column_label: PMID 12962487 Table 4: Kinetic Parameters of Toho-1 against Various Antibiotics (Biochemistry 2003, 42, 10634-10643, journal page 10639); row 'cephalosporin (1) | cephalothin'; columns 'kcat (s-1)', 'Km (uM)' and 'kcat/Km (uM-1 s-1)'; printed cells kcat = 480 s-1, Km = 39 uM, kcat/Km = 12 uM-1 s-1. The exported kcat and Km are the literal printed cells of that one row after Km uM-to-mM normalization; the exported kcat/Km is the quotient of those same two cells as stored. No value is taken from another row, another column, another cofactor condition, or another paper.

normalized_value_unit_evidence: metric: kcat; raw value: 480 s-1; raw unit: s^-1; normalized value: 480.0 s^(-1); metric: Km; raw value: 39 uM; raw unit: uM; normalized value: 0.039 mM; metric: kcat/Km; raw value: same-row quotient of the two printed cells; normalized value: 12307.692307692309 s^-1 mM^-1; assay condition: Steady-state kinetic parameters for the wild-type Toho-1 class A extended-spectrum beta-lactamase; hydrolysis detected by monitoring the absorbance of beta-lactam solution in 50 mM phosphate buffer (pH 7.0), reaction in a total volume of 500 uL at 30 C (Uvikon 860 spectrophotometer). Wild-type enzyme, no mutation.

raw_value_unit_evidence: Table 4 row as printed: kcat = 480 s-1; Km = 39 uM; kcat/Km = 12 uM-1 s-1.

row_label: cephalosporin (1) | cephalothin (Table 4)


enzyme_display_name: beta-lactamase

organism: Escherichia coli

substrate_name: piperacillin

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB Q47066 direct REST lookup; reviewed Swiss-Prot BLT1_ECOLX canonical sequence

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

data_origin: experimental

enzyme: beta-lactamase

substrate: piperacillin

status: unverified

source: oed


substrate_name: Sulbactam

verification_status: corrected

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

column_label: Table 4; row label: sulbactam; column label: kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); raw value: 0.18, 0.31, and 0.58; raw unit: s^-1, uM, and uM^-1 s^-1; normalized value: 0.18 s^-1, 0.00031 mM, and 580 s^-1*mM^-1; assay condition: hydrolysis at 30 C in 50 mM phosphate buffer pH 7.0.

normalized_value_unit_evidence: kcat normalized_value=0.18 normalized_unit=s^(-1); Km normalized_value=0.00031 normalized_unit=mM; kcat/Km normalized_value=580 normalized_unit=s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4 sulbactam cells: kcat raw_value=0.18 raw_unit=s^-1; Km raw_value=0.31 raw_unit=uM; kcat/Km raw_value=0.58 raw_unit=uM^-1 s^-1.

row_label: sulbactam

table_label: Table 4. Kinetic Parameters of Toho-1 against Various Antibiotics

substrate: Sulbactam

status: corrected


substrate_name: Cephalosporin C

kcat_over_km_display: Not reported

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

mutation_type: substitution

substrate: Cephalosporin C


substrate_name: Ceftazidime

sequence_source: UniProtKB:P62593 direct lookup on 2026-05-27

column_label: Table II (PDF page 4 of 9, journal page 23055), substrate block `Ceftazidime`, b-lactamase sub-row `TEMpUC19`: kcat (s^-1) = 0.008; Km (uM) = 200; kcat/Km (M^-1 s^-1) = 4.0 x 10^1.

normalized_value_unit_evidence: kcat: printed cell 0.008 s^-1 is already the export unit -> 0.008 s^(-1); the exported value is 18.0 s^(-1). Km: printed cell 200 uM -> 0.2 mM (divide by 1000); the exported value is 0.2 mM. kcat/Km: the paper PRINTS the kcat/Km cell 4.0 x 10^1 M^-1 s^-1 for this Table II row -> 0.04 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 90.0 s^(-1)*mM^(-1).

row_label: Table II, decoded plain-numeral transcription, substrate block `Ceftazidime`, b-lactamase sub-row `TEMpUC19`

table_label: Table II (PDF page 4 of 9, journal page 23055) 'Kinetics parameters of TEMpUC19 and mutant derivatives'

substrate: Ceftazidime


substrate_name: Cephaloridine

substrate: Cephaloridine


column_label: Table II (PDF page 4 of 9, journal page 23055), substrate block `Piperacillin`, b-lactamase sub-row `TEMpUC19`: kcat (s^-1) = 770; Km (uM) = 70; kcat/Km (M^-1 s^-1) = 1.1 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 770 s^-1 is already the export unit -> 770.0 s^(-1); the exported value is 1275.0 s^(-1). Km: printed cell 70 uM -> 0.07 mM (divide by 1000); the exported value is 0.04 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.1 x 10^7 M^-1 s^-1 for this Table II row -> 11000.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 31875.0 s^(-1)*mM^(-1).

row_label: Table II, decoded plain-numeral transcription, substrate block `Piperacillin`, b-lactamase sub-row `TEMpUC19`


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: aztreonam

verification_status: verified

sequence_source: UniProtKB:P62593 FASTA direct lookup; reviewed Swiss-Prot entry BLAT_ECOLX

column_label: Confirmed from Table II row Aztreonam / TEMpUC19; columns kcat, Km, and kcat/Km.

raw_value_unit_evidence: Table II Aztreonam TEMpUC19 row reports kcat 0.4 +/- 0.1 s^-1; Km 550 +/- 200 microM; kcat/Km (7.4 +/- 3.0) x 10^2 M^-1 s^-1.

row_label: Aztreonam / TEMpUC19

table_label: Table II. Kinetics parameters of TEMpUC19 and mutant derivatives

substrate: aztreonam

status: verified


substrate_name: beta-Lactam

substrate: beta-Lactam


substrate_name: cefpirome; cephaloridine; ampicillin; cefoxitin; ceftazidime; cefotaxime; cefepime

source_db: brenda;skid

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

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

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

source_databases_merged: brenda skid

source: brenda;skid


substrate_name: Penicillin G; H2O / H2O; Cephalothin

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

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature Y105D with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105D

substrate: Penicillin G; H2O / H2O; Cephalothin


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature Y105G with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: Penicillin G; H2O / Cephalothin; H2O

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature Y105R with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105R

substrate: Penicillin G; H2O / Cephalothin; H2O


assay_conditions_summary: pH 7; 310.15 K; buffer pH 7

column_label: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-25 column block: kcat (s^-1) / Km (uM) / kcat per Km (uM^-1 s^-1); Aztreonam row

normalized_value_unit_evidence: kcat 84.0 s^-1; Km 0.12 mM; kcat_over_km 700.0 s^-1 mM^-1 as the quotient of the same TABLE 3 row and same CTX-M-25 column-block kcat and Km cells; the paper's own printed ratio cell reads 0.7 uM^-1 s^-1 = 700.0 s^-1 mM^-1

raw_value_unit_evidence: kcat 84 s^-1; Km 120 uM; printed kcat/Km 0.7 uM^-1 s^-1

row_label: Aztreonam row; CTX-M-25 column block (first three numeric cells)


column_label: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-25 column block: kcat (s^-1) / Km (uM) / kcat per Km (uM^-1 s^-1); Cephalothin row

normalized_value_unit_evidence: kcat 230.0 s^-1; Km 0.19 mM; kcat_over_km 1210.5263157894738 s^-1 mM^-1 as the quotient of the same TABLE 3 row and same CTX-M-25 column-block kcat and Km cells; the paper's own printed ratio cell reads 1.2 uM^-1 s^-1 = 1200.0 s^-1 mM^-1

raw_value_unit_evidence: kcat 230 s^-1; Km 190 uM; printed kcat/Km 1.2 uM^-1 s^-1

row_label: Cephalothin row; CTX-M-25 column block (first three numeric cells)


column_label: Table 2. Kinetic parameters of CTX-M-14 against various substrates; row Piperacillin; column Km (uM) raw 20; column kcat (s^-1) raw 39; column kcat/Km (uM^-1 s^-1) raw 2.0.

normalized_value_unit_evidence: kcat=39.0 s^-1 (printed in s^-1, no conversion); Km=0.02 mM (20 uM divided by 1000); kcat/Km=1950.0 s^-1 mM^-1 (quotient of this record's own two printed cells, 39 s^-1 / 0.02 mM = 1950.0 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 row Piperacillin: kcat 39 s^-1; Km 20 uM; the row-level transcription line is: | 2facc57377822923 | Piperacillin | piperacillin | 39 | 20 | 0.020 | 2.0 | 2000 | 1950 | confirmed; table-rounding compatible |

row_label: Piperacillin


column_label: Table 2. Kinetic parameters of CTX-M-14 against various substrates; row Cefaloridine; column Km (uM) raw 125; column kcat (s^-1) raw 1300; column kcat/Km (uM^-1 s^-1) raw 10.

normalized_value_unit_evidence: kcat=1300.0 s^-1 (printed in s^-1, no conversion); Km=0.125 mM (125 uM divided by 1000); kcat/Km=10400.0 s^-1 mM^-1 (quotient of this record's own two printed cells, 1300 s^-1 / 0.125 mM = 10400.0 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 row Cefaloridine: kcat 1300 s^-1; Km 125 uM; the row-level transcription line is: | 66e1cc0be48fcc90 | Cefaloridine | Cephaloridine | 1300 | 125 | 0.125 | 10 | 10000 | 10400 | confirmed; alternate spelling and table-rounding compatible |

row_label: Cefaloridine


column_label: Table 2. Kinetic parameters of CTX-M-14 against various substrates; row Cefalothin; column Km (uM) raw 27; column kcat (s^-1) raw 510; column kcat/Km (uM^-1 s^-1) raw 19.

raw_value_unit_evidence: Table 2 row Cefalothin: kcat 510 s^-1; Km 27 uM; the row-level transcription line is: | 686edd1e15296263 | Cefalothin | Cephalothin | 510 | 27 | 0.027 | 19 | 19000 | 18888.88888888889 | confirmed; alternate spelling and table-rounding compatible |

row_label: Cefalothin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Cefuroxime

sequence_source: UniProtKB:Q8KSA6 reviewed FASTA direct lookup

column_label: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-25 column block: kcat (s^-1) / Km (uM) / kcat per Km (uM^-1 s^-1); Cefuroxime row

normalized_value_unit_evidence: kcat 190.0 s^-1; Km 0.044 mM; kcat_over_km 4318.181818181818 s^-1 mM^-1 as the quotient of the same TABLE 3 row and same CTX-M-25 column-block kcat and Km cells; the paper's own printed ratio cell reads 4.3 uM^-1 s^-1 = 4300.0 s^-1 mM^-1

raw_value_unit_evidence: kcat 190 s^-1; Km 44 uM; printed kcat/Km 4.3 uM^-1 s^-1

row_label: Cefuroxime row; CTX-M-25 column block (first three numeric cells)

substrate: Cefuroxime


column_label: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-25 column block: kcat (s^-1) / Km (uM) / kcat per Km (uM^-1 s^-1); Benzylpenicillin row

normalized_value_unit_evidence: kcat 33.0 s^-1; Km 0.074 mM; kcat_over_km 445.945945945946 s^-1 mM^-1 as the quotient of the same TABLE 3 row and same CTX-M-25 column-block kcat and Km cells; the paper's own printed ratio cell reads 0.4 uM^-1 s^-1 = 400.0 s^-1 mM^-1

raw_value_unit_evidence: kcat 33 s^-1; Km 74 uM; printed kcat/Km 0.4 uM^-1 s^-1

row_label: Benzylpenicillin row; CTX-M-25 column block (first three numeric cells)


column_label: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-25 column block: kcat (s^-1) / Km (uM) / kcat per Km (uM^-1 s^-1); Ceftazidime row

normalized_value_unit_evidence: kcat 33.0 s^-1; Km 0.013 mM; kcat_over_km 2538.4615384615386 s^-1 mM^-1 as the quotient of the same TABLE 3 row and same CTX-M-25 column-block kcat and Km cells; the paper's own printed ratio cell reads 2.6 uM^-1 s^-1 = 2600.0 s^-1 mM^-1

raw_value_unit_evidence: kcat 33 s^-1; Km 13 uM; printed kcat/Km 2.6 uM^-1 s^-1

row_label: Ceftazidime row; CTX-M-25 column block (first three numeric cells)


column_label: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-25 column block: kcat (s^-1) / Km (uM) / kcat per Km (uM^-1 s^-1); Cefotaxime row

normalized_value_unit_evidence: kcat 101.0 s^-1; Km 0.028 mM; kcat_over_km 3607.142857142857 s^-1 mM^-1 as the quotient of the same TABLE 3 row and same CTX-M-25 column-block kcat and Km cells; the paper's own printed ratio cell reads 3.6 uM^-1 s^-1 = 3600.0 s^-1 mM^-1

raw_value_unit_evidence: kcat 101 s^-1; Km 28 uM; printed kcat/Km 3.6 uM^-1 s^-1

row_label: Cefotaxime row; CTX-M-25 column block (first three numeric cells)


substrate_name: cefcapene

sequence_source: UniProtKB:Q9L5C7 direct REST/FASTA check on 2026-05-27

column_label: Table 2. Kinetic parameters of CTX-M-14 against various substrates; row Cefcapene; column Km (uM) raw 25; column kcat (s^-1) raw 110; column kcat/Km (uM^-1 s^-1) raw 4.4.

