substrate_name: piperacillin

sequence_source: UniProtKB:P80545 direct accession lookup

column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Piperacillin. Column labels read: k cat (s^-1) cell 255, K m (uM) cell 23, k cat / K m (mM^-1 s^-1) cell 11 000. captured primary segment: Piperacillin 255 23 11 000 forms of the b-lactamase from S. fonticola CUV was. The printed k cat cell 255 s^-1 decimal-matches the exported kcat 255.0 s^(-1); the printed K m cell 23 uM normalizes to 0.023 mM and decimal-matches the exported km; the exported kcat_over_km 11086.95652173913 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row Piperacillin of Table 2; no value is taken from another row, another column, another table or another paper. assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer).

normalized_value_unit_evidence: metric: kcat; raw value: 255; raw unit: s^-1; normalized value: 255.0 s^(-1); metric: Km; raw value: 23; raw unit: uM; normalized value: 0.023 mM; metric: kcat/Km; derived from this row's own printed cells 255.0 s^-1 / 0.023 mM; normalized value: 11086.95652173913 s^-1 mM^-1; assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer). Conversion arithmetic (disclosed separately from the stated normalized values): kcat 255 s^-1 is already in s^-1, so the normalized kcat is 255.0 s^(-1). Km 23 uM = 23/1000 = 0.023 mM. kcat/Km is NOT read from the table's separately printed rounded cell; it is this row's own kcat divided by this row's own Km: 255.0 / 0.023 = 11086.95652173913 s^(-1)*mM^(-1). Two-sided round-trip against the separately printed k cat r K m cell 11 000: that cell is printed to a granularity of 1000, so it stands for the interval [10500, 11500); the quotient 11086.95652173913 of this row's own two printed cells falls inside that interval, and rounding 11086.95652173913 to the printed cell's granularity returns 11 000 exactly. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the micro sign renders as the letter m and parentheses render as the characters Zh and ., so the printed K m column header (uM) appears as ZhmM. and the printed k cat r K m column header (mM^-1 s^-1) appears as ZhmMy1 sy1 .

raw_value_unit_evidence: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV | printed column header line: Antibiotics k cat Km k cat r K m | printed row: Piperacillin 255 23 11 000 forms of the b-lactamase from S. fonticola CUV was | k cat cell as printed for this row: 255, printed unit s^-1 | K m cell as printed for this row: 23, printed unit uM | k cat r K m cell as printed for this row: 11 000, printed unit mM^-1 s^-1, retained as rounded corroboration only and not used as the exported ratio.

row_label: Piperacillin

substrate: piperacillin


enzyme_display_name: beta-lactamase

organism: Serratia fonticola

substrate_name: Cephaloridine

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

column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Cephaloridine. Column labels read: k cat (s^-1) cell 2530, K m (uM) cell 175, k cat / K m (mM^-1 s^-1) cell 14 500. captured primary segment: Cephaloridine 2530 175 14 500 with trypsin, endoproteinase Asp-N and chy-. The printed k cat cell 2530 s^-1 decimal-matches the exported kcat 2530.0 s^(-1); the printed K m cell 175 uM normalizes to 0.175 mM and decimal-matches the exported km; the exported kcat_over_km 14457.142857142859 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row Cephaloridine of Table 2; no value is taken from another row, another column, another table or another paper. assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer).

normalized_value_unit_evidence: metric: kcat; raw value: 2530; raw unit: s^-1; normalized value: 2530.0 s^(-1); metric: Km; raw value: 175; raw unit: uM; normalized value: 0.175 mM; metric: kcat/Km; derived from this row's own printed cells 2530.0 s^-1 / 0.175 mM; normalized value: 14457.142857142859 s^-1 mM^-1; assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer). Conversion arithmetic (disclosed separately from the stated normalized values): kcat 2530 s^-1 is already in s^-1, so the normalized kcat is 2530.0 s^(-1). Km 175 uM = 175/1000 = 0.175 mM. kcat/Km is NOT read from the table's separately printed rounded cell; it is this row's own kcat divided by this row's own Km: 2530.0 / 0.175 = 14457.142857142859 s^(-1)*mM^(-1). Two-sided round-trip against the separately printed k cat r K m cell 14 500: that cell is printed to a granularity of 100, so it stands for the interval [14450, 14550); the quotient 14457.142857142859 of this row's own two printed cells falls inside that interval, and rounding 14457.142857142859 to the printed cell's granularity returns 14 500 exactly. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the micro sign renders as the letter m and parentheses render as the characters Zh and ., so the printed K m column header (uM) appears as ZhmM. and the printed k cat r K m column header (mM^-1 s^-1) appears as ZhmMy1 sy1 .

raw_value_unit_evidence: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV | printed column header line: Antibiotics k cat Km k cat r K m | printed row: Cephaloridine 2530 175 14 500 with trypsin, endoproteinase Asp-N and chy- | k cat cell as printed for this row: 2530, printed unit s^-1 | K m cell as printed for this row: 175, printed unit uM | k cat r K m cell as printed for this row: 14 500, printed unit mM^-1 s^-1, retained as rounded corroboration only and not used as the exported ratio.

row_label: Cephaloridine

data_origin: experimental

enzyme: beta-lactamase

substrate: Cephaloridine

status: verified

source: oed


substrate_name: Cefamandole

column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Cefamandole. Column labels read: k cat (s^-1) cell 6105, K m (uM) cell 200, k cat / K m (mM^-1 s^-1) cell 30 500. captured primary segment: Cefamandole 6105 200 30 500 lish the complete sequences is shown in Fig. 1.. The printed k cat cell 6105 s^-1 decimal-matches the exported kcat 6105.0 s^(-1); the printed K m cell 200 uM normalizes to 0.2 mM and decimal-matches the exported km; the exported kcat_over_km 30525.0 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row Cefamandole of Table 2; no value is taken from another row, another column, another table or another paper. assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer).

normalized_value_unit_evidence: metric: kcat; raw value: 6105; raw unit: s^-1; normalized value: 6105.0 s^(-1); metric: Km; raw value: 200; raw unit: uM; normalized value: 0.2 mM; metric: kcat/Km; derived from this row's own printed cells 6105.0 s^-1 / 0.2 mM; normalized value: 30525.0 s^-1 mM^-1; assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer). Conversion arithmetic (disclosed separately from the stated normalized values): kcat 6105 s^-1 is already in s^-1, so the normalized kcat is 6105.0 s^(-1). Km 200 uM = 200/1000 = 0.2 mM. kcat/Km is NOT read from the table's separately printed rounded cell; it is this row's own kcat divided by this row's own Km: 6105.0 / 0.2 = 30525.0 s^(-1)*mM^(-1). Two-sided round-trip against the separately printed k cat r K m cell 30 500: that cell is printed to a granularity of 100, so it stands for the interval [30450, 30550); the quotient 30525.0 of this row's own two printed cells falls inside that interval, and rounding 30525.0 to the printed cell's granularity returns 30 500 exactly. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the micro sign renders as the letter m and parentheses render as the characters Zh and ., so the printed K m column header (uM) appears as ZhmM. and the printed k cat r K m column header (mM^-1 s^-1) appears as ZhmMy1 sy1 .

