitutions and applied mutation signature N13D/N57S/N255D/N268D with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

substrate: H2O2 / 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)


substrate_name: 2,2'-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid); H2O2 / 2,2'-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) / H2O2 / H2O / Oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) / Guaiacol; H2O2 / Guaiacol / Oxidized donor / 4-Cresol; H2O2 / 4-Cresol / 4-Methylcatechol


substrate_name: Guaiacol

substrate: Guaiacol


organism: Chromolaena odorata

substrate_name: pyrogallol

proof_lines: 30°C, pH 5.5, cosubstrate: pyrogallol, isoenzyme E5

proof_lines: 30°C, pH 5.5, cosubstrate: o-phenylenediamine, isoenzyme E5

substrate: pyrogallol


organism: Fagopyrum esculentum

substrate_name: ascorbic acid

proof_lines:
isoenzyme POX II
isoenzyme POX I

substrate: ascorbic acid


organism: Ficus carica

proof_lines: pH 5.5, temperature not specified in the publication, isoenzyme FP3

proof_lines: pH 5.5, temperature not specified in the publication, isoenzyme FP2

proof_lines: pH 5.5, temperature not specified in the publication, isoenzyme FP1


organism: Nicotiana tabacum

proof_lines:
isozyme Af
isozyme Cn


organism: Arabidopsis thaliana

substrate_name: phosphoenolpyruvate (for the phosphatase activity)


organism: Auricularia auricula-judae

substrate_name: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) (Dye-decolorizing peroxidase AauDyP1, at pH 4.5)


organism: Bubalus bubalis

substrate_name: 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (at pH 6.0 and 60 degrees Celsius)

assay_conditions_summary: pH 6


organism: Exidia glandulosa


organism: Mycena epipterygia


organism: Mycetinis scorodonius


organism: Sus scrofa

substrate_name: cloride

substrate: cloride


organism: Taiwanofungus camphoratus

substrate_name: veratryl alcohol

substrate: veratryl alcohol


proof_lines: cosubstrate 2,4,6-tribromophenol, pH 7.0, temperature not specified in the publication


organism: Anabaena sp.

substrate_name: Reactive Blue 5

substrate: Reactive Blue 5


substrate_name: 4-Methoxyphenol; H2O2

assay_conditions_summary: pH 7; 298.15 K; buffer potassium phosphate

proof_lines: in the presence of 25% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C

proof_lines: in the presence of 20% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C

substrate: 4-Methoxyphenol; H2O2


organism: Armoracia sp.


organism: Artocarpus heterophyllus

proof_lines: pH 6.0, temperature not specified in the publication, cosubstrate: gallic acid

proof_lines: pH 6.0, temperature not specified in the publication, cosubstrate: o-phenylenediamine


organism: Beta vulgaris

assay_conditions_summary: pH 5.5; 298.15 K; buffer 0.2 M sodium phosphate

proof_lines: at 25°C in 0.2 M sodium phosphate buffer (pH 6.0)


organism: Bjerkandera adusta

substrate_name: Pentachlorophenol

assay_conditions_summary: pH 4

proof_lines: pH 4, oxidative dehalogenation of pentachlorophenol

proof_lines: pH 4, oxidative dehalogenation of 3,5-dibromo-4-hydroxybenzonitrile

substrate: Pentachlorophenol


organism: Boucerosia umbellata


organism: Brassica napus

proof_lines: 25°C, pH 6.0, partially deglycosylated enzyme


organism: Brassica oleracea

substrate_name: H2O2; Guaiacol

proof_lines: membrane-bound isoform, pH not specified in the publication, temperature not specified in the publication

