substrate_name: cephaloridin

column_label: PMC1132494 page 154 Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row cephaloridin: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM-to-mM normalization, and their same-row quotient reproduces the exported kcat/Km.

normalized_value_unit_evidence: metric: kcat; raw value: 28; raw unit: s^-1; normalized value: 28.0; normalized unit: s^-1; metric: Km; raw value: 300 +/- 50; raw unit: uM; normalized value: 0.3; normalized unit: mM; metric: kcat/Km; normalized value: 93.33333333333334; normalized unit: s^-1 mM^-1; assay condition: Table 3 kinetic determinations for the class B beta-lactamase of the Pseudomonas maltophilia ULA-511 L-1 column of Table 3 (the package's Table 3 extract labels this column Stenotrophomonas maltophilia and its header identifies it as the Pseudomonas maltophilia ULA-511 L-1 column); Materials and methods: the experiments for ULA-511 and A. hydrophila were performed in 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2, at 35 C and 30 C respectively, so 35 C applies to this enzyme; the export row carries pH 7.0 and 308.15 K.

raw_value_unit_evidence: Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row cephaloridin: Km cell 300 +/- 50 uM; kcat cell 28 s^-1.

row_label: Stenotrophomonas maltophilia (Pseudomonas maltophilia ULA-511 L-1) beta-lactamase | cephaloridin

substrate: cephaloridin


enzyme_display_name: beta-lactamase

organism: Stenotrophomonas maltophilia

substrate_name: Oxacillin

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB:O51899 direct REST lookup on 2026-05-27

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

assay_conditions_summary: pH 7; 308.15 K; buffer 50 mM sodium cacodylate

column_label: PMC1132494 page 154 Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row oxacillin: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM-to-mM normalization, and their same-row quotient reproduces the exported kcat/Km.

normalized_value_unit_evidence: metric: kcat; raw value: 285; raw unit: s^-1; normalized value: 285.0; normalized unit: s^-1; metric: Km; raw value: 27 +/- 3; raw unit: uM; normalized value: 0.027; normalized unit: mM; metric: kcat/Km; normalized value: 10555.555555555557; normalized unit: s^-1 mM^-1; assay condition: Table 3 kinetic determinations for the class B beta-lactamase of the Pseudomonas maltophilia ULA-511 L-1 column of Table 3 (the package's Table 3 extract labels this column Stenotrophomonas maltophilia and its header identifies it as the Pseudomonas maltophilia ULA-511 L-1 column); Materials and methods: the experiments for ULA-511 and A. hydrophila were performed in 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2, at 35 C and 30 C respectively, so 35 C applies to this enzyme; the export row carries pH 7.0 and 308.15 K.

raw_value_unit_evidence: Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row oxacillin: Km cell 27 +/- 3 uM; kcat cell 285 s^-1.

row_label: Stenotrophomonas maltophilia (Pseudomonas maltophilia ULA-511 L-1) beta-lactamase | oxacillin

table_label: Table 3 Kinetic parameters determined for class B beta-lactamases (PMC1132494 scanned page 154), Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column

data_origin: experimental

enzyme: beta-lactamase

substrate: Oxacillin

status: verified

source: oed


substrate_name: Penicillin G

column_label: PMC1132494 scanned page 154 Table 3; organism/enzyme column Pseudomonas maltophilia ULA-511; row Penicillin G; Km column=50 +/- 6 uM; kcat column=1100 s^-1; kcat/Km column=2.20 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: normalized km=0.05 mM; export km=0.05 mM; normalized kcat=1100 s^-1; export kcat=1100 s^-1; normalized kcat_over_km=22000 s^-1 mM^-1; export kcat_over_km=22000 s^-1 mM^-1

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 / Penicillin G; Km = 50 +/- 6 uM; kcat = 1100 s^-1; kcat/Km = 2.20 x 10^7 M^-1 s^-1

table_label: PMC1132494 scanned page 154 Table 3

substrate: Penicillin G


substrate_name: Asparenomycin A

assay_conditions_summary: pH 6.5; 303.15 K; buffer 30 mM sodium cacodylate

column_label: Table label: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibioticsa. Row: Asparenomycin A. Enzyme column group: X. maltophilia ULA-511. Columns read: Km (uM) cell 2 ± 0.1, kcat (s^-1) cell 14, kcat/Km (M^-1 s^-1) cell 7.00 x 10^6. Km 2 ± 0.1 uM normalizes to 0.002 mM and equals the exported km; kcat 14 s^-1 equals the exported kcat; kcat/Km (M^-1 s^-1) cell 7.00 x 10^6 M^-1 s^-1 normalizes to 7000.0 s^-1 mM^-1 and decimal-matches the exported kcat_over_km (the quotient of this row's own printed kcat and Km cells gives the same number).

normalized_value_unit_evidence: X. maltophilia ULA-511 columns of Table 7 row Asparenomycin A: Km 2 ± 0.1 uM = 0.002 mM; kcat 14 s^-1 = 14.0 s^-1; kcat/Km 7000.0 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibioticsa | enzyme column group: X. maltophilia ULA-511 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Asparenomycin A             170 6 5            475        2.80 3 106          20 6 1          100          5.00 3 106        2 6 0.1b            14      7.00 3 106

row_label: X. maltophilia ULA-511 | Asparenomycin A

substrate: Asparenomycin A


substrate_name: Sulbenicillin

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Sulbenicillin. Enzyme column group: X. maltophilia ULA-511. Columns read: Km (uM) cell 190 ± 5, kcat (s^-1) cell 225, kcat/Km (M^-1 s^-1) cell 1.20 x 10^6. Km 190 ± 5 uM normalizes to 0.19 mM and equals the exported km; kcat 225 s^-1 equals the exported kcat; the separately rounded kcat/Km (M^-1 s^-1) cell 1.20 x 10^6 M^-1 s^-1 (= 1200.0 s^-1 mM^-1) is disclosed but not used; the exported kcat_over_km 1184.2105263157894 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells.

normalized_value_unit_evidence: X. maltophilia ULA-511 columns of Table 4 row Sulbenicillin: Km 190 ± 5 uM = 0.19 mM; kcat 225 s^-1 = 225.0 s^-1; kcat/Km 1184.2105263157894 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: X. maltophilia ULA-511 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Sulbenicillin        230 6 10         0.50        2.10 3 103          .2,000          .300            1.93 3 105c     190 6 5            225       1.20 3 106

row_label: X. maltophilia ULA-511 | Sulbenicillin

substrate: Sulbenicillin


substrate_name: Ticarcillin

verification_status: corrected

assay_conditions_summary: pH 6.5; 303.15 K; buffer this record. Assay condition: 30 mM sodium cacodylate

column_label: Table 4 (PDF page 5 of 8, printed page 196), antibiotic row `Ticarcillin`, enzyme block `X. maltophilia ULA-511`: Km (uM) = 140 +/- 2; kcat (s-1) = 375; kcat/Km (M-1 s-1) = 2.70 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 375 s-1 -> 375 s^(-1) (the printed unit is already per second); the exported value is 440 s^(-1). Km: printed cell 140 +/- 2 uM -> 0.14 mM (divide by 1000); the exported value is 0.14 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.70 x 10^6 M-1 s-1 for this cell block -> 2700 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1; the per-second part is unchanged); the exported value is 3142.8571428571427 s^(-1)*mM^(-1).

row_label: Table 4, decoded plain-numeral transcription, antibiotic row `Ticarcillin`, enzyme block `X. maltophilia ULA-511`

table_label: Table 4 (PDF page 5 of 8, printed page 196) 'Kinetic parameters of metallo-b-lactamases with penicillins'

substrate: Ticarcillin

status: corrected


substrate_name: Imipenem

column_label: Table 3 (PDF page 4 of 8, printed page 195), antibiotic row `Imipenem`, enzyme block `X. maltophilia ULA-511`: Km (uM) = 100 +/- 8; kcat (s-1) = 75; kcat/Km (M-1 s-1) = 7.50 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 75 s-1 -> 75 s^(-1) (the printed unit is already per second); the exported value is 370 s^(-1). Km: printed cell 100 +/- 8 uM -> 0.1 mM (divide by 1000); the exported value is 0.057 mM. kcat/Km: the paper PRINTS the kcat/Km cell 7.50 x 10^5 M-1 s-1 for this cell block -> 750 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1; the per-second part is unchanged); the exported value is 6491.228070175438 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, antibiotic row `Imipenem`, enzyme block `X. maltophilia ULA-511`

table_label: Table 3 (PDF page 4 of 8, printed page 195) 'Kinetic parameters of metallo-b-lactamases with benzylpenicillin and imipenem after purification'

substrate: Imipenem


substrate_name: Epicillin

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Epicillin. Enzyme column group: X. maltophilia ULA-511. Columns read: Km (uM) cell 50 ± 2, kcat (s^-1) cell 265, kcat/Km (M^-1 s^-1) cell 5.30 x 10^6. Km 50 ± 2 uM normalizes to 0.05 mM and equals the exported km; kcat 265 s^-1 equals the exported kcat; kcat/Km (M^-1 s^-1) cell 5.30 x 10^6 M^-1 s^-1 normalizes to 5300.0 s^-1 mM^-1 and decimal-matches the exported kcat_over_km (the quotient of this row's own printed kcat and Km cells gives the same number).

normalized_value_unit_evidence: X. maltophilia ULA-511 columns of Table 4 row Epicillin: Km 50 ± 2 uM = 0.05 mM; kcat 265 s^-1 = 265.0 s^-1; kcat/Km 5300.0 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: X. maltophilia ULA-511 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Epicillin            300 6 10         0.60        2.00 3 103         550 6 10          160            2.90 3 105       50 6 2            265       5.30 3 106

row_label: X. maltophilia ULA-511 | Epicillin

substrate: Epicillin


substrate_name: tazobactam

column_label: Table label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonama. Row: Tazobactam. Enzyme column group: X. maltophilia ULA-511. Columns read: Km (uM) cell 190 ± 5, kcat (s^-1) cell 270.0, kcat/Km (M^-1 s^-1) cell 1.40 x 10^6. Km 190 ± 5 uM normalizes to 0.19 mM and equals the exported km; kcat 270.0 s^-1 equals the exported kcat; the separately rounded kcat/Km (M^-1 s^-1) cell 1.40 x 10^6 M^-1 s^-1 (= 1400.0 s^-1 mM^-1) is disclosed but not used; the exported kcat_over_km 1421.0526315789473 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells.