raw_value_unit_evidence: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV | printed column header line: Antibiotics k cat Km k cat r K m | printed row: Cefamandole 6105 200 30 500 lish the complete sequences is shown in Fig. 1. | k cat cell as printed for this row: 6105, printed unit s^-1 | K m cell as printed for this row: 200, printed unit uM | k cat r K m cell as printed for this row: 30 500, printed unit mM^-1 s^-1, retained as rounded corroboration only and not used as the exported ratio.

row_label: Cefamandole

substrate: Cefamandole


substrate_name: Penicillin G

column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Benzylpenicillin. Column labels read: k cat (s^-1) cell 770, K m (uM) cell 23, k cat / K m (mM^-1 s^-1) cell 33 500. captured primary segment: Benzylpenicillin 770 23 33 500. The printed k cat cell 770 s^-1 decimal-matches the exported kcat 770.0 s^(-1); the printed K m cell 23 uM normalizes to 0.023 mM and decimal-matches the exported km; the exported kcat_over_km 33478.260869565216 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row Benzylpenicillin of Table 2; no value is taken from another row, another column, another table or another paper. assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer).

normalized_value_unit_evidence: metric: kcat; raw value: 770; raw unit: s^-1; normalized value: 770.0 s^(-1); metric: Km; raw value: 23; raw unit: uM; normalized value: 0.023 mM; metric: kcat/Km; derived from this row's own printed cells 770.0 s^-1 / 0.023 mM; normalized value: 33478.260869565216 s^-1 mM^-1; assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer). Conversion arithmetic (disclosed separately from the stated normalized values): kcat 770 s^-1 is already in s^-1, so the normalized kcat is 770.0 s^(-1). Km 23 uM = 23/1000 = 0.023 mM. kcat/Km is NOT read from the table's separately printed rounded cell; it is this row's own kcat divided by this row's own Km: 770.0 / 0.023 = 33478.260869565216 s^(-1)*mM^(-1). Two-sided round-trip against the separately printed k cat r K m cell 33 500: that cell is printed to a granularity of 100, so it stands for the interval [33450, 33550); the quotient 33478.260869565216 of this row's own two printed cells falls inside that interval, and rounding 33478.260869565216 to the printed cell's granularity returns 33 500 exactly. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the micro sign renders as the letter m and parentheses render as the characters Zh and ., so the printed K m column header (uM) appears as ZhmM. and the printed k cat r K m column header (mM^-1 s^-1) appears as ZhmMy1 sy1 .

raw_value_unit_evidence: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV | printed column header line: Antibiotics k cat Km k cat r K m | printed row: Benzylpenicillin 770 23 33 500 | k cat cell as printed for this row: 770, printed unit s^-1 | K m cell as printed for this row: 23, printed unit uM | k cat r K m cell as printed for this row: 33 500, printed unit mM^-1 s^-1, retained as rounded corroboration only and not used as the exported ratio.

row_label: Benzylpenicillin

substrate: Penicillin G


substrate_name: Oxacillin

column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Oxacillin. Column labels read: k cat (s^-1) cell 105, K m (uM) cell 42, k cat / K m (mM^-1 s^-1) cell 2 500. captured primary segment: Oxacillin 105 42 2 500 Cloxacillin 90 43 2 100. The printed k cat cell 105 s^-1 decimal-matches the exported kcat 105.0 s^(-1); the printed K m cell 42 uM normalizes to 0.042 mM and decimal-matches the exported km; the exported kcat_over_km 2500.0 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row Oxacillin of Table 2; no value is taken from another row, another column, another table or another paper. assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer).

normalized_value_unit_evidence: metric: kcat; raw value: 105; raw unit: s^-1; normalized value: 105.0 s^(-1); metric: Km; raw value: 42; raw unit: uM; normalized value: 0.042 mM; metric: kcat/Km; derived from this row's own printed cells 105.0 s^-1 / 0.042 mM; normalized value: 2500.0 s^-1 mM^-1; assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer). Conversion arithmetic (disclosed separately from the stated normalized values): kcat 105 s^-1 is already in s^-1, so the normalized kcat is 105.0 s^(-1). Km 42 uM = 42/1000 = 0.042 mM. kcat/Km is NOT read from the table's separately printed rounded cell; it is this row's own kcat divided by this row's own Km: 105.0 / 0.042 = 2500.0 s^(-1)*mM^(-1). Two-sided round-trip against the separately printed k cat r K m cell 2 500: that cell is printed to a granularity of 100, so it stands for the interval [2450, 2550); the quotient 2500.0 of this row's own two printed cells falls inside that interval, and rounding 2500.0 to the printed cell's granularity returns 2 500 exactly. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the micro sign renders as the letter m and parentheses render as the characters Zh and ., so the printed K m column header (uM) appears as ZhmM. and the printed k cat r K m column header (mM^-1 s^-1) appears as ZhmMy1 sy1 .

raw_value_unit_evidence: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV | printed column header line: Antibiotics k cat Km k cat r K m | printed row: Oxacillin 105 42 2 500 | k cat cell as printed for this row: 105, printed unit s^-1 | K m cell as printed for this row: 42, printed unit uM | k cat r K m cell as printed for this row: 2 500, printed unit mM^-1 s^-1, retained as rounded corroboration only and not used as the exported ratio.

row_label: Oxacillin

substrate: Oxacillin


substrate_name: aztreonam

column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Aztreonam. Column labels read: k cat (s^-1) cell 38, K m (uM) cell 41, k cat / K m (mM^-1 s^-1) cell 930. captured primary segment: Aztreonam 38 41 930 Cefoxitin a y 1.2 y. The printed k cat cell 38 s^-1 decimal-matches the exported kcat 38.0 s^(-1); the printed K m cell 41 uM normalizes to 0.041 mM and decimal-matches the exported km; the exported kcat_over_km 926.8292682926829 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row Aztreonam of Table 2; no value is taken from another row, another column, another table or another paper. assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer).

normalized_value_unit_evidence: metric: kcat; raw value: 38; raw unit: s^-1; normalized value: 38.0 s^(-1); metric: Km; raw value: 41; raw unit: uM; normalized value: 0.041 mM; metric: kcat/Km; derived from this row's own printed cells 38.0 s^-1 / 0.041 mM; normalized value: 926.8292682926829 s^-1 mM^-1; assay condition: Purified b-lactamase of Serratia fonticola CUV; Methods section 2.4 as printed: the kinetic parameters (k cat and K m) for various substrates were determined at 378C (37 C) by computerized microacidimetry with purified enzyme in presence of serum albumine bovine (0.05 mgrml, i.e. 0.05 mg/ml); the export row carries pH 7 and 310.15 K (37 C) for the same measurement; printed table footnotes: "Hydrolytic activity was not detected." (marker a, which marks only the Cefoxitin / Cefotetan / Latamoxef / Imipenem rows, none of which is transcribed here), "K m values were determined as K i by substrate competition with benzylpenicillin." and "Standard deviations F10%." (the standard-deviation bound glyph renders as the letter F in this PDF text layer). Conversion arithmetic (disclosed separately from the stated normalized values): kcat 38 s^-1 is already in s^-1, so the normalized kcat is 38.0 s^(-1). Km 41 uM = 41/1000 = 0.041 mM. kcat/Km is NOT read from the table's separately printed rounded cell; it is this row's own kcat divided by this row's own Km: 38.0 / 0.041 = 926.8292682926829 s^(-1)*mM^(-1). Two-sided round-trip against the separately printed k cat r K m cell 930: that cell is printed to a granularity of 10, so it stands for the interval [925, 935); the quotient 926.8292682926829 of this row's own two printed cells falls inside that interval, and rounding 926.8292682926829 to the printed cell's granularity returns 930 exactly. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the micro sign renders as the letter m and parentheses render as the characters Zh and ., so the printed K m column header (uM) appears as ZhmM. and the printed k cat r K m column header (mM^-1 s^-1) appears as ZhmMy1 sy1 .