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

substrate: H2O2; Guaiacol


organism: Euphorbia characias

sequence_source: UniProtKB:Q6PQF2 canonical sequence fetched by exact accession lookup


organism: Homo sapiens

substrate_name: 3,3',5,5'-Tetramethylbenzidine; H2O2

sequence_source: UniProtKB:Q92626 canonical sequence fetched by exact accession lookup

substrate: 3,3',5,5'-Tetramethylbenzidine; H2O2


organism: Lepidium draba

sequence_source: UniProtKB:A0A076L8M7 canonical sequence fetched by exact accession lookup

proof_lines:
pH 6.5, 30°C, 300 mM glycine
pH 6.5, 30°C
pH 6.5, 30°C, 600 mM sorbitol


organism: Neisseria gonorrhoeae


organism: Pleurotus eryngii

sequence_source: UniProtKB:O94753 canonical sequence fetched by exact accession lookup

proof_lines:
24°C, pH 3, wild-type enzyme
24°C, pH 3.5, wild-type enzyme
24°C, pH 5, wild-type enzyme


substrate_name: Reactive Black 5

sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature P76H with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines:
24°C, pH 3.5, mutant enzyme P76H
24°C, pH 3, mutant enzyme P76H
24°C, pH 5, mutant enzyme P76H

substrate: Reactive Black 5


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature W164S/P76H with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature W164S with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature W164H with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature H232F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines:
24°C, pH 3, mutant enzyme H232F
24°C, pH 3.5, mutant enzyme H232F
24°C, pH 5, mutant enzyme H232F


organism: Trachycarpus fortunei

sequence_source: UniProtKB:A0A0A0Y4H8 canonical sequence fetched by exact accession lookup

proof_lines:
pH 3.0, 23°C
Raw SKiD Env: Temp=23°C, pH=3


organism: Brassica oleracea var. capitata f. rubra

substrate_name: guaiacol

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


organism: Brassica rapa

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

assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.01 M phosphate

proof_lines: native enzyme, in 0.01 M phosphate buffer at pH 7.5 and 25°C

proof_lines: pyromellitic dianhydride-modified enzyme, in 0.01 M phosphate buffer at pH 7.5 and 25°C


organism: Calotropis procera

substrate_name: o-Dianisidine

proof_lines: pH 6.0, temperature not specified in the publication

substrate: o-Dianisidine


organism: Camellia sinensis


organism: Capsicum annuum

assay_conditions_summary: pH 5; 298.15 K; buffer pH 5

proof_lines: in 50 mM sodium citrate buffer (pH 5.0), at 25°C


organism: Citrus jambhiri

assay_conditions_summary: pH 5.5; buffer 50 mM sodium acetate

proof_lines: in 50 mM sodium acetate buffer, at pH 5.5


organism: Commiphora gileadensis

proof_lines: pH 7.0, temperature not specified in the publication, immobilized enzyme (entrapped onto a carboxymethyl cellulose/Fe3O4 magnetic hybrid material)

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


organism: Coprinopsis cinerea

substrate_name: 2,2'-Dihydroxyazobenzene; H2O2

substrate: 2,2'-Dihydroxyazobenzene; H2O2


organism: Cucumis melo

substrate_name: 3,4-dihydroxyphenylacetic acid

proof_lines: for Cucumis melo L. cantalupensis cv. Charentais

proof_lines: for Cucumis melo L. inodorus cv. Amarillo

substrate: 3,4-dihydroxyphenylacetic acid


organism: Cucumis melo var. cantalupo


organism: Cucumis melo var. inodorus


organism: Cynara cardunculus

substrate_name: ferulic acid

proof_lines: covalently bound POD from artichoke leaves, apparent Km value

proof_lines: covalently bound POD from artichoke heads, apparent Km value

proof_lines: soluble POD from artichoke leaves, apparent Km value

substrate: ferulic acid


organism: Amycolatopsis sp. (strain ATCC 39116 / 75iv2)

substrate_name: ABTS

proof_lines: kcat is 87 sec(-1) for peroxidase activity with ABTS as substrate. kcat is 34 sec(-1) for peroxidase activity with Reactive Blue 5 as substrate. kcat is 0.38 sec(-1) for peroxidase activity with Reactive Black 5 as substrate. kcat is 68 sec

substrate: ABTS


organism: Zea mays

substrate_name: Unknown

substrate: Unknown