substrate_name: Oxacillin

column_label: PMC1132494 page 154 Table 3, Bacillus cereus beta-lactamase II block, row Oxacillin: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM -> mM normalization, and their same-row quotient reproduces the exported kcat/Km.

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

row_label: Bacillus cereus beta-lactamase II | Oxacillin

substrate: Oxacillin


enzyme_display_name: beta-lactamase

organism: Enterobacter cloacae

substrate_name: Cephalosporin C

source_db: oed

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

enzyme: beta-lactamase

substrate: Cephalosporin C

source: oed


substrate_name: Ceftazidime

substrate: Ceftazidime


substrate_name: H2O; Cephalosporin C

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

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N346I

substrate: H2O; Cephalosporin C


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N346A


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant L293C


organism: Burkholderia pseudomallei

substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D170N

substrate: H2O; Nitrocefin


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K232N

substrate: Nitrocefin; H2O


verification_status: unverified

mutation_signature: Unknown

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

status: unverified


organism: Citrobacter diversus

substrate_name: Imipenem

kcat_over_km_origin: calculated

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

data_origin: experimental

substrate: Imipenem


substrate_name: Ampicillin

verification_status: corrected

column_label: Table 4 Form I row Ampicillin columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 Form I Ampicillin cells: Km 22 +/- 4 uM; kcat 119 +/- 4 s^-1; kcat/Km (5.4 +/- 0.8) x 10^6 M^-1 s^-1.

row_label: Form I; Ampicillin

table_label: Table 4, substrate profile of C. diversus beta-lactamases

substrate: Ampicillin

status: corrected


substrate_name: cefazolin

column_label: Table 4 Form I row Cefazolin columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

row_label: Form I; Cefazolin

substrate: cefazolin


column_label: Table 4 Form I row Cephalosporin C columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 Form I Cephalosporin C cells: Km 126 +/- 20 uM; kcat 41 +/- 5 s^-1; kcat/Km (0.3 +/- 0.06) x 10^6 M^-1 s^-1.

row_label: Form I; Cephalosporin C


substrate_name: Penicillin G; H2O

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

substrate: Penicillin G; H2O


substrate_name: Cephalothin

column_label: Table 4 Form I row Cephalothin columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 Form I Cephalothin cells: Km 48 +/- 3 uM; kcat 63 +/- 3 s^-1; kcat/Km (1.3 +/- 0.15) x 10^6 M^-1 s^-1.

row_label: Form I; Cephalothin

substrate: Cephalothin


substrate_name: Cephaloridine

column_label: Table 4 Form I row Cephaloridine columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

row_label: Form I; Cephaloridine

substrate: Cephaloridine


substrate_name: Penicillin G

column_label: Table 4 Form I row Benzylpenicillin columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Benzylpenicillin is the paper synonym for Penicillin G.

raw_value_unit_evidence: Table 4 Form I Benzylpenicillin cells: Km 69 +/- 10 uM; kcat 570 +/- 30 s^-1; kcat/Km (8.3 +/- 0.8) x 10^6 M^-1 s^-1.

row_label: Form I; Benzylpenicillin

substrate: Penicillin G


column_label: Table 4 Form I row Oxacillin columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

row_label: Form I; Oxacillin


substrate_name: Cefuroxime

column_label: Table 4 Form I row Cefuroxime columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

row_label: Form I; Cefuroxime

substrate: Cefuroxime


substrate_name: Methicillin

substrate: Methicillin


substrate_name: carbenicillin

column_label: Table 4 Form I row Carbenicillin columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 Form I Carbenicillin cells: Km 100 +/- 10 uM; kcat 58 +/- 2 s^-1; kcat/Km (0.6 +/- 0.1) x 10^6 M^-1 s^-1.

row_label: Form I; Carbenicillin

substrate: carbenicillin


organism: Citrobacter freundii

substrate_name: H2O; Cephalothin

kcat_display: Not reported

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D217E

substrate: H2O; Cephalothin


substrate_name: H2O; Dexamethasone-Cephem-Methotrexate

sequence_variant_note: Mutation signature Y150S matches the mutant residue at offset +0 and the reference residue at offset +5; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y150S

substrate: H2O; Dexamethasone-Cephem-Methotrexate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +20, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K315H


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y221G


substrate_name: Dexamethasone-Cephem-Methotrexate; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S318T

substrate: Dexamethasone-Cephem-Methotrexate; H2O


column_label: Table 1 (Steady State Parameters for Turnover of Retro-Substrates), substrate row 11, enzyme block P99; column 'kcat (S-1)' = 0.25±0.02; column 'Km (uM)' = 32±7; column 'kcat/Km (s-1M-1)' = 7.9x103. The three P99 columns are the first three numeric columns after the substrate label of that row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.25 under the column head kcat (S-1); the printed unit is already canonical, so kcat = 0.25 s^(-1). Km: printed Table 1 cell 32 under the column head Km (uM); 1 uM is 0.001 mM, so 32 / 1000 = 0.032 mM. kcat/Km: printed Table 1 cell 7.9 x 10^3 under the column head kcat/Km (s-1M-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.9 x 10^3 / 1000 = 7.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 11, P99 enzyme block: printed kcat cell 0.25±0.02 under the column head kcat (S-1); printed Km cell 32±7 under the column head Km (uM); printed kcat/Km cell 7.9x103 under the column head kcat/Km (s-1M-1), which decodes to 7.9 x 10^3 M^-1 s^-1.

table_label: Table 1: Steady State Parameters for Turnover of Retro-Substrates (Bioorg Med Chem 2010, 18(1):282)


column_label: Table 1 (Steady State Parameters for Turnover of Retro-Substrates), substrate row 10, enzyme block P99; column 'kcat (S-1)' = 0.33±0.03; column 'Km (uM)' = 700±140; column 'kcat/Km (s-1M-1)' = 4.7x102. The three P99 columns are the first three numeric columns after the substrate label of that row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.33 under the column head kcat (S-1); the printed unit is already canonical, so kcat = 0.33 s^(-1). Km: printed Table 1 cell 700 under the column head Km (uM); 1 uM is 0.001 mM, so 700 / 1000 = 0.7 mM. kcat/Km: printed Table 1 cell 4.7 x 10^2 under the column head kcat/Km (s-1M-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.7 x 10^2 / 1000 = 0.47 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 10, P99 enzyme block: printed kcat cell 0.33±0.03 under the column head kcat (S-1); printed Km cell 700±140 under the column head Km (uM); printed kcat/Km cell 4.7x102 under the column head kcat/Km (s-1M-1), which decodes to 4.7 x 10^2 M^-1 s^-1.


organism: Bacteroides fragilis


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: Cephalothin; H2O

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

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D217K

substrate: Cephalothin; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D217T with inferred residue-numbering offset +32 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D217T


substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


organism: Enterobacter aerogenes

km_display: Not reported


substrate_name: Cephalosporin C

substrate: Cephalosporin C


substrate_name: cefepime

substrate: cefepime


substrate_name: Imipenem

column_label: Table 2, row Imipenem, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Imipenem: kcat=1040 s^-1; Km=92 uM; kcat/Km=11300 x 10^3 M^-1 s^-1.

row_label: Imipenem

table_label: Table 2

substrate: Imipenem


column_label: Table 2, row Benzylpenicillin, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Benzylpenicillin: kcat=260 s^-1; Km=28 uM; kcat/Km=9300 x 10^3 M^-1 s^-1.

row_label: Benzylpenicillin


substrate_name: Ticarcillin

column_label: Table 2, row Ticarcillin, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Ticarcillin: kcat=81 s^-1; Km=152 uM; kcat/Km=530 x 10^3 M^-1 s^-1.

row_label: Ticarcillin

substrate: Ticarcillin


substrate_name: Ceftazidime

column_label: Table 2, row Ceftazidime^a, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Ceftazidime^a: kcat=4.7 s^-1; Km=90 uM; kcat/Km=52.2 x 10^3 M^-1 s^-1.

row_label: Ceftazidime^a

substrate: Ceftazidime


substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


substrate_name: moxalactam

column_label: Table 2, row Moxalactam^a, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Moxalactam^a: kcat=8.6 s^-1; Km=300 uM; kcat/Km=28.6 x 10^3 M^-1 s^-1.

