column_label: Table label: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a. Row: CGP-31523A. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 75 ± 5, kcat (s^-1) cell 0.05, kcat/Km (M^-1 s^-1) cell 6.00 x 10^2 M^-1 s^-1. Km 75 ± 5 uM normalizes to 0.075 mM and equals the exported km; kcat 0.05 s^-1 equals the exported kcat; the exported kcat_over_km 0.6666666666666667 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 6.00 x 10^2 M^-1 s^-1 = 0.6 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 5 row CGP-31523A: Km 75 ± 5 uM = 0.075 mM; kcat 0.05 s^-1 = 0.05 s^-1; kcat/Km 0.6666666666666667 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 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a | enzyme column group: A. hydrophila AE036 | 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: CGP-31523A 75 6 5 0.05 6.00 3 102 250 6 10 25.0 1.00 3 105 27 6 2 38.0 1.40 3 106

row_label: A. hydrophila AE036 | CGP-31523A


enzyme_display_name: beta-lactamase

organism: Aeromonas hydrophila

substrate_name: 6-beta-Iodopenicillanic acid

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: UniProt Q6X1Y9 FASTA; direct lookup on rest.uniprot.org

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

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

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row 6-beta-Iodopenicillanic acid: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM -> mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3 Aeromonas hydrophila A2 enzyme column, 6-beta-Iodopenicillanic acid row: Km 530 +/- 50 uM uM; kcat 0.64 s^-1.

row_label: Aeromonas hydrophila A2 enzyme | 6-beta-Iodopenicillanic acid

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

data_origin: experimental

enzyme: beta-lactamase

substrate: 6-beta-Iodopenicillanic acid

status: verified

source: oed


substrate_name: Sulbactam

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Sulbactam: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM -> mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3 Aeromonas hydrophila A2 enzyme column, Sulbactam row: Km 37 +/- 4 uM uM; kcat 0.12 s^-1.

row_label: Aeromonas hydrophila A2 enzyme | Sulbactam

substrate: Sulbactam


substrate_name: Imipenem

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Imipenem: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM -> mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3 Aeromonas hydrophila A2 enzyme column, Imipenem row: Km 80 +/- 8 uM uM; kcat 168 s^-1.

row_label: Aeromonas hydrophila A2 enzyme | Imipenem

substrate: Imipenem


substrate_name: cephaloridin

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, 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.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Cephaloridin: Km cell 190 +/- 8 uM; kcat cell 0.12 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Cephaloridin

table_label: Table 3 Kinetic parameters determined for class B beta-lactamases (PMC1132494 scanned page 154)

substrate: cephaloridin


substrate_name: Oxacillin

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, 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.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Oxacillin: Km cell 25 +/- 3 uM; kcat cell 0.75 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Oxacillin

substrate: Oxacillin


substrate_name: Penicillin G

sequence_source: UniProtKB Q6X1Y9 FASTA and JSON retrieved directly on 2026-05-27; sequence version 1

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Penicillin G: 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.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Penicillin G: Km cell 700 +/- 50 uM; kcat cell 5.21 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Penicillin G

substrate: Penicillin G


substrate_name: carbenicillin

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, 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.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Carbenicillin: Km cell 450 +/- 30 uM; kcat cell 16 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Carbenicillin

substrate: carbenicillin


substrate_name: cefotaxime

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Cefotaxime: 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.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Cefotaxime: Km cell 26 +/- 3 uM; kcat cell 0.07 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Cefotaxime

substrate: cefotaxime


substrate_name: Nitrocefin

verification_status: unverified

substrate: Nitrocefin

status: unverified


substrate_name: cephalexin

substrate: cephalexin


substrate_name: Cefuroxime

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, 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.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Cefuroxime: Km cell 20 +/- 3 uM; kcat cell 0.07 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Cefuroxime

substrate: Cefuroxime


substrate_name: Cephaloglycin

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Cephaloglycin: 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.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Cephaloglycin: Km cell 280 +/- 30 uM; kcat cell 0.2 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Cephaloglycin

substrate: Cephaloglycin


organism: Aliivibrio salmonicida

substrate_name: cefuroxime

column_label: table label: Table 1. Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-119 and VIM-2.23; row label: Cefuroxime; column label: ALI-1 column of the kcat (s-1) group, ALI-1 column of the KM (uM) group and ALI-1 column of the kcat/KM (1/uM*s) group of this one printed row; no cell is taken from the IMP-1 or VIM-2 columns and no cell is taken from any other row; raw value: KM 68 ± 30 uM, kcat 11 ± 3 s-1, kcat/KM 0.16 1/uM*s; raw unit: uM for KM, s-1 for kcat, 1/uM*s for kcat/KM; normalized value: KM 0.068 mM, kcat 11.0 s^-1, kcat/KM 161.76470588235293 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Table 1 kinetic analysis of ALI-1: the substrates were dissolved in a solution of 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the solutions for the kinetic analysis were made in the range of 2-1,000 uM; the kinetic analysis was performed in a reaction mixture containing 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the reaction mixture was pre-incubated for 5 min at 30 degrees Celsius. This record reads only the ALI-1 column of each metric group of Table 1; the IMP-1 and VIM-2 columns of the same printed row are literature comparison values for other enzymes and no cell is taken from them. Exported assay conditions: pH 7.2, 310.15 K. The exported pH equals the paper's printed pH 7.2. The exported temperature 310.15 K does not correspond to the 30 degrees Celsius pre-incubation the paper prints for this kinetic analysis, so this record certifies only the printed kinetic cells and asserts no temperature value. The exported row carries no cofactor_name, so nothing in the exported row conflicts with the 100 uM ZnCl2 the paper prints for this assay.

normalized_value_unit_evidence: KM 68 ± 30 uM divided by 1000 gives 0.068 mM at the export's stored precision; exported KM 0.068 mM. kcat 11 ± 3 s-1 is already in s^-1 and at the export's stored precision is 11.0 s^-1; exported kcat 11.0 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 11.0 s^-1 divided by 0.068 mM giving 161.76470588235293 s^-1 mM^-1, and of nothing else; exported kcat/Km 161.76470588235293 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, printed row Cefuroxime, ALI-1 columns: KM 68 ± 30 uM; kcat 11 ± 3 s-1; kcat/KM 0.16 1/uM*s.

row_label: Cefuroxime

substrate: cefuroxime


substrate_name: cefoxitin

column_label: table label: Table 1. Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-119 and VIM-2.23; row label: Cefoxitin; column label: ALI-1 column of the kcat (s-1) group, ALI-1 column of the KM (uM) group and ALI-1 column of the kcat/KM (1/uM*s) group of this one printed row; no cell is taken from the IMP-1 or VIM-2 columns and no cell is taken from any other row; raw value: KM 79 ± 30 uM, kcat 0.27 ± 0.09 s-1, kcat/KM 0.0034 1/uM*s; raw unit: uM for KM, s-1 for kcat, 1/uM*s for kcat/KM; normalized value: KM 0.079 mM, kcat 0.27 s^-1, kcat/KM 3.4177215189873418 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Table 1 kinetic analysis of ALI-1: the substrates were dissolved in a solution of 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the solutions for the kinetic analysis were made in the range of 2-1,000 uM; the kinetic analysis was performed in a reaction mixture containing 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the reaction mixture was pre-incubated for 5 min at 30 degrees Celsius. This record reads only the ALI-1 column of each metric group of Table 1; the IMP-1 and VIM-2 columns of the same printed row are literature comparison values for other enzymes and no cell is taken from them. Exported assay conditions: pH 7.2, 310.15 K. The exported pH equals the paper's printed pH 7.2. The exported temperature 310.15 K does not correspond to the 30 degrees Celsius pre-incubation the paper prints for this kinetic analysis, so this record certifies only the printed kinetic cells and asserts no temperature value. The exported row carries no cofactor_name, so nothing in the exported row conflicts with the 100 uM ZnCl2 the paper prints for this assay.

normalized_value_unit_evidence: KM 79 ± 30 uM divided by 1000 gives 0.079 mM at the export's stored precision; exported KM 0.079 mM. kcat 0.27 ± 0.09 s-1 is already in s^-1 and at the export's stored precision is 0.27 s^-1; exported kcat 0.27 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.27 s^-1 divided by 0.079 mM giving 3.4177215189873418 s^-1 mM^-1, and of nothing else; exported kcat/Km 3.4177215189873418 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, printed row Cefoxitin, ALI-1 columns: KM 79 ± 30 uM; kcat 0.27 ± 0.09 s-1; kcat/KM 0.0034 1/uM*s.

row_label: Cefoxitin

substrate: cefoxitin


substrate_name: ceftazidime

column_label: table label: Table 1. Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-119 and VIM-2.23; row label: Ceftazidime; column label: ALI-1 column of the kcat (s-1) group, ALI-1 column of the KM (uM) group and ALI-1 column of the kcat/KM (1/uM*s) group of this one printed row; no cell is taken from the IMP-1 or VIM-2 columns and no cell is taken from any other row; raw value: KM 37 ± 12 uM, kcat 0.09 ± 0.03 s-1, kcat/KM 0.0024 1/uM*s; raw unit: uM for KM, s-1 for kcat, 1/uM*s for kcat/KM; normalized value: KM 0.037 mM, kcat 0.09 s^-1, kcat/KM 2.4324324324324325 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Table 1 kinetic analysis of ALI-1: the substrates were dissolved in a solution of 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the solutions for the kinetic analysis were made in the range of 2-1,000 uM; the kinetic analysis was performed in a reaction mixture containing 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the reaction mixture was pre-incubated for 5 min at 30 degrees Celsius. This record reads only the ALI-1 column of each metric group of Table 1; the IMP-1 and VIM-2 columns of the same printed row are literature comparison values for other enzymes and no cell is taken from them. Exported assay conditions: pH 7.2, 310.15 K. The exported pH equals the paper's printed pH 7.2. The exported temperature 310.15 K does not correspond to the 30 degrees Celsius pre-incubation the paper prints for this kinetic analysis, so this record certifies only the printed kinetic cells and asserts no temperature value. The exported row carries no cofactor_name, so nothing in the exported row conflicts with the 100 uM ZnCl2 the paper prints for this assay.