normalized_value_unit_evidence: X. maltophilia ULA-511 columns of Table 6 row Tazobactam: Km 190 ± 5 uM = 0.19 mM; kcat 270.0 s^-1 = 270.0 s^-1; kcat/Km 1421.0526315789473 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonama | enzyme column group: X. maltophilia ULA-511 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Tazobactam              440 6 10           0.65       1.50 3 103          420 6 10         6.5          1.55 3 104       190 6 5               270.0     1.40 3 106

row_label: X. maltophilia ULA-511 | Tazobactam

substrate: tazobactam


substrate_name: Temocillin

substrate: Temocillin


substrate_name: piperacillin

substrate: piperacillin


substrate_name: carbenicillin

sequence_source: UniProtKB REST primary accession O51899, fetched 2026-05-27

column_label: PMC1132494 page 154 Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row carbenicillin: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM-to-mM normalization, and their same-row quotient reproduces the exported kcat/Km.

normalized_value_unit_evidence: metric: kcat; raw value: 277; raw unit: s^-1; normalized value: 277.0; normalized unit: s^-1; metric: Km; raw value: 194 +/- 15; raw unit: uM; normalized value: 0.194; normalized unit: mM; metric: kcat/Km; normalized value: 1427.8350515463917; normalized unit: s^-1 mM^-1; assay condition: Table 3 kinetic determinations for the class B beta-lactamase of the Pseudomonas maltophilia ULA-511 L-1 column of Table 3 (the package's Table 3 extract labels this column Stenotrophomonas maltophilia and its header identifies it as the Pseudomonas maltophilia ULA-511 L-1 column); Materials and methods: the experiments for ULA-511 and A. hydrophila were performed in 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2, at 35 C and 30 C respectively, so 35 C applies to this enzyme; the export row carries pH 7.0 and 308.15 K.

raw_value_unit_evidence: Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row carbenicillin: Km cell 194 +/- 15 uM; kcat cell 277 s^-1.

row_label: Stenotrophomonas maltophilia (Pseudomonas maltophilia ULA-511 L-1) beta-lactamase | carbenicillin

substrate: carbenicillin


substrate_name: moxalactam

column_label: PMC1132494 scanned page 154 Table 3; organism/enzyme column Pseudomonas maltophilia ULA-511; row moxalactam; Km column=1 +/- 0.05 uM; kcat column=0.29 s^-1; kcat/Km column=2.90 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: normalized km=0.001 mM; export km=0.001 mM; normalized kcat=0.29 s^-1; export kcat=0.29 s^-1; normalized kcat_over_km=290 s^-1 mM^-1; export kcat_over_km=290 s^-1 mM^-1

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 / moxalactam; Km = 1 +/- 0.05 uM; kcat = 0.29 s^-1; kcat/Km = 2.90 x 10^5 M^-1 s^-1

substrate: moxalactam


substrate_name: Cefuroxime

column_label: PMC1132494 page 154 Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row cefuroxime: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM-to-mM normalization, and their same-row quotient reproduces the exported kcat/Km.

normalized_value_unit_evidence: metric: kcat; raw value: 80; raw unit: s^-1; normalized value: 80.0; normalized unit: s^-1; metric: Km; raw value: 30 +/- 3; raw unit: uM; normalized value: 0.03; normalized unit: mM; metric: kcat/Km; normalized value: 2666.666666666667; normalized unit: s^-1 mM^-1; assay condition: Table 3 kinetic determinations for the class B beta-lactamase of the Pseudomonas maltophilia ULA-511 L-1 column of Table 3 (the package's Table 3 extract labels this column Stenotrophomonas maltophilia and its header identifies it as the Pseudomonas maltophilia ULA-511 L-1 column); Materials and methods: the experiments for ULA-511 and A. hydrophila were performed in 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2, at 35 C and 30 C respectively, so 35 C applies to this enzyme; the export row carries pH 7.0 and 308.15 K.

raw_value_unit_evidence: Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row cefuroxime: Km cell 30 +/- 3 uM; kcat cell 80 s^-1.

row_label: Stenotrophomonas maltophilia (Pseudomonas maltophilia ULA-511 L-1) beta-lactamase | cefuroxime

substrate: Cefuroxime


substrate_name: Cephalosporin C

sequence_source: UniProtKB REST primary accession P52700, fetched 2026-05-27

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM phosphate

column_label: Table 1, row Cephalosporin C, recombinant L1 block: column Km (uM) raw value 180 ± 18; column kcat (s^-1) raw value 280 ± 13; column kcat/Km (s^-1 uM^-1) raw value 1.6. The independently printed kcat/Km cell normalizes to 1600 s^-1 mM^-1 rather than the current export ratio 1555.5555555555557 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 recombinant L1 row Cephalosporin C: Km (uM) 180 ± 18; kcat (s^-1) 280 ± 13; kcat/Km (s^-1 uM^-1) 1.6

row_label: Cephalosporin C

table_label: TABLE 1. Steady-state kinetic constants of recombinant L1 and metallo-beta-lactamase isolated from S. maltophilia ULA-511

substrate: Cephalosporin C


substrate_name: Cephalothin

verification_status: unverified

substrate: Cephalothin

status: unverified


substrate_name: Cefaclor

substrate: Cefaclor


substrate_name: cefmetazole

column_label: Table 1, row Cefmetazole, recombinant L1 block: column Km (uM) raw value 4.1 ± 0.2; column kcat (s^-1) raw value 4.7 ± 0.1; column kcat/Km (s^-1 uM^-1) raw value 1.1. The printed Km normalizes to 0.0041 mM rather than the current export 0.004 mM, and the independently printed kcat/Km normalizes to 1100 s^-1 mM^-1 rather than the current export 1175.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 recombinant L1 row Cefmetazole: Km (uM) 4.1 ± 0.2; kcat (s^-1) 4.7 ± 0.1; kcat/Km (s^-1 uM^-1) 1.1

row_label: Cefmetazole

substrate: cefmetazole


substrate_name: cefepime

substrate: cefepime


substrate_name: Ampicillin

sequence_source: UniProtKB:P52700 reviewed Swiss-Prot direct lookup

substrate: Ampicillin


column_label: Table 1, recombinant L1 section, row Moxalactam; Recombinant L1 columns: Km (uM); kcat (s^-1); kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 recombinant L1 row Moxalactam: Km (uM) 5 ± 1; kcat (s^-1) 0.15 ± 0.01; kcat/Km (s^-1 uM^-1) 0.030

row_label: Recombinant L1 | Moxalactam


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: cefprozil

column_label: Table 1, recombinant L1 section, row Cefprozil; Recombinant L1 columns: Km (uM); kcat (s^-1); kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 recombinant L1 row Cefprozil: Km (uM) 100 ± 20; kcat (s^-1) 15 ± 1; kcat/Km (s^-1 uM^-1) 0.15

row_label: Recombinant L1 | Cefprozil

substrate: cefprozil


column_label: Table 1, recombinant L1 section, row Cefuroxime; Recombinant L1 columns: Km (uM); kcat (s^-1); kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 recombinant L1 row Cefuroxime: Km (uM) 130 ± 40; kcat (s^-1) 53 ± 9; kcat/Km (s^-1 uM^-1) 0.41

row_label: Recombinant L1 | Cefuroxime


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: biapenem

substrate: biapenem


enzyme_display_name: pyruvate kinase

organism: Canis familiaris

substrate_name: ADP; Phosphoenolpyruvate

kcat_display: Not reported

kcat_over_km_display: Not reported

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

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

assay_conditions_summary: cofactor ATP

enzyme: pyruvate kinase

substrate: ADP; Phosphoenolpyruvate


substrate_name: cephalexin

sequence_source: UniProtKB O51899 FASTA via rest.uniprot.org direct lookup on 2026-05-27

column_label: PMC1132494 scanned page 154 Table 3; organism/enzyme column Pseudomonas maltophilia ULA-511; row cephalexin; Km column=100 +/- 8 uM; kcat column=37 s^-1; kcat/Km column=3.70 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: normalized km=0.1 mM; export km=0.1 mM; normalized kcat=37 s^-1; export kcat=37 s^-1; normalized kcat_over_km=370 s^-1 mM^-1; export kcat_over_km=370 s^-1 mM^-1

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 / cephalexin; Km = 100 +/- 8 uM; kcat = 37 s^-1; kcat/Km = 3.70 x 10^5 M^-1 s^-1

substrate: cephalexin


column_label: Table 3 Pseudomonas maltophilia ULA-511 L-1 Ampicillin row; Km cell 40 +/- 3 uM; kcat cell 175 s^-1; independent efficiency cell 4.40 x 10^6 M^-1 s^-1. Current quotient 4375 lies in [4058.13953488, 4743.24324324].

normalized_value_unit_evidence: Km 40 uM = 0.04 mM; kcat 175 s^-1; same-row quotient 175 / 0.04 = 4375 s^-1 mM^-1. The independent printed efficiency is 4400 s^-1 mM^-1 and remains preserved separately.

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 L-1 Ampicillin row: Km 40 +/- 3 uM; kcat 175 s^-1; independently printed kcat/Km 4.40 x 10^6 M^-1 s^-1.

row_label: Pseudomonas maltophilia ULA-511 L-1 | Ampicillin

table_label: Table 3. Kinetic parameters determined for class B beta-lactamases


substrate_name: 6-beta-Iodopenicillanic acid

column_label: Table 3 Pseudomonas maltophilia ULA-511 L-1 6-beta-iodopenicillanic acid row; Km cell 640 +/- 30 uM; kcat cell 648 s^-1; independent efficiency cell 1.00 x 10^6 M^-1 s^-1. Current quotient 1012.5 lies in [966.417910448, 1063.1147541].

normalized_value_unit_evidence: Km 640 uM = 0.64 mM; kcat 648 s^-1; same-row quotient 648 / 0.64 = 1012.5 s^-1 mM^-1. The independent printed efficiency is 1000 s^-1 mM^-1 and remains preserved separately.