row_label: Moxalactam^a

substrate: moxalactam


substrate_name: cefotaxime

column_label: Table 2, row Cefotaxime, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Cefotaxime: kcat=286 s^-1; Km=956 uM; kcat/Km=300 x 10^3 M^-1 s^-1.

row_label: Cefotaxime

substrate: cefotaxime


column_label: Table 2, row Cefoxitin^a, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Cefoxitin^a: kcat=5.0 s^-1; Km=93 uM; kcat/Km=62.3 x 10^3 M^-1 s^-1.

row_label: Cefoxitin^a


substrate_name: cefotetan

column_label: Table 2, row Cefotetan^a, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Cefotetan^a: kcat=5.3 s^-1; Km=80 uM; kcat/Km=72.2 x 10^3 M^-1 s^-1.

row_label: Cefotetan^a

substrate: cefotetan


substrate_name: Meropenem

column_label: Table 2, row Meropenem, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Meropenem: kcat=12 s^-1; Km=4.35 uM; kcat/Km=2750 x 10^3 M^-1 s^-1.

row_label: Meropenem

substrate: Meropenem


substrate_name: Cephalothin

column_label: Table 2, row Cephalothin, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Cephalothin: kcat=2820 s^-1; Km=185 uM; kcat/Km=15200 x 10^3 M^-1 s^-1.

row_label: Cephalothin

substrate: Cephalothin


substrate_name: amoxicillin

column_label: Table 2, row Amoxicillin, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Amoxicillin: kcat=816 s^-1; Km=90 uM; kcat/Km=9060 x 10^3 M^-1 s^-1.

row_label: Amoxicillin

substrate: amoxicillin


substrate_name: aztreonam

column_label: Table 2, row Aztreonam, columns kcat (s^-1), Km (uM), and kcat/Km (x10^3 M^-1 s^-1).

raw_value_unit_evidence: Table 2 row Aztreonam: kcat=707 s^-1; Km=125 uM; kcat/Km=5600 x 10^3 M^-1 s^-1.

row_label: Aztreonam

substrate: aztreonam


substrate_name: Cefuroxime

substrate: Cefuroxime


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: 7-aminocephalosporanic acid

source_db: skid

source_license: CC BY-NC-ND 4.0

substrate: 7-aminocephalosporanic acid

source: skid


organism: Escherichia coli

substrate_name: H2O; Cephaloridine

ki_unit: mM

substrate: H2O; Cephaloridine


column_label: Table II (PDF page 4 of 9, journal page 23055), substrate block `Cefotaxime`, b-lactamase sub-row `TEMpUC19`: kcat (s^-1) = 0.18; Km (uM) = 230; kcat/Km (M^-1 s^-1) = 7.8 x 10^2.

normalized_value_unit_evidence: kcat: printed cell 0.18 s^-1 is already the export unit -> 0.18 s^(-1); the exported value is 202.0 s^(-1). Km: printed cell 230 uM -> 0.23 mM (divide by 1000); the exported value is 0.1 mM. kcat/Km: the paper PRINTS the kcat/Km cell 7.8 x 10^2 M^-1 s^-1 for this Table II row -> 0.78 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 2020.0 s^(-1)*mM^(-1).

row_label: Table II, decoded plain-numeral transcription, substrate block `Cefotaxime`, 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_name: Cephaloridine

substrate: Cephaloridine


substrate_name: Cephalosporin C

substrate: Cephalosporin C


substrate_name: piperacillin

substrate: piperacillin


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: H2O; Cephalosporin C

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEMpUC19 R164N

substrate: H2O; Cephalosporin C


substrate_name: Ceftazidime

substrate: Ceftazidime


verification_status: verified

column_label: Table 1; row depsipeptide 3; columns kcat (s^-1), Km (uM), kcat/Km (s^-1 M^-1); Scheme 1 maps compound 3 to the expected aminothiazolyl methoxyiminoacetylglycyl oxybenzoic acid

raw_value_unit_evidence: Table 1: depsipeptide 3 kcat 19 +/- 2 s^-1; Km 59 +/- 15 uM; kcat/Km 3.3 x 10^5 s^-1 M^-1

row_label: depsipeptide 3

table_label: Table 1

status: verified


substrate_name: H2O; Cefotaxime

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: H2O; Cefotaxime


substrate_name: cefotaxime

column_label: Table 1; row cefotaxime; columns kcat (s^-1), Km (uM), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: kcat 0.41 s^-1; Km 0.0172 mM (exported as 0.017 mM rounded); kcat_over_km 24.117647058823525 s^-1 mM^-1 from exported rounded Km; table rounded ratio 23 s^-1 mM^-1

row_label: cefotaxime

substrate: cefotaxime


substrate_name: 3-[(Phenylacetyl)glycyl]oxybenzoic acid

column_label: Table 1; row depsipeptide 7; columns kcat (s^-1), Km (uM), kcat/Km (s^-1 M^-1); compound-numbering page maps compound 7 to 3-[[N-(Phenylacetyl)glycyl]oxy]benzoic acid

raw_value_unit_evidence: Table 1: depsipeptide 7 kcat 125 s^-1; Km 230 uM; kcat/Km 5.4 x 10^5 s^-1 M^-1

row_label: depsipeptide 7

substrate: 3-[(Phenylacetyl)glycyl]oxybenzoic acid


substrate_name: H2O; Cephalosporin

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

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant P99-210-1A

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant P99-210-2A

substrate: H2O; Cephalosporin


substrate_name: Cephalothin

substrate: Cephalothin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEMpUC19 D179G


column_label: Table II. Kinetics parameters of TEMpUC19 and mutant derivatives; row Piperacillin / TEMpUC19

normalized_value_unit_evidence: Per-metric normalized values and units are preserved in paper_metric_evidence.

raw_value_unit_evidence: Per-metric raw values and units are preserved in paper_metric_evidence; captured_primary_segment preserves the exact source transcription.

row_label: Piperacillin / TEMpUC19


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

raw_value_unit_evidence: Table II Cephalosporin C TEMpUC19 row reports kcat 33 +/- 3 s^-1; Km 950 +/- 80 microM; kcat/Km (3.5 +/- 0.4) x 10^4 M^-1 s^-1.

row_label: Cephalosporin C / TEMpUC19

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


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEMpUC19 R164S


substrate_name: cefcapene

substrate: cefcapene


substrate_name: Sulbactam

substrate: Sulbactam


substrate_name: beta-Lactam

substrate: beta-Lactam


substrate_name: Penicillin G; H2O

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

substrate: Penicillin G; H2O


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


substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105G

substrate: H2O; Penicillin G


substrate_name: Cefuroxime

column_label: Table 2 'Table 2: Kinetics parameters of TEM-89 beta-lactamase compared with those of TEM-2, TEM-3, and TEM-59 beta-lactamases'; row Cefuroxime; TEM-3 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Cefuroxime, TEM-3 normalized: kcat 28 s^-1; Km 0.09 mM; kcat/Km 310 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Cefuroxime, TEM-3 columns: kcat 28 s^-1; Km 90 uM; kcat/Km 0.31 uM^-1 s^-1.

row_label: Cefuroxime

substrate: Cefuroxime


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

column_label: Table 4; row cefotaxime; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized values: kcat=250 s^-1; Km=0.12 mM; kcat/Km=2100 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row cefotaxime; columns: kcat=250 s^-1; Km=120 uM; kcat/Km=2.1 uM^-1 s^-1.

table_label: Table 4


substrate_name: Cefdinir

column_label: Table 4; row cefdinir; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized values: kcat=2.1 s^-1; Km=0.0014 mM; kcat/Km=1500 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row cefdinir; columns: kcat=2.1 s^-1; Km=1.4 uM; kcat/Km=1.5 uM^-1 s^-1.

row_label: cefdinir

substrate: Cefdinir


column_label: Table 4; row benzylpenicillin/Penicillin G; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized values: kcat=68 s^-1; Km=0.023 mM; kcat/Km=3000 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row benzylpenicillin; columns: kcat=68 s^-1; Km=23 uM; kcat/Km=3.0 uM^-1 s^-1.