normalized_value_unit_evidence: KM 37 ± 12 uM divided by 1000 gives 0.037 mM at the export's stored precision; exported KM 0.037 mM. kcat 0.09 ± 0.03 s-1 is already in s^-1 and at the export's stored precision is 0.09 s^-1; exported kcat 0.09 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.09 s^-1 divided by 0.037 mM giving 2.4324324324324325 s^-1 mM^-1, and of nothing else; exported kcat/Km 2.4324324324324325 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, printed row Ceftazidime, ALI-1 columns: KM 37 ± 12 uM; kcat 0.09 ± 0.03 s-1; kcat/KM 0.0024 1/uM*s.

row_label: Ceftazidime

substrate: ceftazidime


verification_status: corrected

column_label: Table 1 (Comparison of kcat, KM and catalytic efficiency for ALI-1, IMP-1 and VIM-2), row 'Imipenem', ALI-1 columns: 'kcat (s^-1)' = 8.0; 'KM (uM)' = 933; 'kcat/KM (uM^-1 s^-1)' = 0.0085. The Km and efficiency column headers are printed with the Greek letter mu for micromolar; pdftotext renders that glyph as a plain 'm', so the printed text shows 'KM (mM)' and 'kcat/KM (mM^-1 s^-1)', but the true printed unit, confirmed against a rendered page image, is micromolar (uM / uM^-1 s^-1).

normalized_value_unit_evidence: kcat: printed Table 1 cell 8.0 s^-1; already in s^-1, no conversion needed; normalized value 8.0 s^(-1). Km: printed Table 1 cell 933 uM; 933 / 1000 = 0.933 mM; normalized value 0.933 mM. kcat/Km: printed Table 1 cell 0.0085 uM^-1 s^-1 (same micromolar unit); 0.0085 * 1000 = 8.5 s^-1 mM^-1. This printed efficiency cell is the paper's own independently fitted value for this row and condition, carried forward as-is; it is a separate figure from the quotient of the row's own kcat and Km cells (8.0 / 0.933 = 8.5744908896034 s^-1 mM^-1).

raw_value_unit_evidence: Table 1, ALI-1 columns, row 'Imipenem': kcat = 8.0 s^-1; KM = 933 (column head prints the Greek mu for micromolar, rendered here as 'm'; true unit uM); printed kcat/KM = 0.0085 uM^-1 s^-1 (same micromolar-based ratio unit).

row_label: Table 1, row 'Imipenem' (ALI-1 columns)

table_label: Table 1: Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-1 and VIM-2 (J Antimicrob Chemother 2015, 70(3):766-772)

status: corrected


enzyme_display_name: Metallo-beta-lactamase type 2

substrate_name: Asparenomycin A

sequence_source: UniProtKB:P26918 reviewed Swiss-Prot FASTA

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: A. hydrophila AE036. Columns read: Km (uM) cell 170 ± 5, kcat (s^-1) cell 475, kcat/Km (M^-1 s^-1) cell 2.80 x 10^6 M^-1 s^-1. Km 170 ± 5 uM normalizes to 0.17 mM and equals the exported km; kcat 475 s^-1 equals the exported kcat; the table's printed kcat/Km cell 2.80 x 10^6 M^-1 s^-1 normalizes to 2800.0 s^-1 mM^-1 and decimal-matches the exported kcat_over_km.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 7 row Asparenomycin A: Km 170 ± 5 uM = 0.17 mM; kcat 475 s^-1 = 475.0 s^-1; kcat/Km 2800.0 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: A. hydrophila AE036 | 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: A. hydrophila AE036 | Asparenomycin A

enzyme: Metallo-beta-lactamase type 2

substrate: Asparenomycin A


column_label: Table label: TABLE 3. Kinetic parameters of metallo-b-lactamases with benzylpenicillin and imipenem after purificationa. Row: Penicillin G. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 680 ± 30, kcat (s^-1) cell 5, kcat/Km (M^-1 s^-1) cell 7.35 x 10^3 M^-1 s^-1. Km 680 ± 30 uM normalizes to 0.68 mM and equals the exported km; kcat 5 s^-1 equals the exported kcat; the table's printed kcat/Km cell 7.35 x 10^3 M^-1 s^-1 normalizes to 7.35 s^-1 mM^-1 and decimal-matches the exported kcat_over_km.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 3 row Penicillin G: Km 680 ± 30 uM = 0.68 mM; kcat 5 s^-1 = 5.0 s^-1; kcat/Km 7.35 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 3. Kinetic parameters of metallo-b-lactamases with benzylpenicillin and imipenem after purificationa | enzyme column group: A. hydrophila AE036 | 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: Penicillin G 680 6 30 5 7.35 3 103 1,550 6 100 691 4.60 3 105 55 6 4 1,120 2.05 3 107

row_label: A. hydrophila AE036 | Penicillin G


substrate_name: tazobactam

column_label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row Tazobactam; enzyme column block A. hydrophila AE036; column Km (uM) raw value 440; column kcat (s^-1) raw value 0.65; column kcat/Km (M^-1 s^-1) raw value 1.50 3 103 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 1.50e3 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 0.65 s^-1; raw unit: s^-1; normalized value: 0.65 s^(-1); metric: Km; raw value: 440 uM; raw unit: uM; normalized value: 0.44 mM; metric: kcat/Km; normalized value: 1.5 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 0.65 s^-1 is already in s^-1. Km 440 uM = 440/1000 = 0.44 mM. kcat/Km table cell is printed as 1.50 3 103 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 1500 M^-1 s^-1; 1500/1000 = 1.5 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row Tazobactam; A. hydrophila AE036 block; metric: kcat; raw value: 0.65; raw unit: s^-1; metric: Km; raw value: 440; raw unit: uM; metric: kcat/Km; raw value: 1500; raw unit: M^-1 s^-1; normalized value: 1.5 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.

row_label: Tazobactam

substrate: tazobactam


substrate_name: Epicillin

column_label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillins; row Epicillin; enzyme column block A. hydrophila AE036; column Km (uM) raw value 300; column kcat (s^-1) raw value 0.60; column kcat/Km (M^-1 s^-1) raw value 2.00 3 103 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 2.00e3 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 0.60 s^-1; raw unit: s^-1; normalized value: 0.6 s^(-1); metric: Km; raw value: 300 uM; raw unit: uM; normalized value: 0.3 mM; metric: kcat/Km; normalized value: 2.0 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 0.60 s^-1 is already in s^-1. Km 300 uM = 300/1000 = 0.3 mM. kcat/Km table cell is printed as 2.00 3 103 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 2000 M^-1 s^-1; 2000/1000 = 2.0 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillins; row Epicillin; A. hydrophila AE036 block; metric: kcat; raw value: 0.60; raw unit: s^-1; metric: Km; raw value: 300; raw unit: uM; metric: kcat/Km; raw value: 2000; raw unit: M^-1 s^-1; normalized value: 2.0 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.

row_label: Epicillin

substrate: Epicillin


column_label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row HRE-664; enzyme column block A. hydrophila AE036; column Km (uM) raw value 140; column kcat (s^-1) raw value 10.0; column kcat/Km (M^-1 s^-1) raw value 7.15 3 104 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 7.15e4 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 10.0 s^-1; raw unit: s^-1; normalized value: 10.0 s^(-1); metric: Km; raw value: 140 uM; raw unit: uM; normalized value: 0.14 mM; metric: kcat/Km; normalized value: 71.5 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 10.0 s^-1 is already in s^-1. Km 140 uM = 140/1000 = 0.14 mM. kcat/Km table cell is printed as 7.15 3 104 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 71500 M^-1 s^-1; 71500/1000 = 71.5 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row HRE-664; A. hydrophila AE036 block; metric: kcat; raw value: 10.0; raw unit: s^-1; metric: Km; raw value: 140; raw unit: uM; metric: kcat/Km; raw value: 71500; raw unit: M^-1 s^-1; normalized value: 71.5 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.


substrate_name: H2O; HRE-664 / mixed beta-lactam source group

kcat_over_km_display: Not reported

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

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


substrate_name: Meropenem

column_label: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibiotics; row Meropenem; enzyme column block A. hydrophila AE036; column Km (uM) raw value 250; column kcat (s^-1) raw value 440; column kcat/Km (M^-1 s^-1) raw value 1.75 3 106 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 1.75e6 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 440 s^-1; raw unit: s^-1; normalized value: 440.0 s^(-1); metric: Km; raw value: 250 uM; raw unit: uM; normalized value: 0.25 mM; metric: kcat/Km; normalized value: 1750.0 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 440 s^-1 is already in s^-1. Km 250 uM = 250/1000 = 0.25 mM. kcat/Km table cell is printed as 1.75 3 106 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 1750000 M^-1 s^-1; 1750000/1000 = 1750.0 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibiotics; row Meropenem; A. hydrophila AE036 block; metric: kcat; raw value: 440; raw unit: s^-1; metric: Km; raw value: 250; raw unit: uM; metric: kcat/Km; raw value: 1750000; raw unit: M^-1 s^-1; normalized value: 1750.0 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.

row_label: Meropenem

substrate: Meropenem


substrate_name: Temocillin

column_label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillins; row Temocillin; enzyme column block A. hydrophila AE036; column Km (uM) raw value 65; column kcat (s^-1) raw value 1.75; column kcat/Km (M^-1 s^-1) raw value 2.70 3 104 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 2.70e4 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 1.75 s^-1; raw unit: s^-1; normalized value: 1.75 s^(-1); metric: Km; raw value: 65 uM; raw unit: uM; normalized value: 0.065 mM; metric: kcat/Km; normalized value: 27.0 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 1.75 s^-1 is already in s^-1. Km 65 uM = 65/1000 = 0.065 mM. kcat/Km table cell is printed as 2.70 3 104 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 27000 M^-1 s^-1; 27000/1000 = 27.0 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillins; row Temocillin; A. hydrophila AE036 block; metric: kcat; raw value: 1.75; raw unit: s^-1; metric: Km; raw value: 65; raw unit: uM; metric: kcat/Km; raw value: 27000; raw unit: M^-1 s^-1; normalized value: 27.0 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.

row_label: Temocillin

substrate: Temocillin


substrate_name: Cephaloridine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P26918 plus PDBe/RCSB 1X8G author-residue mapping and applied mutation signature R121H to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: Cephaloridine


sequence_source: UniProtKB reviewed accession P26918 plus PDBe/RCSB 1X8G author-residue mapping

sequence_variant_note: Mutation signature N116H/N220G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature N116H/R121H/N220G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: Oxacillin

substrate: Oxacillin


organism: Aeromonas enteropelogenes

substrate_name: cephalothin

sequence_source: UniProtKB B2BSN6 direct FASTA lookup, retrieved 2026-05-27; entry is Aeromonas enteropelogenes beta-lactamase ampC with EC 3.5.2.6.