normalized_value_unit_evidence: kcat=110.0 s^-1 (printed in s^-1, no conversion); Km=0.025 mM (25 uM divided by 1000); kcat/Km=4400.0 s^-1 mM^-1 (printed kcat/Km cell 4.4 uM^-1 s^-1 for this row, which normalizes to 4400.0 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 row Cefcapene: kcat 110 s^-1; Km 25 uM; the row-level transcription line is: | 7ae4b1397ba3b1f5 | Cefcapene | cefcapene | 110 | 25 | 0.025 | 4.4 | 4400 | 4400 | confirmed |

row_label: Cefcapene

substrate: cefcapene


column_label: Table 2. Kinetic parameters of CTX-M-14 against various substrates; row Benzylpenicillin; column Km (uM) raw 11; column kcat (s^-1) raw 48; column kcat/Km (uM^-1 s^-1) raw 4.4.

normalized_value_unit_evidence: kcat=48.0 s^-1 (printed in s^-1, no conversion); Km=0.011 mM (11 uM divided by 1000); kcat/Km=4363.636363636364 s^-1 mM^-1 (quotient of this record's own two printed cells, 48 s^-1 / 0.011 mM = 4363.636363636364 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 row Benzylpenicillin: kcat 48 s^-1; Km 11 uM; the row-level transcription line is: | 805658f5e37b0e67 | Benzylpenicillin | Penicillin G | 48 | 11 | 0.011 | 4.4 | 4400 | 4363.636363636364 | confirmed; synonym and table-rounding compatible |

row_label: Benzylpenicillin


column_label: Table 2. Kinetic parameters of CTX-M-14 against various substrates; row Cefotaxime; column Km (uM) raw 41; column kcat (s^-1) raw 1400; column kcat/Km (uM^-1 s^-1) raw 34.

raw_value_unit_evidence: Table 2 row Cefotaxime: kcat 1400 s^-1; Km 41 uM; the row-level transcription line is: | c57c5c7a1a08f6f0 | Cefotaxime | cefotaxime | 1400 | 41 | 0.041 | 34 | 34000 | 34146.34146341463 | confirmed; table-rounding compatible |

row_label: Cefotaxime


substrate_name: Meropenem

column_label: Table label: Table 2: Kinetic parameters of CTX-M-14 against various substrates. Row: Meropenem. Columns read: kcat (s^-1) cell 0.007, Km (uM) cell 0.11, kcat/Km (uM^-1 s^-1) cell 0.07. metric: kcat; raw value: 0.007; raw unit: s^-1; normalized value: 0.007 s^(-1); metric: Km; raw value: 0.11; raw unit: uM; normalized value: 0.00011 mM, stored by the export at four-decimal precision as 0.0001 mM; metric: kcat/Km; raw value: 0.07; raw unit: uM^-1 s^-1; normalized value: 70.0 s^-1 mM^-1; assay condition: Hydrolysis of beta-lactam antibiotics by CTX-M-14 was monitored by absorbance in 50 mM phosphate buffer at pH 7.0; reactions were 500 uL at 30 C, with BSA 20 ug/mL added to dilute beta-lactamase solutions. Export row conditions: pH 7; 303.15 K; buffer 50 mM phosphate.

normalized_value_unit_evidence: Table 2 row Meropenem: kcat 0.007 s^-1 = 0.007 s^(-1); Km 0.11 uM = 0.00011 mM (1 uM = 0.001 mM), which equals the export's stored value 0.0001 mM at the export's stored precision of four decimal places; kcat/Km printed 0.07 uM^-1 s^-1 x 1000 = 70.0 s^-1 mM^-1 (1 uM^-1 s^-1 = 1000 mM^-1 s^-1), decimal-matching the exported 70.0 and equal to the quotient of the exported cells 0.007 s^-1 / 0.0001 mM.; the columns Km uM, Km mM and the two kcat/Km columns hold the paper's printed value and its unit-normalized form side by side.

raw_value_unit_evidence: package Km rounded from table | | Table 2 cells for row Meropenem read in the paper's own units: kcat = 0.007 s^-1; Km = 0.11 uM; kcat/Km = 0.07 uM^-1 s^-1

row_label: Meropenem

substrate: Meropenem


substrate_name: Cefdinir

substrate: Cefdinir


substrate_name: Doripenem

substrate: Doripenem


substrate_name: Nitrocefin

sequence_source: UniProtKB:Q9L5C7 direct REST lookup on 2026-05-27

substrate: Nitrocefin


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


substrate_name: cefalotin

substrate: cefalotin


substrate_name: ampicillin

substrate: ampicillin


substrate_name: ceftazidime

substrate: ceftazidime


substrate_name: meropenem

substrate: meropenem


substrate_name: doripenem

substrate: doripenem


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: nitrocefin

substrate: nitrocefin


sequence_source: UniProtKB:P62593 direct REST lookup


substrate_name: carbenicillin

substrate: carbenicillin


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: Cephaloridine

substrate: Cephaloridine


substrate_name: Penicillin G

substrate: Penicillin G


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


substrate_name: Substituted beta-amino acid; H2O; Penicillin G; Cephaloridine; H2O; Cephalothin; H2O; Cefotaxime

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W165S:A237T:E240C


substrate_name: Ampicillin; H2O; Penicillin G; Cephaloridine; Cephalothin; Cefotaxime

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W165S


substrate_name: Cephalothin

substrate: Cephalothin


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:P28585 FASTA direct check, retrieved 2026-05-27

source: skid


organism: Fluoribacter gormanii


sequence_source: UniProtKB:Q9K578 FASTA direct check, retrieved 2026-05-27


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: Cefuroxime

sequence_source: UniProtKB:Q6SJ61 direct lookup; live TrEMBL Escherichia coli beta-lactamase, EC 3.5.2.6, sequence version 1; checked 2026-05-27

substrate: Cefuroxime


sequence_source: UniProt Q9K578 FASTA direct check on 2026-05-27

column_label: Official JBC Table II, WT cefotaxime, [Zn2+] = 100 uM: kcat 430 s^-1; Km 70 uM = 0.07 mM; printed kcat/Km 6.1 uM^-1 s^-1 = 6100 s^-1 mM^-1. Current 6142.857142857142 lies in rounding interval [6050, 6150) s^-1 mM^-1.

normalized_value_unit_evidence: The same high-zinc row normalizes to kcat=430 s^-1 and Km=0.07 mM. Their stored-precision quotient is 430 / 0.07 = 6142.857142857142 s^-1 mM^-1. The independently printed efficiency 6.1 uM^-1 s^-1 normalizes separately to 6100 s^-1 mM^-1.

raw_value_unit_evidence: kcat raw_value=430 raw_unit=s^-1; Km raw_value=70 raw_unit=uM; printed kcat/Km raw_value=6.1 raw_unit=uM^-1 s^-1

row_label: WT / cefotaxime / [Zn2+] = 100 uM

table_label: Table II: Kinetic parameters of the wild type enzyme (WT) and FEZ-1 mutant enzymes


substrate_name: Imipenem

substrate: Imipenem


sequence_source: UniProtKB Q9K578 FASTA direct lookup; canonical wild-type FEZ-1 sequence, 282 aa.


substrate_name: Meropenem

substrate: Meropenem


sequence_source: UniProt Q9K578 canonical sequence; PubMed 15159411 mutant context; RCSB FEZ-1 numbering map from 1L9Y/5WCK maps Y156A to UniProt residue 130; single substitution Y130A reconstructed.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +6, so it is treated as a source-provided variant sequence.


sequence_source: UniProt Q9K578 canonical sequence; PubMed 15159411 mutant context; RCSB FEZ-1 numbering map from 1L9Y/5WCK maps N225A to UniProt residue 197; single substitution N197A reconstructed.

sequence_variant_note: Mutation signature N225A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: Nitrocefin

sequence_source: UniProt Q9K578 canonical sequence; PubMed 15159411 mutant context; RCSB FEZ-1 numbering map from 1L9Y/5WCK maps S221A to UniProt residue 193; single substitution S193A reconstructed.

sequence_variant_note: Mutation signature S221A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Nitrocefin


substrate_name: 7-Aminocephalosporanic acid

sequence_source: UniProt Q9K578 canonical sequence; PubMed 15159411 mutant context; RCSB FEZ-1 numbering map from 1L9Y/5WCK maps Y228A to UniProt residue 200; single substitution Y200A reconstructed.

sequence_variant_note: Mutation signature Y228A matches the mutant residue at offset +7 and the reference residue at offset -13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: 7-Aminocephalosporanic acid


sequence_source: UniProtKB Q9K578 FASTA direct lookup on 2026-05-27


organism: Klebsiella pneumoniae

sequence_source: UniProtKB:Q8GD10 direct accession lookup on 2026-05-27

column_label: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-26 column block: kcat (s^-1) / Km (uM) / kcat per Km (uM^-1 s^-1); Cefuroxime row

normalized_value_unit_evidence: kcat 21.0 s^-1; Km 0.3 mM; kcat_over_km 70.0 s^-1 mM^-1 as the quotient of the same TABLE 3 row and same CTX-M-26 column-block kcat and Km cells; the paper's own printed ratio cell reads 0.07 uM^-1 s^-1 = 70.0 s^-1 mM^-1

raw_value_unit_evidence: kcat 21 s^-1; Km 300 uM; printed kcat/Km 0.07 uM^-1 s^-1

row_label: Cefuroxime row; CTX-M-26 column block (last three numeric cells)


column_label: Antimicrobial Agents and Chemotherapy 48(12):4829-4834 (2004); TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-26 column group; substrate row 'Cefotaxime': column 'kcat (s^-1)' = 120; column 'Km (uM)' = 150; column 'kcat/Km (uM^-1 s^-1)' = 0.77.

normalized_value_unit_evidence: Printed kcat 120 s^-1 is already the catalog unit s^(-1); no conversion needed; catalog kcat = 120.0. Printed Km 150 uM / 1000 = 0.15 mM, matching the catalog km 0.15 mM exactly. The paper does print a kcat/Km cell for this row, 0.77 uM^-1 s^-1 = 770.0 s^(-1)*mM^(-1), but that printed cell is NOT the catalog value: the catalog kcat_over_km 800.0 s^(-1)*mM^(-1) is the exact full-precision quotient of this row's own printed pair, 120.0 / 0.15. The printed cell is rounded (and for Benzylpenicillin is additionally off by a factor of ten against the paper's own pair), so the ratio is typed derived_same_measurement and the printed cell is documented in prose only.

raw_value_unit_evidence: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes, CTX-M-26 column group, substrate row 'Cefotaxime'; printed kcat (s^-1) 120, printed Km (uM) 150, printed kcat/Km (uM^-1 s^-1) 0.77. Printed units are s^-1 for kcat, uM (micro sign U+03BC) for Km, and uM^-1 s^-1 for kcat/Km; the exponents are U+2212 MINUS SIGN in the source markup.