raw_value_unit_evidence: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV | printed column header line: Antibiotics k cat Km k cat r K m | printed row: Aztreonam 38 41 930 | k cat cell as printed for this row: 38, printed unit s^-1 | K m cell as printed for this row: 41, printed unit uM | k cat r K m cell as printed for this row: 930, printed unit mM^-1 s^-1, retained as rounded corroboration only and not used as the exported ratio.

row_label: Aztreonam

substrate: aztreonam


organism: Serratia marcescens

substrate_name: Nitrocefin

assay_conditions_summary: pH 8.2; 303.15 K; buffer 50 mM-Hepes

column_label: Table label: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2. Row: Nitrocefin. Columns read from that one row: kcat (s^-1) cell 1240 + 60, Km (uM) cell 40+2, kcat./Km (M^-1 s^-1) cell as printed. kcat normalizes to 1240.0 s^(-1); Km 40 uM normalizes to 0.04 mM; kcat/Km printed ratio cell `31 x 106` = 31 x 10^6 M^-1 s^-1; 31 x 10^6 / 1000 = 31000.0 s^-1 mM^-1, which decimal-matches the export; this row's own quotient 1240.0 / 0.04 = 31000.0 agrees with the printed cell exactly. No value is taken from another table row, another table, or another paper.

normalized_value_unit_evidence: metric: kcat; normalized value: 1240.0 s^(-1); metric: Km; normalized value: 0.04 mM; metric: kcat/Km; normalized value: 31000.0 s^-1 mM^-1; assay condition: Purified wild-type Serratia marcescens class C beta-lactamase, strain SC8247. Table 2 legend: the values were obtained in 50 mM-Hepes buffer, pH 8.2, containing 0.2 M-NaCl and 0.2 mg of bovine serum albumin/ml and are given as means + S.D. for four or more measurements. No cofactor or coenzyme column is declared; no mutant row or mutant column group exists in this table. Conversion arithmetic, stated separately from the normalized values: 40 uM / 1000 = 0.04 mM; printed ratio cell `31 x 106` = 31 x 10^6 M^-1 s^-1; 31 x 10^6 / 1000 = 31000.0 s^-1 mM^-1, which decimal-matches the export; this row's own quotient 1240.0 / 0.04 = 31000.0 agrees with the printed cell exactly. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

raw_value_unit_evidence: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2; column header line as printed: `Substrate                kcat (s-1)      Km (JuM)     (M-1. S-1)` with the ratio header `kcat./Km` on the line above; row as printed: `Nitrocefin            1240 + 60         40+2           31 x 106`. Printed cells: kcat 1240 + 60 s^-1; Km 40+2 uM; kcat/Km as printed. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

row_label: Nitrocefin

substrate: Nitrocefin


substrate_name: Cephazoline

column_label: Table label: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2. Row: Cephazoline. Columns read from that one row: kcat (s^-1) cell 1300+ 100, Km (uM) cell 540+45, kcat./Km (M^-1 s^-1) cell as printed. kcat normalizes to 1300.0 s^(-1); Km 540 uM normalizes to 0.54 mM; kcat/Km the printed ratio cell `2.4x 106` = 2.4 x 10^6 M^-1 s^-1 = 2400 s^-1 mM^-1 is a two-significant-figure rounding, so the exported value is recorded as the quotient of this same row's own two printed cells; two-sided round-trip: the quotient 2407.4074074074074 rounded to the paper's two significant figures is 2.4 x 10^6 M^-1 s^-1, matching the printed cell, while the printed cell rounded to the export's precision is 2400.0 and does not reproduce the export, so the difference is printed precision only and not a correction. No value is taken from another table row, another table, or another paper.

normalized_value_unit_evidence: metric: kcat; normalized value: 1300.0 s^(-1); metric: Km; normalized value: 0.54 mM; metric: kcat/Km; normalized value: 2407.4074074074074 s^-1 mM^-1; assay condition: Purified wild-type Serratia marcescens class C beta-lactamase, strain SC8247. Table 2 legend: the values were obtained in 50 mM-Hepes buffer, pH 8.2, containing 0.2 M-NaCl and 0.2 mg of bovine serum albumin/ml and are given as means + S.D. for four or more measurements. No cofactor or coenzyme column is declared; no mutant row or mutant column group exists in this table. Conversion arithmetic, stated separately from the normalized values: 540 uM / 1000 = 0.54 mM; the printed ratio cell `2.4x 106` = 2.4 x 10^6 M^-1 s^-1 = 2400 s^-1 mM^-1 is a two-significant-figure rounding, so the exported value is recorded as the quotient of this same row's own two printed cells; two-sided round-trip: the quotient 2407.4074074074074 rounded to the paper's two significant figures is 2.4 x 10^6 M^-1 s^-1, matching the printed cell, while the printed cell rounded to the export's precision is 2400.0 and does not reproduce the export, so the difference is printed precision only and not a correction. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

raw_value_unit_evidence: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2; column header line as printed: `Substrate                kcat (s-1)      Km (JuM)     (M-1. S-1)` with the ratio header `kcat./Km` on the line above; row as printed: `Cephazoline           1300+ 100       540+45          2.4x 106`. Printed cells: kcat 1300+ 100 s^-1; Km 540+45 uM; kcat/Km as printed. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

row_label: Cephazoline

substrate: Cephazoline


substrate_name: Cefuroxime

column_label: Table label: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2. Row: Cefuroxime. Columns read from that one row: kcat (s^-1) cell 0.8 +0.15, Km (uM) cell 0.6 + 0.06*, kcat./Km (M^-1 s^-1) cell as printed. kcat normalizes to 0.8 s^(-1); Km 0.6 uM normalizes to 0.0006 mM; kcat/Km the printed ratio cell `1.3x 106` = 1.3 x 10^6 M^-1 s^-1 = 1300 s^-1 mM^-1 is a two-significant-figure rounding, so the exported value is recorded as the quotient of this same row's own two printed cells; two-sided round-trip: the quotient 1333.3333333333335 rounded to the paper's two significant figures is 1.3 x 10^6 M^-1 s^-1, matching the printed cell, while the printed cell rounded to the export's precision is 1300.0 and does not reproduce the export, so the difference is printed precision only and not a correction. No value is taken from another table row, another table, or another paper.