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM HEPES

substrate: cephalothin


substrate_name: ampicillin

substrate: ampicillin


substrate_name: cefpirome

substrate: cefpirome


substrate_name: cefazolin

column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Cefazolin ( v o ) e. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 0.55, K m (uM) cell 120, k cat / K m (M^-1 s^-1) cell 4.6 x 10^3. metric: kcat; raw value: 0.55; raw unit: s^-1; normalized value: 0.55 s^(-1); metric: Km; raw value: 120; raw unit: uM; normalized value: 0.12 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 4.583333333333334 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Cefazolin ( v o ) e: kcat 0.55 s^-1 = 0.55 s^(-1); Km 120 uM = 0.12 mM (1 uM = 0.001 mM); kcat/Km 4.583333333333334 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `4.6 × 10 3` is the paper's 4.6 x 10^3 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Cefazolin ( v o ) e 0.55 120 4.6 × 10 3 | TRU-1 cells read: k cat = 0.55 s^-1; K m = 120 uM; k cat / K m = 4.6 x 10^3 M^-1 s^-1

row_label: TRU-1 | Cefazolin ( v o ) e

substrate: cefazolin


substrate_name: cefepime

substrate: cefepime


sequence_source: UniProtKB B6EPH0 FASTA direct check on 2026-05-27

column_label: table label: Table 1. Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-119 and VIM-2.23; row label: Cefepime; column label: ALI-1 column of the kcat (s-1) group, ALI-1 column of the KM (uM) group and ALI-1 column of the kcat/KM (1/uM*s) group of this one printed row; no cell is taken from the IMP-1 or VIM-2 columns and no cell is taken from any other row; raw value: KM 177 ± 14 uM, kcat 0.581 ± 0.005 s-1, kcat/KM 0.0033 1/uM*s; raw unit: uM for KM, s-1 for kcat, 1/uM*s for kcat/KM; normalized value: KM 0.177 mM, kcat 0.58 s^-1, kcat/KM 3.2768361581920904 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Table 1 kinetic analysis of ALI-1: the substrates were dissolved in a solution of 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the solutions for the kinetic analysis were made in the range of 2-1,000 uM; the kinetic analysis was performed in a reaction mixture containing 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the reaction mixture was pre-incubated for 5 min at 30 degrees Celsius. This record reads only the ALI-1 column of each metric group of Table 1; the IMP-1 and VIM-2 columns of the same printed row are literature comparison values for other enzymes and no cell is taken from them. Exported assay conditions: pH 7.2, 310.15 K. The exported pH equals the paper's printed pH 7.2. The exported temperature 310.15 K does not correspond to the 30 degrees Celsius pre-incubation the paper prints for this kinetic analysis, so this record certifies only the printed kinetic cells and asserts no temperature value. The exported row carries no cofactor_name, so nothing in the exported row conflicts with the 100 uM ZnCl2 the paper prints for this assay.

normalized_value_unit_evidence: KM 177 ± 14 uM divided by 1000 gives 0.177 mM at the export's stored precision; exported KM 0.177 mM. kcat 0.581 ± 0.005 s-1 is already in s^-1 and at the export's stored precision is 0.58 s^-1; exported kcat 0.58 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.58 s^-1 divided by 0.177 mM giving 3.2768361581920904 s^-1 mM^-1, and of nothing else; exported kcat/Km 3.2768361581920904 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, printed row Cefepime, ALI-1 columns: KM 177 ± 14 uM; kcat 0.581 ± 0.005 s-1; kcat/KM 0.0033 1/uM*s.

row_label: Cefepime


substrate_name: meropenem

column_label: Table 1 (Comparison of kcat, KM and catalytic efficiency for ALI-1, IMP-1 and VIM-2), row 'Meropenem', ALI-1 columns: 'kcat (s^-1)' = 13; 'KM (uM)' = 142; 'kcat/KM (uM^-1 s^-1)' = 0.094. The Km and efficiency column headers are printed with the Greek letter mu for micromolar; pdftotext renders that glyph as a plain 'm', so the printed text shows 'KM (mM)' and 'kcat/KM (mM^-1 s^-1)', but the true printed unit, confirmed against a rendered page image, is micromolar (uM / uM^-1 s^-1).

normalized_value_unit_evidence: kcat: printed Table 1 cell 13 s^-1; already in s^-1, no conversion needed; normalized value 13.0 s^(-1). Km: printed Table 1 cell 142 uM; 142 / 1000 = 0.142 mM; normalized value 0.142 mM. kcat/Km: printed Table 1 cell 0.094 uM^-1 s^-1 (same micromolar unit); 0.094 * 1000 = 94.0 s^-1 mM^-1. This printed efficiency cell is the paper's own independently fitted value for this row and condition, carried forward as-is; it is a separate figure from the quotient of the row's own kcat and Km cells (13 / 0.142 = 91.5492957746479 s^-1 mM^-1).

raw_value_unit_evidence: Table 1, ALI-1 columns, row 'Meropenem': kcat = 13 s^-1; KM = 142 (column head prints the Greek mu for micromolar, rendered here as 'm'; true unit uM); printed kcat/KM = 0.094 uM^-1 s^-1 (same micromolar-based ratio unit).

row_label: Table 1, row 'Meropenem' (ALI-1 columns)

substrate: meropenem


substrate_name: nitrocefin

column_label: table label: Table 1. Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-119 and VIM-2.23; row label: Nitrocefin; column label: ALI-1 column of the kcat (s-1) group, ALI-1 column of the KM (uM) group and ALI-1 column of the kcat/KM (1/uM*s) group of this one printed row; no cell is taken from the IMP-1 or VIM-2 columns and no cell is taken from any other row; raw value: KM 6±3 uM, kcat 6.3 ± 0.6 s-1, kcat/KM 1.0 1/uM*s; raw unit: uM for KM, s-1 for kcat, 1/uM*s for kcat/KM; normalized value: KM 0.006 mM, kcat 6.3 s^-1, kcat/KM 1050.0 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Table 1 kinetic analysis of ALI-1: the substrates were dissolved in a solution of 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the solutions for the kinetic analysis were made in the range of 2-1,000 uM; the kinetic analysis was performed in a reaction mixture containing 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the reaction mixture was pre-incubated for 5 min at 30 degrees Celsius. This record reads only the ALI-1 column of each metric group of Table 1; the IMP-1 and VIM-2 columns of the same printed row are literature comparison values for other enzymes and no cell is taken from them. Exported assay conditions: pH 7.2, 310.15 K. The exported pH equals the paper's printed pH 7.2. The exported temperature 310.15 K does not correspond to the 30 degrees Celsius pre-incubation the paper prints for this kinetic analysis, so this record certifies only the printed kinetic cells and asserts no temperature value. The exported row carries no cofactor_name, so nothing in the exported row conflicts with the 100 uM ZnCl2 the paper prints for this assay.

normalized_value_unit_evidence: KM 6±3 uM divided by 1000 gives 0.006 mM at the export's stored precision; exported KM 0.006 mM. kcat 6.3 ± 0.6 s-1 is already in s^-1 and at the export's stored precision is 6.3 s^-1; exported kcat 6.3 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 6.3 s^-1 divided by 0.006 mM giving 1050.0 s^-1 mM^-1, and of nothing else; exported kcat/Km 1050.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, printed row Nitrocefin, ALI-1 columns: KM 6±3 uM; kcat 6.3 ± 0.6 s-1; kcat/KM 1.0 1/uM*s.

row_label: Nitrocefin

substrate: nitrocefin


substrate_name: ertapenem

substrate: ertapenem


organism: Bacillus cereus

substrate_name: Penicillin G

sequence_source: Reconstructed from UniProtKB P04190 canonical FASTA by direct H116S substitution on 2026-05-27

sequence_variant_note: Mutation signature H116S 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.

substrate: Penicillin G


substrate_name: Nitrocefin

sequence_source: Reconstructed from UniProtKB P04190 canonical FASTA using RCSB 2NZF alignment to map the BcII C221S label to UniProt full-sequence C198S on 2026-05-27

sequence_variant_note: Mutation signature C221S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Nitrocefin


sequence_source: UniProtKB P04190 FASTA direct check on 2026-05-27


sequence_variant_note: Resolved canonical sequence from Direct UniProt P04190 canonical sequence check; D120N reconstructed after residue 120 was confirmed as D. and applied mutation signature D120N to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04190 and applied mutation signature H118S to reconstruct the assayed variant sequence.

column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'H118S', benzylpenicillin column group; column 'Km (uM)' = 2300; column 'kcat (s^-1)' = 36; column 'kcat/Km (M^-1 s^-1)' = 12200.

normalized_value_unit_evidence: Km: printed Table 3 cell 2300 uM; 2300 / 1000 = 2.3 mM; the paper value is 2.3 mM and the exported value is 2.3 mM. kcat: printed Table 3 cell 36 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 36.0 s^(-1) and the exported value is 36.0 s^(-1). kcat/Km: printed Table 3 cell 12200 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12200 / 1000 = 12.2 s^-1 mM^-1; the paper value is 12.2 s^(-1)*mM^(-1); the exported value is 15.65217391304348 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme row 'H118S', benzylpenicillin column group: Km = 2300 uM; kcat = 36 s^-1; printed kcat/Km = 12200 M^-1 s^-1.

table_label: Table 3: Kinetic parameters with respect to benzylpenicillin and nitrocefin for the enzyme forms of Bacillus cereus 569/H/9 metallo-beta-lactamase BcII in 10 mM Hepes/0.2 M NaCl at pH 7.5 and 30 C (Biochem. J. 2002, 363:687-696)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04190 and applied mutation signature H196S with inferred residue-numbering offset -17 to reconstruct the assayed variant sequence.