row_label: benzylpenicillin


substrate_name: Cephaloridine

column_label: Table 4; row cephaloridine; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized values: kcat=200 s^-1; Km=0.28 mM; kcat/Km=700 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row cephaloridine; columns: kcat=200 s^-1; Km=280 uM; kcat/Km=0.7 uM^-1 s^-1.

row_label: cephaloridine

substrate: Cephaloridine


substrate_name: Nitrocefin

column_label: Table 4; row nitrocefin; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized values: kcat=160 s^-1; Km=0.059 mM; kcat/Km=2700 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row nitrocefin; columns: kcat=160 s^-1; Km=59 uM; kcat/Km=2.7 uM^-1 s^-1.

row_label: nitrocefin

substrate: Nitrocefin


substrate_name: aztreonam

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

substrate: aztreonam


substrate_name: piperacillin

substrate: piperacillin


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: ceftriaxone

column_label: Table 2 'Table 2: Kinetics parameters of TEM-89 beta-lactamase compared with those of TEM-2, TEM-3, and TEM-59 beta-lactamases'; row Ceftriaxone; TEM-3 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Ceftriaxone, TEM-3 normalized: kcat 81 s^-1; Km 0.08 mM; kcat/Km 1000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Ceftriaxone, TEM-3 columns: kcat 81 s^-1; Km 80 uM; kcat/Km 1 uM^-1 s^-1.

row_label: Ceftriaxone

substrate: ceftriaxone


substrate_name: Ticarcillin

column_label: Table 2 'Table 2: Kinetics parameters of TEM-89 beta-lactamase compared with those of TEM-2, TEM-3, and TEM-59 beta-lactamases'; row Ticarcillin; TEM-2 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Ticarcillin, TEM-2 normalized: kcat 195 s^-1; Km 0.012 mM; kcat/Km 16200 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Ticarcillin, TEM-2 columns: kcat 195 s^-1; Km 12 uM; kcat/Km 16.2 uM^-1 s^-1.

row_label: Ticarcillin

substrate: Ticarcillin


substrate_name: amoxicillin

column_label: Table 2 'Table 2: Kinetics parameters of TEM-89 beta-lactamase compared with those of TEM-2, TEM-3, and TEM-59 beta-lactamases'; row Amoxicillin; TEM-2 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Amoxicillin, TEM-2 normalized: kcat 1200 s^-1; Km 0.02 mM; kcat/Km 60000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Amoxicillin, TEM-2 columns: kcat 1200 s^-1; Km 20 uM; kcat/Km 60 uM^-1 s^-1.

substrate: amoxicillin


substrate_name: Cephalosporin C; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEMpUC19 D179N

substrate: Cephalosporin C; H2O


substrate_name: Cephalosporin C

substrate: Cephalosporin C


substrate_name: Ceftazidime

column_label: Table II. Kinetics parameters of TEMpUC19 and mutant derivatives; row Ceftazidime / TEMpUC19

row_label: Ceftazidime / TEMpUC19

substrate: Ceftazidime


substrate_name: Doripenem

substrate: Doripenem


substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


substrate_name: Nitrocefin; H2O

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.2
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: Nitrocefin; H2O


substrate_name: CENTA; H2O

substrate: CENTA; H2O


substrate_name: Imipenem

substrate: Imipenem


substrate_name: cefalotin

substrate: cefalotin


substrate_name: cefotaxime

column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Cefotaxime; CTX-M-25 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 101, 28, 3.6

raw_value_unit_evidence: CTX-M-25 / Cefotaxime: kcat=101 s^-1; Km=28 uM; kcat/Km=3.6 uM^-1 s^-1

row_label: CTX-M-25 / Cefotaxime

substrate: cefotaxime


substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


substrate_name: aztreonam

column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Aztreonam; CTX-M-25 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 84, 120, 0.7

raw_value_unit_evidence: CTX-M-25 / Aztreonam: kcat=84 s^-1; Km=120 uM; kcat/Km=0.7 uM^-1 s^-1

row_label: CTX-M-25 / Aztreonam

substrate: aztreonam


substrate_name: Cephalothin

column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Cephalothin; CTX-M-25 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 230, 190, 1.2

raw_value_unit_evidence: CTX-M-25 / Cephalothin: kcat=230 s^-1; Km=190 uM; kcat/Km=1.2 uM^-1 s^-1

row_label: CTX-M-25 / Cephalothin

substrate: Cephalothin


substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


substrate_name: piperacillin

column_label: Table 2 columns substrate, Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); row matched by Piperacillin.

normalized_value_unit_evidence: kcat 39 s^-1; Km 0.020 mM; printed kcat/Km 2000 s^-1 mM^-1; source quotient 1950 s^-1 mM^-1 is table-rounding compatible.

row_label: Piperacillin

table_label: Table 2, Kinetic parameters of CTX-M-14 against various substrates

substrate: piperacillin


substrate_name: Cephaloridine

column_label: Table 2 columns substrate, Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); row matched by Cefaloridine, the paper spelling for cephaloridine.

normalized_value_unit_evidence: kcat 1300 s^-1; Km 0.125 mM; printed kcat/Km 10000 s^-1 mM^-1; source quotient 10400 s^-1 mM^-1 is table-rounding compatible.

row_label: Cefaloridine (paper spelling; cephaloridine synonym)

substrate: Cephaloridine


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105W


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105N


substrate_name: Cefuroxime

column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Cefuroxime; CTX-M-25 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 190, 44, 4.3

raw_value_unit_evidence: CTX-M-25 / Cefuroxime: kcat=190 s^-1; Km=44 uM; kcat/Km=4.3 uM^-1 s^-1

row_label: CTX-M-25 / Cefuroxime

substrate: Cefuroxime


substrate_name: Penicillin G

column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Benzylpenicillin; CTX-M-25 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 33, 74, 0.4

raw_value_unit_evidence: CTX-M-25 / Benzylpenicillin: kcat=33 s^-1; Km=74 uM; kcat/Km=0.4 uM^-1 s^-1

row_label: CTX-M-25 / Benzylpenicillin

substrate: Penicillin G


column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Ceftazidime; CTX-M-25 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 33, 13, 2.6

raw_value_unit_evidence: CTX-M-25 / Ceftazidime: kcat=33 s^-1; Km=13 uM; kcat/Km=2.6 uM^-1 s^-1

row_label: CTX-M-25 / Ceftazidime


substrate_name: Ampicillin

column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Ampicillin; CTX-M-25 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 5.9, 7.7, 0.8

raw_value_unit_evidence: CTX-M-25 / Ampicillin: kcat=5.9 s^-1; Km=7.7 uM; kcat/Km=0.8 uM^-1 s^-1

row_label: CTX-M-25 / Ampicillin

substrate: Ampicillin


column_label: Table 2 columns substrate, Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); row matched by Cefalothin, the paper spelling for cephalothin.

normalized_value_unit_evidence: kcat 510 s^-1; Km 0.027 mM; printed kcat/Km 19000 s^-1 mM^-1; source quotient 18888.88888888889 s^-1 mM^-1 is table-rounding compatible.

row_label: Cefalothin (paper spelling; cephalothin synonym)


column_label: Table 2 columns substrate, Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); row matched by Imipenem.

normalized_value_unit_evidence: kcat 0.003 s^-1; Km 0.0019 mM; printed kcat/Km 1.0 s^-1 mM^-1, not the package value 1.5 s^-1 mM^-1.

row_label: Imipenem


substrate_name: cefcapene

column_label: Table 2 columns substrate, Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); row matched by Cefcapene.

row_label: Cefcapene

substrate: cefcapene


column_label: Table 2 columns substrate, Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); row matched by Benzylpenicillin, a synonym for Penicillin G.

normalized_value_unit_evidence: kcat 48 s^-1; Km 0.011 mM; printed kcat/Km 4400 s^-1 mM^-1; source quotient 4363.636363636364 s^-1 mM^-1 is table-rounding compatible.

raw_value_unit_evidence: Table 2 row Benzylpenicillin: Km 11 +/- 0.63 uM; kcat 48 +/- 3 s^-1; kcat/Km 4.4 +/- 0.4 uM^-1 s^-1.