normalized_value_unit_evidence: metric: kcat; normalized value: 0.8 s^(-1); metric: Km; normalized value: 0.0006 mM; metric: kcat/Km; normalized value: 1333.3333333333335 s^-1 mM^-1; assay condition: Purified wild-type Serratia marcescens class C beta-lactamase, strain SC8247. Table 2 legend: the values were obtained in 50 mM-Hepes buffer, pH 8.2, containing 0.2 M-NaCl and 0.2 mg of bovine serum albumin/ml and are given as means + S.D. for four or more measurements. No cofactor or coenzyme column is declared; no mutant row or mutant column group exists in this table. Conversion arithmetic, stated separately from the normalized values: 0.6 uM / 1000 = 0.0006 mM; the printed ratio cell `1.3x 106` = 1.3 x 10^6 M^-1 s^-1 = 1300 s^-1 mM^-1 is a two-significant-figure rounding, so the exported value is recorded as the quotient of this same row's own two printed cells; two-sided round-trip: the quotient 1333.3333333333335 rounded to the paper's two significant figures is 1.3 x 10^6 M^-1 s^-1, matching the printed cell, while the printed cell rounded to the export's precision is 1300.0 and does not reproduce the export, so the difference is printed precision only and not a correction. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

raw_value_unit_evidence: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2; column header line as printed: `Substrate                kcat (s-1)      Km (JuM)     (M-1. S-1)` with the ratio header `kcat./Km` on the line above; row as printed: `Cefuroxime              0.8 +0.15      0.6 + 0.06* 1.3x 106`. Printed cells: kcat 0.8 +0.15 s^-1; Km 0.6 + 0.06* uM; kcat/Km as printed. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

row_label: Cefuroxime

substrate: Cefuroxime


substrate_name: cefotaxime

column_label: Table label: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2. Row: Cefotaxime. Columns read from that one row: kcat (s^-1) cell 1.7+0.2, Km (uM) cell 12+3, kcat./Km (M^-1 s^-1) cell as printed. kcat normalizes to 1.7 s^(-1); Km 12 uM normalizes to 0.012 mM; kcat/Km the printed ratio cell `0.14x 106` = 0.14 x 10^6 M^-1 s^-1 = 140 s^-1 mM^-1 is a two-significant-figure rounding, so the exported value is recorded as the quotient of this same row's own two printed cells; two-sided round-trip: the quotient 141.66666666666666 rounded to the paper's two significant figures is 0.14 x 10^6 M^-1 s^-1, matching the printed cell, while the printed cell rounded to the export's precision is 140.0 and does not reproduce the export, so the difference is printed precision only and not a correction. No value is taken from another table row, another table, or another paper.

normalized_value_unit_evidence: metric: kcat; normalized value: 1.7 s^(-1); metric: Km; normalized value: 0.012 mM; metric: kcat/Km; normalized value: 141.66666666666666 s^-1 mM^-1; assay condition: Purified wild-type Serratia marcescens class C beta-lactamase, strain SC8247. Table 2 legend: the values were obtained in 50 mM-Hepes buffer, pH 8.2, containing 0.2 M-NaCl and 0.2 mg of bovine serum albumin/ml and are given as means + S.D. for four or more measurements. No cofactor or coenzyme column is declared; no mutant row or mutant column group exists in this table. Conversion arithmetic, stated separately from the normalized values: 12 uM / 1000 = 0.012 mM; the printed ratio cell `0.14x 106` = 0.14 x 10^6 M^-1 s^-1 = 140 s^-1 mM^-1 is a two-significant-figure rounding, so the exported value is recorded as the quotient of this same row's own two printed cells; two-sided round-trip: the quotient 141.66666666666666 rounded to the paper's two significant figures is 0.14 x 10^6 M^-1 s^-1, matching the printed cell, while the printed cell rounded to the export's precision is 140.0 and does not reproduce the export, so the difference is printed precision only and not a correction. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

raw_value_unit_evidence: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2; column header line as printed: `Substrate                kcat (s-1)      Km (JuM)     (M-1. S-1)` with the ratio header `kcat./Km` on the line above; row as printed: `Cefotaxime              1.7+0.2         12+3        0.14x 106`. Printed cells: kcat 1.7+0.2 s^-1; Km 12+3 uM; kcat/Km as printed. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

row_label: Cefotaxime

substrate: cefotaxime


verification_status: unverified

status: unverified


substrate_name: Imipenem

substrate: Imipenem


organism: Shewanella algae

substrate_name: Ticarcillin

sequence_source: UniProtKB:Q6VCW0 direct REST lookup

column_label: Table label: TABLE 2. Kinetic parameters and relative k cat / K m values of purified β-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1 a. Row: Ticarcillin. Enzyme column group: OXA-55. Columns read: k cat (s^-1) cell 1, K m (uM) cell 20, k cat / K m (mM^-1 s^-1) cell 50. metric: kcat; raw value: 1; raw unit: s^-1; normalized value: 1.0 s^(-1); metric: Km; raw value: 20; raw unit: uM; normalized value: 0.02 mM; metric: kcat/Km; raw value: 50; raw unit: mM^-1 s^-1; normalized value: 50.0 s^-1 mM^-1; assay condition: Purified beta-lactamase OXA-55 from Shewanella algae KB-1; kinetic measurements were performed at 30 degrees C in 100 mM sodium phosphate (pH 7.0); the k cat and K m values were determined by analyzing beta-lactam hydrolysis under initial rate conditions with a UV spectrophotometer. Data are means of three independent experiments. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: OXA-55 columns of Table 2 row Ticarcillin: kcat 1 s^-1 = 1.0 s^(-1); Km 20 uM = 0.02 mM (1 uM = 0.001 mM); kcat/Km 50 mM^-1 s^-1 = 50.0 s^-1 mM^-1, the export's unit being the same quantity written the other way round. The printed ratio cell also equals the quotient of this row's own printed cells, 1 s^-1 divided by 0.02 mM = 50.0 s^-1 mM^-1. In the saved article HTML the superscript minus one is flattened to a spaced −1, the micro sign renders as μ, the multiplication dot as ·, and the metric names render with spaced subscripts as 'k cat' and 'K m'.