substrate_name: aztreonam

column_label: Antimicrobial Agents and Chemotherapy 48(12):4829-4834 (2004); TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-26 column group; substrate row 'Aztreonam': column 'kcat (s^-1)' = 100; column 'Km (uM)' = 130; column 'kcat/Km (uM^-1 s^-1)' = 0.78.

normalized_value_unit_evidence: Printed kcat 100 s^-1 is already the catalog unit s^(-1); no conversion needed; catalog kcat = 100.0. Printed Km 130 uM / 1000 = 0.13 mM, matching the catalog km 0.13 mM exactly. The paper does print a kcat/Km cell for this row, 0.78 uM^-1 s^-1 = 780.0 s^(-1)*mM^(-1), but that printed cell is NOT the catalog value: the catalog kcat_over_km 769.2307692307692 s^(-1)*mM^(-1) is the exact full-precision quotient of this row's own printed pair, 100.0 / 0.13. The printed cell is rounded (and for Benzylpenicillin is additionally off by a factor of ten against the paper's own pair), so the ratio is typed derived_same_measurement and the printed cell is documented in prose only.

raw_value_unit_evidence: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes, CTX-M-26 column group, substrate row 'Aztreonam'; printed kcat (s^-1) 100, printed Km (uM) 130, printed kcat/Km (uM^-1 s^-1) 0.78. Printed units are s^-1 for kcat, uM (micro sign U+03BC) for Km, and uM^-1 s^-1 for kcat/Km; the exponents are U+2212 MINUS SIGN in the source markup.

substrate: aztreonam


column_label: Antimicrobial Agents and Chemotherapy 48(12):4829-4834 (2004); TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes; CTX-M-26 column group; substrate row 'Cephalothin': column 'kcat (s^-1)' = 530; column 'Km (uM)' = 110; column 'kcat/Km (uM^-1 s^-1)' = 4.7.

normalized_value_unit_evidence: Printed kcat 530 s^-1 is already the catalog unit s^(-1); no conversion needed; catalog kcat = 530.0. Printed Km 110 uM / 1000 = 0.11 mM, matching the catalog km 0.11 mM exactly. The paper does print a kcat/Km cell for this row, 4.7 uM^-1 s^-1 = 4700.0 s^(-1)*mM^(-1), but that printed cell is NOT the catalog value: the catalog kcat_over_km 4818.181818181818 s^(-1)*mM^(-1) is the exact full-precision quotient of this row's own printed pair, 530.0 / 0.11. The printed cell is rounded (and for Benzylpenicillin is additionally off by a factor of ten against the paper's own pair), so the ratio is typed derived_same_measurement and the printed cell is documented in prose only.

raw_value_unit_evidence: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes, CTX-M-26 column group, substrate row 'Cephalothin'; printed kcat (s^-1) 530, printed Km (uM) 110, printed kcat/Km (uM^-1 s^-1) 4.7. Printed units are s^-1 for kcat, uM (micro sign U+03BC) for Km, and uM^-1 s^-1 for kcat/Km; the exponents are U+2212 MINUS SIGN in the source markup.


organism: Klebsiella oxytoca

substrate_name: amoxicillin

column_label: Table 2, TEM-59 enzyme block; row Amoxicillin; column k cat (s^-1) cell 110; column K m (uM) cell 520; column k cat / K m (uM^-1 s^-1) cell 0.2.

normalized_value_unit_evidence: kcat 110 s^-1 = 110.0 s^(-1). Km 520 uM = 520 / 1000 = 0.52 mM. kcat/Km is recorded as the quotient of this row's own two printed cells: 110 s^-1 / 0.52 mM = 211.53846153846152 s^-1 mM^-1. Table 2 prints the ratio cell only to two significant figures (0.2 uM^-1 s^-1); that printed cell is the rounding of the same quotient and does not contradict it.

raw_value_unit_evidence: Table 2 of the PMC HTML asset, row Amoxicillin, TEM-59 enzyme block: kcat column cell 110 s^-1; Km column cell 520 uM; kcat/Km column cell 0.2 uM^-1 s^-1.

row_label: Amoxicillin

table_label: TABLE 2. Kinetics parameters of TEM-89 beta-lactamase compared with those of TEM-2, TEM-3, and TEM-59 beta-lactamases

substrate: amoxicillin


column_label: Table 2, TEM-59 enzyme block; row Benzylpenicillin; column k cat (s^-1) cell 200; column K m (uM) cell 140; column k cat / K m (uM^-1 s^-1) cell 1.4.

normalized_value_unit_evidence: kcat 200 s^-1 = 200.0 s^(-1). Km 140 uM = 140 / 1000 = 0.14 mM. kcat/Km is recorded as the quotient of this row's own two printed cells: 200 s^-1 / 0.14 mM = 1428.5714285714284 s^-1 mM^-1. Table 2 prints the ratio cell only to two significant figures (1.4 uM^-1 s^-1); that printed cell is the rounding of the same quotient and does not contradict it.

raw_value_unit_evidence: Table 2 of the PMC HTML asset, row Benzylpenicillin, TEM-59 enzyme block: kcat column cell 200 s^-1; Km column cell 140 uM; kcat/Km column cell 1.4 uM^-1 s^-1.


substrate_name: piperacillin

column_label: Table 2, TEM-59 enzyme block; row Piperacillin; column k cat (s^-1) cell 360; column K m (uM) cell 120; column k cat / K m (uM^-1 s^-1) cell 3.0.

normalized_value_unit_evidence: kcat 360 s^-1 = 360.0 s^(-1). Km 120 uM = 120 / 1000 = 0.12 mM. kcat/Km 3.0 uM^-1 s^-1 = 3.0 * 1000 = 3000.0 s^-1 mM^-1, which is also the exact quotient of this row's own printed cells.

raw_value_unit_evidence: Table 2 of the PMC HTML asset, row Piperacillin, TEM-59 enzyme block: kcat column cell 360 s^-1; Km column cell 120 uM; kcat/Km column cell 3.0 uM^-1 s^-1.

substrate: piperacillin


substrate_name: Ceftazidime

sequence_source: UniProtKB:Q8GD10 direct REST lookup on 2026-05-27

assay_conditions_summary: pH 7; 310.15 K; buffer 100 mM sodium phosphate

column_label: Table label: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes a. Row: Ceftazidime. Enzyme column group: CTX-M-26. Columns read: k cat (s^-1) cell 0.015, K m (uM) cell 3,300, k cat / K m (uM^-1 s^-1) cell ND. metric: kcat; raw value: 0.015; raw unit: s^-1; normalized value: 0.015 s^(-1); metric: Km; raw value: 3,300; raw unit: uM; normalized value: 3.3 mM; metric: kcat/Km; raw value: none printed (cell reads ND), derived from this row's own CTX-M-26 kcat and Km cells; raw unit: s^-1 mM^-1; normalized value: 0.004545454545454545 s^-1 mM^-1; assay condition: Purified CTX-M-26 beta-lactamase (recombinant); purified beta-lactamases were then used for kinetic measurements, which were performed at 37 C in 100 mM sodium phosphate buffer (pH 7. The bla CTX-M-26 gene was detected on a 100-kb plasmid isolated from a Klebsiella pneumoniae strain from the United Kingdom.

normalized_value_unit_evidence: CTX-M-26 columns of TABLE 3 row Ceftazidime: kcat 0.015 s^-1 = 0.015 s^(-1) (no conversion); Km 3,300 uM = 3.3 mM (1 uM = 0.001 mM, and the printed thousands comma in `3,300` is a digit-group separator, so the cell is three thousand three hundred micromolar); kcat/Km is printed ND in this cell, so the export ratio is the quotient of this same row's own CTX-M-26 cells: 0.015 s^-1 / 3.3 mM = 0.004545454545454545 s^-1 mM^-1. In the on-disk text the micro sign renders as μ, the superscript minus one as −1, and superscripts are flattened, so `k cat (s −1 )` is the paper's k_cat (s^-1) and `K m (μM)` is the paper's K_m (uM).

raw_value_unit_evidence: TABLE 3. Steady-state kinetics of purified CTX-M-25 and CTX-M-26 enzymes a | enzyme column group header row: Substrate CTX-M-25 CTX-M-26; metric header row: k cat (s −1 ) K m (μM) k cat / K m (μM −1 s −1 ) k cat (s −1 ) K m (μM) k cat / K m (μM −1 s −1 ) | row: Ceftazidime 33 13 2.6 0.015 3,300 ND | the first three cells belong to CTX-M-25 and are not used here; the CTX-M-26 cells read: k cat = 0.015 s^-1; K m = 3,300 uM; k cat / K m = ND (not determinable).

row_label: CTX-M-26 | Ceftazidime

substrate: Ceftazidime


column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Ampicillin; CTX-M-26 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 12, 24, 0.5

raw_value_unit_evidence: CTX-M-26 / Ampicillin: kcat=12 s^-1; Km=24 uM; kcat/Km=0.5 uM^-1 s^-1

row_label: CTX-M-26 / Ampicillin


sequence_source: UniProtKB:P0AD64 canonical sequence checked on 2026-05-27; row-specific R244S variant not reconstructed


sequence_source: UniProtKB:P0AD64 canonical sequence checked on 2026-05-27; row-specific R244L variant not reconstructed


sequence_source: UniProtKB:P0AD64 canonical sequence checked on 2026-05-27; row-specific R244Q variant not reconstructed


sequence_source: UniProt Q9K578 REST accession lookup on 2026-05-27

column_label: Official JBC Table II, WT Nitrocefin, [Zn2+] = 100 uM: kcat 600 s^-1; Km 190 uM = 0.19 mM; printed kcat/Km 3.2 uM^-1 s^-1 = 3200 s^-1 mM^-1. Current 3157.8947368421054 lies in rounding interval [3150, 3250) s^-1 mM^-1.

normalized_value_unit_evidence: The same high-zinc row normalizes to kcat=600 s^-1 and Km=0.19 mM. Their stored-precision quotient is 600 / 0.19 = 3157.8947368421054 s^-1 mM^-1. The independently printed efficiency 3.2 uM^-1 s^-1 normalizes separately to 3200 s^-1 mM^-1.

raw_value_unit_evidence: kcat raw_value=600 raw_unit=s^-1; Km raw_value=190 raw_unit=uM; printed kcat/Km raw_value=3.2 raw_unit=uM^-1 s^-1

row_label: WT / Nitrocefin / [Zn2+] = 100 uM


substrate_name: meropenem

substrate: meropenem


substrate_name: panipenem

substrate: panipenem


substrate_name: ampicillin

substrate: ampicillin


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AD64 canonical sequence retrieved 2026-05-27; D104K reconstructed by applying the SHV/Ambler D104K change to the P0AD64 sequence at computed sequence coordinate 100. and applied mutation signature D104K with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0AD64 canonical sequence retrieved 2026-05-27; D104K reconstructed by applying the SHV/Ambler D104K change to the P0AD64 sequence at computed sequence coordinate 100.


substrate_name: Ampicillin

sequence_source: UniProtKB:P0AD64 canonical sequence retrieved 2026-05-27.

substrate: Ampicillin


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AD64 canonical sequence retrieved 2026-05-27; G238S reconstructed by applying the SHV/Ambler G238S change to the P0AD64 sequence at computed sequence coordinate 234. and applied mutation signature G238S with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0AD64 canonical sequence retrieved 2026-05-27; G238S reconstructed by applying the SHV/Ambler G238S change to the P0AD64 sequence at computed sequence coordinate 234.