row_label: Benzylpenicillin (Penicillin G synonym)


substrate_name: Sulbactam

substrate: Sulbactam


column_label: Table 2 columns substrate, Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); row matched by Cefotaxime.

normalized_value_unit_evidence: kcat 1400 s^-1; Km 0.041 mM; printed kcat/Km 34000 s^-1 mM^-1; source quotient 34146.34146341463 s^-1 mM^-1 is table-rounding compatible.

row_label: Cefotaxime


substrate_name: Meropenem

column_label: Table 2 columns substrate, Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); row matched by Meropenem.

normalized_value_unit_evidence: kcat 0.007 s^-1; Km 0.00011 mM; kcat/Km 70 s^-1 mM^-1; package Km 0.0001 mM is rounded from the table cell.

row_label: Meropenem

substrate: Meropenem


substrate_name: Cefdinir

substrate: Cefdinir


substrate_name: H2O; Cephaloridine

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant A273T

substrate: H2O; Cephaloridine


substrate_name: H2O; Ampicillin

substrate: H2O; Ampicillin


substrate_name: Ampicillin; H2O

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

substrate: Ampicillin; H2O


substrate_name: cefpirome

substrate: cefpirome


substrate_name: carbenicillin

substrate: carbenicillin


substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N132D

substrate: H2O; Penicillin G


substrate_name: 6-beta-Iodopenicillanic acid; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant AmpC T316A

substrate: 6-beta-Iodopenicillanic acid; H2O


substrate_name: Aztreonam; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEM-1 S235A

substrate: Aztreonam; H2O


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


organism: Fluoribacter gormanii

substrate_name: Cefuroxime

substrate: Cefuroxime


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: 7-Aminocephalosporanic acid

substrate: 7-Aminocephalosporanic acid


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: cefalotin

substrate: cefalotin


sequence_source: UniProt Q6SJ61 canonical sequence

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

column_label: Table 4, substrate row 'Cefuroxime', enzyme column 'TEM-1 WT': kcat column = 6+1; Km column = 1050+150 (uM); kcat/Km column = 5.7+1.3 (mM-1 s-1).

normalized_value_unit_evidence: kcat: printed Table 4 cell 6 (Cefuroxime, TEM-1 WT); no unit conversion, value already s-1; exported value 6.0 s-1. Km: printed Table 4 cell 1050 uM; 1050 / 1000 = 1.05 mM; exported value 1.05 mM. kcat/Km: derived as the exact quotient of the paper's own kcat and Km cells, 6 / 1.05 = 5.714285714285714 s-1 mM-1, matching the exported kcat_over_km; the paper's own printed cell rounds to 5.7 at its own one-decimal precision, consistent with this quotient.

raw_value_unit_evidence: Table 4, substrate row Cefuroxime, TEM-1 WT columns: kcat = 6+1; Km = 1050+150 (uM); printed kcat/Km = 5.7+1.3 (mM-1 s-1).

row_label: Table 4, substrate row 'Cefuroxime', TEM-1 WT columns

table_label: Table 4: Kinetic parameters for the WT and mutant TEM enzymes (Biochem. J. 1994, 301:485-494)


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant AmpC T316V


substrate_name: Cefuroxime; H2O

substrate: Cefuroxime; H2O


substrate_name: H2O; Ampicillin

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

substrate: H2O; Ampicillin


substrate_name: Ampicillin; H2O

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

substrate: Ampicillin; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W165S:A273T:E240C


substrate_name: Cephaloridine

substrate: Cephaloridine


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


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: Substituted beta-amino acid

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

substrate: Substituted beta-amino acid


substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y156A

substrate: H2O; Penicillin G


substrate_name: Penicillin G; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N225A

substrate: Penicillin G; H2O


sequence_source: UniProt Q9K578 canonical sequence


substrate_name: Meropenem

substrate: Meropenem


organism: Klebsiella oxytoca

substrate_name: piperacillin

substrate: piperacillin


organism: Klebsiella pneumoniae

substrate_name: Cephalothin; H2O

substrate: Cephalothin; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K161A


substrate_name: H2O; Cephalothin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K161E

substrate: H2O; Cephalothin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K161R


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N167A


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N167D


substrate_name: Cefuroxime

substrate: Cefuroxime


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y228A


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H121A


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: Imipenem

substrate: Imipenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S221A


substrate_name: Nitrocefin

substrate: Nitrocefin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244E


column_label: Table II columns under [Zn2+] = 100 uM: kcat [s^-1], Km [uM], kcat/Km [uM^-1 s^-1]; WT Nitrocefin cells 600, 190, 3.2.

normalized_value_unit_evidence: Km 190 uM = 0.19 mM; kcat 600 s^-1; printed kcat/Km 3.2 uM^-1 s^-1 = 3200 s^-1 mM^-1; expected computed ratio 3157.8947368421054 s^-1 mM^-1 is within table precision/rounding.

raw_value_unit_evidence: Table II WT Nitrocefin at [Zn2+] = 100 uM: kcat 600 s^-1, Km 190 uM, kcat/Km 3.2 uM^-1 s^-1.

row_label: WT / Nitrocefin

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


substrate_name: Penicillin G

substrate: Penicillin G


organism: Homo sapiens

substrate_name: Cefotaxime; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant evMBL8

substrate: Cefotaxime; H2O


substrate_name: Imipenem; H2O

substrate: Imipenem; H2O


substrate_name: amoxicillin

column_label: Table 2 'Table 2: Kinetics parameters of TEM-89 beta-lactamase compared with those of TEM-2, TEM-3, and TEM-59 beta-lactamases'; row Amoxicillin; TEM-59 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Amoxicillin, TEM-59 normalized: kcat 110 s^-1; Km 0.52 mM; kcat/Km 200 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Amoxicillin, TEM-59 columns: kcat 110 s^-1; Km 520 uM; kcat/Km 0.2 uM^-1 s^-1.

row_label: Amoxicillin

substrate: amoxicillin


column_label: Table 2 'Table 2: Kinetics parameters of TEM-89 beta-lactamase compared with those of TEM-2, TEM-3, and TEM-59 beta-lactamases'; row Benzylpenicillin; TEM-59 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Benzylpenicillin, TEM-59 normalized: kcat 200 s^-1; Km 0.14 mM; kcat/Km 1400 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Benzylpenicillin, TEM-59 columns: kcat 200 s^-1; Km 140 uM; kcat/Km 1.4 uM^-1 s^-1.

row_label: Benzylpenicillin


substrate_name: Cephalothin

raw_value_unit_evidence: Table 4 SHV-1 row for cephalothin reports Km = 48 +/- 3 uM, kcat = 25.0 +/- 0.7 s^-1, and kcat/Km = 0.50 +/- 0.03 uM^-1 s^-1.

row_label: Cephalothin / SHV-1

table_label: Table 4. Steady-state kinetic parameters

substrate: Cephalothin


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D104K

substrate: Nitrocefin; H2O


substrate_name: Ampicillin

sequence_variant_note: Mutation signature D104K could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Ampicillin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D104K,G238S


column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Cefotaxime; CTX-M-26 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 120, 150, 0.77

raw_value_unit_evidence: CTX-M-26 / Cefotaxime: kcat=120 s^-1; Km=150 uM; kcat/Km=0.77 uM^-1 s^-1

row_label: CTX-M-26 / Cefotaxime


substrate_name: aztreonam

column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Aztreonam; CTX-M-26 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 100, 130, 0.78

raw_value_unit_evidence: CTX-M-26 / Aztreonam: kcat=100 s^-1; Km=130 uM; kcat/Km=0.78 uM^-1 s^-1

row_label: CTX-M-26 / Aztreonam

substrate: aztreonam


column_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases; row Cephalothin; CTX-M-26 columns kcat (s^-1), Km (uM), kcat/Km (uM^-1 s^-1); cells 530, 110, 4.7

raw_value_unit_evidence: CTX-M-26 / Cephalothin: kcat=530 s^-1; Km=110 uM; kcat/Km=4.7 uM^-1 s^-1

row_label: CTX-M-26 / Cephalothin


substrate_name: Ceftazidime

column_label: Table 4 CTX-M-26 / Ceftazidime row, kcat and Km cells and their same-row quotient.