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 L-1 6-beta-iodopenicillanic acid row: Km 640 +/- 30 uM; kcat 648 s^-1; independently printed kcat/Km 1.00 x 10^6 M^-1 s^-1.

row_label: Pseudomonas maltophilia ULA-511 L-1 | 6-beta-iodopenicillanic acid

substrate: 6-beta-Iodopenicillanic acid


substrate_name: Imipenem

column_label: Table 3 Pseudomonas maltophilia ULA-511 L-1 Imipenem row; Km cell 90 +/- 8 uM; kcat cell 65 s^-1; independent efficiency cell 7.30 x 10^5 M^-1 s^-1. Current quotient 722.2222222222223 lies in [658.163265306, 798.780487805].

normalized_value_unit_evidence: Km 90 uM = 0.09 mM; kcat 65 s^-1; same-row quotient 65 / 0.09 = 722.2222222222223 s^-1 mM^-1. The independent printed efficiency is 730 s^-1 mM^-1 and remains preserved separately.

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 L-1 Imipenem row: Km 90 +/- 8 uM; kcat 65 s^-1; independently printed kcat/Km 7.30 x 10^5 M^-1 s^-1.

row_label: Pseudomonas maltophilia ULA-511 L-1 | Imipenem

substrate: Imipenem


substrate_name: Cephaloglycin

column_label: Table 3 Pseudomonas maltophilia ULA-511 L-1 Cephaloglycin row; Km cell 36 +/- 2 uM; kcat cell 19 s^-1; independent efficiency cell 5.30 x 10^5 M^-1 s^-1. Current quotient 527.7777777777778 lies in [486.842105263, 573.529411765].

normalized_value_unit_evidence: Km 36 uM = 0.036 mM; kcat 19 s^-1; same-row quotient 19 / 0.036 = 527.7777777777778 s^-1 mM^-1. The independent printed efficiency is 530 s^-1 mM^-1 and remains preserved separately.

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 L-1 Cephaloglycin row: Km 36 +/- 2 uM; kcat 19 s^-1; independently printed kcat/Km 5.30 x 10^5 M^-1 s^-1.

row_label: Pseudomonas maltophilia ULA-511 L-1 | Cephaloglycin

substrate: Cephaloglycin


column_label: PMC1132494 scanned page 154 Table 3; organism/enzyme column Pseudomonas maltophilia ULA-511; row cefoxitin; Km column=2 +/- 0.05 uM; kcat column=1.10 s^-1; kcat/Km column=5.50 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: normalized km=0.002 mM; export km=0.002 mM; normalized kcat=1.1 s^-1; export kcat=1.1 s^-1; normalized kcat_over_km=550 s^-1 mM^-1; export kcat_over_km=550 s^-1 mM^-1

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 / cefoxitin; Km = 2 +/- 0.05 uM; kcat = 1.10 s^-1; kcat/Km = 5.50 x 10^5 M^-1 s^-1


substrate_name: cefotaxime

column_label: Table 3 Pseudomonas maltophilia ULA-511 L-1 cefotaxime row; Km cell 26 +/- 3 uM; kcat cell 66 s^-1; independent efficiency cell 2.60 x 10^6 M^-1 s^-1. Current quotient 2538.4615384615386 lies in [2258.62068966, 2891.30434783].

normalized_value_unit_evidence: Km 26 uM = 0.026 mM; kcat 66 s^-1; same-row quotient 66 / 0.026 = 2538.4615384615386 s^-1 mM^-1. The independent printed efficiency is 2600 s^-1 mM^-1 and remains preserved separately.

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 L-1 cefotaxime row: Km 26 +/- 3 uM; kcat 66 s^-1; independently printed kcat/Km 2.60 x 10^6 M^-1 s^-1.

row_label: Pseudomonas maltophilia ULA-511 L-1 | cefotaxime

substrate: cefotaxime


substrate_name: Sulbactam

column_label: Table 3 Pseudomonas maltophilia ULA-511 L-1 Sulbactam row; Km cell 76 +/- 4 uM; kcat cell 210 s^-1; independent efficiency cell 2.80 x 10^6 M^-1 s^-1. Current quotient 2763.157894736842 lies in [2618.75, 2923.61111111].

normalized_value_unit_evidence: Km 76 uM = 0.076 mM; kcat 210 s^-1; same-row quotient 210 / 0.076 = 2763.157894736842 s^-1 mM^-1. The independent printed efficiency is 2800 s^-1 mM^-1 and remains preserved separately.

raw_value_unit_evidence: Table 3 Pseudomonas maltophilia ULA-511 L-1 Sulbactam row: Km 76 +/- 4 uM; kcat 210 s^-1; independently printed kcat/Km 2.80 x 10^6 M^-1 s^-1.

row_label: Pseudomonas maltophilia ULA-511 L-1 | Sulbactam

substrate: Sulbactam


sequence_source: UniProtKB:P52700 canonical FASTA fetched from rest.uniprot.org on 2026-05-27

column_label: Table 1, recombinant L1 section, row Cefotaxime; Recombinant L1 columns: Km (uM); kcat (s^-1); kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 recombinant L1 row Cefotaxime: Km (uM) 160 ± 20; kcat (s^-1) 140 ± 9; kcat/Km (s^-1 uM^-1) 0.88

row_label: Recombinant L1 | Cefotaxime


substrate_name: Cephaloridine

column_label: Table 1, recombinant L1 section, row Cephaloridine; Recombinant L1 columns: Km (uM); kcat (s^-1); kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 recombinant L1 row Cephaloridine: Km (uM) 170 ± 30; kcat (s^-1) 67 ± 5; kcat/Km (s^-1 uM^-1) 0.39

row_label: Recombinant L1 | Cephaloridine

substrate: Cephaloridine


substrate_name: cefadroxil

column_label: TABLE 1, recombinant L1 block, compound row `Cefadroxil`: column `Km (uM)` = 250 +/- 50; column `kcat (s^-1)` = 23 +/- 2; column `kcat/Km (s^-1 uM^-1)` = 0.092.

normalized_value_unit_evidence: Km: paper cell 250 +/- 50 uM; 250.0 uM / 1000 = 0.25 mM, exactly the catalog km. kcat: paper cell 23 +/- 2 s^-1; already s^-1, exactly the catalog kcat 23.0 s^(-1). kcat/Km: printed cell 0.092 s^-1 uM^-1; 1 uM^-1 = 1000 mM^-1, so 0.092 x 1000 = 92.0 s^(-1)*mM^(-1), exactly the catalog kcat_over_km 92.0.

raw_value_unit_evidence: Table 1, recombinant L1 row Cefadroxil: Km = `250 +/- 50` uM; kcat = `23 +/- 2` s^-1; kcat/Km = `0.092` s^-1 uM^-1.

row_label: Table 1, recombinant L1 block, compound row `Cefadroxil`

substrate: cefadroxil


substrate_name: clavulanic acid

column_label: TABLE 1, recombinant L1 block, compound row `Clavulanic acid`: column `Km (uM)` = 22 +/- 2; column `kcat (s^-1)` = 11 +/- 1; column `kcat/Km (s^-1 uM^-1)` = 0.50.

normalized_value_unit_evidence: Km: paper cell 22 +/- 2 uM; 22.0 uM / 1000 = 0.022 mM, exactly the catalog km. kcat: paper cell 11 +/- 1 s^-1; already s^-1, exactly the catalog kcat 11.0 s^(-1). kcat/Km: printed cell 0.50 s^-1 uM^-1 x 1000 = 500.0 s^(-1)*mM^(-1); the catalog stores 500.00000000000006, i.e. the same number carried at binary-float precision from 11.0 / 0.022, differing from the printed value only in the 14th significant digit.

raw_value_unit_evidence: Table 1, recombinant L1 row Clavulanic acid: Km = `22 +/- 2` uM; kcat = `11 +/- 1` s^-1; kcat/Km = `0.50` s^-1 uM^-1.

row_label: Table 1, recombinant L1 block, compound row `Clavulanic acid`

substrate: clavulanic acid


substrate_name: Ceftizoxime

column_label: TABLE 1, recombinant L1 block, compound row `Ceftizoxime`: column `Km (uM)` = 7.9 +/- 1.6; column `kcat (s^-1)` = 2.7 +/- 0.1; column `kcat/Km (s^-1 uM^-1)` = 0.34.

normalized_value_unit_evidence: kcat: printed cell 2.7 +/- 0.1 s^-1 -> 2.7 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 7.9 +/- 1.6 uM -> 7.9 uM / 1000 = 0.0079 mM. kcat/Km: printed cell 0.34 s^-1 uM^-1 x 1000 = 340.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, recombinant L1 row Ceftizoxime: Km = `7.9 +/- 1.6` uM; kcat = `2.7 +/- 0.1` s^-1; kcat/Km = `0.34` s^-1 uM^-1.

row_label: Table 1, recombinant L1 block, compound row `Ceftizoxime`

substrate: Ceftizoxime


organism: Treponema pallidum

substrate_name: Cloxacillin

sequence_source: UniProtKB:P29723 canonical FASTA fetched from rest.uniprot.org on 2026-05-27

substrate: Cloxacillin


substrate_name: carbenicillin

substrate: carbenicillin


organism: Arabidopsis thaliana

substrate_name: ADP

source_db: brenda

sequence_source: UniProtKB:Q9FFP6 direct accession lookup on 2026-05-28

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ADP

source: brenda


sequence_source: UniProtKB:Q9FM97 direct accession lookup on 2026-05-28


sequence_source: UniProtKB:Q94KE3 direct accession lookup on 2026-05-28


sequence_source: UniProtKB:Q9SJQ0 direct accession lookup on 2026-05-28


sequence_source: UniProtKB:Q9FNN1 direct accession lookup on 2026-05-28


organism: Rattus norvegicus

substrate_name: Phosphoenolpyruvate; ADP

sequence_source: UniProtKB:P11980 direct fetch

sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 direct fetch and applied mutation signature A398R/E432A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432A

substrate: Phosphoenolpyruvate; ADP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 direct fetch and applied mutation signature A398R/E432K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 direct fetch and applied mutation signature E432A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 direct fetch and applied mutation signature E432D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 direct fetch and applied mutation signature E432K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 direct fetch and applied mutation signature A398R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R


organism: Saccharomyces cerevisiae

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

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R336K


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R336Q


organism: Chryseobacterium indologenes

sequence_source: UniProtKB REST direct lookup: Q6JE29

assay_conditions_summary: pH 6.5; buffer note

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


organism: Escherichia coli

substrate_name: cefotaxime; cefalotin

sequence_variant_note: Mutation signature R276G matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: cefotaxime; cefalotin


sequence_variant_note: Mutation signature R276N matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature R276S matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: cefalotin; cefotaxime

sequence_variant_note: Mutation signature R276H matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: cefalotin; cefotaxime


substrate_name: cephalothin; penicillin G; cefotaxime; cefoxitin; ceftazidime

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


organism: Synechococcus elongatus

substrate_name: ADP; Phosphoenolpyruvate

substrate: ADP; Phosphoenolpyruvate


sequence_source: UniProtKB P0AD61 canonical sequence from direct accession lookup.


organism: Homo sapiens

sequence_source: UniProtKB P30613 canonical sequence; reconstructed R510Q after direct residue check confirmed R at position 510.