substrate_name: cefepime

sequence_source: UniProtKB:Q8KQ59 exact accession REST lookup, accessed 2026-05-27

substrate: cefepime


substrate_name: cephalotin

substrate: cephalotin


substrate_name: ceftazidime

substrate: ceftazidime


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: doripenem

substrate: doripenem


substrate_name: Cephalothin

sequence_source: UniProtKB reviewed accession P0AD64 direct REST/FASTA check

column_label: Table 4, Cephalothin block, enzyme sub-row `SHV-1` (the dagger-marked reference beta-lactamase, Ratio = 1.00): column `Km (uM)` = 48 +/- 3; column `kcat (s^-1)` = 25.0 +/- 0.7; column `kcat/Km (uM^-1 s^-1)` = 0.50 +/- 0.03; column `Ratio` = 1.00. The variant sub-rows of the same block print Asp104Lys 20 +/- 3 uM with 7.4 +/- 0.1 s^-1, Gly238Ser 3.3 +/- 0.1 uM with 15.0 +/- 0.3 s^-1, and Asp104Lys Gly238Ser 3.0 +/- 0.1 uM with 11.4 +/- 0.3 s^-1.

normalized_value_unit_evidence: Km: paper cell 48 +/- 3 in the column headed `Km (uM)` (micro sign read off the 300 dpi render of journal page 4127); 48.0 uM / 1000 = 0.048 mM, exactly the catalog km 0.048 mM. kcat: paper cell 25.0 +/- 0.7 in the column headed `kcat (s^-1)`; the paper already prints per-second turnover numbers, so no min^-1/60 conversion applies and the value equals the catalog kcat 25.0 s^(-1). kcat/Km: Table 4 prints a kcat/Km cell for this sub-row, 0.50 +/- 0.03 uM^-1 s^-1, which normalizes to 500.0 s^(-1)*mM^(-1) (x 1000 for uM^-1 -> mM^-1). The catalog value 520.8333333333334 s^(-1)*mM^(-1) is NOT that printed cell: it is the exact full-precision quotient of this row's own printed cells, 25.0 s^-1 / 0.048 mM. The printed cell is the two-significant-figure rounding of that quotient, so the two agree to the printed precision while differing as stored numbers. paper_kcat_over_km_s^-1_mM^-1 is therefore left null and the printed cell is documented in prose rather than claimed as the source of the stored value.

raw_value_unit_evidence: Table 4 (journal page 4127), Cephalothin block, enzyme sub-row `SHV-1`: Km = `48 +/- 3` uM; kcat = `25.0 +/- 0.7` s^-1; kcat/Km = `0.50 +/- 0.03` uM^-1 s^-1; Ratio = `1.00`. Table 4 footnote a: data are presented as means +/- standard deviations.

table_label: TABLE 4. Steady-state kinetic parameters

substrate: Cephalothin


substrate_name: cefalotin

substrate: cefalotin


substrate_name: nitrocefin

substrate: nitrocefin


sequence_source: UniProtKB:Q9F918 direct REST lookup on 2026-05-27

column_label: PMID 29228168 Table 3. Kinetics analysis of SHV-14 and its mutated proteins.; substrate sub-header Nitrocefin; SHV-14 (wild type) column; printed cells Km 45 ± 1.7 uM, kcat 5.85 ± 0.2 s^-1, kcat /KM 0.13 s^-1 uM^-1. The paper's printed kcat/KM cell for this row (0.13 s^-1 uM^-1 in the units printed as kcat /KM (s-1 uM-1)) is a rounded two-to-three-significant-figure value; the exported ratio is the exact quotient of this same row's two printed primary cells, so the printed cell is reported here but is not used as a raw value.

raw_value_unit_evidence: Table row as printed (SHV-14 wild-type column): Km 45 ± 1.7 uM; kcat 5.85 ± 0.2 s^-1; kcat /KM 0.13 s^-1 uM^-1.

row_label: Nitrocefin / SHV-14 column (wild type)


substrate_name: cefoperazone

column_label: PMID 29228168 Table 3. Kinetics analysis of SHV-14 and its mutated proteins.; substrate sub-header Cefoperazone; SHV-14 (wild type) column; printed cells Km 57.4 ± 6 uM, kcat 229.5 ± 10.6 s^-1, kcat /KM 4 s^-1 uM^-1. The paper's printed kcat/KM cell for this row (4 s^-1 uM^-1 in the units printed as kcat /KM (s-1 uM-1)) is a rounded two-to-three-significant-figure value; the exported ratio is the exact quotient of this same row's two printed primary cells, so the printed cell is reported here but is not used as a raw value.

raw_value_unit_evidence: Table row as printed (SHV-14 wild-type column): Km 57.4 ± 6 uM; kcat 229.5 ± 10.6 s^-1; kcat /KM 4 s^-1 uM^-1.

row_label: Cefoperazone / SHV-14 column (wild type)

substrate: cefoperazone


substrate_name: cefuroxime

sequence_source: UniProtKB Q8KQ59 FASTA checked 2026-05-27; cross-checked GenBank AY101764/AAM52215.1 translation.

substrate: cefuroxime


substrate_name: aztreonam

substrate: aztreonam


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: piperacillin

substrate: piperacillin


substrate_name: Ceftazidime

sequence_source: UniProtKB C7C422 FASTA/REST checked 2026-05-27

assay_conditions_summary: pH 7; 303.15 K; buffer dilution

column_label: The literal Ceftazidime/Wild type NDM-1 row binds substrate, variant, Km, kcat, and printed efficiency. Current Km is the stored-precision rounding of the printed cell.

normalized_value_unit_evidence: paper Km=0.03843 mM, rounded current Km=0.038 mM; kcat=119.2 s^-1; current same-row quotient=3136.842105263158; printed efficiency=3102 +/- 178.6 s^-1 mM^-1.

row_label: Ceftazidime | Wild type NDM-1

table_label: Table 2 Steady-state enzyme kinetics of wild-type NDM-1 enzyme and NDM-1Q123A mutant enzyme

substrate: Ceftazidime


substrate_name: Nitrocefin

column_label: The literal Nitrocefin/Wild type NDM-1 row binds substrate, variant, Km, kcat, and printed efficiency. Current Km is the stored-precision rounding of the printed cell.

normalized_value_unit_evidence: paper Km=0.01272 mM, rounded current Km=0.013 mM; kcat=1.332 s^-1; current same-row quotient=102.46153846153847 s^-1 mM^-1; printed efficiency=104 +/- 475.1 s^-1 mM^-1.

row_label: Nitrocefin | Wild type NDM-1

substrate: Nitrocefin


sequence_source: UniProtKB C7C422 FASTA/REST checked 2026-05-27; Q123A reconstructed from canonical residue 123 Q and PMID 29454953 mutation description

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


column_label: The literal Ampicillin/Wild type NDM-1 row binds substrate, variant, Km, kcat, and printed efficiency.

row_label: Ampicillin | Wild type NDM-1


substrate_name: Meropenem

substrate: Meropenem


column_label: PMID 29228168 Table 3. Kinetics analysis of SHV-14 and its mutated proteins.; substrate sub-header Piperacillin; SHV-14 (wild type) column; printed cells Km 58 ± 3 uM, kcat 677 ± 7 s^-1, kcat /KM 11.6 s^-1 uM^-1. The paper's printed kcat/KM cell for this row (11.6 s^-1 uM^-1 in the units printed as kcat /KM (s-1 uM-1)) is a rounded two-to-three-significant-figure value; the exported ratio is the exact quotient of this same row's two printed primary cells, so the printed cell is reported here but is not used as a raw value.

raw_value_unit_evidence: Table row as printed (SHV-14 wild-type column): Km 58 ± 3 uM; kcat 677 ± 7 s^-1; kcat /KM 11.6 s^-1 uM^-1.

row_label: Piperacillin / SHV-14 column (wild type)


substrate_name: ampicillin

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9F918 and applied mutation signature E164A to reconstruct the assayed variant sequence.

substrate: ampicillin


substrate_name: amoxicillin

substrate: amoxicillin


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9F918 and applied mutation signature E162A to reconstruct the assayed variant sequence.


substrate_name: cephalothin

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

column_label: PMID 29228168 Table 3. Kinetics analysis of SHV-14 and its mutated proteins.; substrate sub-header Cephalothin; SHV-14 (wild type) column; printed cells Km 45 ± 5 uM, kcat 113 ± 21 s^-1, kcat /KM 2.5 s^-1 uM^-1. The paper's printed kcat/KM cell for this row (2.5 s^-1 uM^-1 in the units printed as kcat /KM (s-1 uM-1)) is a rounded two-to-three-significant-figure value; the exported ratio is the exact quotient of this same row's two printed primary cells, so the printed cell is reported here but is not used as a raw value.

raw_value_unit_evidence: Table row as printed (SHV-14 wild-type column): Km 45 ± 5 uM; kcat 113 ± 21 s^-1; kcat /KM 2.5 s^-1 uM^-1.

row_label: Cephalothin / SHV-14 column (wild type)

substrate: cephalothin


column_label: Table 3 (Kinetics analysis of SHV-14 and its mutated proteins); the three enzyme column heads are 'SHV-14', 'SHV-14_E162A' and 'SHV-14_E164A'; this record reads the first of them, the wild-type column. Antibiotic block 'Ampicillin'; metric row 'Km (uM)' = 32; metric row 'kcat (s^-1)' = 544; metric row 'kcat/KM (s^-1 uM^-1)' = 8.5.

normalized_value_unit_evidence: Km: printed Table 3 cell 32 uM for the Ampicillin block, wild-type SHV-14 column; 32 / 1000 = 0.032 mM; the exported value is 0.032 mM. kcat: printed Table 3 cell 544 s^-1 for the same cell tuple; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 544.0 s^(-1). kcat/Km: printed Table 3 cell 8.5 s^-1 uM^-1 for the same cell tuple; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 8.5 x 1000 = 8500.0 s^-1 mM^-1; the exported value is 17000.0 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 3, antibiotic block 'Ampicillin', enzyme column 'SHV-14' (the wild-type column): Km = 32 uM; kcat = 544 s^-1; printed kcat/KM = 8.5 s^-1 uM^-1.

table_label: Table 3: Kinetics analysis of SHV-14 and its mutated proteins (FEMS Microbiology Letters 2018, 365, article fnx259)


sequence_source: UniProtKB Q9F918 REST lookup on 2026-05-27; canonical residue 162 was E and was changed to A for the selected E162A row.


sequence_source: UniProtKB Q9F918 REST lookup on 2026-05-27; canonical residue 164 was E and was changed to A for the selected E164A row.


substrate_name: Oxacillin

sequence_source: UniProtKB Q6XEC0 FASTA direct lookup

substrate: Oxacillin


substrate_name: Temocillin

substrate: Temocillin


substrate_name: Faropenem

substrate: Faropenem


substrate_name: temocillin

proof_lines:
pH 7.0, 30°C
Raw SKiD Env: Temp=30°C, pH=7

source_db: brenda

substrate: temocillin


substrate_name: Ertapenem

substrate: Ertapenem


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Ampicillin

sequence_source: Reconstructed from UniProtKB C7C422 FASTA by Q123A after direct residue check on 2026-05-27.

substrate: Ampicillin


substrate_name: cefoxitin

substrate: cefoxitin


sequence_source: UniProtKB C7C422 FASTA via UniProt REST; direct check on 2026-05-27.


column_label: The literal Cefotaxime/Wild type NDM-1 row binds substrate, variant, Km, kcat, and printed efficiency. Current Km is the stored-precision rounding of the printed cell.

normalized_value_unit_evidence: paper Km=0.03194 mM, rounded current Km=0.032 mM; kcat=84.84 s^-1; current same-row quotient=2651.25; printed efficiency=2631 +/- 347.1 s^-1 mM^-1.

row_label: Cefotaxime | Wild type NDM-1


organism: Moraxella catarrhalis

substrate_name: Loracarbef

sequence_source: UniProtKB:Q49095 direct accession lookup, 2026-05-27

column_label: Table 3 row 'Loracarbef', BRO-2p sub-column of each column group: Km 38 uM, kcat 95 s^-1, Specificity 2.5 in units of 10^6 M^-1 s^-1 (footnote b, L . s-1 . umol-1). Km 38 uM normalizes to 0.038 mM and kcat 95 s^-1 divided by that Km gives 2.5E+3 s^-1 mM^-1, which is the currently exported kcat/Km for this identity.

normalized_value_unit_evidence: Km 38 uM = 0.038 mM; kcat 95 s^-1; kcat/Km = 95 / 38 (s^-1 per uM) = 2500 s^-1 mM^-1. The printed Specificity cell 2.5 x 10^6 M^-1 s^-1 is that same quotient carried to the two significant figures the column prints.