raw_value_unit_evidence: CTX-M-26 Ceftazidime kcat 0.015 s^-1; Km 3,300 uM.

row_label: CTX-M-26 / Ceftazidime

table_label: Table 4. Kinetic parameters of CTX-M-25 and CTX-M-26 beta-lactamases

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


substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


substrate_name: ampicillin

assay_conditions_summary: pH 7; 303.15 K; buffer pH 7

column_label: Table 3 row Ampicillin columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1); footnotes below Table 3 state standard deviations were below 20% and footnote b marks Ki values.

normalized_value_unit_evidence: kcat 5 s^-1; Km-column value 0.001 mM; kcat/Km 4200 s^-1 mM^-1.

raw_value_unit_evidence: Table 3 row Ampicillin cells: kcat 5 s^-1; Km column 1 uM; kcat/Km 4.2e+06 M^-1 s^-1. Footnote b states this Km-column value is Ki (uM).

row_label: Ampicillin

table_label: Table 3, kinetic properties of the purified TEM-107 beta-lactamase with various beta-lactam compounds

substrate: ampicillin


substrate_name: ceftazidime

column_label: Table 3; row Ceftazidime; column kcat (s^-1) raw value 15; column Km (uM) raw value 86; column kcat/Km (M^-1*s^-1) raw value 1.8 x 10^5

normalized_value_unit_evidence: kcat normalized_value=15 normalized_unit=s^-1; Km normalized_value=0.086 normalized_unit=mM; kcat/Km normalized_value=180 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=15 raw_unit=s^-1; Km raw_value=86 raw_unit=uM; kcat/Km raw_value=1.8 x 10^5 raw_unit=M^-1*s^-1

row_label: Ceftazidime

table_label: Table 3. Kinetic properties of the purified TEM-107 beta-lactamase with various beta-lactam compounds

substrate: ceftazidime


column_label: Table 3; row Aztreonam; column kcat (s^-1) raw value 2; column Km (uM) raw value 17; column kcat/Km (M^-1*s^-1) raw value 1.2 x 10^5

normalized_value_unit_evidence: kcat normalized_value=2 normalized_unit=s^-1; Km normalized_value=0.017 normalized_unit=mM; kcat/Km normalized_value=120 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2 raw_unit=s^-1; Km raw_value=17 raw_unit=uM; kcat/Km raw_value=1.2 x 10^5 raw_unit=M^-1*s^-1

row_label: Aztreonam


column_label: Table 3; row Cefotaxime; column kcat (s^-1) raw value 3; column Km (uM) raw value 22; column kcat/Km (M^-1*s^-1) raw value 1.2 x 10^5

normalized_value_unit_evidence: kcat normalized_value=3 normalized_unit=s^-1; Km normalized_value=0.022 normalized_unit=mM; kcat/Km normalized_value=120 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=3 raw_unit=s^-1; Km raw_value=22 raw_unit=uM; kcat/Km raw_value=1.2 x 10^5 raw_unit=M^-1*s^-1


substrate_name: nitrocefin

column_label: Table 3; row Nitrocefin; column kcat (s^-1) raw value 72; column Km (uM) raw value 5; column kcat/Km (M^-1*s^-1) raw value 1.4 x 10^7

normalized_value_unit_evidence: kcat normalized_value=72 normalized_unit=s^-1; Km normalized_value=0.005 normalized_unit=mM; kcat/Km normalized_value=14000 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=72 raw_unit=s^-1; Km raw_value=5 raw_unit=uM; kcat/Km raw_value=1.4 x 10^7 raw_unit=M^-1*s^-1

row_label: Nitrocefin

substrate: nitrocefin


substrate_name: piperacillin

column_label: Table 3 row Piperacillin columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1); footnotes below Table 3 state standard deviations were below 20% and footnote b marks Ki values.

normalized_value_unit_evidence: kcat 11 s^-1; Km-column value 0.003 mM; kcat/Km 3300 s^-1 mM^-1.

raw_value_unit_evidence: Table 3 row Piperacillin cells: kcat 11 s^-1; Km column 3 uM; kcat/Km 3.3e+06 M^-1 s^-1. Footnote b states this Km-column value is Ki (uM).

row_label: Piperacillin

substrate: piperacillin


substrate_name: cefepime

column_label: Table 3; row Cefepime; column kcat (s^-1) raw value 3; column Km (uM) raw value 26; column kcat/Km (M^-1*s^-1) raw value 1.3 x 10^5

normalized_value_unit_evidence: kcat normalized_value=3 normalized_unit=s^-1; Km normalized_value=0.026 normalized_unit=mM; kcat/Km normalized_value=130 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=3 raw_unit=s^-1; Km raw_value=26 raw_unit=uM; kcat/Km raw_value=1.3 x 10^5 raw_unit=M^-1*s^-1

row_label: Cefepime

substrate: cefepime


substrate_name: cephalotin

column_label: Table 3; row Cephalothin; column kcat (s^-1) raw value 1; column Km (uM) raw value 10; column kcat/Km (M^-1*s^-1) raw value 7.9 x 10^4

normalized_value_unit_evidence: kcat normalized_value=1 normalized_unit=s^-1; Km normalized_value=0.01 normalized_unit=mM; kcat/Km normalized_value=79 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1 raw_unit=s^-1; Km raw_value=10 raw_unit=uM; kcat/Km raw_value=7.9 x 10^4 raw_unit=M^-1*s^-1

row_label: Cephalothin

substrate: cephalotin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: doripenem

substrate: doripenem


substrate_name: meropenem

substrate: meropenem


substrate_name: cefalotin

substrate: cefalotin


substrate_name: Oxacillin

column_label: Chemistry & Biology 2009 Table 1, row label Oxacillin; kcat_over_km paper=1400 s^-1 mM^-1; export=1368.421052631579 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=130 s^-1; km=0.095 mM; kcat_over_km=1400 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Oxacillin; kcat 130 s^-1; Km 95 uM; kcat/Km 1.4 x 10^6 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%.

row_label: Oxacillin

table_label: Chemistry & Biology 2009 Table 1

substrate: Oxacillin


substrate_name: temocillin

column_label: Official Cell fulltext HTML Table 1 row Temocillin columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row Temocillin: kcat 0.3 s^-1; Km 45 uM; kcat/Km 6.6 x 10^3 M^-1 s^-1.

row_label: Temocillin

table_label: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates

substrate: temocillin


substrate_name: faropenem

column_label: Official Cell fulltext HTML Table 1 row Faropenem columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row Faropenem: kcat 0.038 s^-1; Km 13 uM; kcat/Km 2.9 x 10^3 M^-1 s^-1.

row_label: Faropenem

substrate: faropenem


substrate_name: ertapenem

column_label: Official Cell fulltext HTML Table 1 row Ertapenem columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: kcat 0.13 s^-1; Km 0.1 mM; metric-labeled kcat/Km 1.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Ertapenem: kcat 0.13 s^-1; Km 100 uM; kcat/Km 1.3 x 10^3 M^-1 s^-1.

row_label: Ertapenem

substrate: ertapenem


column_label: Chemistry & Biology 2009 Table 1, row label Nitrocefin; kcat_over_km paper=7700 s^-1 mM^-1; export=7833.333333333334 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=940 s^-1; km=0.12 mM; kcat_over_km=7700 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Nitrocefin; kcat 940 s^-1; Km 120 uM; kcat/Km 7.7 x 10^6 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%.


column_label: Chemistry & Biology 2009 Table 1, row label Imipenem; kcat_over_km paper=370 s^-1 mM^-1; export=369.2307692307692 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=4.8 s^-1; km=0.013 mM; kcat_over_km=370 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Imipenem; kcat 4.8 s^-1; Km 13 uM; kcat/Km 3.7 x 10^5 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%.

row_label: Imipenem


substrate_name: cephalothin

column_label: Chemistry & Biology 2009 Table 1, row label Cephalothin (footnote a); kcat_over_km paper=230 s^-1 mM^-1; export=225.64102564102564 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=44 s^-1; km=0.195 mM; kcat_over_km=230 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Cephalothin (footnote a); kcat 44 s^-1; Km 195 uM; kcat/Km 2.3 x 10^5 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%. Footnote for this substrate: Biphasic kinetics were observed with this substrate. However, the rapid establishment of the steady state did not allow the measurement of initial rate kinetic parameters.