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R510Q


organism: Leishmania mexicana

sequence_source: UniProtKB direct accession lookup Q27686, retrieved 2026-05-29

assay_conditions_summary: pH 7.5; buffer is pH 7; cofactor ADP


organism: Trypanosoma brucei


organism: Aeromonas hydrophila

substrate_name: H2O; Imipenem

source_db: merged

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

sequence_source: UniProtKB:P26918 canonical sequence checked on 2026-05-29; variant sequence unresolved

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

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

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N116H/N220G

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

substrate: H2O; Imipenem

source: merged


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N220G


organism: Bacillus cereus

substrate_name: Nitrocefin; H2O / Imipenem; H2O / related beta-lactam source rows

ki_unit: mM

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant BcII delta IMP


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant BcII delta IMP W64A

substrate: Nitrocefin; H2O / Imipenem; H2O / related beta-lactam source rows


substrate_name: Cefotaxime / Cephapirin / Imipenem / Nitrocefin source rows


substrate_name: Nitrocefin / Cefotaxime / Imipenem / Penicillin G source rows

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120E; fusion protein to glutathione-S-transferase


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120Q; fusion protein to glutathione-S-transferase

substrate: Nitrocefin / Cefotaxime / Imipenem / Penicillin G source rows


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120N; fusion protein to glutathione-S-transferase


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120S; fusion protein to glutathione-S-transferase


substrate_name: Nitrocefin / Cephalosporin C / 6-Aminopenicillanate / related source rows

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K73R


substrate_name: Sulbactam

sequence_source: UniProtKB Q6JE29 canonical sequence checked 2026-05-29.

assay_conditions_summary: pH 6.5; buffer pH 6


organism: Spinacia oleracea

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


organism: Brassica napus

assay_conditions_summary: pH 6.8; 297.15 K; cofactor ATP


organism: Entamoeba histolytica

substrate_name: phosphoenolpyruvate

assay_conditions_summary: 299.15 K; cofactor ADP

substrate: phosphoenolpyruvate


organism: Mucor rouxii

km_display: Not reported


organism: Plasmodium falciparum


organism: Synechococcus sp.

sequence_source: UniProtKB:A0A0H3K2W0 direct FASTA; organism_id 269084 Synechococcus sp. PCC 6301

proof_lines:
allosteric enzyme, pH 7.5, 24°C
allosteric enzyme, pH 7.0, 24°C


organism: Toxoplasma gondii

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

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


organism: Urocitellus richardsonii

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

proof_lines: purified enzyme, pH 7.0, 25°C/room temperature


organism: Bos taurus


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AD61 REST lookup 2026-05-29; reconstructed variant K382Q from canonical sequence and applied mutation signature K382Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K382Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AD61 REST lookup 2026-05-29; reconstructed variant R431E from canonical sequence and applied mutation signature R431E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R431E


organism: Rattus norvegicus

sequence_source: UniProtKB direct accession lookup for B1WBN9; TrEMBL entry B1WBN9_RAT is Rattus norvegicus pyruvate kinase with EC 2.7.1.40.

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


substrate_name: Pyruvate; ATP

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

substrate: Pyruvate; ATP


organism: Ricinus communis

sequence_source: UniProtKB direct accession lookup for Q43117; reviewed Swiss-Prot entry KPYA_RICCO is Ricinus communis pyruvate kinase isozyme A, chloroplastic, EC 2.7.1.40.


organism: Vibrio cholerae serotype O1

sequence_source: UniProtKB:Q9KUN0 direct REST lookup, retrieved 2026-05-29

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

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:Q9KQJ0 direct REST lookup, retrieved 2026-05-29

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


organism: Homo sapiens

sequence_source: UniProt P30613 reviewed canonical sequence fetched directly; R510Q applied after confirming residue 510 is R.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R510Q


organism: Corynebacterium glutamicum

sequence_source: UniProtKB REST accession Q46078 (UniProtKB reviewed Swiss-Prot), checked 2026-05-29

assay_conditions_summary: pH 7; 308.15 K; cofactor ATP


organism: Oncorhynchus mykiss

substrate_name: AMP; Phosphate; Phosphoenolpyruvate

substrate: AMP; Phosphate; Phosphoenolpyruvate


organism: Oryctolagus cuniculus

sequence_source: uniprot:P11974; direct REST lookup 2026-05-29


sequence_source: UniProtKB:P11980 checked directly; row-specific A398R/E432D sequence not reconstructed because residue coordinates did not validate

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432D


organism: Saccharomyces cerevisiae

sequence_source: UniProt P00549 FASTA checked 2026-05-29; reconstructed R409Q variant after canonical residue validation

sequence_variant_note: Mutation signature R409Q matches the mutant residue at offset +0 and the reference residue at offset +6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R409Q


organism: Trachemys scripta elegans

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


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


organism: Morganella morganii subsp. morganii

substrate_name: cephalothin

sequence_source: UniProtKB direct lookup Q704Y9; EMBL AJ620363 / protein CAF04714.1; strain PP37

assay_conditions_summary: pH 7; 303.15 K; buffer context

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

substrate: cephalothin


organism: Streptococcus sanguis


organism: Vigna radiata

assay_conditions_summary: pH 6.5; 303.15 K; cofactor ADP


organism: Trypanosoma brucei

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant L76R


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R22G


enzyme_display_name: Beta-enolase

sequence_variant_note: Resolved canonical sequence from UniProtKB:P25704 REST FASTA retrieved 2026-05-30 and applied mutation signature G37A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

enzyme: Beta-enolase


sequence_source: UniProtKB:P25704 REST FASTA retrieved 2026-05-30


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25704 REST FASTA retrieved 2026-05-30 and applied mutation signature G41A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphopyruvate hydratase(Enzyme) mutant Enolase G41A


proof_lines: SABIO-RK modifier species: phosphopyruvate hydratase(Enzyme) mutant Enolase G37A


enzyme_display_name: phosphopyruvate hydratase

organism: Canis familiaris

enzyme: phosphopyruvate hydratase


organism: Chloroflexus aurantiacus

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

sequence_source: UniProt REST accession A9WCM4, direct lookup 2026-05-30

proof_lines:
pH 6.5, 80°C
pH 6.5, 25°C
Raw SKiD Env: Temp=80°C, pH=6.5

source_databases_merged: brenda skid


organism: Entamoeba histolytica

substrate_name: H2O; Phosphoenolpyruvate

sequence_source: UniProt REST accession P51555, direct lookup 2026-05-30

substrate: H2O; Phosphoenolpyruvate


organism: Escherichia coli

sequence_source: UniProt REST accession P0A6P9, direct lookup 2026-05-30


organism: Glycine max

sequence_source: UniProt REST accession Q6RIB7, direct lookup 2026-05-30


sequence_source: UniProt REST accession P13929, direct lookup 2026-05-30


sequence_source: UniProt REST accession P06733, direct lookup 2026-05-30


sequence_source: UniProt REST accession P09104, direct lookup 2026-05-30


organism: Leishmania mexicana

sequence_source: UniProtKB Q3HL75 exact accession lookup, fetched 2026-05-30

proof_lines: recombinant protein, substrate 2-phospho-D-glycerate


organism: Leuconostoc mesenteroides

sequence_source: UniProtKB Q1ET73 exact accession lookup, fetched 2026-05-30

proof_lines:
at pH 6.8
in absence of phosphate
in presence of 1 mM phosphate


organism: Mus musculus

sequence_source: UniProtKB P17182 exact accession lookup, fetched 2026-05-30


sequence_source: UniProtKB P17183 exact accession lookup, fetched 2026-05-30


sequence_source: UniProtKB P25704 exact accession lookup plus direct E414L reconstruction, fetched/computed 2026-05-30

proof_lines: SABIO-RK modifier species: phosphopyruvate hydratase(Enzyme) mutant E414L


substrate_name: 3-Fluoro 2-phospholactate

sequence_source: UniProtKB:P25704 direct REST lookup (https://rest.uniprot.org/uniprotkb/P25704.json)

substrate: 3-Fluoro 2-phospholactate


organism: Plasmodium falciparum

sequence_source: UniProtKB:Q8IJN7 direct REST lookup (https://rest.uniprot.org/uniprotkb/Q8IJN7.json)


sequence_source: UniProtKB:Q27727 direct REST lookup (https://rest.uniprot.org/uniprotkb/Q27727.json)

proof_lines:
acitivity for monomers
activity for dimeric form


organism: Pyrococcus furiosus


sequence_source: UniProtKB:Q8U477 direct REST lookup (https://rest.uniprot.org/uniprotkb/Q8U477.json)


organism: Rattus norvegicus

sequence_source: UniProtKB:P04764 direct REST lookup (https://rest.uniprot.org/uniprotkb/P04764.json)


organism: Ricinus communis

sequence_source: UniProtKB:P42896 direct REST lookup (https://rest.uniprot.org/uniprotkb/P42896.json)


organism: Anaplasma phagocytophilum

sequence_source: UniProtKB Q2GK24 direct REST lookup on 2026-05-30


organism: Aphidius ervi

sequence_source: UniProtKB C9YSH7 direct REST lookup on 2026-05-30

proof_lines: in 81 mM triethanolamine/HCl, pH 7.4, at 25°C


organism: Bacillus subtilis

sequence_source: UniProtKB P37869 direct REST lookup on 2026-05-30


organism: Bacteroides fragilis

sequence_source: UniProtKB Q8KNX9 direct REST lookup on 2026-05-30

assay_conditions_summary: 310.15 K; buffer reaction


organism: Bos taurus

sequence_source: UniProtKB Q3ZC09 direct REST lookup on 2026-05-30


sequence_source: UniProtKB Q9XSJ4 direct REST lookup on 2026-05-30


organism: Brucella abortus

sequence_source: UniProtKB Q2YPV0 direct REST lookup on 2026-05-30

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


organism: Oryctolagus cuniculus

sequence_variant_note: Resolved canonical sequence from UniProtKB:P25704 canonical sequence; G37A reconstructed using PMID 15752688 mature-protein numbering with UniProt offset +1 and applied mutation signature G37A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P25704 canonical sequence; G37A reconstructed using PMID 15752688 mature-protein numbering with UniProt offset +1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25704 canonical sequence; G41A reconstructed using PMID 15752688 mature-protein numbering with UniProt offset +1 and applied mutation signature G41A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P25704 canonical sequence


sequence_source: UniProtKB:P25704 canonical sequence; G41A reconstructed using PMID 15752688 mature-protein numbering with UniProt offset +1


organism: Saccharolobus solfataricus

sequence_source: UniProtKB:Q97ZJ3 FASTA fetched directly on 2026-05-30.