raw_value_unit_evidence: TABLE 2. Kinetic parameters and relative k cat / K m values of purified β-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1 a | column group header row of Table 2: Substrate | OXA-55 | OXA-54 (relative k cat / K m ) b | OXA-40 (relative k cat / K m ) c | metric header row: k cat (s −1 ) | K m (μM) | k cat / K m (mM −1 · s −1 ) | Relative k cat / K m | row: Ticarcillin | 1 | 20 | 50 | 31 | 6 | 9 | OXA-55 cells read: k cat = 1 s^-1; K m = 20 uM; k cat / K m = 50 mM^-1 s^-1; Relative k cat / K m = 31 (percent of benzylpenicillin, which was set at 100)

row_label: OXA-55 | Ticarcillin

substrate: Ticarcillin


substrate_name: cefpirome

substrate: cefpirome


substrate_name: Cloxacillin

substrate: Cloxacillin


substrate_name: moxalactam

sequence_source: UniProtKB REST direct lookup for P18539 on 2026-05-27

column_label: Table label: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2. Row: Moxalactam. Columns read from that one row: kcat (s^-1) cell 0.12+0.01, Km (uM) cell 60+7*, kcat./Km (M^-1 s^-1) cell as printed. kcat normalizes to 0.12 s^(-1); Km 60 uM normalizes to 0.06 mM; kcat/Km printed ratio cell `2000` M^-1 s^-1; 2000 / 1000 = 2.0 s^-1 mM^-1, which decimal-matches the export; this row's own quotient 0.12 / 0.06 = 2.0 agrees with the printed cell exactly. No value is taken from another table row, another table, or another paper.

normalized_value_unit_evidence: metric: kcat; normalized value: 0.12 s^(-1); metric: Km; normalized value: 0.06 mM; metric: kcat/Km; normalized value: 2.0 s^-1 mM^-1; assay condition: Purified wild-type Serratia marcescens class C beta-lactamase, strain SC8247. Table 2 legend: the values were obtained in 50 mM-Hepes buffer, pH 8.2, containing 0.2 M-NaCl and 0.2 mg of bovine serum albumin/ml and are given as means + S.D. for four or more measurements. No cofactor or coenzyme column is declared; no mutant row or mutant column group exists in this table. Conversion arithmetic, stated separately from the normalized values: 60 uM / 1000 = 0.06 mM; printed ratio cell `2000` M^-1 s^-1; 2000 / 1000 = 2.0 s^-1 mM^-1, which decimal-matches the export; this row's own quotient 0.12 / 0.06 = 2.0 agrees with the printed cell exactly. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

raw_value_unit_evidence: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2; column header line as printed: `Substrate                kcat (s-1)      Km (JuM)     (M-1. S-1)` with the ratio header `kcat./Km` on the line above; row as printed: `Moxalactam             0.12+0.01        60+7*           2000`. Printed cells: kcat 0.12+0.01 s^-1; Km 60+7* uM; kcat/Km as printed. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

row_label: Moxalactam

substrate: moxalactam


substrate_name: Cephalothin

column_label: Table label: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2. Row: Cephalothin. Columns read from that one row: kcat (s^-1) cell 1100+50, Km (uM) cell 67+4, kcat./Km (M^-1 s^-1) cell as printed. kcat normalizes to 1100.0 s^(-1); Km 67 uM normalizes to 0.067 mM; kcat/Km the printed ratio cell `16x 106` = 16 x 10^6 M^-1 s^-1 = 16000 s^-1 mM^-1 is a two-significant-figure rounding, so the exported value is recorded as the quotient of this same row's own two printed cells; two-sided round-trip: the quotient 16417.910447761195 rounded to the paper's two significant figures is 16 x 10^6 M^-1 s^-1, matching the printed cell, while the printed cell rounded to the export's precision is 16000.0 and does not reproduce the export, so the difference is printed precision only and not a correction. No value is taken from another table row, another table, or another paper.

normalized_value_unit_evidence: metric: kcat; normalized value: 1100.0 s^(-1); metric: Km; normalized value: 0.067 mM; metric: kcat/Km; normalized value: 16417.910447761195 s^-1 mM^-1; assay condition: Purified wild-type Serratia marcescens class C beta-lactamase, strain SC8247. Table 2 legend: the values were obtained in 50 mM-Hepes buffer, pH 8.2, containing 0.2 M-NaCl and 0.2 mg of bovine serum albumin/ml and are given as means + S.D. for four or more measurements. No cofactor or coenzyme column is declared; no mutant row or mutant column group exists in this table. Conversion arithmetic, stated separately from the normalized values: 67 uM / 1000 = 0.067 mM; the printed ratio cell `16x 106` = 16 x 10^6 M^-1 s^-1 = 16000 s^-1 mM^-1 is a two-significant-figure rounding, so the exported value is recorded as the quotient of this same row's own two printed cells; two-sided round-trip: the quotient 16417.910447761195 rounded to the paper's two significant figures is 16 x 10^6 M^-1 s^-1, matching the printed cell, while the printed cell rounded to the export's precision is 16000.0 and does not reproduce the export, so the difference is printed precision only and not a correction. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

raw_value_unit_evidence: Table 2. Kinetic parameters of Serratia marcescens II-lactamase at pH 8.2; column header line as printed: `Substrate                kcat (s-1)      Km (JuM)     (M-1. S-1)` with the ratio header `kcat./Km` on the line above; row as printed: `Cephalothin           1100+50           67+4           16x 106`. Printed cells: kcat 1100+50 s^-1; Km 67+4 uM; kcat/Km as printed. In this PDF text layer superscripts are flattened, so the printed kcat column header kcat (s^-1) reads `kcat (s-1)`, the printed ratio header kcat/Km (M^-1 s^-1) reads `(M-1. S-1)`, the printed Km column header Km (uM) reads `Km (JuM)`, and a printed 10^6 reads `106`.

row_label: Cephalothin

substrate: Cephalothin


substrate_name: cefoxitin

verification_status: corrected

column_label: Retained PDF Table 2, Cefoxitin row: kcat 0.014 +/- 0.002; Km 0.3 +/- 0.03, starred and determined as Ki; kcat/Km 47000.

normalized_value_unit_evidence: Table 2 Cefoxitin row: kcat 0.014 s^-1; Km 0.3 uM = 0.0003 mM; independently printed kcat/Km 47000 M^-1 s^-1 = 47 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Cefoxitin row: kcat 0.014 +/- 0.002 s^-1; Km 0.3 +/- 0.03 uM, starred and determined as Ki; independently printed kcat/Km 47000 M^-1 s^-1.

row_label: Cefoxitin

table_label: Table 2. Kinetic parameters of Serratia marcescens beta-lactamase at pH 8.2

substrate: cefoxitin

status: corrected


sequence_source: UniProtKB REST direct lookup for Q6VCW0 on 2026-05-27


enzyme_display_name: OXA-55 beta-lactamase

substrate_name: Ceftazidime

sequence_source: UniProtKB Q6VCW0 REST/FASTA direct lookup on 2026-05-27; primaryAccession Q6VCW0; sequence version 1; PMID 15105119; EMBL AY343493 protein AAR03105.1