row_label: Cephalothin (footnote a)

substrate: cephalothin


substrate_name: cefuroxime

column_label: Table 3; row Cefuroxime; column kcat (s^-1) raw value 2; column Km (uM) raw value 34; column kcat/Km (M^-1*s^-1) raw value 6.7 x 10^4

normalized_value_unit_evidence: kcat normalized_value=2 normalized_unit=s^-1; Km normalized_value=0.034 normalized_unit=mM; kcat/Km normalized_value=67 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2 raw_unit=s^-1; Km raw_value=34 raw_unit=uM; kcat/Km raw_value=6.7 x 10^4 raw_unit=M^-1*s^-1

row_label: Cefuroxime

substrate: cefuroxime


substrate_name: ampicillin

substrate: ampicillin


substrate_name: Meropenem

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: nitrocefin

column_label: PMID 29228168 PDF page 6, Table 3, Nitrocefin block, SHV-14 column: Km 45 +/- 1.7 uM; kcat 5.85 +/- 0.2 s^-1; kcat/Km 0.13 s^-1 uM^-1.

normalized_value_unit_evidence: Table 3 Nitrocefin/SHV-14: kcat normalized_value=5.85 normalized_unit=s^-1; Km normalized_value=0.045 normalized_unit=mM; kcat/Km normalized_value=130 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Nitrocefin/SHV-14: Km raw_value=45 +/- 1.7 raw_unit=uM; kcat raw_value=5.85 +/- 0.2 raw_unit=s^-1; kcat/Km raw_value=0.13 raw_unit=s^-1*uM^-1.

row_label: Nitrocefin; wild-type SHV-14 column

table_label: Table 3. Kinetics analysis of SHV-14 and its mutated proteins (PDF page 6 of 8)

substrate: nitrocefin


substrate_name: cefoperazone

column_label: PMID 29228168 PDF page 6, Table 3, Cefoperazone block, SHV-14 column: Km 57.4 +/- 6 uM; kcat 229.5 +/- 10.6 s^-1; kcat/Km 4 s^-1 uM^-1.

normalized_value_unit_evidence: Table 3 Cefoperazone/SHV-14: kcat normalized_value=229.5 normalized_unit=s^-1; Km normalized_value=0.0574 normalized_unit=mM; printed kcat/Km normalized_value=4000 normalized_unit=s^-1*mM^-1. The current 3998.257839721254 is the unrounded quotient 229.5/0.0574; strict correction should preserve the printed efficiency cell.

raw_value_unit_evidence: Cefoperazone/SHV-14: Km raw_value=57.4 +/- 6 raw_unit=uM; kcat raw_value=229.5 +/- 10.6 raw_unit=s^-1; kcat/Km raw_value=4 raw_unit=s^-1*uM^-1.

row_label: Cefoperazone; wild-type SHV-14 column

substrate: cefoperazone


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


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


substrate_name: amoxicillin

substrate: amoxicillin


substrate_name: carbenicillin

substrate: carbenicillin


substrate_name: Loracarbef

substrate: Loracarbef


substrate_name: Ceftazidime

column_label: Table 2 wild-type NDM-1 columns Km (uM), Kcat (s^-1), and Kcat/Km (uM^-1 s^-1) for Ceftazidime.

normalized_value_unit_evidence: kcat=119.2 s^-1; Km=0.03843 mM; Kcat/Km=3102 s^-1*mM^-1; package kcat/Km 3136.842105263158 is consistent with displayed-value rounding.

row_label: Wild type NDM-1 / Ceftazidime

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

substrate: Ceftazidime


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Q123A

substrate: Nitrocefin; H2O


substrate_name: Nitrocefin

column_label: Table 2 wild-type NDM-1 columns Km (uM), Kcat (s^-1), and Kcat/Km (uM^-1 s^-1) for Nitrocefin.

normalized_value_unit_evidence: kcat=1.332 s^-1; Km=0.01272 mM; Kcat/Km=104 s^-1*mM^-1; package kcat/Km 102.46153846153847 is consistent with displayed-value rounding.

row_label: Wild type NDM-1 / Nitrocefin

substrate: Nitrocefin


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: Ampicillin

column_label: Table 2 wild-type NDM-1 columns Km (uM), Kcat (s^-1), and Kcat/Km (uM^-1 s^-1) for Ampicillin.

normalized_value_unit_evidence: kcat=469.6 s^-1; Km=0.148 mM; Kcat/Km=3172 s^-1*mM^-1; package kcat/Km 3172.9729729729734 is consistent with displayed-value rounding.

row_label: Wild type NDM-1 / Ampicillin

substrate: Ampicillin


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: piperacillin

substrate: piperacillin


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

substrate: ampicillin


substrate_name: cephalothin

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


substrate_name: ceftaxidime

substrate: ceftaxidime


substrate_name: temocillin

substrate: temocillin


organism: Klebsiella pneumoniae subsp. ozaenae

substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-2(pBP60-1) G238S/E240


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-2(pBP60-1) S238/E240K

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-2(pBP60-1) G238/E240K


organism: Kluyvera ascorbata


substrate_name: Cephalothin

substrate: Cephalothin


organism: Moraxella catarrhalis

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; row BRO-2p / Cephaloridine; kcat column raw 5.6 s^-1 normalized 5.6 s^-1; Km column raw 2.8 uM normalized 0.0028 mM; Specificity (kcat/Km) column raw 2 x 10^6 M^-1 s^-1 normalized 2000 s^-1 mM^-1

row_label: BRO-2p / Cephaloridine

substrate: Cephaloridine


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; row BRO-2p / Cephalosporin C; kcat column raw 4.7 s^-1 normalized 4.7 s^-1; Km column raw 3 uM normalized 0.003 mM; Specificity (kcat/Km) column raw 1.6 x 10^6 M^-1 s^-1 normalized 1600 s^-1 mM^-1

row_label: BRO-2p / Cephalosporin C

substrate: Cephalosporin C


substrate_name: Loracarbef

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 BRO-2p / Loracarbef; kcat column raw 95 s^-1 normalized 95 s^-1; Km column raw 38 uM normalized 0.038 mM; Specificity (kcat/Km) column raw 2.5 x 10^6 M^-1 s^-1 normalized 2500 s^-1 mM^-1

row_label: BRO-2p / Loracarbef

substrate: Loracarbef


substrate_name: mecillinam

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 BRO-2p / Mecillinam; kcat column raw 29 s^-1 normalized 29 s^-1; Km column raw 63 uM normalized 0.063 mM; Specificity (kcat/Km) column raw 0.46 x 10^6 M^-1 s^-1 normalized 460 s^-1 mM^-1

row_label: BRO-2p / Mecillinam

substrate: mecillinam


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 BRO-1p / Loracarbef; kcat column raw 79 s^-1 normalized 79 s^-1; Km column raw 50 uM normalized 0.05 mM; Specificity (kcat/Km) column raw 1.6 x 10^6 M^-1 s^-1 normalized 1600 s^-1 mM^-1

row_label: BRO-1p / Loracarbef


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 BRO-1p / Cephalosporin C; kcat column raw 5 s^-1 normalized 5 s^-1; Km column raw 3.9 uM normalized 0.0039 mM; Specificity (kcat/Km) column raw 1.3 x 10^6 M^-1 s^-1 normalized 1300 s^-1 mM^-1

row_label: BRO-1p / 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; row BRO-2p / Cephalothin; kcat column raw 4.6 s^-1 normalized 4.6 s^-1; Km column raw 1.2 uM normalized 0.0012 mM; Specificity (kcat/Km) column raw 4 x 10^6 M^-1 s^-1 normalized 4000 s^-1 mM^-1

row_label: BRO-2p / 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; row BRO-1p / Cephalothin; kcat column raw 4.9 s^-1 normalized 4.9 s^-1; Km column raw 0.9 uM normalized 0.0009 mM; Specificity (kcat/Km) column raw 5.5 x 10^6 M^-1 s^-1 normalized 5500 s^-1 mM^-1

