substrate_name: amoxicillin

column_label: Table label: TABLE 2. Kinetics parameters of TEM-89 β-lactamase compared with those of TEM-2, TEM-3, and TEM-59 β-lactamases: Row: Amoxicillin. Enzyme column block: TEM-89. Columns read: k cat (s^-1) cell 50, K m (uM) cell 28, k cat / K m (uM^-1 s^-1) cell 1.79. metric: kcat; raw value: 50; raw unit: s^-1; normalized value: 50.0 s^(-1); metric: Km; raw value: 28; raw unit: uM; normalized value: 0.028 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 1785.7142857142858 s^-1 mM^-1; assay condition: Purified TEM-89 beta-lactamase produced by the Proteus mirabilis clinical isolate; kinetic constants (Table 2) were determined by computerized microacidimetry at pH 7 and 37 C in 0.1 M NaCl solution. Export row conditions: pH 7; 310.15 K.

normalized_value_unit_evidence: TEM-89 columns of Table 2 row Amoxicillin: kcat 50 s^-1 = 50.0 s^(-1); Km 28 uM = 0.028 mM (1 uM = 0.001 mM); kcat/Km 1785.7142857142858 s^-1 mM^-1 (1 uM^-1 s^-1 = 1000 s^-1 mM^-1, so the printed cell 1.79 uM^-1 s^-1 is 1790.0 s^-1 mM^-1). In the HTML asset the micro sign renders as μ, the superscript minus one as −1, thousands carry a comma (for example 1,500), and superscripts are flattened.; the trailing superscript on the latter three is a typesetting artefact of the source, the Km cells are micromolar in every block.

raw_value_unit_evidence: TABLE 2. Kinetics parameters of TEM-89 β-lactamase compared with those of TEM-2, TEM-3, and TEM-59 β-lactamases: | column header band as printed: Substrate TEM-2 TEM-3 TEM-89 TEM-59 k cat (s −1 ) K m (μM) k cat / K m (μM −1 s −1 ) k cat (s −1 ) K m (μM −1 ) k cat / K m (μM −1 s −1 ) k cat (s −1 ) K m (μM −1 ) k cat / K m (μM −1 s −1 ) k cat (s −1 ) K m (μM −1 ) k cat / K m (μM −1 s −1 ) | labelled cell line for this row in the appended verbatim transcription: Table 2 row Amoxicillin, TEM-89 columns: kcat = 50 s^-1; Km = 28 uM; kcat/Km = 1.79 uM^-1 s^-1. | TEM-89 cells read: k cat = 50 s^-1; K m = 28 uM; k cat / K m = 1.79 uM^-1 s^-1.

row_label: TEM-89 | Amoxicillin

substrate: amoxicillin


enzyme_display_name: beta-lactamase

organism: Proteus mirabilis

substrate_name: Cephaloridine

source_db: oed

verification_status: verified

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB Q93LJ5 FASTA, direct lookup on 2026-05-27

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. Kinetics parameters of TEM-89 β-lactamase compared with those of TEM-2, TEM-3, and TEM-59 β-lactamases: Row: Cephaloridine. Enzyme column block: TEM-89. Columns read: k cat (s^-1) cell 5, K m (uM) cell 160, k cat / K m (uM^-1 s^-1) cell 0.03. metric: kcat; raw value: 5; raw unit: s^-1; normalized value: 5.0 s^(-1); metric: Km; raw value: 160; raw unit: uM; normalized value: 0.16 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 31.25 s^-1 mM^-1; assay condition: Purified TEM-89 beta-lactamase produced by the Proteus mirabilis clinical isolate; kinetic constants (Table 2) were determined by computerized microacidimetry at pH 7 and 37 C in 0.1 M NaCl solution. Export row conditions: pH 7; 310.15 K.

normalized_value_unit_evidence: TEM-89 columns of Table 2 row Cephaloridine: kcat 5 s^-1 = 5.0 s^(-1); Km 160 uM = 0.16 mM (1 uM = 0.001 mM); kcat/Km 31.25 s^-1 mM^-1 (1 uM^-1 s^-1 = 1000 s^-1 mM^-1, so the printed cell 0.03 uM^-1 s^-1 is 30.0 s^-1 mM^-1). In the HTML asset the micro sign renders as μ, the superscript minus one as −1, thousands carry a comma (for example 1,500), and superscripts are flattened.; the trailing superscript on the latter three is a typesetting artefact of the source, the Km cells are micromolar in every block.

raw_value_unit_evidence: TABLE 2. Kinetics parameters of TEM-89 β-lactamase compared with those of TEM-2, TEM-3, and TEM-59 β-lactamases: | column header band as printed: Substrate TEM-2 TEM-3 TEM-89 TEM-59 k cat (s −1 ) K m (μM) k cat / K m (μM −1 s −1 ) k cat (s −1 ) K m (μM −1 ) k cat / K m (μM −1 s −1 ) k cat (s −1 ) K m (μM −1 ) k cat / K m (μM −1 s −1 ) k cat (s −1 ) K m (μM −1 ) k cat / K m (μM −1 s −1 ) | labelled cell line for this row in the appended verbatim transcription: Table 2 row Cephaloridine, TEM-89 columns: kcat = 5 s^-1; Km = 160 uM; kcat/Km = 0.03 uM^-1 s^-1. | TEM-89 cells read: k cat = 5 s^-1; K m = 160 uM; k cat / K m = 0.03 uM^-1 s^-1.

row_label: TEM-89 | Cephaloridine

data_origin: experimental

enzyme: beta-lactamase

substrate: Cephaloridine

status: verified

source: oed


organism: Mycolicibacterium smegmatis

substrate_name: ceftriaxone

sequence_source: UniProtKB:A0R0P0 direct REST lookup on 2026-05-27

assay_conditions_summary: pH 8; 303.15 K; buffer and no pH for these kinetics

column_label: Table 4  Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics; row `Ceftriazone`; column `Vmax (uM s^-1)` = 0.912; column `Km (uM)` = 11.757; column `Kcat (s^-1)` = 1.825; column `Kcat/Km (uM^-1 s^-1)` = 0.155.

normalized_value_unit_evidence: Km: printed Table 4 cell 11.757 uM; 11.757 uM / 1000 = 0.011757 mM. The catalog stores this Km as 0.01176 mM, which is that same printed cell carried to the catalog's own stored decimal precision (11.76 uM vs printed 11.757 uM, a 0.026% difference confined to the digit beyond the stored precision), so the paper_* fields on this record carry the catalog values. kcat: printed Table 4 cell 1.825 s^-1 = 1.825 s^(-1), which equals the catalog kcat exactly with no conversion. kcat/Km: the printed cell 0.155 uM^-1 s^-1 = 155.0 s^-1 mM^-1, whereas the exact quotient of the row's own printed cells is 155.22667347112358 s^-1 mM^-1 and the catalog kcat_over_km 155.187074829932 s^(-1)*mM^(-1) is the exact quotient of the catalog-precision pair 1.825 / 0.01176.

raw_value_unit_evidence: Table 4 (printed page 225), row `Ceftriazone`: Vmax = 0.912 uM s^-1; Km = 11.757 uM; Kcat = 1.825 s^-1; Kcat/Km = 0.155 uM^-1 s^-1.

row_label: Table 4, antibiotics row `Ceftriazone`

substrate: ceftriaxone


substrate_name: cephalothin

kcat_over_km_origin: calculated

column_label: Table 4  Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics; row `Cephalothin`; column `Vmax (uM s^-1)` = 0.515; column `Km (uM)` = 655.015; column `Kcat (s^-1)` = 1.031; column `Kcat/Km (uM^-1 s^-1)` = 0.001.

normalized_value_unit_evidence: Km: printed Table 4 cell 655.015 uM; 655.015 uM / 1000 = 0.655015 mM. The catalog stores this Km as 0.655 mM, which is that same printed cell carried to the catalog's own stored decimal precision (655 uM vs printed 655.015 uM, a 0.002% difference confined to the digit beyond the stored precision), so the paper_* fields on this record carry the catalog values. kcat: printed Table 4 cell 1.031 s^-1 = 1.031 s^(-1), which equals the catalog kcat exactly with no conversion. kcat/Km: the printed cell 0.001 uM^-1 s^-1 = 1.0 s^-1 mM^-1, whereas the exact quotient of the row's own printed cells is 1.5740097555017822 s^-1 mM^-1 and the catalog kcat_over_km 1.5740458015267174 s^(-1)*mM^(-1) is the exact quotient of the catalog-precision pair 1.031 / 0.655.

raw_value_unit_evidence: Table 4 (printed page 225), row `Cephalothin`: Vmax = 0.515 uM s^-1; Km = 655.015 uM; Kcat = 1.031 s^-1; Kcat/Km = 0.001 uM^-1 s^-1.

row_label: Table 4, antibiotics row `Cephalothin`

substrate: cephalothin


organism: Ochrobactrum anthropi

substrate_name: Nitrocefin

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

mutation_type: substitution

substrate: Nitrocefin


organism: Mycobacterium tuberculosis

verification_status: unverified

sequence_source: UniProtKB A5U493 direct REST lookup on 2026-05-27; reviewed Swiss-Prot BLAC_MYCTA, sequence version 1.

status: unverified


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: carbenicillin

sequence_source: UniProtKB A0R0P0 direct REST lookup on 2026-05-27; TrEMBL A0R0P0_MYCS2, sequence version 1.

column_label: Table 4  Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics (printed page 225; the on-disk pdftotext line prints the Greek beta); row Carbenicillin; the Kcat (s^-1) column cell reads 10.220 and the Km (uM) column cell reads 21.740. Both cells are read from the same single table row and the same wild-type enzyme table (Table 4), under one assay condition; no cross-row, cross-column or cofactor tuple is assembled. The ratio is the quotient of those same two cells, 10.220 s^-1 divided by 0.02174 mM, this row's own two printed Table 4 cells after the uM to mM normalization.

normalized_value_unit_evidence: metric: kcat; raw value: 10.220; raw unit: s^-1; normalized value: 10.22; normalized unit: s^-1; metric: Km; raw value: 21.740; raw unit: uM; normalized value: 0.02174; normalized unit: mM; metric: kcat/Km; normalized value: 470.10119595216196; normalized unit: s^-1 mM^-1; derived from: 10.220 s^-1 divided by 0.02174 mM, this row's own two printed Table 4 cells after the uM to mM normalization; assay condition: Purified soluble wild-type sMSMEG_4455 beta-lactamase; the paper's Methods state "The hydrolysis of b-lactams (20-500 uM) was assessed with 0.5 uM of enzyme at 37 C. Initial reaction rates, Michaelis-Menten constants (Km and Vmax), turn-over number (Kcat) and catalytic efficiency (Kcat/Km) of the enzyme were evaluated. Experiments were done in three replicates for accuracy." Table 4 reports the wild-type enzyme; the mutant proteins s4455YF and s4455EA are reported separately in Table 5 and are not used here.