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

proof_lines: 80°C, pH not specified in the publication

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


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P00924 FASTA fetched directly on 2026-05-30; S39A reconstructed by applying the paper residue numbering to UniProt residue 40.

proof_lines: SABIO-RK modifier species: phosphopyruvate hydratase(Enzyme) mutant S39A


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


sequence_source: UniProtKB:P00924 FASTA fetched directly on 2026-05-30.


sequence_source: UniProtKB:P00924 FASTA fetched directly on 2026-05-30; N80D/N126D reconstructed by applying the paper residue numbering to UniProt residues 81 and 127.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.


sequence_source: UniProtKB:P0CX11 FASTA fetched directly on 2026-05-30.


assay_conditions_summary: pH 6.5; 303.15 K; buffer a standardised reaction

column_label: Section 3.4, decoded plain-ASCII restatement, Eno1p with 3-phosphoglycerate: kcat (s^-1) = 5.07 (SEM 2.9%); Km (mM) = 0.617 (SEM 10.2%). The article prints no kcat/Km value for this measurement.

normalized_value_unit_evidence: kcat: printed value 5.07 s^-1 -> 5.07 s^(-1); the catalog holds 5.07 s^(-1); no unit conversion applied (the paper prints the reciprocal second directly, written s^-1 in the decoded block and s−1 in the article). Km: printed value 0.617 mM -> 0.617 mM; the catalog holds 0.617 mM; no unit conversion applied (the paper prints mM). kcat/Km: The catalog kcat_over_km 8.217179902755268 s^(-1)*mM^(-1) is NOT a printed cell: this paper prints no kcat/Km, catalytic-efficiency or specificity-constant value anywhere, in Table 2 or in its text. The catalog value is the exact full-precision quotient of this measurement's own printed kcat and Km, 5.07 s^-1 / 0.617 mM, so it is typed derived_same_measurement rather than quoted.

row_label: Section 3.4, the sentence reporting 3-phosphoglycerate as a substrate for Eno1p (decoded plain-ASCII restatement)

table_label: Table 2 'Enzyme kinetics parameters determined in this project and contrasted with those of [23]'


sequence_source: UniProtKB:P00925 FASTA fetched directly on 2026-05-30.

assay_conditions_summary: pH 6.5; 303.15 K; buffer a standardised reaction; cofactor NADPH

column_label: Table label: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]". Reaction: ENO. Isoenzyme: Eno2p. Rows read: Parameter kcat, Value cell 19.9, Unit cell s−1; Parameter Kp2g, Value cell 0.104, Unit cell mM. metric: kcat; raw value: 19.9; raw unit: s^-1; normalized value: 19.9 s^(-1); metric: Km; raw value: 0.104; raw unit: mM; normalized value: 0.104 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 191.34615384615384 s^-1 mM^-1; assay condition: Spectrophotometric assays of the glycolytic isoenzymes measuring consumption or production of NADH or NADPH; all assays were performed in a standardised reaction buffer at 30 °C in 384-well format plates with a 60 μl reaction volume, reagents in 45 μl, enzyme in 5 μl and substrate in 10 μl, with duplicate initial-rate measurements fitted to Michaelis-Menten kinetics. Export row conditions: pH 6.5; 303.15 K.

normalized_value_unit_evidence: Table 2 rows for ENO | Eno2p: kcat 19.9 s−1 = 19.9 s^(-1) (the paper's unit s−1 is already the export unit s^(-1), no conversion); Kp2g 0.104 mM = 0.104 mM (the paper's Km-equivalent cell is already in the export unit mM, no conversion); kcat/Km 19.9 s^-1 mM^-1 = 191.34615384615384 s^-1 mM^-1 divided as 19.9 / 0.104. In the on-disk transcription the superscript minus one renders as the flattened `s−1` (U+2212 minus sign) and empty SEM/Ref cells render as empty ` | ` fields, so the kcat row prints as `ENO | Eno2p | kcat | 19.9 |  |  | s−1`.

raw_value_unit_evidence: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]" | header row: Reaction | Isoenzyme | Parameter | Value | SEM (%) | Ref. [23] | Unit | kcat row: ENO | Eno2p | kcat | 19.9 |  |  | s−1 | Kp2g row: ENO | Eno2p | Kp2g | 0.104 |  | 0.04 | mM | cells read: kcat = 19.9 s−1 (Value column, Unit column s−1); Kp2g = 0.104 mM (Value column, Unit column mM)

row_label: ENO | Eno2p


proof_lines:
cytosolic isoenzyme
plastidic isoenzyme


sequence_source: UniProtKB:P00924 FASTA


sequence_source: UniProtKB:P00925 FASTA

assay_conditions_summary: 303.15 K; buffer a standardised reaction; cofactor NADPH

column_label: Table label: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]". Reaction: ENO. Isoenzyme: Eno2p. Rows read: ENO | Eno2p | kcat -> Value cell 19.9, Unit cell s−1; ENO | Eno2p | Kp2g -> Value cell 0.104, Unit cell mM. kcat/Km: no printed cell (Table 2 has no kcat/Km column).

normalized_value_unit_evidence: kcat 19.9 s−1 = 19.9 s^(-1) (printed unit s−1 is the export unit s^(-1), no conversion); decimal-equal to the catalog kcat 19.9; Km (Kp2g) 0.104 mM = 0.104 mM (already the export unit, no conversion); decimal-equal to the catalog km 0.104. In the on-disk transcription the printed superscript minus renders as the flattened `s−1` (U+2212) and empty SEM/Ref cells render as empty ` | ` fields.

raw_value_unit_evidence: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]" | header row: Reaction | Isoenzyme | Parameter | Value | SEM (%) | Ref. [23] | Unit | kcat evidence: ENO | Eno2p | kcat | 19.9 |  |  | s−1 | Km evidence: ENO | Eno2p | Kp2g | 0.104 |  | 0.04 | mM | cells read: kcat = 19.9 s−1 (Value column); Kp2g = 0.104 mM


sequence_source: UniProtKB:P42222 FASTA


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


organism: Spinacia oleracea

sequence_source: UniProtKB Q9LEE0 direct lookup on 2026-05-30; entry Q9LEE0_SPIOL, unreviewed, phosphopyruvate hydratase, organism Spinacia oleracea, EC 4.2.1.11.


organism: Streptococcus iniae

sequence_source: UniProtKB T1TFA0 direct lookup on 2026-05-30; entry T1TFA0_STRIN, unreviewed, enolase, organism Streptococcus iniae, EC 4.2.1.11.

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


organism: Streptococcus mutans

sequence_source: UniProtKB Q8DTS9 direct lookup on 2026-05-30; entry ENO_STRMU, reviewed, enolase, organism Streptococcus mutans serotype c strain ATCC 700610 / UA159, EC 4.2.1.11.


organism: Streptococcus pneumoniae

sequence_source: UniProtKB Q97QS2 direct lookup on 2026-05-30; entry ENO_STRPN, reviewed, enolase, organism Streptococcus pneumoniae serotype 4 strain ATCC BAA-334 / TIGR4, EC 4.2.1.11.


organism: Streptococcus pyogenes

sequence_source: UniProtKB Q5XD01 direct lookup on 2026-05-30; entry ENO_STRP6, reviewed, enolase, organism Streptococcus pyogenes serotype M6 strain ATCC BAA-946 / MGAS10394, EC 4.2.1.11.


organism: Streptococcus sanguis

sequence_source: UniProtKB A0A024F8D9 direct lookup on 2026-05-30; entry A0A024F8D9_STRSA, unreviewed, enolase, organism Streptococcus sanguinis, EC 4.2.1.11.


organism: Streptococcus suis

sequence_source: UniProtKB C6GGT7 direct lookup on 2026-05-30; entry C6GGT7_STRSU, unreviewed, enolase, organism Streptococcus suis, EC 4.2.1.11.

proof_lines: in 100 mM HEPES, 10 mM MgCl2, and 7.7 mM KCl, pH 7.0, at 37°C


organism: Sus scrofa

sequence_source: UniProtKB Q1KYT0 direct lookup on 2026-05-30; entry ENOB_PIG, reviewed, beta-enolase, organism Sus scrofa, EC 4.2.1.11.


organism: Trypanosoma brucei

sequence_source: UniProtKB REST accession lookup for Q9NDH8 on 2026-05-30

proof_lines: at pH 7.2, binds in the same way as phosphoenolpyruvate and phosphonoacetohydroxamate


sequence_source: UniProtKB REST accession lookup for Q38BV6 on 2026-05-30


organism: Ustilago maydis

sequence_source: UniProtKB REST accession lookup for A0A0D1E2E4 on 2026-05-30


organism: Vibrio parahaemolyticus

sequence_source: UniProtKB REST accession lookup for W6ABG9 on 2026-05-30

assay_conditions_summary: pH 8.5; 298.15 K; buffer conditions

proof_lines: in 100 mM HEPES buffer, pH 8.5, 7.7 mM KCl, 10 mM MgSO4, at 25°C


organism: Xenopus laevis

sequence_source: UniProtKB REST accession lookup for P08734 on 2026-05-30


organism: Zymomonas mobilis

sequence_source: UniProtKB REST accession lookup for P33675 on 2026-05-30


organism: Arabidopsis thaliana

substrate_name: 2-PGA (at pH 8)

source_db: uniprot

assay_conditions_summary: pH 8

substrate: 2-PGA (at pH 8)

source: uniprot


organism: Bacillus subtilis (strain 168)


organism: Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)

substrate_name: 2-phosphoglycerate (2-PG) at 80 degrees Celsius


organism: Escherichia coli (strain K12)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: phosphoenolpyruvate (expression in E.coli)


organism: Nitratidesulfovibrio vulgaris (strain DSM 19637 / Miyazaki F)

substrate_name: 2-phosphoglycerate (at 25 degrees Celsius and pH 8)