row_label: BRO-1p / Cephalothin


substrate_name: 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; row BRO-2p / Methicillin; kcat column raw 190 s^-1 normalized 190 s^-1; Km column raw 26 uM normalized 0.026 mM; Specificity (kcat/Km) column raw 7.3 x 10^6 M^-1 s^-1 normalized 7300 s^-1 mM^-1

row_label: BRO-2p / Methicillin

substrate: Methicillin


substrate_name: Penicillin G

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 BRO-2p / Benzylpenicillin; kcat column raw 41 s^-1 normalized 41 s^-1; Km column raw 2.9 uM normalized 0.0029 mM; Specificity (kcat/Km) column raw 14 x 10^6 M^-1 s^-1 normalized 14000 s^-1 mM^-1

row_label: BRO-2p / Benzylpenicillin

substrate: Penicillin G


substrate_name: Cefaclor

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 BRO-1p / Cefaclor; kcat column raw 65 s^-1 normalized 65 s^-1; Km column raw 34 uM normalized 0.034 mM; Specificity (kcat/Km) column raw 1.9 x 10^6 M^-1 s^-1 normalized 1900 s^-1 mM^-1

row_label: BRO-1p / 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; row BRO-1p / Cloxacillin; kcat column raw 5 s^-1 normalized 5 s^-1; Km column raw 1.4 uM normalized 0.0014 mM; Specificity (kcat/Km) column raw 3.6 x 10^6 M^-1 s^-1 normalized 3600 s^-1 mM^-1

row_label: BRO-1p / Cloxacillin

substrate: Cloxacillin


substrate_name: Nitrocefin

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 BRO-2p / Nitrocefin; kcat column raw 233 s^-1 normalized 233 s^-1; Km column raw 11 uM normalized 0.011 mM; Specificity (kcat/Km) column raw 21 x 10^6 M^-1 s^-1 normalized 21000 s^-1 mM^-1

row_label: BRO-2p / Nitrocefin

substrate: Nitrocefin


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; row BRO-2p / Ampicillin; kcat column raw 32 s^-1 normalized 32 s^-1; Km column raw 4.6 uM normalized 0.0046 mM; Specificity (kcat/Km) column raw 7.1 x 10^6 M^-1 s^-1 normalized 7100 s^-1 mM^-1

row_label: BRO-2p / Ampicillin

substrate: Ampicillin


substrate_name: Cefuroxime

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 BRO-2p / Cefuroxime; kcat column raw 4.8 s^-1 normalized 4.8 s^-1; Km column raw 56 uM normalized 0.056 mM; Specificity (kcat/Km) column raw 0.086 x 10^6 M^-1 s^-1 normalized 86 s^-1 mM^-1

row_label: BRO-2p / Cefuroxime

substrate: Cefuroxime


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 BRO-2p / Cloxacillin; kcat column raw 8.6 s^-1 normalized 8.6 s^-1; Km column raw 1.5 uM normalized 0.0015 mM; Specificity (kcat/Km) column raw 5.7 x 10^6 M^-1 s^-1 normalized 5700 s^-1 mM^-1

row_label: BRO-2p / Cloxacillin


organism: Morganella morganii

substrate_name: cefepime

substrate: cefepime


substrate_name: H2O; Cefotaxime

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant M19

substrate: H2O; Cefotaxime


substrate_name: piperacillin

substrate: piperacillin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Ceftazidime

substrate: Ceftazidime


substrate_name: cefoxitin

substrate: cefoxitin


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; row BRO-1p / Cephaloridine; kcat column raw 4.8 s^-1 normalized 4.8 s^-1; Km column raw 1.7 uM normalized 0.0017 mM; Specificity (kcat/Km) column raw 2.8 x 10^6 M^-1 s^-1 normalized 2800 s^-1 mM^-1

row_label: BRO-1p / Cephaloridine

substrate: Cephaloridine


substrate_name: H2O; Amoxicillin

substrate: H2O; Amoxicillin


substrate_name: Amoxicillin; H2O

substrate: Amoxicillin; H2O


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 BRO-1p / Cefuroxime; kcat column raw 4.1 s^-1 normalized 4.1 s^-1; Km column raw 68 uM normalized 0.068 mM; Specificity (kcat/Km) column raw 0.061 x 10^6 M^-1 s^-1 normalized 61 s^-1 mM^-1

row_label: BRO-1p / Cefuroxime


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 BRO-1p / Methicillin; kcat column raw 168 s^-1 normalized 168 s^-1; Km column raw 34 uM normalized 0.034 mM; Specificity (kcat/Km) column raw 4.9 x 10^6 M^-1 s^-1 normalized 4900 s^-1 mM^-1

row_label: BRO-1p / 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; row BRO-1p / Nitrocefin; kcat column raw 151 s^-1 normalized 151 s^-1; Km column raw 6.9 uM normalized 0.0069 mM; Specificity (kcat/Km) column raw 22 x 10^6 M^-1 s^-1 normalized 22000 s^-1 mM^-1

row_label: BRO-1p / Nitrocefin


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 BRO-1p / Ampicillin; kcat column raw 33 s^-1 normalized 33 s^-1; Km column raw 2.5 uM normalized 0.0025 mM; Specificity (kcat/Km) column raw 14 x 10^6 M^-1 s^-1 normalized 14000 s^-1 mM^-1

row_label: BRO-1p / 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; row BRO-1p / Benzylpenicillin; kcat column raw 40 s^-1 normalized 40 s^-1; Km column raw 2.7 uM normalized 0.0027 mM; Specificity (kcat/Km) column raw 14 x 10^6 M^-1 s^-1 normalized 14000 s^-1 mM^-1

row_label: BRO-1p / Benzylpenicillin


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 BRO-2p / Cefaclor; kcat column raw 69 s^-1 normalized 69 s^-1; Km column raw 43 uM normalized 0.043 mM; Specificity (kcat/Km) column raw 1.6 x 10^6 M^-1 s^-1 normalized 1600 s^-1 mM^-1

row_label: BRO-2p / Cefaclor


substrate_name: mecillinam

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 BRO-1p / Mecillinam; kcat column raw 31 s^-1 normalized 31 s^-1; Km column raw 40 uM normalized 0.04 mM; Specificity (kcat/Km) column raw 0.78 x 10^6 M^-1 s^-1 normalized 780 s^-1 mM^-1

row_label: BRO-1p / Mecillinam

substrate: mecillinam


substrate_name: H2O; Ampicillin

substrate: H2O; Ampicillin


substrate_name: Cephalothin

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: Cephalothin


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


substrate_name: Penicillin G

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: Penicillin G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant M37


substrate_name: Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant G238S

substrate: Nitrocefin


substrate_name: Ampicillin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244S

substrate: Ampicillin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244Q


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244L


substrate_name: meropenem

column_label: Official Cell fulltext HTML Table 1 row Meropenem columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row Meropenem: kcat 0.07 s^-1; Km 11 uM; kcat/Km 6.2 x 10^3 M^-1 s^-1.

row_label: Meropenem

substrate: meropenem


substrate_name: panipenem

column_label: Chemistry & Biology 2009 Table 1, row label Panipenem

normalized_value_unit_evidence: Normalized evidence: kcat=1.4 s^-1; km=0.014 mM; kcat_over_km=100 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Panipenem; kcat 1.4 s^-1; Km 14 uM; kcat/Km 1.0 x 10^5 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%.

row_label: Panipenem

substrate: panipenem


substrate_name: ampicillin

column_label: Chemistry & Biology 2009 Table 1, row label Ampicillin; kcat_over_km paper=2400 s^-1 mM^-1; export=2417.721518987342 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=955 s^-1; km=0.395 mM; kcat_over_km=2400 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Ampicillin; kcat 955 s^-1; Km 395 uM; kcat/Km 2.4 x 10^6 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%.

row_label: Ampicillin

substrate: ampicillin


organism: Mycobacterium tuberculosis


substrate_name: Cephapirin

substrate: Cephapirin


substrate_name: amoxicillin

substrate: amoxicillin


substrate_name: cefazolin

substrate: cefazolin


substrate_name: Penicillin V

substrate: Penicillin V


substrate_name: azlocillin

substrate: azlocillin


substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


substrate_name: Cefotaxime; H2O

substrate: Cefotaxime; H2O


substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


column_label: Scheme 2 columns kcat (min^-1), Km (uM), and kcat/Km (min^-1 M^-1); row Meropenem.