column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'H196S', benzylpenicillin column group; column 'Km (uM)' = 5700; column 'kcat (s^-1)' = 7; column 'kcat/Km (M^-1 s^-1)' = 1230.

normalized_value_unit_evidence: Km: printed Table 3 cell 5700 uM; 5700 / 1000 = 5.7 mM; the paper value is 5.7 mM and the exported value is 5.7 mM. kcat: printed Table 3 cell 7 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 7.0 s^(-1) and the exported value is 7.0 s^(-1). kcat/Km: printed Table 3 cell 1230 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1230 / 1000 = 1.23 s^-1 mM^-1; the paper value is 1.23 s^(-1)*mM^(-1); the exported value is 1.2280701754385965 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme row 'H196S', benzylpenicillin column group: Km = 5700 uM; kcat = 7 s^-1; printed kcat/Km = 1230 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04190 and applied mutation signature H263S with inferred residue-numbering offset -23 to reconstruct the assayed variant sequence.

column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'H263S', nitrocefin column group; column 'Km (uM)' = 365; column 'kcat (s^-1)' = 1.3; column 'kcat/Km (M^-1 s^-1)' = 3600.

normalized_value_unit_evidence: Km: printed Table 3 cell 365 uM; 365 / 1000 = 0.365 mM; the paper value is 0.365 mM and the exported value is 0.365 mM. kcat: printed Table 3 cell 1.3 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 1.3 s^(-1) and the exported value is 1.3 s^(-1). kcat/Km: printed Table 3 cell 3600 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3600 / 1000 = 3.6 s^-1 mM^-1; the paper value is 3.6 s^(-1)*mM^(-1); the exported value is 3.5616438356164384 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme row 'H263S', nitrocefin column group: Km = 365 uM; kcat = 1.3 s^-1; printed kcat/Km = 3600 M^-1 s^-1.


column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'H118S', nitrocefin column group; column 'Km (uM)' = 220; column 'kcat (s^-1)' = 5; column 'kcat/Km (M^-1 s^-1)' = 21600.

normalized_value_unit_evidence: Km: printed Table 3 cell 220 uM; 220 / 1000 = 0.22 mM; the paper value is 0.22 mM and the exported value is 0.22 mM. kcat: printed Table 3 cell 5 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 5.0 s^(-1) and the exported value is 5.0 s^(-1). kcat/Km: printed Table 3 cell 21600 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21600 / 1000 = 21.6 s^-1 mM^-1; the paper value is 21.6 s^(-1)*mM^(-1); the exported value is 22.727272727272727 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme row 'H118S', nitrocefin column group: Km = 220 uM; kcat = 5 s^-1; printed kcat/Km = 21600 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04190 and applied mutation signature H116S to reconstruct the assayed variant sequence.

column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'H116S', nitrocefin column group; column 'Km (uM)' = 180; column 'kcat (s^-1)' = 44; column 'kcat/Km (M^-1 s^-1)' = 227000.

normalized_value_unit_evidence: Km: printed Table 3 cell 180 uM; 180 / 1000 = 0.18 mM; the paper value is 0.18 mM and the exported value is 0.18 mM. kcat: printed Table 3 cell 44 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 44.0 s^(-1) and the exported value is 44.0 s^(-1). kcat/Km: printed Table 3 cell 227000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 227000 / 1000 = 227.0 s^-1 mM^-1; the paper value is 227.0 s^(-1)*mM^(-1); the exported value is 244.44444444444446 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme row 'H116S', nitrocefin column group: Km = 180 uM; kcat = 44 s^-1; printed kcat/Km = 227000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04190 canonical sequence with reconstructed D120N variant; direct P04190 coordinate; D120N primer maps to P04190 114-128 and applied mutation signature D120N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04190 and applied mutation signature C221S with inferred residue-numbering offset -23 to reconstruct the assayed variant sequence.

column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'C221S (100 uM Zn2+)', benzylpenicillin column group; column 'Km (uM)' = 775; column 'kcat (s^-1)' = 200; column 'kcat/Km (M^-1 s^-1)' = 262000.

normalized_value_unit_evidence: Km: printed Table 3 cell 775 uM; 775 / 1000 = 0.775 mM; the paper value is 0.775 mM and the exported value is 0.775 mM. kcat: printed Table 3 cell 200 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 200.0 s^(-1) and the exported value is 200.0 s^(-1). kcat/Km: printed Table 3 cell 262000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 262000 / 1000 = 262.0 s^-1 mM^-1; the paper value is 262.0 s^(-1)*mM^(-1); the exported value is 258.06451612903226 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme row 'C221S (100 uM Zn2+)', benzylpenicillin column group: Km = 775 uM; kcat = 200 s^-1; printed kcat/Km = 262000 M^-1 s^-1.


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: Cephapirin

sequence_source: UniProtKB reviewed P04190 (BLA2_BACCE), fetched 2026-05-27

substrate: Cephapirin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: cefotaxime

substrate: cefotaxime


sequence_source: UniProtKB reviewed P04190 (BLA2_BACCE), fetched 2026-05-27; D120S substituted during review after confirming P04190 residue 120 is D

sequence_variant_note: Mutation signature D120S 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.


sequence_source: UniProtKB:P04190 direct FASTA/API lookup


substrate_name: cephaloridin

substrate: cephaloridin


sequence_variant_note: Resolved canonical sequence from UniProt:P04190 direct REST lookup; D120 substitution applied to canonical precursor sequence and applied mutation signature D120Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P04190 direct REST lookup; D120 substitution applied to canonical precursor sequence and applied mutation signature D120N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P04190 direct REST lookup; D120 substitution applied to canonical precursor sequence and applied mutation signature D120E to reconstruct the assayed variant sequence.


sequence_source: UniProt:P04190 direct REST lookup; D120 substitution applied to canonical precursor sequence


sequence_variant_note: Resolved canonical sequence from UniProt:P04190 direct REST lookup; D120 substitution applied to canonical precursor sequence and applied mutation signature D120S to reconstruct the assayed variant sequence.


substrate_name: Cephalosporin C

substrate: Cephalosporin C


substrate_name: Ampicillin

substrate: Ampicillin


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


assay_conditions_summary: pH 7; 293.15 K; buffer 0.1 M-sodium phosphate

column_label: Table 2 (journal page 616), substrate row `Ampicillin`, column `Wild-type`: panel `Km (uM)` = 250; panel `kcat. (s^-1)` = 5000; panel `kcat./Km (mM^-1 . s^-1)` = 20000. The wild-type column prints bare numbers with no error term.

normalized_value_unit_evidence: Km: printed cell 250 uM; 250 / 1000 = 0.25 mM = catalog 0.25 mM. kcat: printed cell 5000 s^-1; no conversion; = catalog 5000 s^(-1). kcat/Km: printed cell 20000 mM^-1 . s^-1; mM^-1 . s^-1 is the canonical s^(-1)*mM^(-1), so 20000 = catalog 20000.0 s^(-1)*mM^(-1). Ampicillin is the only Table 2 substrate whose printed ratio cell is also the exact quotient of its own printed kcat and Km cells.

raw_value_unit_evidence: Table 2 (journal page 616), row `Ampicillin`, column `Wild-type`: Km = 250 uM; kcat. = 5000 s^-1; kcat./Km = 20000 mM^-1 . s^-1.

row_label: Table 2, substrate row `Ampicillin`, column `Wild-type` (all three panels)

table_label: Table 2. Kinetic parameters for hydrolysis of beta-lactams by mutant enzymes (journal page 616)


sequence_source: UniProtKB:P00809 direct FASTA lookup on 2026-05-27

assay_conditions_summary: pH 7; 293.15 K; buffer containing 0

column_label: Table 2: Kinetic parameters for hydrolysis of pI-lactams by mutant enzymes (Biochem. J. 1990, 272:613-619), wild-type column, substrate row '6-Aminopenicillanic acid'; column 'Km (uM)' = 1600; column 'kcat. (s-1)' = 260; column 'kcat /Km (mM- *.s-), decoded as kcat/Km in mM^-1 s^-1' = 170.

normalized_value_unit_evidence: Km: printed cell 1600 uM; 1600 / 1000 = 1.6 mM. kcat: printed cell 260 s^-1; already in s^-1, no unit conversion applies, so the cell is 260.0 s^(-1). kcat/Km: printed cell 170 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, no unit conversion applies, so the cell is 170.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2. Kinetic parameters for hydrolysis of pI-lactams by mutant enzymes, wild-type column, substrate row '6-Aminopenicillanic acid': Km = 1600 uM; kcat = 260 s^-1; printed kcat/Km = 170 mM^-1 s^-1.

row_label: Table 2, wild-type column, substrate row '6-Aminopenicillanic acid'


substrate_name: carbenicillin

column_label: Table 2: Kinetic parameters for hydrolysis of pI-lactams by mutant enzymes (Biochem. J. 1990, 272:613-619), wild-type column, substrate row 'Carbenicillin'; column 'Km (uM)' = 150; column 'kcat. (s-1)' = 440; column 'kcat /Km (mM- *.s-), decoded as kcat/Km in mM^-1 s^-1' = 2800.

normalized_value_unit_evidence: Km: printed cell 150 uM; 150 / 1000 = 0.15 mM. kcat: printed cell 440 s^-1; already in s^-1, no unit conversion applies, so the cell is 440.0 s^(-1). kcat/Km: printed cell 2800 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, no unit conversion applies, so the cell is 2800.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2. Kinetic parameters for hydrolysis of pI-lactams by mutant enzymes, wild-type column, substrate row 'Carbenicillin': Km = 150 uM; kcat = 440 s^-1; printed kcat/Km = 2800 mM^-1 s^-1.