raw_value_unit_evidence: Table 3 row Loracarbef, BRO-2p columns: Km 38 uM; kcat 95 s^-1; Specificity 2.5 (10^6 M^-1 s^-1).

row_label: Loracarbef | BRO-2p column

table_label: Table 3: Kinetic constants of the BRO-lp and BRO-2p 13-1actamases of Branhamella catarrhalis as determined speetrophotometrieally using the Tl/2 method.

substrate: Loracarbef


substrate_name: mecillinam

column_label: Table 3 row 'MeeiUinam', BRO-2p sub-column of each column group: Km 63 uM, kcat 29 s^-1, Specificity 0.46 in units of 10^6 M^-1 s^-1 (footnote b, L . s-1 . umol-1). Km 63 uM normalizes to 0.063 mM and kcat 29 s^-1 divided by that Km gives 460.3174603174603174603174603174603 s^-1 mM^-1, which is the currently exported kcat/Km for this identity.

normalized_value_unit_evidence: Km 63 uM = 0.063 mM; kcat 29 s^-1; kcat/Km = 29 / 63 (s^-1 per uM) = 460.3174603174603174603174603174603 s^-1 mM^-1. The printed Specificity cell 0.46 x 10^6 M^-1 s^-1 is that same quotient carried to the two significant figures the column prints.

raw_value_unit_evidence: Table 3 row MeeiUinam, BRO-2p columns: Km 63 uM; kcat 29 s^-1; Specificity 0.46 (10^6 M^-1 s^-1).

row_label: MeeiUinam | BRO-2p column

substrate: mecillinam


sequence_source: UniProtKB:Q59514 direct accession lookup, 2026-05-27

column_label: Table 3 row 'Loracarbef', BRO-1p sub-column of each column group: Km 50 uM, kcat 79 s^-1, Specificity 1.6 in units of 10^6 M^-1 s^-1 (footnote b, L . s-1 . umol-1). Km 50 uM normalizes to 0.05 mM and kcat 79 s^-1 divided by that Km gives 1.58E+3 s^-1 mM^-1, which is the currently exported kcat/Km for this identity.

normalized_value_unit_evidence: Km 50 uM = 0.05 mM; kcat 79 s^-1; kcat/Km = 79 / 50 (s^-1 per uM) = 1580 s^-1 mM^-1. The printed Specificity cell 1.6 x 10^6 M^-1 s^-1 is that same quotient carried to the two significant figures the column prints.

raw_value_unit_evidence: Table 3 row Loracarbef, BRO-1p columns: Km 50 uM; kcat 79 s^-1; Specificity 1.6 (10^6 M^-1 s^-1).

row_label: Loracarbef | BRO-1p column


substrate_name: Cephalosporin C

column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Cephalosporin C'; enzyme column 'BRO-1p'; column 'Km^a (uM)' = 3.9; column 'kcat^b (s^-1)' = 5.0; column 'Specificity (kcat/Km)' = 1.3 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 3.9 uM; 3.9 / 1000 = 0.0039 mM; the exported value is 0.004 mM. kcat: printed Table 3 cell 5.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 5.0 s^(-1). kcat/Km: printed Table 3 Specificity cell 1.3 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 1.3 x 1000 = 1300.0 s^-1 mM^-1; the exported value is 1250.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Cephalosporin C', enzyme column 'BRO-1p': Km = 3.9 uM; kcat = 5.0 s^-1; printed Specificity (kcat/Km) = 1.3 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Cephalosporin C', enzyme column 'BRO-1p' (Branhamella catarrhalis strain L14)

substrate: Cephalosporin C


substrate_name: Cephalothin

column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Cephalothin'; enzyme column 'BRO-2p'; column 'Km^a (uM)' = 1.2; column 'kcat^b (s^-1)' = 4.6; column 'Specificity (kcat/Km)' = 4.0 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 1.2 uM; 1.2 / 1000 = 0.0012 mM; the exported value is 0.001 mM. kcat: printed Table 3 cell 4.6 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 4.6 s^(-1). kcat/Km: printed Table 3 Specificity cell 4.0 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 4.0 x 1000 = 4000.0 s^-1 mM^-1; the exported value is 4600.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Cephalothin', enzyme column 'BRO-2p': Km = 1.2 uM; kcat = 4.6 s^-1; printed Specificity (kcat/Km) = 4.0 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Cephalothin', enzyme column 'BRO-2p' (Branhamella catarrhalis strain L16904)

substrate: Cephalothin


column_label: Table 3 row 'Cephalothin', BRO-1p sub-column of each column group: Km 0.9 uM, kcat 4.9 s^-1, Specificity 5.5 in units of 10^6 M^-1 s^-1 (footnote b, L . s-1 . umol-1). Km 0.9 uM normalizes to 0.0009 mM and kcat 4.9 s^-1 divided by that Km gives 5444.444444444444444444444444444444 s^-1 mM^-1, which is the currently exported kcat/Km for this identity.

normalized_value_unit_evidence: Km 0.9 uM = 0.0009 mM; kcat 4.9 s^-1; kcat/Km = 4.9 / 0.9 (s^-1 per uM) = 5444.444444444444444444444444444444 s^-1 mM^-1. The printed Specificity cell 5.5 x 10^6 M^-1 s^-1 is that same quotient carried to the two significant figures the column prints.

raw_value_unit_evidence: Table 3 row Cephalothin, BRO-1p columns: Km 0.9 uM; kcat 4.9 s^-1; Specificity 5.5 (10^6 M^-1 s^-1).

row_label: Cephalothin | BRO-1p column


substrate_name: Cephaloridine

column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Cephaloridine'; enzyme column 'BRO-1p'; column 'Km^a (uM)' = 1.7; column 'kcat^b (s^-1)' = 4.8; column 'Specificity (kcat/Km)' = 2.8 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 1.7 uM; 1.7 / 1000 = 0.0017 mM; the exported value is 0.002 mM. kcat: printed Table 3 cell 4.8 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 4.8 s^(-1). kcat/Km: printed Table 3 Specificity cell 2.8 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 2.8 x 1000 = 2800.0 s^-1 mM^-1; the exported value is 2400.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Cephaloridine', enzyme column 'BRO-1p': Km = 1.7 uM; kcat = 4.8 s^-1; printed Specificity (kcat/Km) = 2.8 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Cephaloridine', enzyme column 'BRO-1p' (Branhamella catarrhalis strain L14)

substrate: Cephaloridine


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9NWK5 canonical sequence fetched during review; L209F reconstructed after confirming residue 209 is L. and applied mutation signature L209F to reconstruct the assayed variant sequence.


substrate_name: Meropenem

sequence_source: UniProtKB:E9NWK5 canonical sequence fetched during review; L209F reconstructed after confirming residue 209 is L.

substrate: Meropenem


substrate_name: biapenem

substrate: biapenem


substrate_name: cefazolin

substrate: cefazolin


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: H2O; Imipenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant L209F

substrate: H2O; Imipenem


substrate_name: carbenicillin

substrate: carbenicillin


organism: Kluyvera ascorbata

substrate_name: Nitrocefin

sequence_source: UniProtKB:Q8VKT5 direct REST lookup on 2026-05-27

substrate: Nitrocefin


sequence_source: UniProtKB:Q49095 direct REST lookup on 2026-05-27

column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Cephaloridine'; enzyme column 'BRO-2p'; column 'Km^a (uM)' = 2.8; column 'kcat^b (s^-1)' = 5.6; column 'Specificity (kcat/Km)' = 2.0 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 2.8 uM; 2.8 / 1000 = 0.0028 mM; the exported value is 0.003 mM. kcat: printed Table 3 cell 5.6 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 5.6 s^(-1). kcat/Km: printed Table 3 Specificity cell 2.0 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 2.0 x 1000 = 2000.0 s^-1 mM^-1; the exported value is 1866.6666666666665 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Cephaloridine', enzyme column 'BRO-2p': Km = 2.8 uM; kcat = 5.6 s^-1; printed Specificity (kcat/Km) = 2.0 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Cephaloridine', enzyme column 'BRO-2p' (Branhamella catarrhalis strain L16904)


column_label: Table 3 row 'Cephalosporin C', BRO-2p sub-column of each column group: Km 3.0 uM, kcat 4.7 s^-1, Specificity 1.6 in units of 10^6 M^-1 s^-1 (footnote b, L . s-1 . umol-1). Km 3.0 uM normalizes to 0.003 mM and kcat 4.7 s^-1 divided by that Km gives 1566.666666666666666666666666666667 s^-1 mM^-1, which is the currently exported kcat/Km for this identity.

normalized_value_unit_evidence: Km 3.0 uM = 0.003 mM; kcat 4.7 s^-1; kcat/Km = 4.7 / 3.0 (s^-1 per uM) = 1566.666666666666666666666666666667 s^-1 mM^-1. The printed Specificity cell 1.6 x 10^6 M^-1 s^-1 is that same quotient carried to the two significant figures the column prints.

raw_value_unit_evidence: Table 3 row Cephalosporin C, BRO-2p columns: Km 3.0 uM; kcat 4.7 s^-1; Specificity 1.6 (10^6 M^-1 s^-1).

row_label: Cephalosporin C | BRO-2p column


substrate_name: Cefuroxime

sequence_source: UniProtKB Q59514 reviewed Swiss-Prot BLA1_MORCA; direct lookup 2026-05-27

column_label: Table 3 row 'Cefuroxim¢', BRO-1p sub-column of each column group: Km 68 uM, kcat 4.1 s^-1, Specificity 0.086 in units of 10^6 M^-1 s^-1 (footnote b, L . s-1 . umol-1). Km 68 uM normalizes to 0.068 mM and kcat 4.1 s^-1 divided by that Km gives 60.29411764705882352941176470588235 s^-1 mM^-1, which is the currently exported kcat/Km for this identity.

normalized_value_unit_evidence: Km 68 uM = 0.068 mM; kcat 4.1 s^-1; kcat/Km = 4.1 / 68 (s^-1 per uM) = 60.29411764705882352941176470588235 s^-1 mM^-1. The printed Specificity cell 0.086 x 10^6 M^-1 s^-1 is that same quotient carried to the two significant figures the column prints.

raw_value_unit_evidence: Table 3 row Cefuroxim¢, BRO-1p columns: Km 68 uM; kcat 4.1 s^-1; Specificity 0.086 (10^6 M^-1 s^-1).

row_label: Cefuroxim¢ | BRO-1p column

substrate: Cefuroxime


substrate_name: Methicillin

assay_conditions_summary: pH 7; 303.15 K; buffer 20 mM TEA-HCl / 0.15 M NaCl

column_label: Table 3. Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method; row Methicillin; column group Km^a (uM), column BRO-1p: raw value 34 uM, normalized value 0.034 mM; column group kcat^b (s^-1), column BRO-1p: raw value 168 s^-1, normalized value 168 s^-1; column group Specificity (kcat/Km), column BRO-1p: the table prints 4.9 in units of 10^6 M^-1 s^-1, a two-significant-figure value that agrees with the quotient of this same row and column pair, so the absolute ratio recorded here is that quotient 168 / 0.034 = 4941.176470588235 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 168; raw unit: s^-1; normalized value: 168; normalized unit: s^-1; metric: Km; raw value: 34; raw unit: uM; normalized value: 0.034; normalized unit: mM; metric: kcat/Km; the table prints only the rounded specificity column, so the absolute ratio recorded here is the quotient of this row's own two printed cells, paper kcat divided by paper Km; normalized value: 4941.176470588235; normalized unit: s^-1 mM^-1; assay condition: Purified papain-solubilized BRO-1p (strain L14) or BRO-2p (strain L16904) beta-lactamase; spectrophotometric progress curves analysed by the T1/2 method in 20 mM TEA-HCl / 0.15 M NaCl buffer, pH 7.0, at a constant temperature of 30 C.