raw_value_unit_evidence: Table 4  Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics (printed page 225; the on-disk pdftotext line prints the Greek beta); row label: Carbenicillin; column labels: Antibiotics | Vmax (uMs^-1) | Km (uM) | Kcat (s^-1) | Kcat/Km (uM^-1 s^-1). Transcribed line, verbatim: "Carbenicillin    5.110           21.740   10.220        0.470"; metric: kcat; raw value: 10.220; raw unit: s^-1; metric: Km; raw value: 21.740; raw unit: uM;

row_label: Carbenicillin

substrate: carbenicillin


substrate_name: Oxacillin

column_label: Table label: Table 4 Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics. Row: Oxacillin. Columns read: Kcat (s^-1) cell 11.900, Km (uM) cell 193.120, Kcat/Km (uM^-1 s^-1) cell 0.061. metric: kcat; raw value: 11.900; raw unit: s^-1; normalized value: 11.9 s^(-1); metric: Km; raw value: 193.120; raw unit: uM; normalized value: 0.19312 mM, stored by the export as 0.1931 mM at its stored decimal precision; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 61.626100466079755 s^-1 mM^-1, the quotient of this row's Kcat and stored-precision Km; assay condition: Wild-type soluble sMSMEG_4455 beta-lactamase; beta-lactam antibiotics (20-500 uM) assessed with 0.5 uM enzyme at 37 C; initial rates were used to determine the Michaelis-Menten constants, Kcat and Kcat/Km; experiments performed in three replicates.

normalized_value_unit_evidence: Row Oxacillin of Table 4, wild-type sMSMEG_4455: Kcat 11.900 s^-1 = 11.9 s^(-1); Km 193.120 uM = 0.19312 mM (1 uM = 0.001 mM), which is 0.1931 mM at the export's stored 4-decimal precision; the difference is the export's own stored rounding of the same printed cell; Kcat/Km: the export value 61.626100466079755 s^-1 mM^-1 equals the quotient 11.9 s^-1 / 0.1931 mM of this row's Kcat and its Km at the export's stored precision. The paper's printed ratio cell 0.061 uM^-1 s^-1 is truncated at three decimals; the export ratio equals 0.0616261 uM^-1 s^-1, which lies inside the printed cell's truncated three-decimal window that begins at 0.061, exactly as this row's own printed-cell quotient 11.900 / 193.120 = 0.06161 uM^-1 s^-1 does, so the printed cell and the export ratio agree at the printed cell's own precision. In the PDF text extraction the micro sign renders as u/µ and the superscript minus one is flattened, so the header cell (uM-1 s-1) is the paper's uM^-1 s^-1.

raw_value_unit_evidence: Table 4 Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics | metric header rows of Table 4: Antibiotics Vmax (uMs-1) Km (uM) Kcat (s-1) Kcat/Km, continued (uM-1 s-1) | row: Oxacillin 5.954 193.120 11.900 0.061 | cells read: Vmax = 5.954 uM s^-1; Km = 193.120 uM; Kcat = 11.900 s^-1; Kcat/Km = 0.061 uM^-1 s^-1

row_label: sMSMEG_4455 | Oxacillin

substrate: Oxacillin


substrate_name: penicillin G

column_label: Table 4  Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics; row `PenicillinG`; column `Vmax (uM s^-1)` = 13.800; column `Km (uM)` = 3.345; column `Kcat (s^-1)` = 27.600; column `Kcat/Km (uM^-1 s^-1)` = 8.250.

normalized_value_unit_evidence: Km: printed Table 4 cell 3.345 uM; 3.345 uM / 1000 = 0.003345 mM. The catalog stores this Km as 0.00335 mM, which is that same printed cell carried to the catalog's own stored decimal precision (3.35 uM vs printed 3.345 uM, a 0.149% difference confined to the digit beyond the stored precision), so the paper_* fields on this record carry the catalog values. kcat: printed Table 4 cell 27.600 s^-1 = 27.6 s^(-1), which equals the catalog kcat exactly with no conversion. kcat/Km: the printed cell 8.250 uM^-1 s^-1 = 8250.0 s^-1 mM^-1, whereas the exact quotient of the row's own printed cells is 8251.121076233183 s^-1 mM^-1 and the catalog kcat_over_km 8238.805970149253 s^(-1)*mM^(-1) is the exact quotient of the catalog-precision pair 27.6 / 0.00335.

raw_value_unit_evidence: Table 4 (printed page 225), row `PenicillinG`: Vmax = 13.800 uM s^-1; Km = 3.345 uM; Kcat = 27.600 s^-1; Kcat/Km = 8.250 uM^-1 s^-1.

row_label: Table 4, antibiotics row `PenicillinG`

substrate: penicillin G


substrate_name: nitrocefin

column_label: Table label: Table 4 Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics. Row: Nitrocefin. Columns read: Kcat (s^-1) cell 0.014, Km (uM) cell 9.477, Kcat/Km (uM^-1 s^-1) cell 0.001. metric: kcat; raw value: 0.014; raw unit: s^-1; normalized value: 0.014 s^(-1); metric: Km; raw value: 9.477; raw unit: uM; normalized value: 0.009477 mM, stored by the export as 0.00948 mM at its stored decimal precision; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 1.4767932489451476 s^-1 mM^-1, the quotient of this row's Kcat and stored-precision Km; assay condition: Wild-type soluble sMSMEG_4455 beta-lactamase; beta-lactam antibiotics (20-500 uM) assessed with 0.5 uM enzyme at 37 C; initial rates were used to determine the Michaelis-Menten constants, Kcat and Kcat/Km; experiments performed in three replicates.

normalized_value_unit_evidence: Row Nitrocefin of Table 4, wild-type sMSMEG_4455: Kcat 0.014 s^-1 = 0.014 s^(-1); Km 9.477 uM = 0.009477 mM (1 uM = 0.001 mM), which is 0.00948 mM at the export's stored 5-decimal precision; the difference is the export's own stored rounding of the same printed cell; Kcat/Km: the export value 1.4767932489451476 s^-1 mM^-1 equals the quotient 0.014 s^-1 / 0.00948 mM of this row's Kcat and its Km at the export's stored precision. The paper's printed ratio cell 0.001 uM^-1 s^-1 agrees with the export ratio at the printed cell's own three-decimal precision: the export ratio equals 0.0014768 uM^-1 s^-1, which prints as 0.001 under the column's truncation and also under rounding. In the PDF text extraction the micro sign renders as u/µ and the superscript minus one is flattened, so the header cell (uM-1 s-1) is the paper's uM^-1 s^-1.

raw_value_unit_evidence: Table 4 Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics | metric header rows of Table 4: Antibiotics Vmax (uMs-1) Km (uM) Kcat (s-1) Kcat/Km, continued (uM-1 s-1) | row: Nitrocefin 0.007 9.477 0.014 0.001 | cells read: Vmax = 0.007 uM s^-1; Km = 9.477 uM; Kcat = 0.014 s^-1; Kcat/Km = 0.001 uM^-1 s^-1

row_label: sMSMEG_4455 | Nitrocefin

substrate: nitrocefin


substrate_name: cephalexin

column_label: Table label: Table 4 Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics. Row: Cephalexin. Columns read: Kcat (s^-1) cell 0.079, Km (uM) cell 8.969, Kcat/Km (uM^-1 s^-1) cell 0.008. metric: kcat; raw value: 0.079; raw unit: s^-1; normalized value: 0.079 s^(-1); metric: Km; raw value: 8.969; raw unit: uM; normalized value: 0.008969 mM, stored by the export as 0.00897 mM at its stored decimal precision; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 8.807134894091416 s^-1 mM^-1, the quotient of this row's Kcat and stored-precision Km; assay condition: Wild-type soluble sMSMEG_4455 beta-lactamase; beta-lactam antibiotics (20-500 uM) assessed with 0.5 uM enzyme at 37 C; initial rates were used to determine the Michaelis-Menten constants, Kcat and Kcat/Km; experiments performed in three replicates.

normalized_value_unit_evidence: Row Cephalexin of Table 4, wild-type sMSMEG_4455: Kcat 0.079 s^-1 = 0.079 s^(-1); Km 8.969 uM = 0.008969 mM (1 uM = 0.001 mM), which is 0.00897 mM at the export's stored 5-decimal precision; the difference is the export's own stored rounding of the same printed cell; Kcat/Km: the export value 8.807134894091416 s^-1 mM^-1 equals the quotient 0.079 s^-1 / 0.00897 mM of this row's Kcat and its Km at the export's stored precision. The paper's printed ratio cell 0.008 uM^-1 s^-1 is truncated at three decimals; the export ratio equals 0.0088071 uM^-1 s^-1, which lies inside the printed cell's truncated three-decimal window that begins at 0.008, exactly as this row's own printed-cell quotient 0.079 / 8.969 = 0.00880 uM^-1 s^-1 does, so the printed cell and the export ratio agree at the printed cell's own precision. In the PDF text extraction the micro sign renders as u/µ and the superscript minus one is flattened, so the header cell (uM-1 s-1) is the paper's uM^-1 s^-1.

raw_value_unit_evidence: Table 4 Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics | metric header rows of Table 4: Antibiotics Vmax (uMs-1) Km (uM) Kcat (s-1) Kcat/Km, continued (uM-1 s-1) | row: Cephalexin 0.039 8.969 0.079 0.008 | cells read: Vmax = 0.039 uM s^-1; Km = 8.969 uM; Kcat = 0.079 s^-1; Kcat/Km = 0.008 uM^-1 s^-1

row_label: sMSMEG_4455 | Cephalexin

substrate: cephalexin


organism: Pseudomonas aeruginosa

substrate_name: cefoxitin

substrate: cefoxitin


verification_status: corrected

sequence_source: UniProtKB Q79MP6 direct accession lookup

status: corrected


substrate_name: Imipenem

substrate: Imipenem


substrate_name: cephaloridin

substrate: cephaloridin


substrate_name: cefepime

sequence_source: UniProtKB:Q3SAW3 direct accession lookup (REST API, 2026-05-27)

substrate: cefepime


substrate_name: Meropenem

sequence_source: UniProtKB:Q9XAY4 direct accession lookup (REST API, 2026-05-27)

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM HEPES

column_label: Table 4, substrate row Meropenem, enzyme column VIM-1: kcat cell 20 +/- 0.2 s^-1, Km cell 72 +/- 7.7 uM, kcat/Km cell 2.8E5 M^-1 s^-1. The exported kcat 20 s^-1 and Km 0.072 mM select the VIM-1 column of the Meropenem row uniquely: the other enzyme column of that row prints different cells.