row_label: Table 2, wild-type column, substrate row 'Carbenicillin'

substrate: carbenicillin


column_label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row HRE-664; enzyme column block B. cereus 5/B/6; column Km (uM) raw value 25; column kcat (s^-1) raw value 10.0; column kcat/Km (M^-1 s^-1) raw value 4.00 3 105 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 4.00e5 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 10.0 s^-1; raw unit: s^-1; normalized value: 10.0 s^(-1); metric: Km; raw value: 25 uM; raw unit: uM; normalized value: 0.025 mM; metric: kcat/Km; normalized value: 400.0 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 10.0 s^-1 is already in s^-1. Km 25 uM = 25/1000 = 0.025 mM. kcat/Km table cell is printed as 4.00 3 105 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 400000 M^-1 s^-1; 400000/1000 = 400.0 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row HRE-664; B. cereus 5/B/6 block; metric: kcat; raw value: 10.0; raw unit: s^-1; metric: Km; raw value: 25; raw unit: uM; metric: kcat/Km; raw value: 400000; raw unit: M^-1 s^-1; normalized value: 400.0 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.


substrate_name: tazobactam

column_label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row Tazobactam; enzyme column block B. cereus 5/B/6; column Km (uM) raw value 420; column kcat (s^-1) raw value 6.5; column kcat/Km (M^-1 s^-1) raw value 1.55 3 104 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 1.55e4 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 6.5 s^-1; raw unit: s^-1; normalized value: 6.5 s^(-1); metric: Km; raw value: 420 uM; raw unit: uM; normalized value: 0.42 mM; metric: kcat/Km; normalized value: 15.476190476190476 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 6.5 s^-1 is already in s^-1. Km 420 uM = 420/1000 = 0.42 mM. kcat/Km is recorded as the quotient of this row's own two printed cells: paper kcat / paper Km = 6.5 / 0.42 = 15.476190476190476 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row Tazobactam; B. cereus 5/B/6 block; metric: kcat; raw value: 6.5; raw unit: s^-1; metric: Km; raw value: 420; raw unit: uM; metric: kcat/Km; raw value: null (not taken from a printed cell); normalized value: 15.476190476190476 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.

substrate: tazobactam


substrate_name: Cephradine

substrate: Cephradine


column_label: Table 5: Kinetic parameters of metallo-beta-lactamases with cephalosporins (Delta3-cephems); organism block B. cereus 5/B/6; row CGP-31523A; Km raw 250 uM normalized 0.25 mM; kcat raw 25.0 s^-1 normalized 25 s^-1; kcat/Km raw 100000.0 M^-1 s^-1 normalized 100 s^-1 mM^-1.

row_label: B. cereus 5/B/6 / CGP-31523A


substrate_name: azlocillin

substrate: azlocillin


substrate_name: Cefsulodin

column_label: Table label: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a. Row: Cefsulodin. Enzyme column group: B. cereus 5/B/6. Columns read: Km (uM) cell 230 ± 20, kcat (s^-1) cell 12.5, kcat/Km (M^-1 s^-1) cell 5.40 x 10^4. Km 230 ± 20 uM normalizes to 0.23 mM and equals the exported km; kcat 12.5 s^-1 equals the exported kcat; the separately rounded kcat/Km (M^-1 s^-1) cell 5.40 x 10^4 M^-1 s^-1 (= 54.0 s^-1 mM^-1) is disclosed but not used; the exported kcat_over_km 54.347826086956516 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells.

normalized_value_unit_evidence: B. cereus 5/B/6 columns of Table 5 row Cefsulodin: Km 230 ± 20 uM = 0.23 mM; kcat 12.5 s^-1 = 12.5 s^-1; kcat/Km 54.347826086956516 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 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a | enzyme column group: B. cereus 5/B/6 | 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: Cefsulodin          130 6 10          0.05        3.50 3 102        230 6 20        12.5             5.40 3 104       5 6 0.3d          7.5       1.50 3 106

row_label: B. cereus 5/B/6 | Cefsulodin

substrate: Cefsulodin


substrate_name: Meropenem

column_label: Table 7: Kinetic parameters of metallo-beta-lactamases with carbapenem antibiotics; organism block B. cereus 5/B/6; row Meropenem; Km raw 400 uM normalized 0.4 mM; kcat raw 580 s^-1 normalized 580 s^-1; kcat/Km raw 1450000.0 M^-1 s^-1 normalized 1450 s^-1 mM^-1.

row_label: B. cereus 5/B/6 / Meropenem

substrate: Meropenem


substrate_name: piperacillin

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Piperacillin. Enzyme column group: B. cereus 5/B/6. Columns read: Km (uM) cell 450 ± 10, kcat (s^-1) cell 75, kcat/Km (M^-1 s^-1) cell 1.70 x 10^5. Km 450 ± 10 uM normalizes to 0.45 mM and equals the exported km; kcat 75 s^-1 equals the exported kcat; the separately rounded kcat/Km (M^-1 s^-1) cell 1.70 x 10^5 M^-1 s^-1 (= 170.0 s^-1 mM^-1) is disclosed but not used; the exported kcat_over_km 166.66666666666666 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells.

normalized_value_unit_evidence: B. cereus 5/B/6 columns of Table 4 row Piperacillin: Km 450 ± 10 uM = 0.45 mM; kcat 75 s^-1 = 75.0 s^-1; kcat/Km 166.66666666666666 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: B. cereus 5/B/6 | 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: Piperacillin          55 6 2          0.43        7.80 3 103         450 6 10           75            1.70 3 105       20 6 1            140       7.00 3 106

row_label: B. cereus 5/B/6 | Piperacillin

substrate: piperacillin


substrate_name: Asparenomycin A

sequence_source: UniProtKB:P14488 FASTA retrieved by direct REST check; reviewed Swiss-Prot BLAB_BACCE, Bacillus cereus, EC 3.5.2.6.

column_label: Table 7: Kinetic parameters of metallo-beta-lactamases with carbapenem antibiotics; organism block B. cereus 5/B/6; row Asparenomycin A; Km raw 20 uM normalized 0.02 mM; kcat raw 100 s^-1 normalized 100 s^-1; kcat/Km raw 5000000.0 M^-1 s^-1 normalized 5000 s^-1 mM^-1.

row_label: B. cereus 5/B/6 / Asparenomycin A

substrate: Asparenomycin A


substrate_name: Epicillin

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Epicillin. Enzyme column group: B. cereus 5/B/6. Columns read: Km (uM) cell 550 ± 10, kcat (s^-1) cell 160, kcat/Km (M^-1 s^-1) cell 2.90 x 10^5. Km 550 ± 10 uM normalizes to 0.55 mM and equals the exported km; kcat 160 s^-1 equals the exported kcat; the separately rounded kcat/Km (M^-1 s^-1) cell 2.90 x 10^5 M^-1 s^-1 (= 290.0 s^-1 mM^-1) is disclosed but not used; the exported kcat_over_km 290.9090909090909 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells.

normalized_value_unit_evidence: B. cereus 5/B/6 columns of Table 4 row Epicillin: Km 550 ± 10 uM = 0.55 mM; kcat 160 s^-1 = 160.0 s^-1; kcat/Km 290.9090909090909 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: B. cereus 5/B/6 | 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: B. cereus 5/B/6 | Epicillin

substrate: Epicillin


substrate_name: Penicillin V

sequence_source: UniProtKB:P00809 FASTA retrieved by direct REST check; reviewed Swiss-Prot BLAC_BACCE, Bacillus cereus, EC 3.5.2.6.

assay_conditions_summary: pH 7; 293.15 K; buffer 50 mM sodium phosphate

column_label: Table 3 Kinetic parameters for hydrolysis of beta-lactams by mutant enzymes. The steady-state kinetic parameters were determined from initial rates. The reactions were carried out in 50 mM sodium phosphate buffer, pH 7, containing 0.5 M NaCl and 0.1 mM EDTA at 20 C. Substrate row 'Penicillin V'; enzyme column 'Wild-type'; column group 'Km (uM)' = 132.9; column group 'kcat. (s^-1)' = 4525; column group 'kcat./Km (uM^-1 . s^-1)' = 34.1.

normalized_value_unit_evidence: Km: printed Table 3 Wild-type cell 132.9 uM; 132.9 / 1000 = 0.1329 mM; the exported value is 0.133 mM. kcat: printed Table 3 Wild-type cell 4525 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 4525.0 s^(-1). kcat/Km: printed Table 3 Wild-type cell 34.1 uM^-1 . s^-1; the printed column-group unit literal is uM^-1 . s^-1 and 1 uM^-1 s^-1 is 1000 mM^-1 s^-1, so 34.1 x 1000 = 34100.0 s^-1 mM^-1; the exported value is 34022.55639097744 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 676), substrate row 'Penicillin V', enzyme column 'Wild-type': Km = 132.9 uM; kcat = 4525 s^-1; printed kcat./Km = 34.1 uM^-1 . s^-1.

row_label: Table 3, substrate row 'Penicillin V', enzyme column 'Wild-type'

substrate: Penicillin V


substrate_name: Penicillin G

column_label: Table 3 Kinetic parameters for hydrolysis of beta-lactams by mutant enzymes. The steady-state kinetic parameters were determined from initial rates. The reactions were carried out in 50 mM sodium phosphate buffer, pH 7, containing 0.5 M NaCl and 0.1 mM EDTA at 20 C. Substrate row 'Penicillin G'; enzyme column 'Wild-type'; column group 'Km (uM)' = 118.4; column group 'kcat. (s^-1)' = 4515; column group 'kcat./Km (uM^-1 . s^-1)' = 38.1.

normalized_value_unit_evidence: Km: printed Table 3 Wild-type cell 118.4 uM; 118.4 / 1000 = 0.1184 mM; the exported value is 0.118 mM. kcat: printed Table 3 Wild-type cell 4515 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 4515.0 s^(-1). kcat/Km: printed Table 3 Wild-type cell 38.1 uM^-1 . s^-1; the printed column-group unit literal is uM^-1 . s^-1 and 1 uM^-1 s^-1 is 1000 mM^-1 s^-1, so 38.1 x 1000 = 38100.0 s^-1 mM^-1; the exported value is 38262.71186440678 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 676), substrate row 'Penicillin G', enzyme column 'Wild-type': Km = 118.4 uM; kcat = 4515 s^-1; printed kcat./Km = 38.1 uM^-1 . s^-1.

row_label: Table 3, substrate row 'Penicillin G', enzyme column 'Wild-type'

substrate: Penicillin G


sequence_source: Canonical UniProtKB:P00809 was checked, but no row-specific E166C variant sequence was applied.