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: 2-phospho-D-glycerate (at 75 degrees Celsius)


organism: Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)


organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)


organism: Busycon canaliculatum


organism: Candida albicans

proof_lines: pH 6.8, 30ºC, in the absence of phosphate


organism: Cyprinus carpio


organism: Gallus gallus

proof_lines: brain enolase I, brain enolase II, brain enolase III


organism: Homo sapiens

assay_conditions_summary: pH 6.8; buffer 50 mM imidazole-HCl

proof_lines: in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl

proof_lines: native enzyme, in the absence of methyglyoxal, in 50 mM imidazole-HCl buffer, pH 6.8, with 0.4 M KCl and 3 mM MgSO4


organism: Ilyanassa obsoleta


organism: Actinomyces naeslundii


proof_lines:
at pH 8.0
at pH 7.0


organism: Archaeoglobus fulgidus

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


organism: Bacillus anthracis


organism: Bacillus megaterium


organism: Bacteroides fragilis

proof_lines: pH and temperature not specified in the publication


organism: Klebsiella pneumoniae

assay_conditions_summary: pH 7.8; buffer 50 mM imidazole-HCl

proof_lines: at low phosphate concentrations (4-6 mM), in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl


organism: Lactobacillus rhamnosus


organism: Littorina littorea


organism: Macaca mulatta


organism: Mercenaria mercenaria


organism: Mus musculus


organism: Mytilus edulis


organism: Nucella lapillus


organism: Oncorhynchus keta


organism: Oncorhynchus kisutch


organism: Oryctolagus cuniculus


organism: Pagrus major


organism: Planorbis corneus


organism: Plasmodium falciparum

proof_lines: recombinant, His-tagged, hexameric enzyme


organism: Priestia megaterium


organism: Rattus norvegicus

substrate_name: Phosphoenolpyruvate; H2O

proof_lines:
liver enzyme
muscle enzyme
enolase III

substrate: Phosphoenolpyruvate; H2O


organism: Saccharomyces cerevisiae

proof_lines: isoform Eno1p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication

proof_lines: isoform Err2p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication


proof_lines:
wild-type enzyme
wild type enzyme


proof_lines: in presence of 1 mM Mg2+, mutant enzyme S39A


organism: Scomber japonicus


organism: Spinacia oleracea


organism: Streptococcus mutans


organism: Streptococcus ratti


organism: Streptococcus salivarius


organism: Streptococcus sanguis


organism: Sus scrofa

proof_lines:
pH 6.8, liver enolase
pH 7.4, muscle enolase
pH 6.8, muscle enolase


organism: Teladorsagia circumcincta


organism: Thermotoga maritima

sequence_source: UniProtKB:P42848 reviewed Swiss-Prot ENO_THEMA; EC 4.2.1.11 evidence includes PMID:7757011


organism: Taenia pisiformis

sequence_source: UniProtKB REST exact accession lookup: T1WGD6

proof_lines: 22°C, pH not specified in the publication


organism: Taenia solium

sequence_source: UniProtKB REST exact accession lookup: V5T827

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


organism: Theileria annulata

sequence_source: UniProtKB REST exact accession lookup: E9NJD0


proof_lines: 1.5 mM MgCl2 in 50 mM Tris/HCl (pH 7.4), at 25°C


organism: Toxoplasma gondii

sequence_source: UniProtKB REST exact accession lookup: Q9BPL7


sequence_source: UniProtKB REST exact accession lookup: Q9UAE6


proof_lines: SABIO-RK modifier species: phosphopyruvate hydratase(Enzyme) mutant ENO1deltaEWGYS

proof_lines: SABIO-RK modifier species: phosphopyruvate hydratase(Enzyme) mutant ENO1deltaEKdeltaEWGYS


organism: Trachemys scripta

sequence_source: UniProtKB REST exact accession lookup: Q9W7L1


organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)

substrate_name: 2-phosphoglycerate (at pH 7 and 37 degrees Celsius)

proof_lines: kcat is 170 sec(-1) with 2-phosphoglycerate as substrate (at pH 7 and 37 degrees Celsius) (PubMed:15794763). kcat is 147 sec(-1) with 2-phosphoglycerate as substrate (at pH 6 and 37 degrees Celsius) (PubMed:15794763). kcat is 43 sec(-1) wit


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: 2-phosphoglyceric acid (at 21 degrees Celsius and pH 7.5)

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

proof_lines: kcat is 20.6 sec(-1) with 2-phosphoglyceric acid as substrate (at 21 degrees Celsius and pH 7.5).


organism: Staphylococcus aureus

substrate_name: 2-phosphoglycerate by octamer

substrate: 2-phosphoglycerate by octamer


organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

proof_lines: Also catalytically active when expressed on the bacterial cell surface.


organism: Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)

proof_lines: Catalytically active also when expressed on the bacterial cell surface.


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


organism: Amycolatopsis methanolica

substrate_name: Phosphoenolpyruvate; ADP

sequence_source: UniProtKB A0A076MW80 REST lookup, checked 2026-05-30

assay_conditions_summary: cofactor ATP


organism: Bos taurus


organism: Chlamydia trachomatis


organism: Corynebacterium glutamicum

substrate_name: ADP; Phosphoenolpyruvate


organism: Escherichia coli

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K382Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R431E


sequence_source: UniProtKB:P0AD61 canonical sequence checked on 2026-05-30; selected payload has no mutation signature.


organism: Homo sapiens

sequence_source: UniProt P30613 direct accession lookup


organism: Lactococcus lactis subsp. cremoris

sequence_source: UniProt A2RKA3 direct accession lookup


organism: Lactococcus lactis subsp. lactis

sequence_source: UniProt Q07637 direct accession lookup


organism: Saccharomyces cerevisiae

sequence_source: UniProt P00549 canonical sequence retrieved 2026-05-30; Y436F applied after confirming residue 436 is Y.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant Y436F


sequence_source: UniProt P00549 canonical sequence retrieved 2026-05-30; Q299N applied after confirming residue 299 is Q.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant Q299N


sequence_source: UniProt P00549 canonical sequence retrieved 2026-05-30; A458K applied after confirming residue 458 is A.

sequence_variant_note: Mutation signature A458K matches the mutant residue at offset +0 and the reference residue at offset +9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant A458K


sequence_source: UniProt P00549 canonical sequence retrieved 2026-05-30; K236Q applied after confirming residue 236 is K.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K236Q


sequence_source: UniProt P00549 canonical sequence retrieved 2026-05-30; Y436S applied after confirming residue 436 is Y.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant Y436S


sequence_source: UniProt P00549 canonical sequence retrieved 2026-05-30; T406R applied after confirming residue 406 is T.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T406R


sequence_source: UniProt P00549 canonical sequence retrieved 2026-05-30; R409Q applied after confirming residue 409 is R.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R409Q


sequence_source: UniProtKB P00549 canonical sequence checked directly; reconstructed by applying R369A after residue validation.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R369A


sequence_source: UniProtKB P00549 canonical sequence checked directly; reconstructed by applying T403K after residue validation.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T403K


sequence_source: UniProtKB P00549 canonical sequence checked directly; reconstructed by applying R459Q after residue validation.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R459Q


sequence_source: UniProtKB P00549 canonical sequence checked directly; reconstructed by applying K292Q after residue validation.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K292Q


sequence_source: UniProtKB P00549 canonical sequence checked directly; reconstructed by applying T311M after residue validation.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T311M


sequence_source: UniProtKB P00549 canonical sequence checked directly; reconstructed by applying E392A after residue validation.

sequence_variant_note: Mutation signature E392A matches the mutant residue at offset +0 and the reference residue at offset -12; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant E392A


sequence_source: UniProtKB P00549 canonical sequence checked directly; reconstructed by applying R77Q after residue validation.

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R77Q


sequence_source: UniProtKB P00549 canonical sequence checked directly; reconstructed by applying T298S after residue validation.

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant isoenzyme Pyk1 T298S


organism: Selenomonas ruminantium

substrate_name: phosphoenolpyruvate

sequence_source: UniProtKB Q9LBS6 direct lookup


organism: Thermofilum pendens

substrate_name: ADP

sequence_source: UniProtKB A1RX09 direct lookup

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

substrate: ADP


sequence_source: UniProtKB REST accession check for P00549 on 2026-05-30 with T403E substitution applied after confirming canonical residue T at position 403

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T403E


organism: Trichomonas vaginalis

substrate: Phosphoenolpyruvate; ADP


organism: Ustilago maydis

sequence_source: UniProtKB A0A0D1E735 REST accession lookup on 2026-05-30


organism: Zymomonas mobilis

sequence_source: UniProtKB Q5NR78 REST accession lookup on 2026-05-30


organism: Chryseobacterium indologenes

substrate_name: Sulbactam

sequence_source: UniProtKB Q6JE29 direct REST check on 2026-05-30

assay_conditions_summary: pH 6.5; buffer the selected row: 30 mM sodium cacodylate

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

substrate: Sulbactam


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ADP

proof_lines:
apparent value
pH 7.1, 37°C
R-type isozyme, pH 7.4, 37°C


organism: Psychrobacter immobilis

substrate_name: ampicillin

sequence_source: UniProtKB:O05465 reviewed Psychrobacter immobilis ampC, PMID 9063463

assay_conditions_summary: pH 7; 303.15 K; buffer condition note 30 C in sodium phosphate

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

substrate: ampicillin


enzyme_display_name: laccase

organism: Aeromonas hydrophila

substrate_name: 2,2'-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid); O2 / 2,6-Dimethoxyphenol; O2

sequence_source: UniProtKB:D5FL31 REST lookup on 2026-05-30

enzyme: laccase


organism: alpha proteobacterium Q-1

substrate_name: 2,2'-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid); O2 / I-; H+; O2


organism: Acidobacteriaceae


organism: Bacillus amyloliquefaciens

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant Lac3A/S, chimeric LacA (domain1 and 2)/LacS (domain 3) from Bacillus subtilis LS02


organism: Amycolatopsis sp.