raw_value_unit_evidence: Table 4 row Meropenem | VIM-1: kcat 20 +/- 0.2 s^-1; Km 72 +/- 7.7 uM; kcat/Km 2.8E5 M^-1 s^-1.

row_label: Meropenem | VIM-1

table_label: Table 4. Kinetic parameters for VIM-13 enzyme with various beta-lactams in comparison with those for VIM-1

substrate: Meropenem


sequence_source: UniProtKB:Q2HY42 direct accession lookup (REST API, 2026-05-27)

column_label: Table 4, substrate row Meropenem, enzyme column VIM-13: kcat cell 9 +/- 1.5 s^-1, Km cell 15.5 +/- 2.3 uM, kcat/Km cell 5.92E5 M^-1 s^-1. The exported kcat 9 s^-1 and Km 0.015 mM select the VIM-13 column of the Meropenem row uniquely: the other enzyme column of that row prints different cells.

row_label: Meropenem | VIM-13


column_label: Table 4, substrate row Cefepime, enzyme column VIM-1: kcat cell 119 +/- 17 s^-1, Km cell 337 +/- 110 uM, kcat/Km cell 3.5E5 M^-1 s^-1. The exported kcat 119 s^-1 and Km 0.337 mM select the VIM-1 column of the Cefepime row uniquely: the other enzyme column of that row prints different cells.

row_label: Cefepime | VIM-1


substrate_name: Cefuroxime

column_label: Table 4; row Cefuroxime; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 239 +/- 22, Km 148 +/- 36, kcat/Km 1.6E6

normalized_value_unit_evidence: kcat=239 s^-1; Km=0.148 mM; kcat/Km=1600 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Cefuroxime

substrate: Cefuroxime


column_label: Table 4; row Imipenem; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 3.4 +/- 1.2, Km 4 +/- 1.9, kcat/Km 8.38E5

normalized_value_unit_evidence: kcat=3.4 s^-1; Km=0.004 mM; kcat/Km=838 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Imipenem


sequence_source: UniProtKB Q2HY42 direct REST lookup on 2026-05-27

column_label: Table 4, substrate row Cefuroxime, enzyme column VIM-13: kcat cell 283 +/- 99 s^-1, Km cell 56 +/- 5 uM, kcat/Km cell 5E6 M^-1 s^-1. The exported kcat 283.0 s^-1 and Km 0.056 mM select the VIM-13 column of the Cefuroxime row uniquely: the other enzyme column of that row prints different cells.

raw_value_unit_evidence: Table 4 row Cefuroxime | VIM-13: kcat 283 +/- 99 s^-1; Km 56 +/- 5 uM; kcat/Km 5E6 M^-1 s^-1.

row_label: Cefuroxime | VIM-13


substrate_name: piperacillin

column_label: Table 4, substrate row Piperacillin, enzyme column VIM-13: kcat cell 362 +/- 15 s^-1, Km cell 729 +/- 96 uM, kcat/Km cell 4.9E5 M^-1 s^-1. The exported kcat 362.0 s^-1 and Km 0.729 mM select the VIM-13 column of the Piperacillin row uniquely: the other enzyme column of that row prints different cells.

raw_value_unit_evidence: Table 4 row Piperacillin | VIM-13: kcat 362 +/- 15 s^-1; Km 729 +/- 96 uM; kcat/Km 4.9E5 M^-1 s^-1.

row_label: Piperacillin | VIM-13

substrate: piperacillin


substrate_name: Ampicillin

column_label: Table 4, substrate row Ampicillin, enzyme column VIM-13: kcat cell 67 +/- 9.5 s^-1, Km cell 197 +/- 48 uM, kcat/Km cell 3.4 E5 M^-1 s^-1. The exported kcat 67.0 s^-1 and Km 0.197 mM select the VIM-13 column of the Ampicillin row uniquely: the other enzyme column of that row prints different cells.

raw_value_unit_evidence: Table 4 row Ampicillin | VIM-13: kcat 67 +/- 9.5 s^-1; Km 197 +/- 48 uM; kcat/Km 3.4 E5 M^-1 s^-1.

row_label: Ampicillin | VIM-13

substrate: Ampicillin


substrate_name: cefotaxime

column_label: Table 4, substrate row Cefotaxime, enzyme column VIM-13: kcat cell 612 +/- 120 s^-1, Km cell 233 +/- 46 uM, kcat/Km cell 2.6E6 M^-1 s^-1. The exported kcat 612.0 s^-1 and Km 0.233 mM select the VIM-13 column of the Cefotaxime row uniquely: the other enzyme column of that row prints different cells.

row_label: Cefotaxime | VIM-13

substrate: cefotaxime


sequence_source: UniProtKB Q9XAY4 direct REST lookup on 2026-05-27

column_label: Table 4, substrate row Cefotaxime, enzyme column VIM-1: kcat cell 204 +/- 26 s^-1, Km cell 285 +/- 25 uM, kcat/Km cell 7.18E5 M^-1 s^-1. The exported kcat 204.0 s^-1 and Km 0.285 mM select the VIM-1 column of the Cefotaxime row uniquely: the other enzyme column of that row prints different cells.

raw_value_unit_evidence: Table 4 row Cefotaxime | VIM-1: kcat 204 +/- 26 s^-1; Km 285 +/- 25 uM; kcat/Km 7.18E5 M^-1 s^-1.

row_label: Cefotaxime | VIM-1


sequence_source: UniProtKB:Q9XAY4 direct lookup on 2026-05-27

column_label: Table 4, substrate row Penicillin G, enzyme column VIM-1: kcat cell 418 +/- 116 s^-1, Km cell 1,303 +/- 393 uM, kcat/Km cell 3.2E5 M^-1 s^-1. The exported kcat 418.0 s^-1 and Km 1.303 mM select the VIM-1 column of the Penicillin G row uniquely: the other enzyme column of that row prints different cells.

row_label: Penicillin G | VIM-1


sequence_source: UniProtKB:Q7WYA8 direct lookup on 2026-05-27


substrate_name: cephalotin

substrate: cephalotin


substrate_name: meropenem

assay_conditions_summary: pH 7.5; 310.15 K; buffer HB (50 mM HEPES

column_label: TABLE 1. Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymesa; substrate row Meropenemd; IMP-13 column block; column "kcat (s−1)" = 1.4 ± 0.1; column "Km (μM)" = 10 ± 2; column "kcat/Km (μM−1·s−1)" = 0.14.

normalized_value_unit_evidence: kcat: printed cell 1.4 ± 0.1 s−1; unit is already s^-1, so 1.4 s^-1. Km: printed cell 10 ± 2 μM; 10.0 μM / 1000 = 0.01 mM. kcat/Km: printed cell 0.14 μM−1·s−1; μM−1·s−1 × 1000 = mM−1·s−1, so 140.0 s^-1 mM^-1. The exact quotient of the paper's own two printed cells is 1.4 s^-1 / 0.01 mM = 140.0 s^-1 mM^-1 = 0.14 μM−1·s−1, which the paper prints as 0.14.

raw_value_unit_evidence: TABLE 1, IMP-13 columns, substrate row Meropenemd: kcat = 1.4 ± 0.1 s−1; Km = 10 ± 2 μM; printed kcat/Km = 0.14 μM−1·s−1.

row_label: TABLE 1, substrate row Meropenemd, IMP-13 columns

substrate: meropenem


substrate_name: ertapenem

substrate: ertapenem


substrate_name: ticarcillin

column_label: Table 1 (Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymes), substrate row 'Ticarcillin', IMP-13 column group; column 'kcat (s^-1)' = 220; column 'Km (uM)' = 130; column 'kcat/Km (uM^-1 s^-1)' = 1.8. The three IMP-1 columns and the three IMP-2 columns further along the same printed line belong to the two comparison enzymes and were not read.

normalized_value_unit_evidence: kcat: printed Table 1 cell 220 s^-1; the cell is already per second, so no unit conversion applies and the canonical value is 220.0 s^(-1). Km: printed Table 1 cell 130 uM; 130 / 1000 = 0.13 mM. kcat/Km: printed Table 1 cell 1.8 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.8 x 1000 = 1800.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, IMP-13 column group, substrate row 'Ticarcillin': kcat = 220 s^-1; Km = 130 uM; printed kcat/Km = 1.8 uM^-1 s^-1.

table_label: Table 1: Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymes (Antimicrob. Agents Chemother. 2011, 55(1):399-401)

substrate: ticarcillin


column_label: Table label: TABLE 1. Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymesa. Row: Cefotaxime. Enzyme column group: IMP-13. Columns read: kcat (s^-1) cell 33 ± 2, Km (uM) cell 21 ± 2, kcat/Km (uM^-1 s^-1) cell 1.6. metric: kcat; raw value: 33; raw unit: s^-1; normalized value: 33.0 s^(-1); metric: Km; raw value: 21; raw unit: uM; normalized value: 0.021 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 1571.4285714285713 s^-1 mM^-1; assay condition: Purified IMP-13 metallo-beta-lactamase; the kinetic parameters of IMP-13 were determined at 37 degrees C in HB (50 mM HEPES with 50 uM ZnSO4, pH 7.5). Export row conditions: pH 7.5; 310.15 K.

normalized_value_unit_evidence: IMP-13 columns of Table 1 row Cefotaxime: kcat 33 s^-1 = 33.0 s^(-1); Km 21 uM = 0.021 mM (1 uM = 0.001 mM); kcat/Km 1571.4285714285713 s^-1 mM^-1. In the appended verbatim transcription the superscript minus one renders as − 1 flattened to −1, the micro sign renders as μ, the plus-minus sign as ±, an empty or unavailable IMP-1/IMP-2 cell as −, and table footnote letters are flattened onto the end of the cell they mark, so the printed cell `1.6` is the paper's 1.6 μM−1·s−1.

raw_value_unit_evidence: TABLE 1. Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymesa | header rows: Substrate | IMP-13 | IMP-1b | IMP-2c ; metric header row: kcat (s−1) | Km (μM) | kcat/Km (μM−1·s−1) | kcat (s−1) | Km (μM) | kcat/Km (μM−1·s−1) | kcat (s−1) | Km (μM) | kcat/Km (μM−1·s−1) | row: Cefotaxime | 33 ± 2 | 21 ± 2 | 1.6 | 1.3 | 4 | 0.35 | − | − | − | IMP-13 cells read: kcat = 33 ± 2 s^-1; Km = 21 ± 2 uM; kcat/Km = 1.6 uM^-1 s^-1

row_label: IMP-13 | Cefotaxime


column_label: Table 1 'Table 1: Kinetic parameters of IMP-13, IMP-1, and IMP-2'; row Cefepime; IMP-13 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row Cefepime, IMP-13 normalized: kcat 12 s^-1; Km 0.008 mM; kcat/Km 1500 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Cefepime, IMP-13 columns: kcat 12 ± 1 s^-1; Km 8 ± 1 uM; kcat/Km 1.5 uM^-1 s^-1.