enzyme: OXA-55 beta-lactamase

substrate: Ceftazidime


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: Meropenem

substrate: Meropenem


substrate_name: Cephaloridine

substrate: Cephaloridine


substrate_name: piperacillin

substrate: piperacillin


substrate_name: Penicillin G

substrate: Penicillin G


organism: Staphylococcus aureus

sequence_source: UniProtKB FASTA direct lookup for P00807

column_label: PMID 1605608 TABLE 1. Km values for ,B-lactam antibiotics of purified ,3-lactamases of S. aureus (Mean (SEM) Km, micromolar, for 1-lactamase type (strain)); row Cefuroxime / type A (PC1); column type A (PC1) Km (micromolar); printed cell Km 378 (64) micromolar. PMID 1605608 TABLE 2. kcat values for P-lactam antibiotics of purified P-lactamases of S. aureus (Mean (SEM) kcat values (s-1) for P-lactamase type (strain)); row Cefuroxime / type A (PC1); column type A (PC1) kcat (s-1); printed cell kcat 0.009 (0.001) s-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.009 s^-1 / 0.378 mM = 0.023809523809523808 s^-1 mM^-1); neither Table 1 nor Table 2 prints a kcat/Km cell, and Table 4 prints only a relative efficiency of hydrolysis (REH) percentage normalized to type A cephaloridine, which is not an absolute kcat/Km value and is not used here. Table 1 column headers as printed: 'A (PC1)        B (22260)       C (V137)       D (FAR10)'. Table 1 footnote a: 'Km values were determined by the use of [s]/v-against-[s] plots and expressed as micromolar concentrations. Each value is derived from 3 to 11 determinations.' Footnote b: 'ND, not determined.' Table 2 column headers as printed: 'A (PC1)                              B (22260)                          C (V137)                            D (FAR10)'. Table 2 footnote a: 'Determined from [s]/v-against-[s] plots, assuming a molecular weight of the purified ,-lactamase of 30,000. Each value is derived from 3 to 11 determinations.'

normalized_value_unit_evidence: metric: kcat; raw value: 0.009 (0.001) s-1; raw unit: s^-1; normalized value: 0.009 s^(-1); metric: Km; raw value: 378 (64) uM; raw unit: uM; normalized value: 0.378 mM; metric: kcat/Km; raw value: null (not printed by the paper); raw unit: s^-1 mM^-1; normalized value: 0.023809523809523808 s^(-1)*mM^(-1); assay condition: 0.1 M sodium phosphate buffer, pH 6.0; 1-cm cuvettes; 37 degrees C; DU-70 recording spectrophotometer; purified extracellular beta-lactamase; wild-type enzyme; no mutation.

raw_value_unit_evidence: Table cells as printed: Km 378 (64) micromolar (Table 1, type A (PC1) column); kcat 0.009 (0.001) s-1 (Table 2, type A (PC1) column). Parenthesized figures are the printed SEM.

row_label: Cefuroxime / type A (PC1)

table_label: PMID 1605608 TABLE 1. Km values for ,B-lactam antibiotics of purified ,3-lactamases of S. aureus (Mean (SEM) Km, micromolar, for 1-lactamase type (strain)) and PMID 1605608 TABLE 2. kcat values for P-lactam antibiotics of purified P-lactamases of S. aureus (Mean (SEM) kcat values (s-1) for P-lactamase type (strain))


substrate_name: cefazolin

substrate: cefazolin


substrate_name: Cephapirin

substrate: Cephapirin


substrate_name: Nitrocefin

substrate: Nitrocefin


organism: Pseudomonas aeruginosa

substrate_name: cefuroxime

sequence_source: UniProtKB REST accession Q8KRJ3, checked 2026-05-27

substrate: cefuroxime


substrate_name: cephalotin

substrate: cephalotin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: ampicillin

substrate: ampicillin


substrate_name: biapenem

substrate: biapenem


substrate_name: benzylpenicillin

substrate: benzylpenicillin


substrate_name: Cefamandole

column_label: PMID 1605608 TABLE 1. Km values for ,B-lactam antibiotics of purified ,3-lactamases of S. aureus (Mean (SEM) Km, micromolar, for 1-lactamase type (strain)); row Cefamandole / type B (22260); column type B (22260) Km (micromolar); printed cell Km 6.0 (0.3) micromolar. PMID 1605608 TABLE 2. kcat values for P-lactam antibiotics of purified P-lactamases of S. aureus (Mean (SEM) kcat values (s-1) for P-lactamase type (strain)); row Cefamandole / type B (22260); column type B (22260) kcat (s-1); printed cell kcat 0.357 (0.003) s-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.357 s^-1 / 0.006 mM = 59.49999999999999 s^-1 mM^-1); neither Table 1 nor Table 2 prints a kcat/Km cell, and Table 4 prints only a relative efficiency of hydrolysis (REH) percentage normalized to type A cephaloridine, which is not an absolute kcat/Km value and is not used here. Table 1 column headers as printed: 'A (PC1)        B (22260)       C (V137)       D (FAR10)'. Table 1 footnote a: 'Km values were determined by the use of [s]/v-against-[s] plots and expressed as micromolar concentrations. Each value is derived from 3 to 11 determinations.' Footnote b: 'ND, not determined.' Table 2 column headers as printed: 'A (PC1)                              B (22260)                          C (V137)                            D (FAR10)'. Table 2 footnote a: 'Determined from [s]/v-against-[s] plots, assuming a molecular weight of the purified ,-lactamase of 30,000. Each value is derived from 3 to 11 determinations.'

normalized_value_unit_evidence: metric: kcat; raw value: 0.357 (0.003) s-1; raw unit: s^-1; normalized value: 0.357 s^(-1); metric: Km; raw value: 6.0 (0.3) uM; raw unit: uM; normalized value: 0.006 mM; metric: kcat/Km; raw value: null (not printed by the paper); raw unit: s^-1 mM^-1; normalized value: 59.49999999999999 s^(-1)*mM^(-1); assay condition: 0.1 M sodium phosphate buffer, pH 6.0; 1-cm cuvettes; 37 degrees C; DU-70 recording spectrophotometer; purified extracellular beta-lactamase; wild-type enzyme; no mutation.

raw_value_unit_evidence: Table cells as printed: Km 6.0 (0.3) micromolar (Table 1, type B (22260) column); kcat 0.357 (0.003) s-1 (Table 2, type B (22260) column). Parenthesized figures are the printed SEM.

row_label: Cefamandole / type B (22260)

substrate: Cefamandole


substrate_name: multiple beta-lactam substrates

kcat_over_km_display: Not reported

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

substrate: multiple beta-lactam substrates


substrate_name: Cephalothin

substrate: Cephalothin


organism: Stenotrophomonas maltophilia

substrate_name: Ampicillin

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature Y228A with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: Ampicillin


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature Y228F with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


substrate_name: Cefaclor

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -16, so it is treated as a source-provided variant sequence.

substrate: Cefaclor


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature N233L with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


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


substrate_name: Meropenem

substrate: Meropenem


sequence_variant_note: Resolved canonical sequence from UniProt P52700 canonical sequence reconstructed with PMID 11876827 Table 1 mutagenesis primer; BBL numbering offset -16 and applied mutation signature S224D with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P52700 canonical sequence reconstructed with PMID 11876827 Table 1 mutagenesis primer; BBL numbering offset -16 and applied mutation signature N233D with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


substrate_name: cefoxitin

sequence_source: UniProt P52700 canonical sequence reconstructed with PMID 11876827 Table 1 mutagenesis primer; BBL numbering offset -16

substrate: cefoxitin


sequence_variant_note: Resolved canonical sequence from UniProt P52700 canonical sequence reconstructed with PMID 11876827 Table 1 mutagenesis primer; BBL numbering offset -16 and applied mutation signature N233L with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