substrate_name: Nitrocefin

sequence_source: Canonical UniProtKB:P00809 was checked, but no row-specific E166A variant sequence was applied.

substrate: Nitrocefin


sequence_variant_note: Resolved canonical sequence from Direct UniProt P00809 canonical sequence; E166A reconstructed by changing the UniProt natural-numbered active-site Glu at position 185 to Ala after checking the P00809 feature table and Ambler-numbering caveat. and applied mutation signature E166A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


substrate_name: Sulbactam

sequence_source: Direct UniProt P14488 canonical reviewed sequence.

assay_conditions_summary: pH 6; 303.15 K; buffer 10 mM sodium cacodylate

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, row Sulbactam: 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.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II block, row Sulbactam: Km cell 5200 + 325 uM; kcat cell 10 s^-1.

row_label: Bacillus cereus beta-lactamase II | Sulbactam

substrate: Sulbactam


column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, row Nitrocefin: 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: 45; raw unit: s^-1; normalized value: 45.0; normalized unit: s^-1; metric: Km; raw value: 70+5; raw unit: uM; normalized value: 0.07; normalized unit: mM; metric: kcat/Km; normalized value: 642.8571428571428; normalized unit: s^-1 mM^-1; assay condition: 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II block, row Nitrocefin: Km cell 70+5 uM; kcat cell 45 s^-1.

row_label: Bacillus cereus beta-lactamase II | Nitrocefin

table_label: Table 3 Kinetic parameters determined for class B f-lactamases (PMC1132494 scanned page 154), Bacillus cereus f-lactamase II block


organism: Bacillus licheniformis

sequence_source: UniProtKB:P00808 direct REST FASTA check

column_label: ACS PDF page 5, Table II wild-type nitrocefin (IV) row reports kcat 1088 s^-1 and Km 0.041 mM; kcat_over_km is exact arithmetic from those same row cells.

normalized_value_unit_evidence: kcat normalized_value=1088 normalized_unit=s^-1; Km normalized_value=0.041 normalized_unit=mM; kcat_over_km normalized_value=26536.585365853658 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1088 raw_unit=s^-1; Km raw_value=0.041 raw_unit=mM; table kcat/Km raw_value=2.64 x 10^7 raw_unit=M^-1*s^-1 rounded

row_label: wild type; nitrocefin (IV)

table_label: Table II. Substrate Specificity Profiles of Wild-Type beta-Lactamase from B. licheniformis and the K234E and K234A Mutants


substrate_name: cefotaxime

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, row Cefotaxime: 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: 60; raw unit: s^-1; normalized value: 60.0; normalized unit: s^-1; metric: Km; raw value: 90 + 10; raw unit: uM; normalized value: 0.09; normalized unit: mM; metric: kcat/Km; normalized value: 666.6666666666667; normalized unit: s^-1 mM^-1; assay condition: 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II block, row Cefotaxime: Km cell 90 + 10 uM; kcat cell 60 s^-1.

row_label: Bacillus cereus beta-lactamase II | Cefotaxime

substrate: cefotaxime


substrate_name: Oxacillin

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, 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: 325; raw unit: s^-1; normalized value: 325.0; normalized unit: s^-1; metric: Km; raw value: 1750 + 20; raw unit: uM; normalized value: 1.75; normalized unit: mM; metric: kcat/Km; normalized value: 185.71428571428572; normalized unit: s^-1 mM^-1; assay condition: 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II block, row Oxacillin: Km cell 1750 + 20 uM; kcat cell 325 s^-1.

row_label: Bacillus cereus beta-lactamase II | Oxacillin

substrate: Oxacillin


sequence_source: UniProtKB:P00808 FASTA retrieved by direct REST check; reviewed Swiss-Prot BLAC_BACLI, Bacillus licheniformis, EC 3.5.2.6.

column_label: ACS PDF page 5, Table II wild-type ampicillin (III) row reports kcat 2241 s^-1 and Km 0.21 mM; kcat_over_km is exact arithmetic from those same row cells.

normalized_value_unit_evidence: kcat normalized_value=2241 normalized_unit=s^-1; Km normalized_value=0.21 normalized_unit=mM; kcat_over_km normalized_value=10671.428571428572 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2241 raw_unit=s^-1; Km raw_value=0.21 raw_unit=mM; table kcat/Km raw_value=1.06 x 10^7 raw_unit=M^-1*s^-1 rounded

row_label: wild type; ampicillin (III)


sequence_source: Canonical UniProtKB:P00808 was checked, but no row-specific K234E variant sequence was applied.


column_label: ACS PDF page 5, Table II wild-type PADAC (V) row reports kcat 667 s^-1 and Km 0.14 mM; kcat_over_km is exact arithmetic from those same row cells.

normalized_value_unit_evidence: kcat normalized_value=667 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM; kcat_over_km normalized_value=4764.285714285714 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=667 raw_unit=s^-1; Km raw_value=0.14 raw_unit=mM; table kcat/Km raw_value=4.63 x 10^6 raw_unit=M^-1*s^-1 rounded

row_label: wild type; PADAC (V)


substrate_name: penicillin G

sequence_variant_note: Resolved canonical sequence from UniProtKB:P00808 and applied mutation signature E166C with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

substrate: penicillin G


substrate_name: cefuroxime

substrate: cefuroxime


organism: Bacteroides fragilis

sequence_variant_note: Resolved canonical sequence from UniProtKB:P25910 and applied mutation signature H99N to reconstruct the assayed variant sequence.


substrate_name: Ampicillin

sequence_source: UniProtKB:P14488 direct REST/FASTA lookup (reviewed Swiss-Prot, checked 2026-05-27)

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, row Ampicillin: 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: 1105; raw unit: s^-1; normalized value: 1105.0; normalized unit: s^-1; metric: Km; raw value: 1530 +115; raw unit: uM; normalized value: 1.53; normalized unit: mM; metric: kcat/Km; normalized value: 722.2222222222222; normalized unit: s^-1 mM^-1; assay condition: 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II block, row Ampicillin: Km cell 1530 +115 uM; kcat cell 1105 s^-1.

row_label: Bacillus cereus beta-lactamase II | Ampicillin

substrate: Ampicillin


substrate_name: 6-beta-Iodopenicillanic acid

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, row 6-f-IP: 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: 450; raw unit: s^-1; normalized value: 450.0; normalized unit: s^-1; metric: Km; raw value: 7460 + 590; raw unit: uM; normalized value: 7.46; normalized unit: mM; metric: kcat/Km; normalized value: 60.32171581769437; normalized unit: s^-1 mM^-1; assay condition: 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II block, row 6-f-IP: Km cell 7460 + 590 uM; kcat cell 450 s^-1.

row_label: Bacillus cereus beta-lactamase II | 6-f-IP

substrate: 6-beta-Iodopenicillanic acid


substrate_name: cephalexin

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, row Cephalexin: 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: 1.7; raw unit: s^-1; normalized value: 1.7; normalized unit: s^-1; metric: Km; raw value: 300 + 26; raw unit: uM; normalized value: 0.3; normalized unit: mM; metric: kcat/Km; normalized value: 5.666666666666667; normalized unit: s^-1 mM^-1; assay condition: 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II block, row Cephalexin: Km cell 300 + 26 uM; kcat cell 1.7 s^-1.

row_label: Bacillus cereus beta-lactamase II | Cephalexin

substrate: cephalexin


substrate_name: Cephaloglycin

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, row Cephaloglycin: 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: 61; raw unit: s^-1; normalized value: 61.0; normalized unit: s^-1; metric: Km; raw value: 190 +5; raw unit: uM; normalized value: 0.19; normalized unit: mM; metric: kcat/Km; normalized value: 321.05263157894734; normalized unit: s^-1 mM^-1; assay condition: 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II block, row Cephaloglycin: Km cell 190 +5 uM; kcat cell 61 s^-1.

row_label: Bacillus cereus beta-lactamase II | Cephaloglycin

substrate: Cephaloglycin


substrate_name: Cefuroxime

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, 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: 35; raw unit: s^-1; normalized value: 35.0; normalized unit: s^-1; metric: Km; raw value: 45+5; raw unit: uM; normalized value: 0.045; normalized unit: mM; metric: kcat/Km; normalized value: 777.7777777777778; normalized unit: s^-1 mM^-1; assay condition: 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II block, row Cefuroxime: Km cell 45+5 uM; kcat cell 35 s^-1.

row_label: Bacillus cereus beta-lactamase II | Cefuroxime

substrate: Cefuroxime


substrate_name: carbenicillin

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II 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: 755; raw unit: s^-1; normalized value: 755.0; normalized unit: s^-1; metric: Km; raw value: 4200 + 300; raw unit: uM; normalized value: 4.2; normalized unit: mM; metric: kcat/Km; normalized value: 179.76190476190476; normalized unit: s^-1 mM^-1; assay condition: Table 3 kinetic determinations for the Bacillus cereus beta-lactamase II column of Table 3; Materials and methods: for Bacillus cereus beta-lactamase all the experiments were performed at 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4; the export row carries pH 6.0 and 303.15 K.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II column, row Carbenicillin: Km cell 4200 + 300 uM; kcat cell 755 s^-1.

row_label: Bacillus cereus beta-lactamase II | Carbenicillin

table_label: Table 3 Kinetic parameters determined for class B beta-lactamases (PMC1132494 scanned page 154), Bacillus cereus beta-lactamase II column

substrate: carbenicillin


substrate_name: moxalactam

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II column, row Moxalactam: 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: 1.2; raw unit: s^-1; normalized value: 1.2; normalized unit: s^-1; metric: Km; raw value: 644 + 90; raw unit: uM; normalized value: 0.644; normalized unit: mM; metric: kcat/Km; normalized value: 1.8633540372670807; normalized unit: s^-1 mM^-1; assay condition: Table 3 kinetic determinations for the Bacillus cereus beta-lactamase II column of Table 3; Materials and methods: for Bacillus cereus beta-lactamase all the experiments were performed at 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4; the export row carries pH 6.0 and 303.15 K.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II column, row Moxalactam: Km cell 644 + 90 uM; kcat cell 1.2 s^-1.

row_label: Bacillus cereus beta-lactamase II | Moxalactam

substrate: moxalactam


substrate_name: cefoxitin

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II column, row Cefoxitin: 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: 0.2; raw unit: s^-1; normalized value: 0.2; normalized unit: s^-1; metric: Km; raw value: 2100 + 465; raw unit: uM; normalized value: 2.1; normalized unit: mM; metric: kcat/Km; normalized value: 0.09523809523809523; normalized unit: s^-1 mM^-1; assay condition: Table 3 kinetic determinations for the Bacillus cereus beta-lactamase II column of Table 3; Materials and methods: for Bacillus cereus beta-lactamase all the experiments were performed at 30 C in 10 mM sodium cacodylate buffer, pH 6.0, containing 0.5 M NaCl and 0.3 mM ZnSO4; the export row carries pH 6.0 and 303.15 K.

raw_value_unit_evidence: Table 3, Bacillus cereus beta-lactamase II column, row Cefoxitin: Km cell 2100 + 465 uM; kcat cell 0.2 s^-1.

row_label: Bacillus cereus beta-lactamase II | Cefoxitin

substrate: cefoxitin


sequence_source: UniProtKB P25910 canonical sequence checked by REST lookup; residue 193 was N and was replaced with D for the N193D variant.

sequence_variant_note: Mutation signature N193D matches the mutant residue at offset +0 and the reference residue at offset -7; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: Imipenem

sequence_source: UniProtKB P25910 canonical sequence checked by REST lookup; residue 103 was D and was replaced with N for the D103N variant.