row_label: Cefepime


substrate_name: cefuroxime

substrate: cefuroxime


substrate_name: ceftazidime

column_label: Table label: TABLE 1. Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymesa. Row: Ceftazidime. Enzyme column group: IMP-13. Columns read: kcat (s^-1) cell 9 ± 1, Km (uM) cell 15 ± 3, kcat/Km (uM^-1 s^-1) cell 0.60. metric: kcat; raw value: 9; raw unit: s^-1; normalized value: 9.0 s^(-1); metric: Km; raw value: 15; raw unit: uM; normalized value: 0.015 mM; metric: kcat/Km; raw value: 0.60; raw unit: uM^-1 s^-1; normalized value: 600.0 s^-1 mM^-1; assay condition: Purified IMP-13 metallo-beta-lactamase; the kinetic parameters of IMP-13 were determined at 37 degrees C in HB (50 mM HEPES with 50 uM ZnSO4, pH 7.5). Export row conditions: pH 7.5; 310.15 K.

normalized_value_unit_evidence: IMP-13 columns of Table 1 row Ceftazidime: kcat 9 s^-1 = 9.0 s^(-1); Km 15 uM = 0.015 mM (1 uM = 0.001 mM); kcat/Km 0.60 uM^-1 s^-1 = 600.0 s^-1 mM^-1 (1 uM^-1 s^-1 = 1000 mM^-1 s^-1). In the appended verbatim transcription the superscript minus one renders as −1, the micro sign as μ and the plus-minus sign as ±, so the printed cell `0.60` is the paper's 0.60 μM−1·s−1.

raw_value_unit_evidence: TABLE 1. Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymesa | header rows: Substrate | IMP-13 | IMP-1b | IMP-2c ; metric header row: kcat (s−1) | Km (μM) | kcat/Km (μM−1·s−1) | kcat (s−1) | Km (μM) | kcat/Km (μM−1·s−1) | kcat (s−1) | Km (μM) | kcat/Km (μM−1·s−1) | row: Ceftazidime | 9 ± 1 | 15 ± 3 | 0.60 | 8 | 44 | 0.18 | 21 | 111 | 0.19 | IMP-13 cells read: kcat = 9 ± 1 s^-1; Km = 15 ± 3 uM; kcat/Km = 0.60 uM^-1 s^-1

row_label: IMP-13 | Ceftazidime

substrate: ceftazidime


substrate_name: ampicillin

column_label: Table 1 (Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymes), substrate row 'Ampicillin', IMP-13 column group; column 'kcat (s^-1)' = 82; column 'Km (uM)' = 210; column 'kcat/Km (uM^-1 s^-1)' = 0.38. The three IMP-1 columns and the three IMP-2 columns further along the same printed line belong to the two comparison enzymes and were not read.

normalized_value_unit_evidence: kcat: printed Table 1 cell 82 s^-1; the cell is already per second, so no unit conversion applies and the canonical value is 82.0 s^(-1). Km: printed Table 1 cell 210 uM; 210 / 1000 = 0.21 mM. kcat/Km: printed Table 1 cell 0.38 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.38 x 1000 = 380.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, IMP-13 column group, substrate row 'Ampicillin': kcat = 82 s^-1; Km = 210 uM; printed kcat/Km = 0.38 uM^-1 s^-1.

substrate: ampicillin


column_label: Table 1 (Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymes), substrate row 'Imipenem', IMP-13 column group; column 'kcat (s^-1)' = 120; column 'Km (uM)' = 49; column 'kcat/Km (uM^-1 s^-1)' = 2.5. The three IMP-1 columns and the three IMP-2 columns further along the same printed line belong to the two comparison enzymes and were not read.

normalized_value_unit_evidence: kcat: printed Table 1 cell 120 s^-1; the cell is already per second, so no unit conversion applies and the canonical value is 120.0 s^(-1). Km: printed Table 1 cell 49 uM; 49 / 1000 = 0.049 mM. kcat/Km: printed Table 1 cell 2.5 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 2.5 x 1000 = 2500.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, IMP-13 column group, substrate row 'Imipenem': kcat = 120 s^-1; Km = 49 uM; printed kcat/Km = 2.5 uM^-1 s^-1.


substrate_name: nitrocefin

assay_conditions_summary: pH 7.5; 303.15 K; buffer 10 mM HEPES

column_label: table label: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d; row label: Nitrocefin; column label: the IMP-18 kcat (s^-1) and IMP-18 Km (uM) cells of this one TABLE 2 row only; no cell is taken from the IMP-1 column group, from another TABLE 2 row, or from any other table; raw value: kcat 55 s^-1, Km 9 uM; raw unit: s^-1 for kcat, uM for Km; normalized value: kcat 55.0 s^-1, Km 0.009 mM, kcat/Km 6111.111111111111 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: All measurements were performed on a Cary 100 UV-Vis spectrophotometer (Varian, Walnut Creek, CA) at 30 C in 10 mM HEPES buffer (pH 7.5) containing 50 uM ZnSO4, using a reaction volume of 500 ul. The purified IMP-18 was diluted in the same buffer supplemented with 20 ug/ml bovine serum albumin (BSA) to prevent enzyme denaturation. The steady-state kinetic parameters (kcat and Km) were calculated after direct fit of the initial rates to the Henri-Michaelis-Menten equation or using the Hanes-Woolf linearization. Exported assay conditions: pH 7.5; 303.15 K, which is the 30 C of this Methods paragraph. Table 2 Km cells below 10 uM were measured as inhibition constants: the Methods paragraph states that Km values lower than 10 uM were measured as inhibition constants by using a competitive inhibition model and 100 uM nitrocefin as the reporter substrate.

normalized_value_unit_evidence: kcat 55 s^-1 is already s^-1, giving 55.0 s^-1 at the export's stored precision; exported kcat 55.0 s^(-1). Km 9 uM divided by 1000 gives 0.009 mM at the export's stored precision; exported Km 0.009 mM. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 55.0 s^-1 divided by 0.009 mM giving 6111.111111111111 s^-1 mM^-1, and of nothing else; exported kcat/Km 6111.111111111111 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d, row Nitrocefin, IMP-18 column group: kcat 55 s^-1; Km 9 uM; printed kcat/Km 6.1 x 10^6 M^-1 s^-1.

row_label: Nitrocefin

substrate: nitrocefin


enzyme_display_name: pyruvate kinase

organism: Arabidopsis thaliana

substrate_name: ADP

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

enzyme: pyruvate kinase

substrate: ADP


substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 7; 308.15 K; cofactor ADP


organism: Entamoeba histolytica

sequence_source: UniProtKB C4LXC4 REST lookup on 2026-05-27


organism: Escherichia coli

sequence_source: UniProtKB P0AD61 canonical sequence reconstructed with K413Q on 2026-05-27

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


sequence_source: UniProtKB P0AD61 canonical sequence reconstructed with K382Q on 2026-05-27


sequence_source: UniProtKB P0AD61 canonical sequence reconstructed with R271L on 2026-05-27

sequence_variant_note: Mutation signature R271L matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


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


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: Cephaloridine

substrate: Cephaloridine


organism: Homo sapiens

substrate_name: Phosphoenolpyruvate

sequence_source: UniProt P30613 canonical sequence; R510Q reconstructed after residue check

substrate: Phosphoenolpyruvate


substrate_name: Fructose 1,6-bisphosphate

substrate: Fructose 1,6-bisphosphate


sequence_source: UniProt P30613 canonical sequence

assay_conditions_summary: pH 8; 310.15 K; cofactor ADP


sequence_source: UniProtKB:P30613 canonical sequence with R510Q reconstructed during review


sequence_source: UniProtKB Q5U807 REST/FASTA direct lookup; accessed 2026-05-27


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: Imipenem

substrate: Imipenem


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P00549 canonical FASTA fetched 2026-05-27


assay_conditions_summary: pH 6.5; 303.15 K; cofactor ADP


substrate_name: ADP; Phosphoenolpyruvate

kcat_display: Not reported

km_display: Not reported

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

sequence_source: UniProtKB reviewed P00549; variant reconstructed after direct residue check

assay_conditions_summary: cofactor ATP

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

substrate: ADP; Phosphoenolpyruvate


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


substrate_name: Phosphoenolpyruvate; ADP

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

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

substrate: Phosphoenolpyruvate; ADP


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


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


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


organism: Trypanosoma brucei


organism: Trypanosoma brucei brucei

sequence_source: UniProtKB direct accession lookup P30615; reviewed Swiss-Prot; EC 2.7.1.40; organism Trypanosoma brucei brucei


organism: Trypanosoma congolense

sequence_source: UniProtKB direct accession lookup G0UYF4; unreviewed TrEMBL; EC 2.7.1.40; organism Trypanosoma congolense strain IL3000


organism: Rattus norvegicus

sequence_source: UniProtKB:P11980 reviewed entry, direct REST lookup


substrate_name: Penicillin G

sequence_source: UniProtKB Q9F0F5 REST/FASTA direct lookup on 2026-05-27; sequence version 1; MD5 023b32b5f4802de3e1dd853936efd561.

substrate: Penicillin G


substrate_name: Nitrocefin

column_label: PMC Table 2 'Kinetic parameters for TEM-87 beta-lactamase', row Nitrocefin, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km normalized=0.016 mM; kcat normalized=31 s^-1; kcat/Km normalized=1937.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Nitrocefin: Km=16 uM; kcat=31 s^-1; kcat/Km=1.9 x 10^6 M^-1 s^-1.

table_label: Table 2. Kinetic parameters for TEM-87 beta-lactamase

substrate: Nitrocefin


substrate_name: piperacillin

column_label: PMC Table 2 'Kinetic parameters for TEM-87 beta-lactamase', row piperacillin, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km normalized=0.014 mM; kcat normalized=70 s^-1; kcat/Km normalized=5000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row piperacillin: Km=14 uM; kcat=70 s^-1; kcat/Km=5.0 x 10^6 M^-1 s^-1.

row_label: piperacillin

substrate: piperacillin


organism: Providencia stuartii

sequence_source: UniProtKB O68473 REST/FASTA direct lookup on 2026-05-27 plus K104E mutation applied with residue-numbering offset -2.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB O68473 REST/FASTA direct lookup on 2026-05-27 plus S164R mutation applied with residue-numbering offset -2. and applied mutation signature S164R with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


substrate_name: Ampicillin

sequence_source: UniProtKB O68473 REST/FASTA direct lookup on 2026-05-27 plus S164R mutation applied with residue-numbering offset -2.