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


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y228F

substrate: Nitrocefin; H2O


sequence_source: RCSB 1SML entity sequence mapped to UniProt P52700; D120 variant reconstructed from PMID 14573595 mutation label

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


sequence_source: Reconstructed from UniProt P52700 after direct RCSB mapping of paper D120 nomenclature to the P52700 sequence.


sequence_variant_note: Mutation signature D120N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -11, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession_and_bbl_alignment and applied mutation signature S224A with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


substrate_name: multiple SABIO-RK substrate rows: H2O; Nitrocefin, Cefoxitin; H2O, Cefaclor; H2O, H2O; Cephalothin

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession_and_bbl_alignment and applied mutation signature S224K with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S224K


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession_and_bbl_alignment and applied mutation signature Y228F with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession_and_bbl_alignment and applied mutation signature S224D with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


sequence_source: UniProt REST direct check of P52700; canonical sequence only, variant sequence not accepted for this row.


substrate_name: Nitrocefin


sequence_variant_note: Mutation signature W39F/D160W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_P52700_with_PMID_15271998_mutagenesis_primer_mapping and applied mutation signature W206F with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_P52700_with_PMID_15271998_mutagenesis_primer_mapping and applied mutation signature W204F with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_P52700_with_PMID_15271998_mutagenesis_primer_mapping and applied mutation signature W53F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_P52700_with_PMID_15271998_mutagenesis_primer_mapping and applied mutation signature W39F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


substrate_name: Cephradine

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

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

column_label: Table 5 (PDF page 5 of 8, printed page 196), antibiotic row `Cephradine`, enzyme block `X. maltophilia ULA-511`: Km (uM) = 50 +/- 5; kcat (s-1) = 12.5; kcat/Km (M-1 s-1) = 2.50 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 12.5 s-1 -> 12.5 s^(-1) (the printed unit is already per second); the exported value is 16 s^(-1). Km: printed cell 50 +/- 5 uM -> 0.05 mM (divide by 1000); the exported value is 0.05 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.50 x 10^5 M-1 s-1 for this cell block -> 250 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1; the per-second part is unchanged); the exported value is 320.0 s^(-1)*mM^(-1).

row_label: Table 5, decoded plain-numeral transcription, antibiotic row `Cephradine`, enzyme block `X. maltophilia ULA-511`

table_label: Table 5 (PDF page 5 of 8, printed page 196) 'Kinetic parameters of metallo-b-lactamases with cephalosporins (Delta3-cephems)'

substrate: Cephradine


substrate_name: cefpirome

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

column_label: Table label: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a. Row: Cefpirome. Enzyme column group: X. maltophilia ULA-511. Columns read: Km (uM) cell 320 ± 20, kcat (s^-1) cell 85.0, kcat/Km (M^-1 s^-1) cell 2.65 x 10^5. Km 320 ± 20 uM normalizes to 0.32 mM and equals the exported km; kcat 85.0 s^-1 equals the exported kcat; the separately rounded kcat/Km (M^-1 s^-1) cell 2.65 x 10^5 M^-1 s^-1 (= 265.0 s^-1 mM^-1) is disclosed but not used; the exported kcat_over_km 265.625 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells.

normalized_value_unit_evidence: X. maltophilia ULA-511 columns of Table 5 row Cefpirome: Km 320 ± 20 uM = 0.32 mM; kcat 85.0 s^-1 = 85.0 s^-1; kcat/Km 265.625 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: X. maltophilia ULA-511 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Cefpirome              —              —                —             .1,000       .150               1.70 3 105c    320 6 20           85.0       2.65 3 105

row_label: X. maltophilia ULA-511 | Cefpirome

substrate: cefpirome


substrate_name: Cefsulodin

column_label: Table 5: Kinetic parameters of metallo-beta-lactamases with cephalosporins (Delta3-cephems); organism block X. maltophilia ULA-511 (now Stenotrophomonas maltophilia); row Cefsulodin; Km raw 5 uM normalized 0.005 mM; kcat raw 7.5 s^-1 normalized 7.5 s^-1; kcat/Km raw 1500000.0 M^-1 s^-1 normalized 1500 s^-1 mM^-1.

row_label: X. maltophilia ULA-511 (now Stenotrophomonas maltophilia) / Cefsulodin

substrate: Cefsulodin


substrate_name: Talampicillin

substrate: Talampicillin


column_label: Table label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonama. Row: HRE-664. Enzyme column group: X. maltophilia ULA-511. Columns read: Km (uM) cell 20 ± 2, kcat (s^-1) cell 1.5, kcat/Km (M^-1 s^-1) cell 7.50 x 10^4. Km 20 ± 2 uM normalizes to 0.02 mM and equals the exported km; kcat 1.5 s^-1 equals the exported kcat; kcat/Km (M^-1 s^-1) cell 7.50 x 10^4 M^-1 s^-1 normalizes to 75.0 s^-1 mM^-1 and decimal-matches the exported kcat_over_km.

normalized_value_unit_evidence: X. maltophilia ULA-511 columns of Table 6 row HRE-664: Km 20 ± 2 uM = 0.02 mM; kcat 1.5 s^-1 = 1.5 s^-1; kcat/Km 75.0 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 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonama | enzyme column group: X. maltophilia ULA-511 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: HRE-664                 140 6 10          10.0        7.15 3 104           25 6 2         10.0          4.00 3 105        20 6 2                 1.5     7.50 3 104

row_label: X. maltophilia ULA-511 | HRE-664


column_label: Table label: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a. Row: CGP-31523A. Enzyme column group: X. maltophilia ULA-511. Columns read: Km (uM) cell 27 ± 2, kcat (s^-1) cell 38.0, kcat/Km (M^-1 s^-1) cell 1.40 x 10^6. Km 27 ± 2 uM normalizes to 0.027 mM and equals the exported km; kcat 38.0 s^-1 equals the exported kcat; the separately rounded kcat/Km (M^-1 s^-1) cell 1.40 x 10^6 M^-1 s^-1 (= 1400.0 s^-1 mM^-1) is disclosed but not used; the exported kcat_over_km 1407.4074074074074 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells.

normalized_value_unit_evidence: X. maltophilia ULA-511 columns of Table 5 row CGP-31523A: Km 27 ± 2 uM = 0.027 mM; kcat 38.0 s^-1 = 38.0 s^-1; kcat/Km 1407.4074074074074 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: X. maltophilia ULA-511 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: 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: X. maltophilia ULA-511 | CGP-31523A


substrate_name: azlocillin

sequence_source: UniProtKB:P52700 direct REST lookup on 2026-05-27

column_label: Table 4, row Azlocillin, X. maltophilia ULA-511 column group: Km 6 ± 0.1 uM (footnote b: Km calculated as Ki using nitrocefin), kcat 75 s^-1, and independently printed kcat/Km 1.30 x 10^7 M^-1 s^-1. The current 0.006 mM and 75 s^-1 exactly bind those cells; current 12500 s^-1 mM^-1 is their exact quotient, while the table's independently printed 13000 s^-1 mM^-1 remains explicitly preserved.