sequence_source: UniProtKB:J9PBQ8 direct accession lookup on 2026-05-30


organism: Aquifex aeolicus

mutation_type: deletion

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deltaP321-V363


organism: Bacillus licheniformis

sequence_source: UniProtKB:A0A0A6ZHX8 TrEMBL sequenceVersion 1, retrieved 2026-05-30


sequence_source: Reconstructed from UniProtKB:H8WGE4 TrEMBL sequenceVersion 1 by applying D500G; residue 500 was D in direct lookup, retrieved 2026-05-30

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D500G


sequence_source: UniProtKB Q65MU7 REST lookup checked 2026-05-30; active TrEMBL laccase entry for Bacillus licheniformis strain ATCC 14580 / DSM 13 with EC 1.10.3.2 and 513-aa sequence. Variant sequence was reconstructed from Q65MU7 after residue checks.

assay_conditions_summary: pH 4; buffer 0.1 M citrate/phosphate


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant K316N/D500G


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant K316N


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D501G


organism: Bacillus pumilus


sequence_source: UniProtKB A0A0G2QNK1 canonical sequence fetched by direct REST lookup on 2026-05-30; row-specific substitutions G417L applied after old-residue validation.

sequence_variant_note: Mutation signature G417L matches the mutant residue at offset +0 and the reference residue at offset -13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant G417L N-terminal His6-tag


sequence_source: UniProtKB A0A0G2QNK1 canonical sequence fetched by direct REST lookup on 2026-05-30; row-specific substitutions L386W/G417L/D152W applied after old-residue validation.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W/G417L/D152W N-terminal His6-tag


sequence_source: UniProtKB A0A0G2QNK1 canonical sequence fetched by direct REST lookup on 2026-05-30; row-specific substitutions L386W/G417L/G57L applied after old-residue validation.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W/G417L/G57L N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W/G417L/D152Y N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W/G417L/D195W N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W/G417L/D195F N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W/G417L/D152F N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W/G417L N-terminal His6-tag


sequence_source: UniProtKB:A0A0G2QNK1 canonical sequence checked 2026-05-30; L386W/G417L/G57W substitutions applied after confirming L386, G417, and G57 in the canonical sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W/G417L/G57W N-terminal His6-tag


sequence_source: UniProtKB A0A0G2QNK1 canonical sequence with row mutation signature reconstructed during review

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386W/G417L/G57F N-terminal His6-tag


sequence_variant_note: Mutation signature F227A matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant F227A N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant S208G N-terminal His6-tag


sequence_variant_note: Mutation signature S208G/F227A matches the mutant residue at offset +0 and the reference residue at offset -29; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant S208G/F227A N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T415D N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T415D/Q442A N-terminal His6-tag


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T418K/Q442A N-terminal His6-tag


sequence_source: UniProtKB:A0A0G2QNK1 canonical sequence with K317N/D501G/L386W/G417L/G57F reconstructed after residue-position checks

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant K317N/D501G/L386W/G417L/G57F


sequence_source: UniProtKB:A0A0G2QNK1 canonical sequence with D501G/L386W/G417L/G57F reconstructed after residue-position checks

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D501G/L386W/G417L/G57F


sequence_source: UniProtKB:A0A0G2QNK1 canonical sequence with K317N/L386W/G417L/G57F reconstructed after residue-position checks

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant K317N/L386W/G417L/G57F


sequence_source: UniProtKB:A0A0G2QNK1 canonical sequence from direct accession lookup

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0G2QNK1; variant reconstruction applied from selected mutation_signature when present and applied mutation signature Q442A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant Q442A N-terminal His6-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0G2QNK1; variant reconstruction applied from selected mutation_signature when present and applied mutation signature T418K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T418K N-terminal His6-tag


organism: Bacillus sp.

substrate_name: 2,6-Dimethoxyphenol; O2

sequence_source: UniProtKB exact accession lookup for B9W2C5 on 2026-05-30; active TrEMBL entry for Bacillus sp. HR03 laccase, EC 1.10.3.2, sequenceVersion 1.

substrate: 2,6-Dimethoxyphenol; O2


sequence_source: Unresolved: direct UniProtKB lookup on 2026-05-30 returned A0A222C745 as inactive/deleted with only UniParc UPI0003B0D0D2 exposed.

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


organism: Bacillus sp. HR03

substrate_name: O2; Syringaldazine

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D500S

substrate: O2; Syringaldazine


substrate_name: Syringaldazine; O2

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D500E

substrate: Syringaldazine; O2


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant inserted glycine at position 500


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D500G


sequence_source: reconstructed from UniProtKB B9W2C5 canonical sequence by applying T415I

sequence_variant_note: Mutation signature T415I matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T415I


sequence_source: reconstructed from UniProtKB B9W2C5 canonical sequence by applying T418I

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T418I


sequence_source: reconstructed from UniProtKB B9W2C5 canonical sequence by applying E188V

sequence_variant_note: Mutation signature E188V matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E188V


sequence_source: reconstructed from UniProtKB B9W2C5 canonical sequence by applying E188I

sequence_variant_note: Mutation signature E188I matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E188I


sequence_source: reconstructed from UniProtKB B9W2C5 canonical sequence by applying E188L

sequence_variant_note: Mutation signature E188L matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E188L


sequence_source: UniProtKB B9W2C5 sequence version 1 fetched via UniProt REST on 2026-05-30; E188Y applied after confirming residue 188 is Glu.

sequence_variant_note: Mutation signature E188Y matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E188Y


sequence_source: UniProtKB B9W2C5 sequence version 1 fetched via UniProt REST on 2026-05-30; E188F applied after confirming residue 188 is Glu.

sequence_variant_note: Mutation signature E188F matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E188F


sequence_source: UniProtKB B9W2C5 sequence version 1 fetched via UniProt REST on 2026-05-30; selected record has no mutation signature, so canonical sequence is preserved as identity context.

unit: lgwedgeoneswedgeone


sequence_source: Reconstructed from UniProtKB B9W2C5 canonical sequence retrieved via UniProt REST on 2026-05-30 plus PMID 29425870 mutation signature.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T415G/T418I


sequence_variant_note: Mutation signature T415G matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T415G


organism: Bacillus subtilis

sequence_source: Reconstructed from UniProtKB P07788 canonical FASTA after confirming residue 502 is M and applying M502F; PMID 16680453 supports Met502 replacement by phenylalanine.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant M502F


sequence_source: UniProtKB P07788 FASTA retrieved 2026-05-30; M502L reconstructed by substituting residue 502 M->L after confirming the canonical residue.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant M502L


sequence_source: UniProtKB P07788 FASTA retrieved 2026-05-30; L386A reconstructed by substituting residue 386 L->A after confirming the canonical residue.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L386A


sequence_variant_note: Resolved canonical sequence from UniProtKB P07788 canonical FASTA/JSON fetched 2026-05-30; Residue check: P07788 has Ile at position 494; I494A was reconstructed by substituting Ala at that position. and applied mutation signature I494A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant I494A


sequence_source: UniProtKB P07788 canonical sequence with G417L reconstructed during review after confirming residue 417 is G.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant G417L CotA-ABTS-1


sequence_source: UniProtKB P07788 canonical sequence with E498D reconstructed during review after confirming residue 498 is E.

sequence_variant_note: Mutation signature E498D matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E498D


sequence_source: UniProtKB P07788 canonical sequence with E498T reconstructed during review after confirming residue 498 is E.

sequence_variant_note: Mutation signature E498T matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E498T


sequence_source: UniProtKB P07788 canonical sequence with E498L reconstructed during review after confirming residue 498 is E.

sequence_variant_note: Mutation signature E498L matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E498L


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

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant CotA-ABTS-SD1


sequence_source: UniProtKB:P07788 canonical CotA-laccase sequence, residue check C322, reconstructed by applying C322A.

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant C322A


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9W2C5 REST sequence checked 2026-05-30; reconstructed E188R from PMID 22112616 and SABIO-RK modifier note and applied mutation signature E188R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E188R


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9W2C5 REST sequence checked 2026-05-30; reconstructed E188K from PMID 22112616 and SABIO-RK modifier note and applied mutation signature E188K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E188K


sequence_variant_note: Resolved canonical sequence from UniProtKB:B9W2C5 REST sequence checked 2026-05-30; reconstructed E188A from PMID 22112616 and SABIO-RK modifier note and applied mutation signature E188A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E188A


sequence_source: Reconstructed from UniProtKB P07788 canonical sequence by applying source mutation T415A after confirming residue 415 is T on 2026-05-30

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T415A


sequence_source: UniProtKB:P07788 canonical sequence; reconstructed by applying E498G after direct residue checks on 2026-05-30.

sequence_variant_note: Mutation signature E498G matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E498G


sequence_source: UniProtKB:P07788 canonical sequence; reconstructed by applying E29V after direct residue checks on 2026-05-30.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E29V


sequence_source: UniProtKB:P07788 canonical sequence; reconstructed by applying T480A/E498G after direct residue checks on 2026-05-30.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T480A/E498G


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant F2071Y/V403T/P455S C-terminal His6-tagged


sequence_source: UniProtKB:P07788 canonical sequence; reconstructed by applying V403T/P455S after direct residue checks on 2026-05-30.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant V403T/P455S C-terminal His6-tagged


sequence_source: UniProtKB:P07788 canonical sequence; reconstructed by applying P455S after direct residue checks on 2026-05-30.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant P455S C-terminal His6-tagged


substrate_name: Syringaldazine

sequence_variant_note: Resolved canonical sequence from UniProtKB P07788 canonical CotA sequence with L431F reconstructed after residue-coordinate check; PMID 27050268 Table 4 contains the L431F row. and applied mutation signature L431F to reconstruct the assayed variant sequence.

substrate: Syringaldazine


sequence_variant_note: Resolved canonical sequence from UniProtKB P07788 canonical CotA sequence with R146K reconstructed after residue-coordinate check; PMID 27050268 Table 4 contains the R146K row. and applied mutation signature R146K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07788 canonical CotA sequence with R476K reconstructed after residue-coordinate check; PMID 27050268 Table 4 contains the R476K row. and applied mutation signature R476K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07788 canonical CotA sequence with R429K reconstructed after residue-coordinate check; PMID 27050268 Table 4 contains R429K rows for both ABTS and SGZ. and applied mutation signature R429K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant R429K


sequence_variant_note: Resolved canonical sequence from UniProtKB P07788 canonical CotA sequence with T480A reconstructed after residue-coordinate check; PMID 27050268 Table 4 contains the T480A row. and applied mutation signature T480A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P07788 canonical CotA sequence with L431F reconstructed after residue-coordinate check; PMID 27050268 Table 4 contains the L431F row.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07788 canonical CotA sequence with R429K reconstructed after residue-coordinate check; PMID 27050268 Table 4 contains the R429K row. and applied mutation signature R429K to reconstruct the assayed variant sequence.