substrate: Ampicillin


substrate_name: Ceftazidime

sequence_source: UniProtKB Q9XAY4 direct REST lookup on 2026-05-27

column_label: Table 4, substrate row Ceftazidime, enzyme column VIM-1: kcat cell 42 +/- 9.6 s^-1, Km cell 1,132 +/- 320 uM, kcat/Km cell 3.7E4 M^-1 s^-1. The exported kcat 42.0 s^-1 and Km 1.132 mM select the VIM-1 column of the Ceftazidime row uniquely: the other enzyme column of that row prints different cells.

row_label: Ceftazidime | VIM-1

substrate: Ceftazidime


substrate_name: cephalotin

sequence_source: UniProtKB Q5U807 direct REST lookup on 2026-05-27

column_label: table label: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d; row label: Cephalothin; column label: the IMP-18 kcat (s^-1) and IMP-18 Km (uM) cells of this one TABLE 2 row only; no cell is taken from the IMP-1 column group, from another TABLE 2 row, or from any other table; raw value: kcat 0.4 s^-1, Km 0.1 uM; raw unit: s^-1 for kcat, uM for Km; normalized value: kcat 0.4 s^-1, Km 0.0001 mM, kcat/Km 4000.0 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: All measurements were performed on a Cary 100 UV-Vis spectrophotometer (Varian, Walnut Creek, CA) at 30 C in 10 mM HEPES buffer (pH 7.5) containing 50 uM ZnSO4, using a reaction volume of 500 ul. The purified IMP-18 was diluted in the same buffer supplemented with 20 ug/ml bovine serum albumin (BSA) to prevent enzyme denaturation. The steady-state kinetic parameters (kcat and Km) were calculated after direct fit of the initial rates to the Henri-Michaelis-Menten equation or using the Hanes-Woolf linearization. Exported assay conditions: pH 7.5; 303.15 K, which is the 30 C of this Methods paragraph. Table 2 Km cells below 10 uM were measured as inhibition constants: the Methods paragraph states that Km values lower than 10 uM were measured as inhibition constants by using a competitive inhibition model and 100 uM nitrocefin as the reporter substrate.

normalized_value_unit_evidence: kcat 0.4 s^-1 is already s^-1, giving 0.4 s^-1 at the export's stored precision; exported kcat 0.4 s^(-1). Km 0.1 uM divided by 1000 gives 0.0001 mM at the export's stored precision; exported Km 0.0001 mM. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.4 s^-1 divided by 0.0001 mM giving 4000.0 s^-1 mM^-1, and of nothing else; exported kcat/Km 4000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d, row Cephalothin, IMP-18 column group: kcat 0.4 s^-1; Km 0.1 uM; printed kcat/Km 4.0 x 10^6 M^-1 s^-1.

row_label: Cephalothin

substrate: cephalotin


substrate_name: cefuroxime

column_label: table label: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d; row label: Cefuroxime; column label: the IMP-18 kcat (s^-1) and IMP-18 Km (uM) cells of this one TABLE 2 row only; no cell is taken from the IMP-1 column group, from another TABLE 2 row, or from any other table; raw value: kcat 0.9 s^-1, Km 7 uM; raw unit: s^-1 for kcat, uM for Km; normalized value: kcat 0.9 s^-1, Km 0.007 mM, kcat/Km 128.57142857142858 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: All measurements were performed on a Cary 100 UV-Vis spectrophotometer (Varian, Walnut Creek, CA) at 30 C in 10 mM HEPES buffer (pH 7.5) containing 50 uM ZnSO4, using a reaction volume of 500 ul. The purified IMP-18 was diluted in the same buffer supplemented with 20 ug/ml bovine serum albumin (BSA) to prevent enzyme denaturation. The steady-state kinetic parameters (kcat and Km) were calculated after direct fit of the initial rates to the Henri-Michaelis-Menten equation or using the Hanes-Woolf linearization. Exported assay conditions: pH 7.5; 303.15 K, which is the 30 C of this Methods paragraph. Table 2 Km cells below 10 uM were measured as inhibition constants: the Methods paragraph states that Km values lower than 10 uM were measured as inhibition constants by using a competitive inhibition model and 100 uM nitrocefin as the reporter substrate.

normalized_value_unit_evidence: kcat 0.9 s^-1 is already s^-1, giving 0.9 s^-1 at the export's stored precision; exported kcat 0.9 s^(-1). Km 7 uM divided by 1000 gives 0.007 mM at the export's stored precision; exported Km 0.007 mM. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.9 s^-1 divided by 0.007 mM giving 128.57142857142858 s^-1 mM^-1, and of nothing else; exported kcat/Km 128.57142857142858 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d, row Cefuroxime, IMP-18 column group: kcat 0.9 s^-1; Km 7 uM; printed kcat/Km 1.3 x 10^5 M^-1 s^-1.

row_label: Cefuroxime

substrate: cefuroxime


substrate_name: benzylpenicillin

substrate: benzylpenicillin


substrate_name: cefepime

substrate: cefepime


substrate_name: nitrocefin

sequence_source: UniProtKB Q8KRJ3 direct REST lookup on 2026-05-27

assay_conditions_summary: pH 7; 298.15 K; buffer a reaction

column_label: Table label: TABLE 3. Kinetic parameters of the purified VIM-4 metallo-β-lactamase compared with those of VIM-1 and VIM-2 a. Row: VIM-4 | Nitrocefin. Enzyme column group: VIM-4. Columns read: k cat (s^-1) cell 690, K m (uM) cell 22, k cat / K m (mM^-1 s^-1) cell 31,000. metric: kcat; raw value: 690; raw unit: s^-1; normalized value: 690.0 s^(-1); metric: Km; raw value: 22; raw unit: uM; normalized value: 0.022 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 31363.636363636364 s^-1 mM^-1; assay condition: Purified VIM-4 metallo-beta-lactamase; hydrolysis of the substrates was monitored by following the absorbance variations; enzyme dilutions were prepared in a reaction buffer composed of buffer A (15 mM HEPES buffer, pH 7.2) supplemented with 20 ug/ml of BSA and 50 uM ZnCl2; the steady-state kinetic parameters (Km and kcat) were determined with the integrated Henri-Michaelis equation or the Hanes-Woolf plots. Export row carries no pH and no temperature.

normalized_value_unit_evidence: VIM-4 columns of the kinetics table, row Nitrocefin: kcat 690 s^-1 = 690.0 s^(-1); Km 22 uM = 0.022 mM (1 uM = 0.001 mM); kcat/Km 31363.636363636364 s^-1 mM^-1. In the article HTML the superscript minus one renders as −, the micro sign as μ, the interpunct as · and superscript exponents are flattened, so the printed header cell `k cat / K m (mM −1 ·s −1 )` is the paper's mM^-1 s^-1, which is the export's s^-1 mM^-1 written the other way round and needs no numeric conversion. Numbering note: the PMC article HTML captions this kinetics table as `TABLE 3.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified VIM-4 metallo-β-lactamase compared with those of VIM-1 and VIM-2 a | metric header row of the kinetics table: Substrate k cat (s −1 ) K m (μM) k cat / K m (mM −1 ·s −1 ); enzyme column group row: VIM-4 VIM-1 VIM-2 VIM-19 VIM-4 VIM-1 VIM-2 VIM-19 VIM-4 VIM-1 VIM-2 VIM-19 | row: Table 4 row Nitrocefin, VIM-4 columns: kcat 690 s^-1; Km 22 uM; kcat/Km 31,000 mM^-1 s^-1. | VIM-4 cells read: k cat = 690 s^-1; K m = 22 uM; k cat / K m = 31,000 mM^-1 s^-1

row_label: VIM-4 | Nitrocefin

substrate: nitrocefin


substrate_name: carbenicillin

substrate: carbenicillin


substrate_name: meropenem

column_label: Table label: TABLE 3. Kinetic parameters of the purified VIM-4 metallo-β-lactamase compared with those of VIM-1 and VIM-2 a. Row: VIM-4 | Meropenem. Enzyme column group: VIM-4. Columns read: k cat (s^-1) cell 7, K m (uM) cell 8, k cat / K m (mM^-1 s^-1) cell 875. metric: kcat; raw value: 7; raw unit: s^-1; normalized value: 7.0 s^(-1); metric: Km; raw value: 8; raw unit: uM; normalized value: 0.008 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 875.0 s^-1 mM^-1; assay condition: Purified VIM-4 metallo-beta-lactamase; hydrolysis of the substrates was monitored by following the absorbance variations; enzyme dilutions were prepared in a reaction buffer composed of buffer A (15 mM HEPES buffer, pH 7.2) supplemented with 20 ug/ml of BSA and 50 uM ZnCl2; the steady-state kinetic parameters (Km and kcat) were determined with the integrated Henri-Michaelis equation or the Hanes-Woolf plots. Export row carries no pH and no temperature.

normalized_value_unit_evidence: VIM-4 columns of the kinetics table, row Meropenem: kcat 7 s^-1 = 7.0 s^(-1); Km 8 uM = 0.008 mM (1 uM = 0.001 mM); kcat/Km 875.0 s^-1 mM^-1. In the article HTML the superscript minus one renders as −, the micro sign as μ, the interpunct as · and superscript exponents are flattened, so the printed header cell `k cat / K m (mM −1 ·s −1 )` is the paper's mM^-1 s^-1, which is the export's s^-1 mM^-1 written the other way round and needs no numeric conversion. Numbering note: the PMC article HTML captions this kinetics table as `TABLE 3.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified VIM-4 metallo-β-lactamase compared with those of VIM-1 and VIM-2 a | metric header row of the kinetics table: Substrate k cat (s −1 ) K m (μM) k cat / K m (mM −1 ·s −1 ); enzyme column group row: VIM-4 VIM-1 VIM-2 VIM-19 VIM-4 VIM-1 VIM-2 VIM-19 VIM-4 VIM-1 VIM-2 VIM-19 | row: Table 4 row Meropenem, VIM-4 columns: kcat 7 s^-1; Km 8 uM; kcat/Km 875 mM^-1 s^-1. | VIM-4 cells read: k cat = 7 s^-1; K m = 8 uM; k cat / K m = 875 mM^-1 s^-1

row_label: VIM-4 | Meropenem

substrate: meropenem


substrate_name: aztreonam

sequence_source: UniProtKB:P37321 direct REST lookup; PubMed:9494118-backed UniProt mutagenesis features for variants

assay_conditions_summary: pH 7; 303.15 K; buffer 0.1 M phosphate

column_label: The literal wild-type PER-1 Aztreonam column group reports Km 44.2 μM and kcat 4.3 s^-1. The current Km lost the printed tenths digit, so the exact identity is retained as a correction-family candidate.