normalized_value_unit_evidence: The printed X. maltophilia ULA-511 cells normalize to Km 0.006 mM and kcat 75 s^-1. The current stored kcat/Km 12500 s^-1 mM^-1 is the exact quotient 75 / 0.006 from those same two primary cells. The independently printed ratio 1.30 x 10^7 M^-1 s^-1 normalizes to 13000 s^-1 mM^-1 and is preserved separately; the difference is within Table 4's stated below-10% dispersion.

raw_value_unit_evidence: TABLE 4 row Azlocillin, X. maltophilia ULA-511 column group: Km cell 6 ± 0.1 uM with footnote b; kcat cell 75 s^-1; kcat/Km cell 1.30 x 10^7 M^-1 s^-1. Footnote b states Km was calculated as Ki using nitrocefin as reporter substrate.

row_label: X. maltophilia ULA-511 | Azlocillin

table_label: TABLE 4. Kinetic parameters of metallo-beta-lactamases with penicillins

substrate: azlocillin


column_label: Table 7 (PDF page 6 of 8, printed page 197), antibiotic row `Meropenem`, enzyme block `X. maltophilia ULA-511`: Km (uM) = 10 +/- 1 (b); kcat (s-1) = 45; kcat/Km (M-1 s-1) = 4.50 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 45 s-1 -> 45 s^(-1) (the printed unit is already per second); the exported value is 157 s^(-1). Km: printed cell 10 +/- 1 (b) uM -> 0.01 mM (divide by 1000); the exported value is 0.01 mM. kcat/Km: the paper PRINTS the kcat/Km cell 4.50 x 10^6 M-1 s-1 for this cell block -> 4500 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1; the per-second part is unchanged); the exported value is 15700.0 s^(-1)*mM^(-1).

row_label: Table 7, decoded plain-numeral transcription, antibiotic row `Meropenem`, enzyme block `X. maltophilia ULA-511`

table_label: Table 7 (PDF page 6 of 8, printed page 197) 'Kinetic parameters of metallo-b-lactamases with carbapenem antibiotics'


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

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

column_label: PMC1132494 page 154 Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row 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: 20; raw unit: s^-1; normalized value: 20.0; normalized unit: s^-1; metric: Km; raw value: 7 +/- 1; raw unit: uM; normalized value: 0.007; normalized unit: mM; metric: kcat/Km; normalized value: 2857.142857142857; normalized unit: s^-1 mM^-1; assay condition: Table 3 kinetic determinations for the class B beta-lactamase of the Pseudomonas maltophilia ULA-511 L-1 column of Table 3 (the package's Table 3 extract labels this column Stenotrophomonas maltophilia and its header identifies it as the Pseudomonas maltophilia ULA-511 L-1 column); Materials and methods: the experiments for ULA-511 and A. hydrophila were performed in 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2, at 35 C and 30 C respectively, so 35 C applies to this enzyme; the export row carries pH 7.0 and 308.15 K.

raw_value_unit_evidence: Table 3, Pseudomonas maltophilia ULA-511 L-1 beta-lactamase column, row nitrocefin: Km cell 7 +/- 1 uM; kcat cell 20 s^-1.

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

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

substrate: Nitrocefin


substrate_name: cephaloridin

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

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

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

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

substrate: cephaloridin


substrate_name: Oxacillin

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

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

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

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

substrate: Oxacillin


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

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

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

table_label: PMC1132494 scanned page 154 Table 3


substrate_name: Asparenomycin A

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

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

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

row_label: X. maltophilia ULA-511 | Asparenomycin A

substrate: Asparenomycin A


substrate_name: Sulbenicillin

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

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

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

row_label: X. maltophilia ULA-511 | Sulbenicillin

substrate: Sulbenicillin


substrate_name: Ticarcillin

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

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

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

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

substrate: Ticarcillin


substrate_name: Imipenem

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

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

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

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

substrate: Imipenem


substrate_name: Epicillin

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

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

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

row_label: X. maltophilia ULA-511 | Epicillin

substrate: Epicillin


substrate_name: tazobactam

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

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

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

row_label: X. maltophilia ULA-511 | Tazobactam

substrate: tazobactam


substrate_name: Temocillin

substrate: Temocillin


substrate_name: piperacillin

substrate: piperacillin


substrate_name: carbenicillin

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

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

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

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

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

substrate: carbenicillin


substrate_name: moxalactam

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

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

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

substrate: moxalactam


substrate_name: Cefuroxime

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

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

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

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

substrate: Cefuroxime


substrate_name: Cephalosporin C

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

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

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

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

row_label: Cephalosporin C

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

substrate: Cephalosporin C


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: Cefaclor

substrate: Cefaclor


substrate_name: cefmetazole

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

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

row_label: Cefmetazole

substrate: cefmetazole


substrate_name: cefepime

substrate: cefepime


substrate_name: Ampicillin

sequence_source: UniProtKB:P52700 reviewed Swiss-Prot direct lookup

substrate: Ampicillin


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

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

row_label: Recombinant L1 | Moxalactam


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: cefprozil

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

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

row_label: Recombinant L1 | Cefprozil

substrate: cefprozil


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

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

row_label: Recombinant L1 | Cefuroxime


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: biapenem

substrate: biapenem


enzyme_display_name: pyruvate kinase

organism: Canis familiaris

substrate_name: ADP; Phosphoenolpyruvate

kcat_display: Not reported

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

assay_conditions_summary: cofactor ATP

enzyme: pyruvate kinase

substrate: ADP; Phosphoenolpyruvate


substrate_name: cephalexin

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

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

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

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

substrate: cephalexin


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

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

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

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

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


substrate_name: 6-beta-Iodopenicillanic acid

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

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

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

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

substrate: 6-beta-Iodopenicillanic acid


substrate_name: Imipenem

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

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

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

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

substrate: Imipenem


substrate_name: Cephaloglycin

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

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

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

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

substrate: Cephaloglycin


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

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

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


substrate_name: cefotaxime

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

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

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

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

substrate: cefotaxime


substrate_name: Sulbactam

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

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

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

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

substrate: Sulbactam


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

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

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

row_label: Recombinant L1 | Cefotaxime


substrate_name: Cephaloridine

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

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

row_label: Recombinant L1 | Cephaloridine

substrate: Cephaloridine


substrate_name: cefadroxil

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

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

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

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

substrate: cefadroxil


substrate_name: clavulanic acid

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

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

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

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

substrate: clavulanic acid


substrate_name: Ceftizoxime

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

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

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

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

substrate: Ceftizoxime


organism: Treponema pallidum

substrate_name: Cloxacillin

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

substrate: Cloxacillin


substrate_name: carbenicillin

substrate: carbenicillin


organism: Arabidopsis thaliana

substrate_name: ADP

source_db: brenda

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ADP

source: brenda


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


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


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


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


organism: Rattus norvegicus

substrate_name: Phosphoenolpyruvate; ADP

sequence_source: UniProtKB:P11980 direct fetch

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

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

substrate: Phosphoenolpyruvate; ADP


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

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


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

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


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

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


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

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