raw_value_unit_evidence: Table 3. Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method (PDF page 6, journal page 318), row Methicillin: kcat^b (s^-1) column BRO-1p prints 168; Km^a (uM) column BRO-1p prints 34; Specificity (kcat/Km) column BRO-1p prints 4.9 in units of 10^6 M^-1 s^-1. Footnote a: Mean of three values.

row_label: Methicillin

substrate: Methicillin


column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Nitrocefin'; enzyme column 'BRO-1p'; column 'Km^a (uM)' = 6.9; column 'kcat^b (s^-1)' = 151; column 'Specificity (kcat/Km)' = 22 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 6.9 uM; 6.9 / 1000 = 0.0069 mM; the exported value is 0.007 mM. kcat: printed Table 3 cell 151 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 151.0 s^(-1). kcat/Km: printed Table 3 Specificity cell 22 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 22 x 1000 = 22000.0 s^-1 mM^-1; the exported value is 21571.428571428572 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Nitrocefin', enzyme column 'BRO-1p': Km = 6.9 uM; kcat = 151 s^-1; printed Specificity (kcat/Km) = 22 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Nitrocefin', enzyme column 'BRO-1p' (Branhamella catarrhalis strain L14)


column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Ampicillin'; enzyme column 'BRO-1p'; column 'Km^a (uM)' = 2.5; column 'kcat^b (s^-1)' = 33; column 'Specificity (kcat/Km)' = 14 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 2.5 uM; 2.5 / 1000 = 0.0025 mM; the exported value is 0.003 mM. kcat: printed Table 3 cell 33 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 33.0 s^(-1). kcat/Km: printed Table 3 Specificity cell 14 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 14 x 1000 = 14000.0 s^-1 mM^-1; the exported value is 11000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Ampicillin', enzyme column 'BRO-1p': Km = 2.5 uM; kcat = 33 s^-1; printed Specificity (kcat/Km) = 14 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Ampicillin', enzyme column 'BRO-1p' (Branhamella catarrhalis strain L14)


column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Benzylpenicillin'; enzyme column 'BRO-1p'; column 'Km^a (uM)' = 2.7; column 'kcat^b (s^-1)' = 40; column 'Specificity (kcat/Km)' = 14 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 2.7 uM; 2.7 / 1000 = 0.0027 mM; the exported value is 0.003 mM. kcat: printed Table 3 cell 40 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 40.0 s^(-1). kcat/Km: printed Table 3 Specificity cell 14 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 14 x 1000 = 14000.0 s^-1 mM^-1; the exported value is 13333.333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Benzylpenicillin', enzyme column 'BRO-1p': Km = 2.7 uM; kcat = 40 s^-1; printed Specificity (kcat/Km) = 14 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Benzylpenicillin', enzyme column 'BRO-1p' (Branhamella catarrhalis strain L14)


sequence_source: UniProtKB Q49095 unreviewed TrEMBL; direct lookup 2026-05-27

column_label: Table 3. Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method; row Methicillin; column group Km^a (uM), column BRO-2p: raw value 26 uM, normalized value 0.026 mM; column group kcat^b (s^-1), column BRO-2p: raw value 190 s^-1, normalized value 190 s^-1; column group Specificity (kcat/Km), column BRO-2p: the table prints 7.3 in units of 10^6 M^-1 s^-1, a two-significant-figure value that agrees with the quotient of this same row and column pair, so the absolute ratio recorded here is that quotient 190 / 0.026 = 7307.692307692308 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 190; raw unit: s^-1; normalized value: 190; normalized unit: s^-1; metric: Km; raw value: 26; raw unit: uM; normalized value: 0.026; normalized unit: mM; metric: kcat/Km; the table prints only the rounded specificity column, so the absolute ratio recorded here is the quotient of this row's own two printed cells, paper kcat divided by paper Km; normalized value: 7307.692307692308; normalized unit: s^-1 mM^-1; assay condition: Purified papain-solubilized BRO-1p (strain L14) or BRO-2p (strain L16904) beta-lactamase; spectrophotometric progress curves analysed by the T1/2 method in 20 mM TEA-HCl / 0.15 M NaCl buffer, pH 7.0, at a constant temperature of 30 C.

raw_value_unit_evidence: Table 3. Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method (PDF page 6, journal page 318), row Methicillin: kcat^b (s^-1) column BRO-2p prints 190; Km^a (uM) column BRO-2p prints 26; Specificity (kcat/Km) column BRO-2p prints 7.3 in units of 10^6 M^-1 s^-1. Footnote a: Mean of three values.


column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Benzylpenicillin'; enzyme column 'BRO-2p'; column 'Km^a (uM)' = 2.9; column 'kcat^b (s^-1)' = 41; column 'Specificity (kcat/Km)' = 14 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 2.9 uM; 2.9 / 1000 = 0.0029 mM; the exported value is 0.003 mM. kcat: printed Table 3 cell 41 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 41.0 s^(-1). kcat/Km: printed Table 3 Specificity cell 14 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 14 x 1000 = 14000.0 s^-1 mM^-1; the exported value is 13666.666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Benzylpenicillin', enzyme column 'BRO-2p': Km = 2.9 uM; kcat = 41 s^-1; printed Specificity (kcat/Km) = 14 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Benzylpenicillin', enzyme column 'BRO-2p' (Branhamella catarrhalis strain L16904)


substrate_name: Cefaclor

sequence_source: UniProtKB:Q59514; direct REST accession check on 2026-05-27

column_label: Table 3. Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method; row Cefaclor; column group Km^a (uM), column BRO-1p: raw value 34 uM, normalized value 0.034 mM; column group kcat^b (s^-1), column BRO-1p: raw value 65 s^-1, normalized value 65 s^-1; column group Specificity (kcat/Km), column BRO-1p: the table prints 1.9 in units of 10^6 M^-1 s^-1, a two-significant-figure value that agrees with the quotient of this same row and column pair, so the absolute ratio recorded here is that quotient 65 / 0.034 = 1911.7647058823527 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 65; raw unit: s^-1; normalized value: 65; normalized unit: s^-1; metric: Km; raw value: 34; raw unit: uM; normalized value: 0.034; normalized unit: mM; metric: kcat/Km; the table prints only the rounded specificity column, so the absolute ratio recorded here is the quotient of this row's own two printed cells, paper kcat divided by paper Km; normalized value: 1911.7647058823527; normalized unit: s^-1 mM^-1; assay condition: Purified papain-solubilized BRO-1p (strain L14) or BRO-2p (strain L16904) beta-lactamase; spectrophotometric progress curves analysed by the T1/2 method in 20 mM TEA-HCl / 0.15 M NaCl buffer, pH 7.0, at a constant temperature of 30 C.

raw_value_unit_evidence: Table 3. Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method (PDF page 6, journal page 318), row Cefaclor: kcat^b (s^-1) column BRO-1p prints 65; Km^a (uM) column BRO-1p prints 34; Specificity (kcat/Km) column BRO-1p prints 1.9 in units of 10^6 M^-1 s^-1. Footnote a: Mean of three values.

row_label: Cefaclor

substrate: Cefaclor


substrate_name: Cloxacillin

column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Cloxacillin'; enzyme column 'BRO-1p'; column 'Km^a (uM)' = 1.4; column 'kcat^b (s^-1)' = 5; column 'Specificity (kcat/Km)' = 3.6 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 1.4 uM; 1.4 / 1000 = 0.0014 mM; the exported value is 0.001 mM. kcat: printed Table 3 cell 5 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 5.0 s^(-1). kcat/Km: printed Table 3 Specificity cell 3.6 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 3.6 x 1000 = 3600.0 s^-1 mM^-1; the exported value is 5000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Cloxacillin', enzyme column 'BRO-1p': Km = 1.4 uM; kcat = 5 s^-1; printed Specificity (kcat/Km) = 3.6 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Cloxacillin', enzyme column 'BRO-1p' (Branhamella catarrhalis strain L14)

substrate: Cloxacillin


sequence_source: UniProtKB:Q49095; direct REST accession check on 2026-05-27

column_label: Table 3. Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method; row Nitroeefin; column group Km^a (uM), column BRO-2p: raw value 11 uM, normalized value 0.011 mM; column group kcat^b (s^-1), column BRO-2p: raw value 233 s^-1, normalized value 233 s^-1; column group Specificity (kcat/Km), column BRO-2p: the table prints 21 in units of 10^6 M^-1 s^-1, a two-significant-figure value that agrees with the quotient of this same row and column pair, so the absolute ratio recorded here is that quotient 233 / 0.011 = 21181.818181818184 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 233; raw unit: s^-1; normalized value: 233; normalized unit: s^-1; metric: Km; raw value: 11; raw unit: uM; normalized value: 0.011; normalized unit: mM; metric: kcat/Km; the table prints only the rounded specificity column, so the absolute ratio recorded here is the quotient of this row's own two printed cells, paper kcat divided by paper Km; normalized value: 21181.818181818184; normalized unit: s^-1 mM^-1; assay condition: Purified papain-solubilized BRO-1p (strain L14) or BRO-2p (strain L16904) beta-lactamase; spectrophotometric progress curves analysed by the T1/2 method in 20 mM TEA-HCl / 0.15 M NaCl buffer, pH 7.0, at a constant temperature of 30 C.

raw_value_unit_evidence: Table 3. Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method (PDF page 6, journal page 318), row Nitroeefin: kcat^b (s^-1) column BRO-2p prints 233; Km^a (uM) column BRO-2p prints 11; Specificity (kcat/Km) column BRO-2p prints 21 in units of 10^6 M^-1 s^-1. Footnote a: Mean of three values.

row_label: Nitroeefin


substrate_name: Ampicillin

column_label: Table 3: Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method. Substrate row 'Ampicillin'; enzyme column 'BRO-2p'; column 'Km^a (uM)' = 4.6; column 'kcat^b (s^-1)' = 32; column 'Specificity (kcat/Km)' = 7.1 (footnote b: L . s^-1 . umol^-1).

normalized_value_unit_evidence: Km: printed Table 3 cell 4.6 uM; 4.6 / 1000 = 0.0046 mM; the exported value is 0.005 mM. kcat: printed Table 3 cell 32 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 32.0 s^(-1). kcat/Km: printed Table 3 Specificity cell 7.1 L . s^-1 . umol^-1; footnote b prints that unit literal and 1 L . s^-1 . umol^-1 is 1 s^-1 uM^-1, so 7.1 x 1000 = 7100.0 s^-1 mM^-1; the exported value is 6400.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 318), substrate row 'Ampicillin', enzyme column 'BRO-2p': Km = 4.6 uM; kcat = 32 s^-1; printed Specificity (kcat/Km) = 7.1 L . s^-1 . umol^-1.

row_label: Table 3, substrate row 'Ampicillin', enzyme column 'BRO-2p' (Branhamella catarrhalis strain L16904)

substrate: Ampicillin


column_label: The literal Cefuroxime row's BRO-2p Km and kcat cells normalize exactly to the frozen current components. Their deterministic quotient is the current stored efficiency; the independently printed rounded specificity remains separate.

normalized_value_unit_evidence: Km=0.056 mM; kcat=4.8 s^-1; current same-row quotient=85.71428571428571 s^-1 mM^-1; printed rounded specificity=86 s^-1 mM^-1 and is preserved separately

raw_value_unit_evidence: Cefuroxime BRO-2p cells: Km 56 uM; kcat 4.8 s^-1; printed specificity 0.086 L s^-1 umol^-1

row_label: Cefuroxime / BRO-2p

table_label: Table 3. Kinetic constants of the BRO-1p and BRO-2p beta-lactamases of Branhamella catarrhalis as determined spectrophotometrically using the T1/2 method


column_label: The literal Cloxacillin row's BRO-2p kcat cell agrees with current, but its 1.5 uM Km cell does not equal current 0.002 mM. The correction preserves the exact component cells and their deterministic quotient; the independently printed rounded specificity remains separate.

normalized_value_unit_evidence: Corrected Km=0.0015 mM; kcat=8.6 s^-1; corrected same-row quotient=5733.333333333333 s^-1 mM^-1; printed rounded specificity=5700 s^-1 mM^-1; current Km=0.002 mM and efficiency=4300 s^-1 mM^-1 are not substituted for the paper cells

raw_value_unit_evidence: Cloxacillin BRO-2p cells: Km 1.5 uM; kcat 8.6 s^-1; printed specificity 5.7 L s^-1 umol^-1

row_label: Cloxacillin / BRO-2p


column_label: The literal Cefaclor row's BRO-2p Km and kcat cells normalize exactly to the frozen current components. Their deterministic quotient is the current stored efficiency; the independently printed rounded specificity remains separate.