normalized_value_unit_evidence: Primary Km=0.0442 mM and kcat=4.3 s^-1; their quotient=97.28506787330316 s^-1 mM^-1; printed efficiency=97.3 s^-1 mM^-1. Current Km=0.044 mM and quotient=97.72727272727273 are not substituted for the paper cells.

raw_value_unit_evidence: Aztreonam PER-1 cells: Km 44.2 ± 5.4 μM; kcat 4.3 ± 0.15 s^-1; printed kcat/Km 97.3 ± 8.7 s^-1 mM^-1.

row_label: PER-1 row / Aztreonam columns

table_label: Table 2. Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes

substrate: aztreonam


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P37321 and applied mutation signature T104E with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row T104E, Ceftazidime column group: column Km = 121; column kcat = 0.16; column kcat/Km = 1.3. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.16 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.16 s^(-1). Km: printed Table 2 cell 121 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 121 / 1000 = 0.121 mM. kcat/Km: printed Table 2 cell 1.3 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 1.3 s^(-1)*mM^(-1). The catalog carries kcat 0.16 s^(-1), Km 0.121 mM and kcat_over_km 1.322314049586777 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row T104E, Ceftazidime column group: Km = 121 uM; kcat = 0.16 s-1; printed kcat/Km = 1.3 s-1 mM-1.

table_label: Table 2: Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes (Biochemical Journal 1998, 330(Pt 3):1443-1449). The table prints one line per enzyme and six substrate column groups, left to right: Penicillin G, Cephalothin, Cephaloridine, Cefotaxime, Ceftazidime and Aztreonam; each group prints three value columns headed Km, kcat and kcat/Km. The printed footnote reads that the units for Km, kcat, and kcat/Km are uM, s-1 and s-1 mM-1 respectively, that N.D. means not determinable, and that the values of S.E.M. are indicated below the kinetic values.


column_label: The literal wild-type PER-1 Penicillin G column group reports Km 31.3 μM and kcat 7.2 s^-1. The current Km lost the printed tenths digit, so the exact identity is retained as a correction-family candidate.

normalized_value_unit_evidence: Primary Km=0.0313 mM and kcat=7.2 s^-1; their quotient=230.03194888178913 s^-1 mM^-1; printed efficiency=230 s^-1 mM^-1. Current Km=0.031 mM and quotient=232.25806451612905 are not substituted for the paper cells.

raw_value_unit_evidence: Penicillin G PER-1 cells: Km 31.3 ± 4.7 μM; kcat 7.2 ± 0.35 s^-1; printed kcat/Km 230 ± 25 s^-1 mM^-1.

row_label: PER-1 row / Penicillin G columns


substrate_name: cefotaxime

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P37321 and applied mutation signature N104G with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row N104G, Cefotaxime column group: column Km = 101; column kcat = 5.6; column kcat/Km = 55.4. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.6 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 5.6 s^(-1). Km: printed Table 2 cell 101 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 101 / 1000 = 0.101 mM. kcat/Km: printed Table 2 cell 55.4 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 55.4 s^(-1)*mM^(-1). The catalog carries kcat 5.6 s^(-1), Km 0.101 mM and kcat_over_km 55.44554455445544 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row N104G, Cefotaxime column group: Km = 101 uM; kcat = 5.6 s-1; printed kcat/Km = 55.4 s-1 mM-1.

substrate: cefotaxime


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P37321 and applied mutation signature A164S with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row A164S, Penicillin G column group: column Km = 30; column kcat = 3.2; column kcat/Km = 106. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.2 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.2 s^(-1). Km: printed Table 2 cell 30 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 30 / 1000 = 0.03 mM. kcat/Km: printed Table 2 cell 106 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 106.0 s^(-1)*mM^(-1). The catalog carries kcat 3.2 s^(-1), Km 0.03 mM and kcat_over_km 106.66666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row A164S, Penicillin G column group: Km = 30 uM; kcat = 3.2 s-1; printed kcat/Km = 106 s-1 mM-1.


column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row N104G, Aztreonam column group: column Km = 14; column kcat = 1.7; column kcat/Km = 121.4. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.7 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.7 s^(-1). Km: printed Table 2 cell 14 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 14 / 1000 = 0.014 mM. kcat/Km: printed Table 2 cell 121.4 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 121.4 s^(-1)*mM^(-1). The catalog carries kcat 1.7 s^(-1), Km 0.014 mM and kcat_over_km 121.42857142857142 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row N104G, Aztreonam column group: Km = 14 uM; kcat = 1.7 s-1; printed kcat/Km = 121.4 s-1 mM-1.


enzyme_display_name: TEM-60 P51L beta-lactamase mutant

sequence_variant_note: Resolved canonical sequence from UniProtKB:O68473 REST/FASTA; PMID:15328132 Table 1 P51L CCT-to-CTC reconstruction and applied mutation signature P51L with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

enzyme: TEM-60 P51L beta-lactamase mutant


enzyme_display_name: BEL-1 beta-lactamase

substrate_name: ceftriaxone

sequence_source: UniProtKB:Q3SAW3 REST/FASTA direct accession lookup

enzyme: BEL-1 beta-lactamase

substrate: ceftriaxone


substrate_name: Cefsulodin

substrate: Cefsulodin


substrate_name: Cephaloridine

sequence_source: UniProtKB P37321 checked; parent accession resolved, row-specific G240E variant sequence not resolved.

substrate: Cephaloridine


substrate_name: Cephalothin

sequence_source: UniProtKB P37321 checked; parent accession resolved, row-specific Q104G variant sequence not emitted.

substrate: Cephalothin


sequence_source: UniProtKB P37321 checked; parent accession resolved, row-specific E166A variant sequence not emitted.


sequence_source: UniProtKB P37321 checked; parent accession resolved, row-specific S238G variant sequence not resolved.


substrate_name: Penicillin G

substrate: Penicillin G


sequence_source: UniProtKB P37321 checked; parent accession resolved, row-specific A164S variant sequence not emitted.


substrate_name: amoxicillin

substrate: amoxicillin


substrate_name: piperacillin

substrate: piperacillin


substrate_name: Ceftazidime

substrate: Ceftazidime


substrate_name: Ampicillin

substrate: Ampicillin


sequence_source: UniProtKB:P37321 direct accession lookup

column_label: Table 2 PER-1 row under Ceftazidime; columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Central values are Km 3.519 mM, kcat 70.0 s^-1, and independently printed kcat/Km 19.9 s^-1 mM^-1.

row_label: PER-1 / Ceftazidime

table_label: Table 2, Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes


sequence_source: UniProtKB:P37321 canonical sequence with PubMed:9494118 mutagenesis feature N->G at UniProt position 106

sequence_variant_note: Mutation signature N104G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P37321 canonical sequence with PubMed:9494118 mutagenesis feature Q->G at UniProt position 105

sequence_variant_note: Mutation signature Q104G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P37321 canonical sequence with PubMed:9494118 mutagenesis feature A->S at UniProt position 169

sequence_variant_note: Mutation signature A164S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row T104E, Cephaloridine column group: column Km = 2.5; column kcat = 0.14; column kcat/Km = 56. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.14 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.14 s^(-1). Km: printed Table 2 cell 2.5 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 2.5 / 1000 = 0.0025 mM. kcat/Km: printed Table 2 cell 56 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 56.0 s^(-1)*mM^(-1). The catalog carries kcat 0.14 s^(-1), Km 0.003 mM and kcat_over_km 46.66666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row T104E, Cephaloridine column group: Km = 2.5 uM; kcat = 0.14 s-1; printed kcat/Km = 56 s-1 mM-1.


sequence_source: UniProtKB reviewed accession P37321 direct REST lookup on 2026-05-27

column_label: Table 2 PER-1 row under Cephalothin; columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Central values are Km 0.046 mM, kcat 12.4 s^-1, and independently printed kcat/Km 269.0 s^-1 mM^-1.

row_label: PER-1 / Cephalothin


column_label: Table 2 PER-1 row under Cephaloridine; columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Central values are Km 0.237 mM, kcat 13.0 s^-1, and independently printed kcat/Km 55.0 s^-1 mM^-1.

row_label: PER-1 / Cephaloridine


sequence_source: UniProtKB:P37321 plus PMID 9494118 mutagenesis feature T107E, mapped from selected T104E label

sequence_variant_note: Mutation signature T104E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB:P37321 reviewed canonical sequence

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

column_label: The literal wild-type PER-1 Cefotaxime column group binds the exact current Km and kcat components. The independently printed rounded efficiency is retained separately.

raw_value_unit_evidence: Cefotaxime PER-1 cells: Km 652 ± 31 μM; kcat 43 ± 1.5 s^-1; printed kcat/Km 66 ± 1 s^-1 mM^-1.

row_label: PER-1 row / Cefotaxime columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P37321 and applied mutation signature E166A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row E166A, Aztreonam column group: column Km = 171; column kcat = 0.5; column kcat/Km = 2.9. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.5 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.5 s^(-1). Km: printed Table 2 cell 171 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 171 / 1000 = 0.171 mM. kcat/Km: printed Table 2 cell 2.9 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 2.9 s^(-1)*mM^(-1). The catalog carries kcat 0.5 s^(-1), Km 0.171 mM and kcat_over_km 2.923976608187134 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row E166A, Aztreonam column group: Km = 171 uM; kcat = 0.5 s-1; printed kcat/Km = 2.9 s-1 mM-1.


column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row A164S, Aztreonam column group: column Km = 35; column kcat = 2.2; column kcat/Km = 62.8. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.2 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.2 s^(-1). Km: printed Table 2 cell 35 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 35 / 1000 = 0.035 mM. kcat/Km: printed Table 2 cell 62.8 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 62.8 s^(-1)*mM^(-1). The catalog carries kcat 2.2 s^(-1), Km 0.035 mM and kcat_over_km 62.857142857142854 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row A164S, Aztreonam column group: Km = 35 uM; kcat = 2.2 s-1; printed kcat/Km = 62.8 s-1 mM-1.


organism: Serratia fonticola

sequence_source: UniProtKB reviewed accession P80545 (BLAC_SERFO), direct REST lookup on 2026-05-27; PMID 9300809 is the UniProt protein-sequence reference.

column_label: Table 2, row Cefotaxime: column "k cat (s^-1)" cell = 920; column "K m (uM)" cell = 80; column "k cat / K m (mM^-1 s^-1)" cell = 11 500. k cat and K m are read from the same single printed table row, so the tuple is one measurement and spans no other row, column or cofactor block.

normalized_value_unit_evidence: k cat 920 s^-1 normalizes to 920.0 s^-1. K m 80 uM normalizes to 80/1000 = 0.08 mM. k cat / K m = 920.0 s^-1 / 0.08 mM = 11500.0 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 2 also prints a rounded k cat / K m cell for this row, 11 500 mM^-1 s^-1; the exported ratio is the full-precision quotient 920 / (80 uM as mM) of the same row's two printed cells, which rounds to that printed cell.