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

substrate: Imipenem


substrate_name: Cephaloridine

sequence_source: UniProtKB P25910 canonical sequence checked by REST lookup; residue 104 was C and was replaced with R for the C104R variant.

substrate: Cephaloridine


sequence_source: UniProtKB P25910 canonical sequence checked by REST lookup; residue 181 was C and was replaced with S for the C181S variant.


substrate_name: Penicillin G

substrate: Penicillin G


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P25910 plus reconstructed C104S substitution and applied mutation signature C104S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P25910 plus reconstructed C104R substitution and applied mutation signature C104R to reconstruct the assayed variant sequence.


sequence_source: uniprot_accession:P25910 plus reconstructed C104S substitution


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P25910 plus reconstructed C155V substitution and applied mutation signature C155V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P25910 plus reconstructed H99N substitution and applied mutation signature H99N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P25910 plus reconstructed N193D substitution and applied mutation signature N193D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25910 direct REST check, reconstructed variant where mutation_signature is present and applied mutation signature C181S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25910 direct REST check, reconstructed variant where mutation_signature is present and applied mutation signature C155V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25910 direct REST check, reconstructed variant where mutation_signature is present and applied mutation signature K184R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P25910 direct REST check, reconstructed variant where mutation_signature is present


sequence_source: UniProtKB P25910 direct FASTA; C104R reconstructed after confirming canonical residue C at position 104.


sequence_source: UniProtKB P25910 direct FASTA; D103N reconstructed after confirming canonical residue D at position 103.


sequence_source: UniProtKB P25910 direct FASTA; C155V reconstructed after confirming canonical residue C at position 155.


substrate_name: amoxicillin

sequence_source: UniProtKB P25910 direct FASTA canonical reviewed sequence.

assay_conditions_summary: pH 7.2; 298.15 K; buffer 50 mM phosphate

column_label: Table 1; row Amoxicillin; column kcat (s^-1) raw value 140; column Km (uM) raw value 81 uM; column relative kcat/Km raw value 35 (relative, not absolute; absolute kcat/Km derived by division).

normalized_value_unit_evidence: kcat 140 s^-1 = 140 s^-1. Km 81 uM = 81/1000 = 0.081 mM. kcat/Km is not printed as an absolute value in the paper, so paper kcat/Km = paper_kcat / paper_km = 140 / 0.081 = 1728.395061728395 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (page 1156), row Amoxicillin: kcat column 140 s^-1; Km column 81 uM; relative kcat/Km column 35. The table prints only a relative kcat/Km; no absolute kcat/Km value is printed.

row_label: Amoxicillin

table_label: Table 1. Kinetic parameters of beta-lactam antibiotics with CcrA Metallo-beta-lactamase

substrate: amoxicillin


sequence_source: UniProtKB:P25910 reviewed Swiss-Prot FASTA direct check 2026-05-27

column_label: Table 1; row Cephalexin; column kcat (s^-1) raw value 95; column Km (uM) raw value 62 uM; column relative kcat/Km raw value 32 (relative, not absolute; absolute kcat/Km derived by division).

normalized_value_unit_evidence: kcat 95 s^-1 = 95 s^-1. Km 62 uM = 62/1000 = 0.062 mM. kcat/Km is not printed as an absolute value in the paper, so paper kcat/Km = paper_kcat / paper_km = 95 / 0.062 = 1532.258064516129 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (page 1156), row Cephalexin: kcat column 95 s^-1; Km column 62 uM; relative kcat/Km column 32. The table prints only a relative kcat/Km; no absolute kcat/Km value is printed.

row_label: Cephalexin


substrate_name: Ticarcillin

column_label: Table 1; row Ticarcillin; column kcat (s^-1) raw value 89; column Km (uM) raw value 70 uM; column relative kcat/Km raw value 26 (relative, not absolute; absolute kcat/Km derived by division).

normalized_value_unit_evidence: kcat 89 s^-1 = 89 s^-1. Km 70 uM = 70/1000 = 0.07 mM. kcat/Km is not printed as an absolute value in the paper, so paper kcat/Km = paper_kcat / paper_km = 89 / 0.07 = 1271.4285714285713 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (page 1156), row Ticarcillin: kcat column 89 s^-1; Km column 70 uM; relative kcat/Km column 26. The table prints only a relative kcat/Km; no absolute kcat/Km value is printed.

row_label: Ticarcillin

substrate: Ticarcillin


substrate_name: Cloxacillin

column_label: Table 1; row Cloxacillin; column kcat (s^-1) raw value 690; column Km (uM) raw value 110 uM; column relative kcat/Km raw value 110 (relative, not absolute; absolute kcat/Km derived by division).

normalized_value_unit_evidence: kcat 690 s^-1 = 690 s^-1. Km 110 uM = 110/1000 = 0.11 mM. kcat/Km is not printed as an absolute value in the paper, so paper kcat/Km = paper_kcat / paper_km = 690 / 0.11 = 6272.727272727273 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (page 1156), row Cloxacillin: kcat column 690 s^-1; Km column 110 uM; relative kcat/Km column 110. The table prints only a relative kcat/Km; no absolute kcat/Km value is printed.

row_label: Cloxacillin

substrate: Cloxacillin


substrate_name: piperacillin

substrate: piperacillin


substrate_name: Ceftazidime

substrate: Ceftazidime


organism: Citrobacter diversus

sequence_source: UniProtKB REST direct lookup for P22390, accessed 2026-05-27


column_label: Table 4 (scanned journal page 889), Form I block, substrate row `Ampicillin (asterisk footnote on the Km cell)`: Km (uM) = 22; kcat (s^-1) = 119; kcat/Km (M^-1 s^-1) = 5.4 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 119 s^-1 -> 119.0 s^(-1) (the unit is already s^-1); the exported value is 119.0 s^(-1). Km: printed cell 22 uM -> 0.022 mM (divide by 1000); the exported value is 0.024 mM. kcat/Km: the paper PRINTS the kcat/Km cell 5.4 x 10^6 M^-1 s^-1 for this row -> 5400.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 4958.333333333333 s^(-1)*mM^(-1).

row_label: Table 4 Form I, decoded plain-numeral transcription, substrate row `Ampicillin (asterisk footnote on the Km cell)`

table_label: Table 4 (scanned journal page 889) 'Substrate profile of C. diversus beta-lactamases'


substrate_name: cefazolin

column_label: Table 4 (scanned journal page 889), Form I block, substrate row `Cefazolin`: Km (uM) = 20; kcat (s^-1) = 166; kcat/Km (M^-1 s^-1) = 8.3 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 166 s^-1 -> 166.0 s^(-1) (the unit is already s^-1); the exported value is 166.0 s^(-1). Km: printed cell 20 uM -> 0.02 mM (divide by 1000); the exported value is 0.027 mM. kcat/Km: the paper PRINTS the kcat/Km cell 8.3 x 10^6 M^-1 s^-1 for this row -> 8300.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 6148.148148148148 s^(-1)*mM^(-1).

row_label: Table 4 Form I, decoded plain-numeral transcription, substrate row `Cefazolin`

substrate: cefazolin


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: Methicillin

substrate: Methicillin


sequence_source: UniProtKB:P22390 direct REST lookup 2026-05-27

column_label: Table 4 (scanned journal page 889), Form I block, substrate row `Carbenicillin`: Km (uM) = 100; kcat (s^-1) = 58; kcat/Km (M^-1 s^-1) = 0.6 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 58 s^-1 -> 58.0 s^(-1) (the unit is already s^-1); the exported value is 58.0 s^(-1). Km: printed cell 100 uM -> 0.1 mM (divide by 1000); the exported value is 0.115 mM. kcat/Km: the paper PRINTS the kcat/Km cell 0.6 x 10^6 M^-1 s^-1 for this row -> 600.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 504.3478260869565 s^(-1)*mM^(-1).