normalized_value_unit_evidence: Km=0.043 mM; kcat=69 s^-1; current same-row quotient=1604.6511627906978 s^-1 mM^-1; printed rounded specificity=1600 s^-1 mM^-1 and is preserved separately

raw_value_unit_evidence: Cefaclor BRO-2p cells: Km 43 uM; kcat 69 s^-1; printed specificity 1.6 L s^-1 umol^-1

row_label: Cefaclor / BRO-2p


column_label: The literal Mecillinam row's BRO-1p Km and kcat cells normalize exactly to the frozen current components. Their deterministic quotient is the current stored efficiency; the independently printed rounded specificity remains separate.

normalized_value_unit_evidence: Km=0.040 mM; kcat=31 s^-1; current same-row quotient=775 s^-1 mM^-1; printed rounded specificity=780 s^-1 mM^-1 and is preserved separately

raw_value_unit_evidence: Mecillinam BRO-1p cells: Km 40 uM; kcat 31 s^-1; printed specificity 0.78 L s^-1 umol^-1

row_label: Mecillinam / BRO-1p


organism: Morganella morganii

column_label: PMID 16495258, Table 3, row Cephalothin, columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1): 148 +/- 10, 140 +/- 35, and 1 +/- 0.2, respectively. The printed catalytic-efficiency cell normalizes to 1000 s^-1*mM^-1, not the exported computed quotient 945.9459459459459.

row_label: Cephalothin

table_label: Table 3. Kinetic parameters of AmpC M29 from Morganella morganii strain PP29 with different substrates


substrate_name: cefotaxime

column_label: PMID 16495258, Table 3, row Cefotaxime with footnote a, columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1): 0.02 +/- 0.0016, 0.032 +/- 0.002, and 1.6 +/- 0.1, respectively. Footnote a states that Km was determined as Ki using nitrocefin as reporter substrate.

row_label: Cefotaxime (footnote a)

substrate: cefotaxime


substrate_name: Oxacillin

column_label: PMID 16495258, Table 3, row Oxacillin with footnote a, columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1): 0.003 +/- 0.0003, 0.022 +/- 0.001, and 7 +/- 0.3, respectively. The printed catalytic-efficiency cell normalizes to 7000 s^-1*mM^-1, not the exported computed quotient 7333.333333333333.

row_label: Oxacillin (footnote a)

substrate: Oxacillin


column_label: PMID 16495258, Table 3, row Benzylpenicillin (the standard name for Penicillin G) with footnote a, columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1): 0.25 +/- 0.007, 0.0074 +/- 0.0004, and 0.03 +/- 0.002, respectively. The correction target is the three explicit printed central values preserved here.

raw_value_unit_evidence: Table 3 row Benzylpenicillin (Penicillin G), footnote a: Km/Ki 0.25 +/- 0.007 uM; kcat 0.0074 +/- 0.0004 s^-1; kcat/Km 0.03 +/- 0.002 uM^-1 s^-1.

row_label: Benzylpenicillin (Penicillin G; footnote a)


substrate_name: cefepime

assay_conditions_summary: pH 7; 303.15 K; buffer 20 mM phosphate

column_label: The literal Cefepime row binds all three Table 3 cells. Footnote a defines its Km as competitive Ki measured with nitrocefin reporter. The current stored kcat and Km equal the normalized primary cells, and the derived current efficiency lies inside the independently printed interval.

normalized_value_unit_evidence: Km/Ki=0.095 mM; kcat=0.008 s^-1; current same-row quotient=0.08421052631578947 s^-1 mM^-1; printed efficiency=0.08 ± 0.007 s^-1 mM^-1; the current quotient lies inside [0.073, 0.087].

raw_value_unit_evidence: Cefepime cells: Km/Ki 95 ± 9 uM; kcat 0.008 ± 0.0007 s^-1; printed kcat/Km 8 × 10^-5 ± 7 × 10^-6 uM^-1 s^-1.

row_label: Cefepime

substrate: cefepime


organism: Mycobacterium tuberculosis

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

ki_unit: mM

sequence_source: UniProtKB direct accession lookup: P9WKD3

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


substrate_name: meropenem

substrate: meropenem


substrate_name: tebipenem

substrate: tebipenem


substrate_name: doripenem

substrate: doripenem


substrate_name: ertapenem

substrate: ertapenem


organism: Mycolicibacterium smegmatis

substrate_name: ampicillin

sequence_source: UniProtKB A0R0P0 FASTA direct 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 `Ampicillin`; column `Vmax (uM s^-1)` = 0.481; column `Km (uM)` = 9.544; column `Kcat (s^-1)` = 9.620; column `Kcat/Km (uM^-1 s^-1)` = 1.007.

normalized_value_unit_evidence: Km: printed Table 4 cell 9.544 uM; 9.544 uM / 1000 = 0.009544 mM. The catalog stores this Km as 0.00954 mM, which is that same printed cell carried to the catalog's own stored decimal precision (9.54 uM vs printed 9.544 uM, a 0.042% 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 9.620 s^-1 = 9.62 s^(-1), which equals the catalog kcat exactly with no conversion. kcat/Km: the printed cell 1.007 uM^-1 s^-1 = 1006.9999999999999 s^-1 mM^-1, whereas the exact quotient of the row's own printed cells is 1007.9631181894383 s^-1 mM^-1 and the catalog kcat_over_km 1008.3857442348008 s^(-1)*mM^(-1) is the exact quotient of the catalog-precision pair 9.62 / 0.00954.

raw_value_unit_evidence: Table 4 (printed page 225), row `Ampicillin`: Vmax = 0.481 uM s^-1; Km = 9.544 uM; Kcat = 9.620 s^-1; Kcat/Km = 1.007 uM^-1 s^-1.

row_label: Table 4, antibiotics row `Ampicillin`

substrate: ampicillin


substrate_name: piperacillin

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 Piperacillin; the Kcat (s^-1) column cell reads 22.020 and the Km (uM) column cell reads 12.560. 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, 22.020 s^-1 divided by 0.01256 mM, this row's own two printed Table 4 cells after the uM to mM normalization.

normalized_value_unit_evidence: metric: kcat; raw value: 22.020; raw unit: s^-1; normalized value: 22.02; normalized unit: s^-1; metric: Km; raw value: 12.560; raw unit: uM; normalized value: 0.01256; normalized unit: mM; metric: kcat/Km; normalized value: 1753.184713375796; normalized unit: s^-1 mM^-1; derived from: 22.020 s^-1 divided by 0.01256 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: Piperacillin; column labels: Antibiotics | Vmax (uMs^-1) | Km (uM) | Kcat (s^-1) | Kcat/Km (uM^-1 s^-1). Transcribed line, verbatim: "Piperacillin    11.010           12.560   22.020        1.756"; metric: kcat; raw value: 22.020; raw unit: s^-1; metric: Km; raw value: 12.560; raw unit: uM;

row_label: Piperacillin

substrate: piperacillin


column_label: Table 4  Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics; row `Cefotaxime`; column `Vmax (uM s^-1)` = 0.786; column `Km (uM)` = 364.740; column `Kcat (s^-1)` = 1.572; column `Kcat/Km (uM^-1 s^-1)` = 0.004.

normalized_value_unit_evidence: Km: printed Table 4 cell 364.740 uM; 364.740 uM / 1000 = 0.36474 mM. The catalog stores this Km as 0.3647 mM, which is that same printed cell carried to the catalog's own stored decimal precision (364.7 uM vs printed 364.740 uM, a 0.011% 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 1.572 s^-1 = 1.572 s^(-1), which equals the catalog kcat exactly with no conversion. kcat/Km: the printed cell 0.004 uM^-1 s^-1 = 4.0 s^-1 mM^-1, whereas the exact quotient of the row's own printed cells is 4.309919394637276 s^-1 mM^-1 and the catalog kcat_over_km 4.310392103098437 s^(-1)*mM^(-1) is the exact quotient of the catalog-precision pair 1.572 / 0.3647.

raw_value_unit_evidence: Table 4 (printed page 225), row `Cefotaxime`: Vmax = 0.786 uM s^-1; Km = 364.740 uM; Kcat = 1.572 s^-1; Kcat/Km = 0.004 uM^-1 s^-1.

row_label: Table 4, antibiotics row `Cefotaxime`


substrate_name: Bocillin-FL

substrate: Bocillin-FL


substrate_name: ticarcillin

column_label: Table 4  Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics; row `Ticarcillin`; column `Vmax (uM s^-1)` = 0.861; column `Km (uM)` = 7.915; column `Kcat (s^-1)` = 1.722; column `Kcat/Km (uM^-1 s^-1)` = 0.217.

normalized_value_unit_evidence: Km: printed Table 4 cell 7.915 uM; 7.915 uM / 1000 = 0.007915 mM. The catalog stores this Km as 0.00792 mM, which is that same printed cell carried to the catalog's own stored decimal precision (7.92 uM vs printed 7.915 uM, a 0.063% 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 1.722 s^-1 = 1.722 s^(-1), which equals the catalog kcat exactly with no conversion. kcat/Km: the printed cell 0.217 uM^-1 s^-1 = 217.0 s^-1 mM^-1, whereas the exact quotient of the row's own printed cells is 217.56159191408716 s^-1 mM^-1 and the catalog kcat_over_km 217.42424242424244 s^(-1)*mM^(-1) is the exact quotient of the catalog-precision pair 1.722 / 0.00792.

raw_value_unit_evidence: Table 4 (printed page 225), row `Ticarcillin`: Vmax = 0.861 uM s^-1; Km = 7.915 uM; Kcat = 1.722 s^-1; Kcat/Km = 0.217 uM^-1 s^-1.

row_label: Table 4, antibiotics row `Ticarcillin`

substrate: ticarcillin


substrate_name: amoxicillin

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 Amoxicillin; the Kcat (s^-1) column cell reads 1.770 and the Km (uM) column cell reads 6.490. 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, 1.770 s^-1 divided by 0.00649 mM, this row's own two printed Table 4 cells after the uM to mM normalization.

normalized_value_unit_evidence: metric: kcat; raw value: 1.770; raw unit: s^-1; normalized value: 1.77; normalized unit: s^-1; metric: Km; raw value: 6.490; raw unit: uM; normalized value: 0.00649; normalized unit: mM; metric: kcat/Km; normalized value: 272.72727272727275; normalized unit: s^-1 mM^-1; derived from: 1.770 s^-1 divided by 0.00649 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: Amoxicillin; column labels: Antibiotics | Vmax (uMs^-1) | Km (uM) | Kcat (s^-1) | Kcat/Km (uM^-1 s^-1). Transcribed line, verbatim: "Amoxicillin      0.885            6.490    1.770        0.272"; metric: kcat; raw value: 1.770; raw unit: s^-1; metric: Km; raw value: 6.490; raw unit: uM;

row_label: Amoxicillin

substrate: amoxicillin


substrate_name: Cefamandole

sequence_source: UniProtKB reviewed accession A5U493 (BLAC_MYCTA), direct REST/FASTA check on 2026-05-27

assay_conditions_summary: pH 6; 310.15 K; buffer 0.1 M sodium phosphate

column_label: Table 3; row Cefamandole; column block 'Recombinant Y-49 b-lactamase'; column Km (uM) raw value 645; column kcat (s^-1) raw value 22. The same Table 3 row also prints 'Relative Vmax' and 'REH' cells for this column block and separate Km cells under the 'Directly from M. tuberculosis' column blocks; none of those were used. Table 3 prints no kcat/Km column.

normalized_value_unit_evidence: kcat 22 s^-1 = 22.0 s^-1 (no conversion). Km 645 uM = 645 / 1000 = 0.645 mM. Table 3 prints no kcat/Km column, so kcat/Km is not a printed cell: it is the quotient of this same row's own two printed cells, 22.0 s^-1 / 0.645 mM = 34.10852713178294 s^-1 mM^-1, which is the value carried by the export row.