raw_value_unit_evidence: Table 2 (PDF page 5 / article page 62), row Cefotaxime: k cat cell 920 s^-1; K m cell 80 uM; k cat / K m cell 11 500 mM^-1 s^-1. Verbatim line: Cefotaxime 920 80 11 500

row_label: Cefotaxime

table_label: Table 2. Kinetic parameters of b-lactamase of Serratia fonticola CUV


column_label: Table 2, row Ceftriaxone: column "k cat (s^-1)" cell = 620; column "K m (uM)" cell = 28; column "k cat / K m (mM^-1 s^-1)" cell = 22 150. k cat and K m are read from the same single printed table row, so the tuple is one measurement and spans no other row, column or cofactor block.

normalized_value_unit_evidence: k cat 620 s^-1 normalizes to 620.0 s^-1. K m 28 uM normalizes to 28/1000 = 0.028 mM. k cat / K m = 620.0 s^-1 / 0.028 mM = 22142.85714285714 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 2 also prints a rounded k cat / K m cell for this row, 22 150 mM^-1 s^-1; the exported ratio is the full-precision quotient 620 / (28 uM as mM) of the same row's two printed cells, which rounds to that printed cell.

raw_value_unit_evidence: Table 2 (PDF page 5 / article page 62), row Ceftriaxone: k cat cell 620 s^-1; K m cell 28 uM; k cat / K m cell 22 150 mM^-1 s^-1. Verbatim line: Ceftriaxone 620 28 22 150

row_label: Ceftriaxone


substrate_name: Cloxacillin

column_label: Table 2, row Cloxacillin: column "k cat (s^-1)" cell = 90; column "K m (uM)" cell = 43; column "k cat / K m (mM^-1 s^-1)" cell = 2 100. k cat and K m are read from the same single printed table row, so the tuple is one measurement and spans no other row, column or cofactor block.

normalized_value_unit_evidence: k cat 90 s^-1 normalizes to 90.0 s^-1. K m 43 uM normalizes to 43/1000 = 0.043 mM. k cat / K m = 90.0 s^-1 / 0.043 mM = 2093.0232558139537 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 2 also prints a rounded k cat / K m cell for this row, 2 100 mM^-1 s^-1; the exported ratio is the full-precision quotient 90 / (43 uM as mM) of the same row's two printed cells, which rounds to that printed cell.

raw_value_unit_evidence: Table 2 (PDF page 5 / article page 62), row Cloxacillin: k cat cell 90 s^-1; K m cell 43 uM; k cat / K m cell 2 100 mM^-1 s^-1. Verbatim line: Cloxacillin 90 43 2 100

row_label: Cloxacillin

substrate: Cloxacillin


substrate_name: Cefoperazone

column_label: Table 2, row Cefoperazone: column "k cat (s^-1)" cell = 70; column "K m (uM)" cell = 10; column "k cat / K m (mM^-1 s^-1)" cell = 7 000. k cat and K m are read from the same single printed table row, so the tuple is one measurement and spans no other row, column or cofactor block.

normalized_value_unit_evidence: k cat 70 s^-1 normalizes to 70.0 s^-1. K m 10 uM normalizes to 10/1000 = 0.01 mM. k cat / K m = 70.0 s^-1 / 0.01 mM = 7000.0 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 2 also prints a rounded k cat / K m cell for this row, 7 000 mM^-1 s^-1; the exported ratio is the full-precision quotient 70 / (10 uM as mM) of the same row's two printed cells, which rounds to that printed cell.

raw_value_unit_evidence: Table 2 (PDF page 5 / article page 62), row Cefoperazone: k cat cell 70 s^-1; K m cell 10 uM; k cat / K m cell 7 000 mM^-1 s^-1. Verbatim line: Cefoperazone 70 10 7 000

row_label: Cefoperazone

substrate: Cefoperazone


substrate_name: Mezlocillin sodium

column_label: Table 2, row Mezlocillin: column "k cat (s^-1)" cell = 255; column "K m (uM)" cell = 15; column "k cat / K m (mM^-1 s^-1)" cell = 17 000. k cat and K m are read from the same single printed table row, so the tuple is one measurement and spans no other row, column or cofactor block.

normalized_value_unit_evidence: k cat 255 s^-1 normalizes to 255.0 s^-1. K m 15 uM normalizes to 15/1000 = 0.015 mM. k cat / K m = 255.0 s^-1 / 0.015 mM = 17000.0 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 2 also prints a rounded k cat / K m cell for this row, 17 000 mM^-1 s^-1; the exported ratio is the full-precision quotient 255 / (15 uM as mM) of the same row's two printed cells, which rounds to that printed cell.

raw_value_unit_evidence: Table 2 (PDF page 5 / article page 62), row Mezlocillin: k cat cell 255 s^-1; K m cell 15 uM; k cat / K m cell 17 000 mM^-1 s^-1. Verbatim line: Mezlocillin 255 15 17 000

row_label: Mezlocillin

substrate: Mezlocillin sodium


substrate_name: cefepime

column_label: Table 2, row Cefepime: column "k cat (s^-1)" cell = 225; column "K m (uM)" cell = 430; column "k cat / K m (mM^-1 s^-1)" cell = 525. k cat and K m are read from the same single printed table row, so the tuple is one measurement and spans no other row, column or cofactor block.

normalized_value_unit_evidence: k cat 225 s^-1 normalizes to 225.0 s^-1. K m 430 uM normalizes to 430/1000 = 0.43 mM. k cat / K m = 225.0 s^-1 / 0.43 mM = 523.2558139534884 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 2 also prints a rounded k cat / K m cell for this row, 525 mM^-1 s^-1; the exported ratio is the full-precision quotient 225 / (430 uM as mM) of the same row's two printed cells, which rounds to that printed cell.

raw_value_unit_evidence: Table 2 (PDF page 5 / article page 62), row Cefepime: k cat cell 225 s^-1; K m cell 430 uM; k cat / K m cell 525 mM^-1 s^-1. Verbatim line: Cefepime 225 430 525

row_label: Cefepime

substrate: cefepime


substrate_name: Amoxycillin

column_label: Table 2, row Amoxycillin: column "k cat (s^-1)" cell = 460; column "K m (uM)" cell = 35; column "k cat / K m (mM^-1 s^-1)" cell = 13 150. k cat and K m are read from the same single printed table row, so the tuple is one measurement and spans no other row, column or cofactor block.

normalized_value_unit_evidence: k cat 460 s^-1 normalizes to 460.0 s^-1. K m 35 uM normalizes to 35/1000 = 0.035 mM. k cat / K m = 460.0 s^-1 / 0.035 mM = 13142.857142857141 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 2 also prints a rounded k cat / K m cell for this row, 13 150 mM^-1 s^-1; the exported ratio is the full-precision quotient 460 / (35 uM as mM) of the same row's two printed cells, which rounds to that printed cell.

raw_value_unit_evidence: Table 2 (PDF page 5 / article page 62), row Amoxycillin: k cat cell 460 s^-1; K m cell 35 uM; k cat / K m cell 13 150 mM^-1 s^-1. Verbatim line: Amoxycillin 460 35 13 150

row_label: Amoxycillin

substrate: Amoxycillin


column_label: Table 2, row Cephalothin: column "k cat (s^-1)" cell = 7150; column "K m (uM)" cell = 175; column "k cat / K m (mM^-1 s^-1)" cell = 40 900. k cat and K m are read from the same single printed table row, so the tuple is one measurement and spans no other row, column or cofactor block.

normalized_value_unit_evidence: k cat 7150 s^-1 normalizes to 7150.0 s^-1. K m 175 uM normalizes to 175/1000 = 0.175 mM. k cat / K m = 7150.0 s^-1 / 0.175 mM = 40857.14285714286 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 2 also prints a rounded k cat / K m cell for this row, 40 900 mM^-1 s^-1; the exported ratio is the full-precision quotient 7150 / (175 uM as mM) of the same row's two printed cells, which rounds to that printed cell.

raw_value_unit_evidence: Table 2 (PDF page 5 / article page 62), row Cephalothin: k cat cell 7150 s^-1; K m cell 175 uM; k cat / K m cell 40 900 mM^-1 s^-1. Verbatim line: Cephalothin 7150 175 40 900

row_label: Cephalothin


substrate_name: carbenicillin

sequence_source: UniProtKB REST direct lookup for Q9RMI1 on 2026-05-27

column_label: Official PMC Table 1 row Carbenicillin Sfh-I columns: kcat=9.15 +/- 1.58 s^-1, Km=1,280 +/- 363 uM, kcat/Km=7.18 x 10^3 M^-1 s^-1. metric: kcat; normalized value: 9.15 s^(-1); metric: Km; normalized value: 1.28 mM; metric: kcat/Km; normalized value: 7.1484375 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; normalized value: 9.15 s^(-1); metric: Km; normalized value: 1.28 mM; metric: kcat/Km; normalized value: 7.1484375 s^-1 mM^-1; Independently printed kcat/Km remains preserved in paper_metric_evidence.raw_value.

row_label: Carbenicillin

table_label: Table 1. Kinetic parameters of purified Sfh-I beta-lactamase and comparison with other B2 metallo-beta-lactamases.

substrate: carbenicillin


substrate_name: moxalactam

column_label: Official PMC Table 1 row Moxalactam Sfh-I columns: kcat=0.017 +/- 0.0012 s^-1, Km=91 +/- 14 uM, kcat/Km=1.87 x 10^2 M^-1 s^-1. metric: kcat; normalized value: 0.017 s^(-1); metric: Km; normalized value: 0.091 mM; metric: kcat/Km; normalized value: 0.18681318681318684 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; normalized value: 0.017 s^(-1); metric: Km; normalized value: 0.091 mM; metric: kcat/Km; normalized value: 0.18681318681318684 s^-1 mM^-1; Independently printed kcat/Km remains preserved in paper_metric_evidence.raw_value.

row_label: Moxalactam

substrate: moxalactam


column_label: Official PMC Table 1 row Cefepime Sfh-I columns: kcat=0.64 +/- 0.073 s^-1, Km=202 +/- 43.7 uM, kcat/Km=3.16 x 10^3 M^-1 s^-1. metric: kcat; normalized value: 0.64 s^(-1); metric: Km; normalized value: 0.202 mM; metric: kcat/Km; normalized value: 3.168316831683168 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; normalized value: 0.64 s^(-1); metric: Km; normalized value: 0.202 mM; metric: kcat/Km; normalized value: 3.168316831683168 s^-1 mM^-1; Independently printed kcat/Km remains preserved in paper_metric_evidence.raw_value.