row_label: Table 4 Form I, decoded plain-numeral transcription, substrate row `Carbenicillin`


organism: Enterobacter cloacae

substrate_name: Cephalosporin C

sequence_source: UniProtKB:P05364 direct REST lookup 2026-05-27

substrate: Cephalosporin C


sequence_source: UniProtKB:P22390 reviewed entry retrieved 2026-05-27

column_label: Evidence location type: table; table/location label: Table 4. Substrate profile of C. diversus beta-lactamases (PMC1135165 scanned page 889); row label: Form I | Cephalosporin C; explicit primary cells: {'captured_segment': 'Table 4 Form I row Cephalosporin C: Km cell 126 +/- 20 uM; kcat cell 41 +/- 5 s^-1; kcat/Km cell (0.3 +/- 0.06) x 10^6 M^-1 s^-1.', 'column_label': 'kcat (s^-1)', 'condition_label': 'Form I beta-lactamase of Citrobacter diversus ULA-27, the chromatofocusing form with pI 6.8; Table 4 substrate profile; the experiments were performed at 30 C in 25 mM-sodium phosphate, pH 7.2, containing 0.2 M-NaCl and bovine serum albumin (0.05 mg/ml).', 'metric': 'kcat', 'normalized_unit': 's^-1', 'normalized_value': 41.0, 'primary_cell': True, 'raw_unit': 's^-1', 'raw_value': '41 +/- 5', 'row_label': 'Form I | Cephalosporin C', 'table_label': 'Table 4. Substrate profile of C. diversus beta-lactamases (PMC1135165 scanned page 889)'}; {'captured_segment': 'Table 4 Form I row Cephalosporin C: Km cell 126 +/- 20 uM; kcat cell 41 +/- 5 s^-1; kcat/Km cell (0.3 +/- 0.06) x 10^6 M^-1 s^-1.', 'column_label': 'Km (uM)', 'condition_label': 'Form I beta-lactamase of Citrobacter diversus ULA-27, the chromatofocusing form with pI 6.8; Table 4 substrate profile; the experiments were performed at 30 C in 25 mM-sodium phosphate, pH 7.2, containing 0.2 M-NaCl and bovine serum albumin (0.05 mg/ml).', 'metric': 'Km', 'normalized_unit': 'mM', 'normalized_value': 0.126, 'primary_cell': True, 'raw_unit': 'uM', 'raw_value': '126 +/- 20', 'row_label': 'Form I | Cephalosporin C', 'table_label': 'Table 4. Substrate profile of C. diversus beta-lactamases (PMC1135165 scanned page 889)'}; kcat/Km raw value: (0.3 +/- 0.06) x 10^6; raw unit: M^-1 s^-1; normalized value: 300 s^-1 mM^-1; assay condition: Form I beta-lactamase of Citrobacter diversus ULA-27, the chromatofocusing form with pI 6.8; Table 4 substrate profile; the experiments were performed at 30 C in 25 mM-sodium phosphate, pH 7.2, containing 0.2 M-NaCl and bovine serum albumin (0.05 mg/ml).; captured primary segment: Table 4 Form I row Cephalosporin C: Km cell 126 +/- 20 uM; kcat cell 41 +/- 5 s^-1; kcat/Km cell (0.3 +/- 0.06) x 10^6 M^-1 s^-1.

normalized_value_unit_evidence: kcat raw 41 +/- 5 s^-1 -> 41.0 s^-1; Km raw 126 +/- 20 uM -> 0.126 mM; explicit printed kcat/Km raw (0.3 +/- 0.06) x 10^6 M^-1 s^-1 -> 300 s^-1 mM^-1. Conversion: 0.3 x 10^6 M^-1 s^-1 x 0.001 M/mM = 300 s^-1 mM^-1. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence: Table 4, Form I block, row Cephalosporin C: Km cell 126 +/- 20 uM; kcat cell 41 +/- 5 s^-1. Explicit printed kcat/Km primary cell: (0.3 +/- 0.06) x 10^6 M^-1 s^-1.

row_label: Form I | Cephalosporin C


substrate_name: Cephalothin

column_label: Evidence location type: table; table/location label: Table 4. Substrate profile of C. diversus beta-lactamases (PMC1135165 scanned page 889); row label: Form I | Cephalothin; explicit primary cells: {'captured_segment': 'Table 4 Form I row Cephalothin: Km cell 48 +/- 3 uM; kcat cell 63 +/- 3 s^-1; kcat/Km cell (1.3 +/- 0.15) x 10^6 M^-1 s^-1.', 'column_label': 'kcat (s^-1)', 'condition_label': 'Form I beta-lactamase of Citrobacter diversus ULA-27, the chromatofocusing form with pI 6.8; Table 4 substrate profile; the experiments were performed at 30 C in 25 mM-sodium phosphate, pH 7.2, containing 0.2 M-NaCl and bovine serum albumin (0.05 mg/ml).', 'metric': 'kcat', 'normalized_unit': 's^-1', 'normalized_value': 63.0, 'primary_cell': True, 'raw_unit': 's^-1', 'raw_value': '63 +/- 3', 'row_label': 'Form I | Cephalothin', 'table_label': 'Table 4. Substrate profile of C. diversus beta-lactamases (PMC1135165 scanned page 889)'}; {'captured_segment': 'Table 4 Form I row Cephalothin: Km cell 48 +/- 3 uM; kcat cell 63 +/- 3 s^-1; kcat/Km cell (1.3 +/- 0.15) x 10^6 M^-1 s^-1.', 'column_label': 'Km (uM)', 'condition_label': 'Form I beta-lactamase of Citrobacter diversus ULA-27, the chromatofocusing form with pI 6.8; Table 4 substrate profile; the experiments were performed at 30 C in 25 mM-sodium phosphate, pH 7.2, containing 0.2 M-NaCl and bovine serum albumin (0.05 mg/ml).', 'metric': 'Km', 'normalized_unit': 'mM', 'normalized_value': 0.048, 'primary_cell': True, 'raw_unit': 'uM', 'raw_value': '48 +/- 3', 'row_label': 'Form I | Cephalothin', 'table_label': 'Table 4. Substrate profile of C. diversus beta-lactamases (PMC1135165 scanned page 889)'}; kcat/Km raw value: (1.3 +/- 0.15) x 10^6; raw unit: M^-1 s^-1; normalized value: 1300 s^-1 mM^-1; assay condition: Form I beta-lactamase of Citrobacter diversus ULA-27, the chromatofocusing form with pI 6.8; Table 4 substrate profile; the experiments were performed at 30 C in 25 mM-sodium phosphate, pH 7.2, containing 0.2 M-NaCl and bovine serum albumin (0.05 mg/ml).; captured primary segment: Table 4 Form I row Cephalothin: Km cell 48 +/- 3 uM; kcat cell 63 +/- 3 s^-1; kcat/Km cell (1.3 +/- 0.15) x 10^6 M^-1 s^-1.

normalized_value_unit_evidence: kcat raw 63 +/- 3 s^-1 -> 63.0 s^-1; Km raw 48 +/- 3 uM -> 0.048 mM; explicit printed kcat/Km raw (1.3 +/- 0.15) x 10^6 M^-1 s^-1 -> 1300 s^-1 mM^-1. Conversion: 1.3 x 10^6 M^-1 s^-1 x 0.001 M/mM = 1300 s^-1 mM^-1. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence: Table 4, Form I block, row Cephalothin: Km cell 48 +/- 3 uM; kcat cell 63 +/- 3 s^-1. Explicit printed kcat/Km primary cell: (1.3 +/- 0.15) x 10^6 M^-1 s^-1.

row_label: Form I | Cephalothin

substrate: Cephalothin


column_label: Evidence location type: table; table/location label: Table 4. Substrate profile of C. diversus beta-lactamases (PMC1135165 scanned page 889); row label: Form I | Cephaloridine; explicit primary cells: {'captured_segment': 'Table 4 Form I row Cephaloridine: Km cell 740 +/- 70 uM; kcat cell 930 +/- 100 s^-1; kcat/Km cell (1.25 +/- 0.25) x 10^6 M^-1 s^-1.', 'column_label': 'kcat (s^-1)', 'condition_label': 'Form I beta-lactamase of Citrobacter diversus ULA-27, the chromatofocusing form with pI 6.8; Table 4 substrate profile; the experiments were performed at 30 C in 25 mM-sodium phosphate, pH 7.2, containing 0.2 M-NaCl and bovine serum albumin (0.05 mg/ml).', 'metric': 'kcat', 'normalized_unit': 's^-1', 'normalized_value': 930.0, 'primary_cell': True, 'raw_unit': 's^-1', 'raw_value': '930 +/- 100', 'row_label': 'Form I | Cephaloridine', 'table_label': 'Table 4. Substrate profile of C. diversus beta-lactamases (PMC1135165 scanned page 889)'}; {'captured_segment': 'Table 4 Form I row Cephaloridine: Km cell 740 +/- 70 uM; kcat cell 930 +/- 100 s^-1; kcat/Km cell (1.25 +/- 0.25) x 10^6 M^-1 s^-1.', 'column_label': 'Km (uM)', 'condition_label': 'Form I beta-lactamase of Citrobacter diversus ULA-27, the chromatofocusing form with pI 6.8; Table 4 substrate profile; the experiments were performed at 30 C in 25 mM-sodium phosphate, pH 7.2, containing 0.2 M-NaCl and bovine serum albumin (0.05 mg/ml).', 'metric': 'Km', 'normalized_unit': 'mM', 'normalized_value': 0.74, 'primary_cell': True, 'raw_unit': 'uM', 'raw_value': '740 +/- 70', 'row_label': 'Form I | Cephaloridine', 'table_label': 'Table 4. Substrate profile of C. diversus beta-lactamases (PMC1135165 scanned page 889)'}; kcat/Km raw value: (1.25 +/- 0.25) x 10^6; raw unit: M^-1 s^-1; normalized value: 1250 s^-1 mM^-1; assay condition: Form I beta-lactamase of Citrobacter diversus ULA-27, the chromatofocusing form with pI 6.8; Table 4 substrate profile; the experiments were performed at 30 C in 25 mM-sodium phosphate, pH 7.2, containing 0.2 M-NaCl and bovine serum albumin (0.05 mg/ml).; captured primary segment: Table 4 Form I row Cephaloridine: Km cell 740 +/- 70 uM; kcat cell 930 +/- 100 s^-1; kcat/Km cell (1.25 +/- 0.25) x 10^6 M^-1 s^-1.

normalized_value_unit_evidence: kcat raw 930 +/- 100 s^-1 -> 930.0 s^-1; Km raw 740 +/- 70 uM -> 0.74 mM; explicit printed kcat/Km raw (1.25 +/- 0.25) x 10^6 M^-1 s^-1 -> 1250 s^-1 mM^-1. Conversion: 1.25 x 10^6 M^-1 s^-1 x 0.001 M/mM = 1250 s^-1 mM^-1. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence: Table 4, Form I block, row Cephaloridine: Km cell 740 +/- 70 uM; kcat cell 930 +/- 100 s^-1. Explicit printed kcat/Km primary cell: (1.25 +/- 0.25) x 10^6 M^-1 s^-1.

row_label: Form I | Cephaloridine