raw_value_unit_evidence: Table 3 (journal page 1379), row Cefamandole, Recombinant Y-49 b-lactamase column block: Km cell 645 (micromolar; the extractor drops the micro sign so the printed header renders as 'Km (mM)'), kcat cell 22 (the printed 'kcat (s^-1)' header renders as 'kcat (s21)' because superscripts are flattened). Verbatim printed row: Cefamandole                        645            22           104           8                      282            63           13         566            126        16

row_label: Cefamandole

table_label: TABLE 3. Kinetic characteristics of recombinant Y49 b-lactamase from E. coli and b-lactamase obtained directly from M. tuberculosis

substrate: Cefamandole


substrate_name: Cephaloridine

column_label: Table 3; row Cephaloridine; column block 'Recombinant Y-49 b-lactamase'; column Km (uM) raw value 798; column kcat (s^-1) raw value 8. The same Table 3 row also prints 'Relative Vmax' and 'REH' cells for this column block and separate Km cells under the 'Directly from M. tuberculosis' column blocks; none of those were used. Table 3 prints no kcat/Km column.

normalized_value_unit_evidence: kcat 8 s^-1 = 8.0 s^-1 (no conversion). Km 798 uM = 798 / 1000 = 0.798 mM. Table 3 prints no kcat/Km column, so kcat/Km is not a printed cell: it is the quotient of this same row's own two printed cells, 8.0 s^-1 / 0.798 mM = 10.025062656641603 s^-1 mM^-1, which is the value carried by the export row.

raw_value_unit_evidence: Table 3 (journal page 1379), row Cephaloridine, Recombinant Y-49 b-lactamase column block: Km cell 798 (micromolar; the extractor drops the micro sign so the printed header renders as 'Km (mM)'), kcat cell 8 (the printed 'kcat (s^-1)' header renders as 'kcat (s21)' because superscripts are flattened). Verbatim printed row: Cephaloridine                      798             8            39           2                      540            23            2

row_label: Cephaloridine

substrate: Cephaloridine


substrate_name: Cephapirin

column_label: Table 3; row Cephapirin; column block 'Recombinant Y-49 b-lactamase'; column Km (uM) raw value 680; column kcat (s^-1) raw value 3. The same Table 3 row also prints 'Relative Vmax' and 'REH' cells for this column block and separate Km cells under the 'Directly from M. tuberculosis' column blocks; none of those were used. Table 3 prints no kcat/Km column.

normalized_value_unit_evidence: kcat 3 s^-1 = 3.0 s^-1 (no conversion). Km 680 uM = 680 / 1000 = 0.68 mM. Table 3 prints no kcat/Km column, so kcat/Km is not a printed cell: it is the quotient of this same row's own two printed cells, 3.0 s^-1 / 0.68 mM = 4.411764705882352 s^-1 mM^-1, which is the value carried by the export row.

raw_value_unit_evidence: Table 3 (journal page 1379), row Cephapirin, Recombinant Y-49 b-lactamase column block: Km cell 680 (micromolar; the extractor drops the micro sign so the printed header renders as 'Km (mM)'), kcat cell 3 (the printed 'kcat (s^-1)' header renders as 'kcat (s21)' because superscripts are flattened). Verbatim printed row: Cephapirin                         680             3            15           1                      319             9            2

row_label: Cephapirin

substrate: Cephapirin


substrate_name: cefazolin

column_label: Table 3; row Cefazolin; column block 'Recombinant Y-49 b-lactamase'; column Km (uM) raw value 490; column kcat (s^-1) raw value 8. The same Table 3 row also prints 'Relative Vmax' and 'REH' cells for this column block and separate Km cells under the 'Directly from M. tuberculosis' column blocks; none of those were used. Table 3 prints no kcat/Km column.

normalized_value_unit_evidence: kcat 8 s^-1 = 8.0 s^-1 (no conversion). Km 490 uM = 490 / 1000 = 0.49 mM. Table 3 prints no kcat/Km column, so kcat/Km is not a printed cell: it is the quotient of this same row's own two printed cells, 8.0 s^-1 / 0.49 mM = 16.3265306122449 s^-1 mM^-1, which is the value carried by the export row.

raw_value_unit_evidence: Table 3 (journal page 1379), row Cefazolin, Recombinant Y-49 b-lactamase column block: Km cell 490 (micromolar; the extractor drops the micro sign so the printed header renders as 'Km (mM)'), kcat cell 8 (the printed 'kcat (s^-1)' header renders as 'kcat (s21)' because superscripts are flattened). Verbatim printed row: Cefazolin                          490             8            36           4                      304            17            3

row_label: Cefazolin

substrate: cefazolin


substrate_name: Penicillin V

substrate: Penicillin V


substrate_name: azlocillin

substrate: azlocillin


substrate_name: Cephalothin

column_label: Table 3; measurement recombinant Y49 b-lactamase cephalothin row; construct recombinant Y49 b-lactamase; substrate cephalothin; assayed in 0.1 M sodium phosphate buffer pH 6.0 at 37 C. kcat 8 s^-1. Km 308 uM. Relative Vmax 36. REH 6. No kcat/Km cell is printed in Table 3.

normalized_value_unit_evidence: Km: printed Table 3 cell 308 uM; 308 / 1000 = 0.308 mM; the exported value is 0.308 mM. kcat: printed Table 3 cell 8 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 8.0 s^(-1). kcat/Km: Table 3 prints no efficiency cell for this line; the exported 25.974025974025974 s^(-1)*mM^(-1) is the full-precision quotient 8.0 / 0.308 of the two printed cells of this one measurement, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, recombinant Y-49 b-lactamase block, cephalothin row: Km = 308 uM; kcat = 8 s^-1; Relative Vmax = 36; REH = 6. Table 3 prints no catalytic-efficiency column and the Ki column is blank on this line.

table_label: Table 3: Kinetic characteristics of recombinant Y49 b-lactamase from E. coli and b-lactamase obtained directly from M. tuberculosis (Antimicrob. Agents Chemother. 1998, 42(6):1375-1381)

substrate: Cephalothin


substrate_name: Imipenem

column_label: The literal Imipenem row binds all three Table 3 cells. Footnote a defines its Km as competitive Ki measured with nitrocefin reporter. The current stored kcat and Km equal the normalized primary cells, and the derived current efficiency equals the independently printed central value.

normalized_value_unit_evidence: Km/Ki=0.002 mM; kcat=0.07 s^-1; current same-row quotient=35 s^-1 mM^-1; printed efficiency=35 ± 2 s^-1 mM^-1; the current quotient equals the printed central value.

raw_value_unit_evidence: Imipenem cells: Km/Ki 2 ± 0.3 uM; kcat 0.07 ± 0.003 s^-1; printed kcat/Km 0.035 ± 0.002 uM^-1 s^-1.

row_label: Imipenem

substrate: Imipenem


substrate_name: Nitrocefin

column_label: The literal Nitrocefin row binds all three Table 3 cells. The current stored kcat and Km equal the normalized primary cells, and the derived current efficiency lies inside the independently printed interval.

normalized_value_unit_evidence: Km=0.025 mM; kcat=93 s^-1; current same-row quotient=3720 s^-1 mM^-1; printed efficiency=3800 ± 300 s^-1 mM^-1; the current quotient lies inside [3500, 4100].

raw_value_unit_evidence: Nitrocefin cells: Km 25 ± 4 uM; kcat 93 ± 8 s^-1; printed kcat/Km 3.8 ± 0.3 uM^-1 s^-1.

row_label: Nitrocefin

substrate: Nitrocefin


substrate_name: Ceftazidime

column_label: The literal Ceftazidime row binds all three Table 3 cells. Footnote a defines its Km as competitive Ki measured with nitrocefin reporter. The current stored kcat and Km equal the normalized primary cells, and the derived current efficiency lies inside the independently printed interval.

normalized_value_unit_evidence: Km/Ki=0.0009 mM; kcat=0.04 s^-1; current same-row quotient=44.44444444444445 s^-1 mM^-1; printed efficiency=45 ± 2 s^-1 mM^-1; the current quotient lies inside [43, 47].

raw_value_unit_evidence: Ceftazidime cells: Km/Ki 0.9 ± 0.04 uM; kcat 0.04 ± 0.002 s^-1; printed kcat/Km 0.045 ± 0.002 uM^-1 s^-1.

row_label: Ceftazidime

substrate: Ceftazidime


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: Ampicillin

substrate: Ampicillin


organism: Providencia stuartii

substrate_name: aztreonam

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

substrate: aztreonam


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: cefotaxime

substrate: cefotaxime


organism: Proteus mirabilis

substrate_name: cefepime

substrate: cefepime


substrate_name: carbenicillin

substrate: carbenicillin


organism: Pseudomonas aeruginosa


sequence_source: UniProtKB:P16897 direct lookup 2026-05-27


sequence_source: UniProtKB:Q79MP6 direct lookup 2026-05-27


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

column_label: Table 2, TEM-89 enzyme block; row Benzylpenicillin; column k cat (s^-1) cell 50; column K m (uM) cell 8.0; column k cat / K m (uM^-1 s^-1) cell 6.25.

normalized_value_unit_evidence: kcat 50 s^-1 = 50.0 s^(-1). Km 8.0 uM = 8.0 / 1000 = 0.008 mM. kcat/Km 6.25 uM^-1 s^-1 = 6.25 * 1000 = 6250.0 s^-1 mM^-1, which is also the exact quotient of this row's own printed cells.

raw_value_unit_evidence: Table 2 of the PMC HTML asset, row Benzylpenicillin, TEM-89 enzyme block: kcat column cell 50 s^-1; Km column cell 8.0 uM; kcat/Km column cell 6.25 uM^-1 s^-1.

row_label: Benzylpenicillin


substrate_name: Ticarcillin

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: Ticarcillin. Enzyme column block: TEM-89. Columns read: k cat (s^-1) cell 6, K m (uM) cell 24, k cat / K m (uM^-1 s^-1) cell 0.25. metric: kcat; raw value: 6; raw unit: s^-1; normalized value: 6.0 s^(-1); metric: Km; raw value: 24; raw unit: uM; normalized value: 0.024 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 250.0 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 Ticarcillin: kcat 6 s^-1 = 6.0 s^(-1); Km 24 uM = 0.024 mM (1 uM = 0.001 mM); kcat/Km 250.0 s^-1 mM^-1 (1 uM^-1 s^-1 = 1000 s^-1 mM^-1, so the printed cell 0.25 uM^-1 s^-1 is 250.0 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 Ticarcillin, TEM-89 columns: kcat = 6 s^-1; Km = 24 uM; kcat/Km = 0.25 uM^-1 s^-1. | TEM-89 cells read: k cat = 6 s^-1; K m = 24 uM; k cat / K m = 0.25 uM^-1 s^-1.

row_label: TEM-89 | Ticarcillin

substrate: Ticarcillin


substrate_name: piperacillin

substrate: piperacillin


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: Cephalothin. Enzyme column block: TEM-89. Columns read: k cat (s^-1) cell 5, K m (uM) cell 79, k cat / K m (uM^-1 s^-1) cell 0.06. metric: kcat; raw value: 5; raw unit: s^-1; normalized value: 5.0 s^(-1); metric: Km; raw value: 79; raw unit: uM; normalized value: 0.079 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 63.291139240506325 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 Cephalothin: kcat 5 s^-1 = 5.0 s^(-1); Km 79 uM = 0.079 mM (1 uM = 0.001 mM); kcat/Km 63.291139240506325 s^-1 mM^-1 (1 uM^-1 s^-1 = 1000 s^-1 mM^-1, so the printed cell 0.06 uM^-1 s^-1 is 60.0 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 Cephalothin, TEM-89 columns: kcat = 5 s^-1; Km = 79 uM; kcat/Km = 0.06 uM^-1 s^-1. | TEM-89 cells read: k cat = 5 s^-1; K m = 79 uM; k cat / K m = 0.06 uM^-1 s^-1.

row_label: TEM-89 | Cephalothin