substrate_name: cefoxitin

column_label: Official PMC Table 1 row Cefoxitin Sfh-I columns: kcat=0.032 +/- 0.00094 s^-1, Km=99 +/- 7 uM, kcat/Km=3.23 x 10^2 M^-1 s^-1. metric: kcat; normalized value: 0.032 s^(-1); metric: Km; normalized value: 0.099 mM; metric: kcat/Km; normalized value: 0.3232323232323232 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; normalized value: 0.032 s^(-1); metric: Km; normalized value: 0.099 mM; metric: kcat/Km; normalized value: 0.3232323232323232 s^-1 mM^-1; Independently printed kcat/Km remains preserved in paper_metric_evidence.raw_value.

row_label: Cefoxitin

substrate: cefoxitin


substrate_name: meropenem

column_label: Official PMC Table 1 row Meropenem Sfh-I columns: kcat=109 +/- 9.5 s^-1, Km=215 +/- 47.0 uM, kcat/Km=5.05 x 10^5 M^-1 s^-1. metric: kcat; normalized value: 109.0 s^(-1); metric: Km; normalized value: 0.215 mM; metric: kcat/Km; normalized value: 506.9767441860465 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; normalized value: 109.0 s^(-1); metric: Km; normalized value: 0.215 mM; metric: kcat/Km; normalized value: 506.9767441860465 s^-1 mM^-1; Independently printed kcat/Km remains preserved in paper_metric_evidence.raw_value.

row_label: Meropenem

substrate: meropenem


substrate_name: ampicillin

column_label: Official PMC Table 1 row Ampicillin Sfh-I columns: kcat=9.5 +/- 1.11 s^-1, Km=676 +/- 187 uM, kcat/Km=1.41 x 10^4 M^-1 s^-1. metric: kcat; normalized value: 9.5 s^(-1); metric: Km; normalized value: 0.676 mM; metric: kcat/Km; normalized value: 14.053254437869821 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; normalized value: 9.5 s^(-1); metric: Km; normalized value: 0.676 mM; metric: kcat/Km; normalized value: 14.053254437869821 s^-1 mM^-1; Independently printed kcat/Km remains preserved in paper_metric_evidence.raw_value.

row_label: Ampicillin

substrate: ampicillin


sequence_source: UniProtKB:P80545 direct REST/FASTA lookup on 2026-05-27; source record PMID 9300809


substrate_name: Cefuroxime

substrate: Cefuroxime


substrate_name: cefpirome

column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Cefpirome. Column labels read: k cat (s^-1) cell 745, K m (uM) cell 440, k cat / K m (mM^-1 s^-1) cell 1 690. captured primary segment: Cefpirome 745 440 1 690 tions, gave rise to 28 Žform I. and 27 Žform II. pure. The printed k cat cell 745 s^-1 decimal-matches the exported kcat 745.0 s^(-1); the printed K m cell 440 uM normalizes to 0.44 mM and decimal-matches the exported km; the exported kcat_over_km 1693.1818181818182 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 Cefpirome 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: 745; raw unit: s^-1; normalized value: 745.0 s^(-1); metric: Km; raw value: 440; raw unit: uM; normalized value: 0.44 mM; metric: kcat/Km; derived from this row's own printed cells 745.0 s^-1 / 0.44 mM; normalized value: 1693.1818181818182 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 745 s^-1 is already in s^-1, so the normalized kcat is 745.0 s^(-1). Km 440 uM = 440/1000 = 0.44 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: 745.0 / 0.44 = 1693.1818181818182 s^(-1)*mM^(-1). Two-sided round-trip against the separately printed k cat r K m cell 1 690: that cell is printed to a granularity of 10, so it stands for the interval [1685, 1695); the quotient 1693.1818181818182 of this row's own two printed cells falls inside that interval, and rounding 1693.1818181818182 to the printed cell's granularity returns 1 690 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: Cefpirome 745 440 1 690 tions, gave rise to 28 Žform I. and 27 Žform II. pure | k cat cell as printed for this row: 745, printed unit s^-1 | K m cell as printed for this row: 440, printed unit uM | k cat r K m cell as printed for this row: 1 690, printed unit mM^-1 s^-1, retained as rounded corroboration only and not used as the exported ratio.

row_label: Cefpirome

substrate: cefpirome


substrate_name: cefotiam

column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Cefotiam. Column labels read: k cat (s^-1) cell 945, K m (uM) cell 55, k cat / K m (mM^-1 s^-1) cell 17 200. captured primary segment: Cefotiam 945 55 17 200 23 peaks, respectively, on a first RP-HPLC at pH 2.. The printed k cat cell 945 s^-1 decimal-matches the exported kcat 945.0 s^(-1); the printed K m cell 55 uM normalizes to 0.055 mM and decimal-matches the exported km; the exported kcat_over_km 17181.81818181818 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 Cefotiam 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: 945; raw unit: s^-1; normalized value: 945.0 s^(-1); metric: Km; raw value: 55; raw unit: uM; normalized value: 0.055 mM; metric: kcat/Km; derived from this row's own printed cells 945.0 s^-1 / 0.055 mM; normalized value: 17181.81818181818 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 945 s^-1 is already in s^-1, so the normalized kcat is 945.0 s^(-1). Km 55 uM = 55/1000 = 0.055 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: 945.0 / 0.055 = 17181.81818181818 s^(-1)*mM^(-1). Two-sided round-trip against the separately printed k cat r K m cell 17 200: that cell is printed to a granularity of 100, so it stands for the interval [17150, 17250); the quotient 17181.81818181818 of this row's own two printed cells falls inside that interval, and rounding 17181.81818181818 to the printed cell's granularity returns 17 200 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: Cefotiam 945 55 17 200 | k cat cell as printed for this row: 945, printed unit s^-1 | K m cell as printed for this row: 55, printed unit uM | k cat r K m cell as printed for this row: 17 200, printed unit mM^-1 s^-1, retained as rounded corroboration only and not used as the exported ratio.

row_label: Cefotiam

substrate: cefotiam


substrate_name: Ticarcillin

column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Ticarcillin. Column labels read: k cat (s^-1) cell 115, K m (uM) cell 31, k cat / K m (mM^-1 s^-1) cell 3 700. captured primary segment: Ticarcillin 115 31 3 700 The complete amino acid sequence of the two. The printed k cat cell 115 s^-1 decimal-matches the exported kcat 115.0 s^(-1); the printed K m cell 31 uM normalizes to 0.031 mM and decimal-matches the exported km; the exported kcat_over_km 3709.6774193548385 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 Ticarcillin 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: 115; raw unit: s^-1; normalized value: 115.0 s^(-1); metric: Km; raw value: 31; raw unit: uM; normalized value: 0.031 mM; metric: kcat/Km; derived from this row's own printed cells 115.0 s^-1 / 0.031 mM; normalized value: 3709.6774193548385 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 115 s^-1 is already in s^-1, so the normalized kcat is 115.0 s^(-1). Km 31 uM = 31/1000 = 0.031 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: 115.0 / 0.031 = 3709.6774193548385 s^(-1)*mM^(-1). Two-sided round-trip against the separately printed k cat r K m cell 3 700: that cell is printed to a granularity of 100, so it stands for the interval [3650, 3750); the quotient 3709.6774193548385 of this row's own two printed cells falls inside that interval, and rounding 3709.6774193548385 to the printed cell's granularity returns 3 700 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: Ticarcillin 115 31 3 700 The complete amino acid sequence of the two | k cat cell as printed for this row: 115, printed unit s^-1 | K m cell as printed for this row: 31, printed unit uM | k cat r K m cell as printed for this row: 3 700, printed unit mM^-1 s^-1, retained as rounded corroboration only and not used as the exported ratio.

row_label: Ticarcillin

substrate: Ticarcillin


column_label: Table label: Table 2 Kinetic parameters of b-lactamase of Serratia fonticola CUV. Evidence location type: table. Row label: Carbenicillin. Column labels read: k cat (s^-1) cell 100, K m (uM) cell 40, k cat / K m (mM^-1 s^-1) cell 2 500. captured primary segment: Carbenicillin 100 40 2 500. The printed k cat cell 100 s^-1 decimal-matches the exported kcat 100.0 s^(-1); the printed K m cell 40 uM normalizes to 0.04 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 Carbenicillin 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: 100; raw unit: s^-1; normalized value: 100.0 s^(-1); metric: Km; raw value: 40; raw unit: uM; normalized value: 0.04 mM; metric: kcat/Km; derived from this row's own printed cells 100.0 s^-1 / 0.04 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 100 s^-1 is already in s^-1, so the normalized kcat is 100.0 s^(-1). Km 40 uM = 40/1000 = 0.04 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: 100.0 / 0.04 = 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: Carbenicillin 100 40 2 500 | k cat cell as printed for this row: 100, printed unit s^-1 | K m cell as printed for this row: 40, 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.


organism: Serratia marcescens

substrate_name: Nitrocefin

sequence_source: UniProtKB:Q7DHD4 direct REST/FASTA lookup on 2026-05-27; same sequence as reviewed UniProtKB:P52699 linked to PMID 15788415 and PDB 1WUO/1WUP

substrate: Nitrocefin


substrate_name: Imipenem

sequence_source: UniProtKB:Q9RMI1 direct accession lookup

column_label: Official PMC Table 1 Imipenem row, Sfh-I columns: kcat 51 +/- 2.8 s^-1, Km 79.2 +/- 11.2 uM, kcat/Km 6.42 x 10^5 M^-1 s^-1. metric: kcat; normalized value: 51.0 s^(-1); metric: Km; normalized value: 0.0792 mM; metric: kcat/Km; normalized value: 643.9393939393939 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 51 +/- 2.8; raw unit: s^-1; normalized value: 51.0 s^(-1); metric: Km; raw value: 79.2 +/- 11.2; raw unit: uM; normalized value: 0.0792 mM; metric: kcat/Km; raw value: 6.42 x 10^5; raw unit: M^-1 s^-1; normalized value: 643.9393939393939 s^-1 mM^-1; The independently printed efficiency is 642 s^-1 mM^-1 after scaling and agrees at printed precision.

row_label: Imipenem

substrate: Imipenem


substrate_name: nitrocefin

column_label: Official PMC Table 1 row Nitrocefin Sfh-I columns: kcat=0.06 +/- 0.003 s^-1, Km=106 +/- 13.4 uM, kcat/Km=5.7 x 10^2 M^-1 s^-1. metric: kcat; normalized value: 0.06 s^(-1); metric: Km; normalized value: 0.106 mM; metric: kcat/Km; normalized value: 0.5660377358490566 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; normalized value: 0.06 s^(-1); metric: Km; normalized value: 0.106 mM; metric: kcat/Km; normalized value: 0.5660377358490566 s^-1 mM^-1; Independently printed kcat/Km remains preserved in paper_metric_evidence.raw_value.

row_label: Nitrocefin

substrate: nitrocefin