organism: Bacillus sp. LS03

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:H8WGE3 reconstructed T232P/Q367R variant and applied mutation signature T232P/Q367R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant 5E29 (T232P/Q367R), His-tag


sequence_source: UniProtKB:H8WGE3 reconstructed T232P/Q367R variant


organism: Bacillus sp. SL-1


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant R155W/M157H (CAWH)


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant R155W (CAW)


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant R155H (CAH2)


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A386JCD3 and applied mutation signature R155W/M157H/A158E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant R155W/M157H/A158E (CAWH1)


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A1W6S310 and applied mutation signature T158A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant T158A (CAHH)


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A386JCD3 and applied mutation signature R155H/A158E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant R155H/A158E (CAHE2)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07788 and applied mutation signature R429K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 313.15 K; buffer 100 mM citrate-phosphate

column_label: Table 4. Kinetic constants of CotA and its mutants for ABTS and SGZ, printed column heads Enzyme | ABTS: Km (uM), kcat (s^-1), kcat/Km (uM^-1 s^-1) | SGZ: Km (uM), kcat (s^-1), kcat/Km (uM^-1 s^-1) | (kcat/Km)ABTS/(kcat/Km)SGZ. Journal page 333 (PDF page 6). Enzyme row R429K; ABTS column group; Km cell = 90.61 uM; kcat cell = 1.71 s^-1; kcat/Km cell = 0.02 uM^-1 s^-1. captured primary segment: Table 4, ABTS column group, enzyme row R429K: Km 90.61 uM; kcat 1.71 s^-1; kcat/Km 0.02 uM^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 4 cell 90.61 uM; 1 uM = 1/1000 mM, so 90.61 / 1000 = 0.09061 mM; the export stores 0.09061 mM, the same value. kcat: printed Table 4 cell 1.71 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 1.71 s^-1; the export stores 1.71 s^-1, the same value. kcat/Km: printed Table 4 cell 0.02 under the column head kcat/Km (uM^-1 s^-1); 1 uM^-1 = 1000 mM^-1, so 1 uM^-1 s^-1 = 1000 s^-1 mM^-1 and 0.02 x 1000 = 20.0 s^-1 mM^-1; the export stores 0.02 s^-1 mM^-1, which is the printed per-micromolar cell carrying the per-millimolar label without being multiplied by 1000.

raw_value_unit_evidence: Journal page 333, Table 4, enzyme row R429K, ABTS column group: Km = 90.61 uM; kcat = 1.71 s^-1; kcat/Km = 0.02 under the printed column head kcat/Km (uM^-1 s^-1).

row_label: Table 4, enzyme row R429K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical CotA sequence, row-specific mutation reconstructed from selected mutation_signature and applied mutation signature L431F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L431F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07788 and applied mutation signature R476K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 313.15 K; buffer ethanol in 100 mM citrate-phosphate

column_label: Table 4. Kinetic constants of CotA and its mutants for ABTS and SGZ, printed column heads Enzyme | ABTS: Km (uM), kcat (s^-1), kcat/Km (uM^-1 s^-1) | SGZ: Km (uM), kcat (s^-1), kcat/Km (uM^-1 s^-1) | (kcat/Km)ABTS/(kcat/Km)SGZ. Journal page 333 (PDF page 6). Enzyme row R476K; SGZ column group; Km cell = 29.32 uM; kcat cell = 4.27 s^-1; kcat/Km cell = 0.15 uM^-1 s^-1. captured primary segment: Table 4, SGZ column group, enzyme row R476K: Km 29.32 uM; kcat 4.27 s^-1; kcat/Km 0.15 uM^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 4 cell 29.32 uM; 1 uM = 1/1000 mM, so 29.32 / 1000 = 0.02932 mM; the export stores 0.02932 mM, the same value. kcat: printed Table 4 cell 4.27 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 4.27 s^-1; the export stores 4.27 s^-1, the same value. kcat/Km: printed Table 4 cell 0.15 under the column head kcat/Km (uM^-1 s^-1); 1 uM^-1 = 1000 mM^-1, so 1 uM^-1 s^-1 = 1000 s^-1 mM^-1 and 0.15 x 1000 = 150.0 s^-1 mM^-1; the export stores 0.15 s^-1 mM^-1, which is the printed per-micromolar cell carrying the per-millimolar label without being multiplied by 1000.

raw_value_unit_evidence: Journal page 333, Table 4, enzyme row R476K, SGZ column group: Km = 29.32 uM; kcat = 4.27 s^-1; kcat/Km = 0.15 under the printed column head kcat/Km (uM^-1 s^-1).

row_label: Table 4, enzyme row R476K


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07788 and applied mutation signature R146K to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constants of CotA and its mutants for ABTS and SGZ, printed column heads Enzyme | ABTS: Km (uM), kcat (s^-1), kcat/Km (uM^-1 s^-1) | SGZ: Km (uM), kcat (s^-1), kcat/Km (uM^-1 s^-1) | (kcat/Km)ABTS/(kcat/Km)SGZ. Journal page 333 (PDF page 6). Enzyme row R146K; SGZ column group; Km cell = 13.45 uM; kcat cell = 0.05 s^-1; kcat/Km cell = 0.004 uM^-1 s^-1. captured primary segment: Table 4, SGZ column group, enzyme row R146K: Km 13.45 uM; kcat 0.05 s^-1; kcat/Km 0.004 uM^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 4 cell 13.45 uM; 1 uM = 1/1000 mM, so 13.45 / 1000 = 0.01345 mM; the export stores 0.01345 mM, the same value. kcat: printed Table 4 cell 0.05 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 0.05 s^-1; the export stores 0.05 s^-1, the same value. kcat/Km: printed Table 4 cell 0.004 under the column head kcat/Km (uM^-1 s^-1); 1 uM^-1 = 1000 mM^-1, so 1 uM^-1 s^-1 = 1000 s^-1 mM^-1 and 0.004 x 1000 = 4.0 s^-1 mM^-1; the export stores 0.004 s^-1 mM^-1, which is the printed per-micromolar cell carrying the per-millimolar label without being multiplied by 1000.

raw_value_unit_evidence: Journal page 333, Table 4, enzyme row R146K, SGZ column group: Km = 13.45 uM; kcat = 0.05 s^-1; kcat/Km = 0.004 under the printed column head kcat/Km (uM^-1 s^-1).

row_label: Table 4, enzyme row R146K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical CotA sequence, row-specific mutation reconstructed from selected mutation_signature and applied mutation signature A478F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant A478F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical CotA sequence, row-specific mutation reconstructed from selected mutation_signature and applied mutation signature R146K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant R146K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical CotA sequence, row-specific mutation reconstructed from selected mutation_signature and applied mutation signature L343S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant L343S


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical CotA sequence, row-specific mutation reconstructed from selected mutation_signature and applied mutation signature E29V/L343S/E498G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant E29V/L343S/E498G


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07788 canonical sequence fetched 2026-05-30; F207Y applied after residue validation. and applied mutation signature F207Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant F207Y C-terminal His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07788 canonical sequence fetched 2026-05-30; V403T applied after residue validation. and applied mutation signature V403T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant V403T C-terminal His6-tagged


sequence_variant_note: Mutation signature R416A matches the mutant residue at offset +0 and the reference residue at offset +13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant R416A


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


organism: Bacteroides thetaiotaomicron

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


organism: basidiomycete PM1

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication, engineered enzyme 7D5

proof_lines: pH 3.0, temperature not specified in the publication, engineered enzyme 7D5

proof_lines: pH 4.0, temperature not specified in the publication, engineered enzyme 7D5


organism: Corynebacterium glutamicum

mutation_signature: Δ1

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

proof_lines: SABIO-RK modifier species: laccase(Enzyme) wildtype N-delta 1-111


organism: Escherichia coli

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

proof_lines:
pH 5, 30°C
presence of 0.25 mM Cu2+, pH 5, 30°C
presence of 0.1 mM Cu2+, pH 5, 30°C


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, P444G

proof_lines: region Pro357-His406 deletion plus P444G mutant, pH 5.5, 25°C


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant P444A

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, P444A


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D439A, P444A

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, D439A, P444A

proof_lines: region Pro357-His406 deletion plus D439A/P444A mutant, pH 5.5, 25°C


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D439A

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, D439A


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant P444L

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, P444L


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant C-terminal addition of 21 methionine rich tail, N-terminal His6-tag

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant delta alpha5-7 (amino acids 357-406 deleted), C-terminal His6-tag


mutation_signature: laccase(Enzyme) mutant C-terminal addition of 21 methionine rich tail / deletion residues 355-398

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant C-terminal addition of 21 methionine rich tail, deletion residues 355-398, N-terminal His6-tag


substrate_name: O2; 2,6-Dimethoxyphenol

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion residues 355-398, N-terminal His6-tag

substrate: O2; 2,6-Dimethoxyphenol


sequence_source: UniProtKB P36649 canonical sequence fetched 2026-05-30; source mutation G276K interpreted against the UniProt mature chain 29-516, so mature residue 276 maps to canonical residue 304

sequence_variant_note: Mutation signature G276K could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant G276K


sequence_source: UniProtKB P36649 canonical sequence fetched 2026-05-30; source mutation G276R interpreted against the UniProt mature chain 29-516, so mature residue 276 maps to canonical residue 304

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +4, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant G276R


sequence_source: UniProtKB P36649 canonical sequence fetched 2026-05-30; source mutation G276Y interpreted against the UniProt mature chain 29-516, so mature residue 276 maps to canonical residue 304

sequence_variant_note: Mutation signature G276Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant G276Y


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant G276N


organism: Geobacillus sp. WSUCF1


organism: Marinomonas mediterranea

mutation_signature: truncated MmPPOA-637

mutation_type: truncation

proof_lines: SABIO-RK modifier species: laccase(Enzyme) wildtype C-terminal His6-tag, truncated MmPPOA-637