raw_value_unit_evidence: Scheme 2 row Meropenem reports kcat 0.08 min^-1, Km 3.4 uM, and kcat/Km 2.4 x 10^4 min^-1 M^-1.

row_label: Scheme 2 row Meropenem, source label ref. 16

table_label: PMID 24846409, Scheme 2: Kinetic Parameters of Carbapenem Hydrolysis by BlaC and Structure of the C2 Substituent


substrate_name: tebipenem

column_label: Scheme 2 columns kcat (min^-1), Km (uM), and kcat/Km (min^-1 M^-1); row Tebipenem.

raw_value_unit_evidence: Scheme 2 row Tebipenem reports kcat 0.03 min^-1, Km 0.8 uM, and kcat/Km 3.8 x 10^4 min^-1 M^-1.

row_label: Scheme 2 row Tebipenem, source label this work

substrate: tebipenem


substrate_name: doripenem

column_label: Scheme 2 columns kcat (min^-1), Km (uM), and kcat/Km (min^-1 M^-1); row Doripenem.

raw_value_unit_evidence: Scheme 2 row Doripenem reports kcat 0.02 min^-1, Km 0.2 uM, and kcat/Km 1.0 x 10^5 min^-1 M^-1.

row_label: Scheme 2 row Doripenem, source label ref. 17

substrate: doripenem


substrate_name: ertapenem

column_label: Scheme 2 columns kcat (min^-1), Km (uM), and kcat/Km (min^-1 M^-1); row Ertapenem.

raw_value_unit_evidence: Scheme 2 row Ertapenem reports kcat 0.02 min^-1, Km 0.2 uM, and kcat/Km 1.0 x 10^5 min^-1 M^-1.

row_label: Scheme 2 row Ertapenem, source label ref. 17

substrate: ertapenem


substrate_name: Cefamandole

assay_conditions_summary: pH 6.4; 310.15 K; buffer 0.1 M sodium phosphate

column_label: Table 3 Cefamandole row under Recombinant Y-49 beta-lactamase reports Km=645 uM and kcat=22 s^-1; no direct kcat/Km column is printed, so catalytic efficiency is calculated from those exact cells.

normalized_value_unit_evidence: Km normalized_value=0.645 normalized_unit=mM; kcat normalized_value=22 normalized_unit=s^-1; kcat_over_km normalized_value=34.10852713178294 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=645 raw_unit=uM; kcat raw_value=22 raw_unit=s^-1; kcat_over_km computed from exact primary cells 22 s^-1 / 0.645 mM

row_label: Cefamandole row; Recombinant Y-49 beta-lactamase columns Km and kcat

table_label: Antimicrobial Agents and Chemotherapy PDF page 5 / journal page 1379, Table 3: Kinetic characteristics of recombinant Y49 beta-lactamase from E. coli and beta-lactamase obtained directly from M. tuberculosis

substrate: Cefamandole


organism: Mycolicibacterium smegmatis

substrate_name: piperacillin

column_label: Table 4 row Piperacillin; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Piperacillin: Vmax 11.01 uM*s^-1; Km 12.56 uM; Kcat 22.02 s^-1; Kcat/Km 1.756 uM^-1*s^-1.

row_label: Piperacillin

table_label: Table 4, Kinetic parameters of sMSMEG_4455 with beta-lactam group antibiotics

substrate: piperacillin


substrate_name: cefotaxime

column_label: Table 4 row Cefotaxime; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Cefotaxime: Vmax 0.786 uM*s^-1; Km 364.74 uM; Kcat 1.572 s^-1; Kcat/Km 0.004 uM^-1*s^-1.

row_label: Cefotaxime

substrate: cefotaxime


substrate_name: Bocillin-FL

substrate: Bocillin-FL


substrate_name: ticarcillin

column_label: Table 4 row Ticarcillin; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 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: Ticarcillin

substrate: ticarcillin


column_label: Table 4 row Amoxicillin; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Amoxicillin: Vmax 0.885 uM*s^-1; Km 6.49 uM; Kcat 1.77 s^-1; Kcat/Km 0.272 uM^-1*s^-1.

row_label: Amoxicillin


substrate_name: ceftriaxone

column_label: Table 4 row Ceftriazone; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Ceftriazone: Vmax 0.912 uM*s^-1; Km 11.757 uM; Kcat 1.825 s^-1; Kcat/Km 0.155 uM^-1*s^-1.

row_label: Ceftriazone

substrate: ceftriaxone


substrate_name: cephalothin

column_label: Table 4 row Cephalothin; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Cephalothin: Vmax 0.515 uM*s^-1; Km 655.015 uM; Kcat 1.031 s^-1; Kcat/Km 0.001 uM^-1*s^-1.

row_label: Cephalothin

substrate: cephalothin


organism: Nocardia asteroides


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: carbenicillin

column_label: Table 4 row Carbenicillin; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Carbenicillin: Vmax 5.11 uM*s^-1; Km 21.74 uM; Kcat 10.22 s^-1; Kcat/Km 0.47 uM^-1*s^-1.

row_label: Carbenicillin

substrate: carbenicillin


substrate_name: Oxacillin

column_label: Table 4 row Oxacillin; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Oxacillin: Vmax 5.954 uM*s^-1; Km 193.12 uM; Kcat 11.9 s^-1; Kcat/Km 0.061 uM^-1*s^-1.

row_label: Oxacillin

substrate: Oxacillin


substrate_name: penicillin G

column_label: Table 4 row PenicillinG; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row PenicillinG: Vmax 13.8 uM*s^-1; Km 3.345 uM; Kcat 27.6 s^-1; Kcat/Km 8.25 uM^-1*s^-1.

row_label: PenicillinG

substrate: penicillin G


substrate_name: nitrocefin

column_label: Table 4 row Nitrocefin; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Nitrocefin: Vmax 0.007 uM*s^-1; Km 9.477 uM; Kcat 0.014 s^-1; Kcat/Km 0.001 uM^-1*s^-1.

row_label: Nitrocefin

substrate: nitrocefin


substrate_name: cephalexin

column_label: Table 4 row Cephalexin; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Cephalexin: Vmax 0.039 uM*s^-1; Km 8.969 uM; Kcat 0.079 s^-1; Kcat/Km 0.008 uM^-1*s^-1.

row_label: Cephalexin

substrate: cephalexin


substrate_name: ampicillin

column_label: Table 4 row Ampicillin; columns Km, Kcat, and Kcat/Km.

raw_value_unit_evidence: Table 4 row Ampicillin: Vmax 0.481 uM*s^-1; Km 9.544 uM; Kcat 9.62 s^-1; Kcat/Km 1.007 uM^-1*s^-1.

row_label: Ampicillin

substrate: ampicillin


organism: Nocardia farcinica

substrate_name: H2O; Nitrocefin

sequence_source: UniProtKB Q5YXD6

unit: Mswedgeone

substrate: H2O; Nitrocefin


organism: Ochrobactrum anthropi

sequence_source: UniProtKB Q9ZBA9 + N275R reconstruction

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9ZBA9 + N275R reconstruction and applied mutation signature N275R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant DAP-475G487-N275R


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant DAP-475G487


organism: Proteus mirabilis

sequence_source: UniProtKB Q93LJ5

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

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_name: H2O; Penicillin G

substrate: H2O; Penicillin G


substrate_name: Ticarcillin

column_label: Table 2, TEM-89 enzyme block; row Ticarcillin; column k cat (s^-1) cell 6; column K m (uM) cell 24; column k cat / K m (uM^-1 s^-1) cell 0.25.

normalized_value_unit_evidence: kcat 6 s^-1 = 6.0 s^(-1). Km 24 uM = 24 / 1000 = 0.024 mM. kcat/Km 0.25 uM^-1 s^-1 = 0.25 * 1000 = 250.0 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 Ticarcillin, TEM-89 enzyme block: kcat column cell 6 s^-1; Km column cell 24 uM; kcat/Km column cell 0.25 uM^-1 s^-1.

substrate: Ticarcillin


substrate_name: piperacillin

substrate: piperacillin


organism: Providencia stuartii

substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: Cephaloridine

substrate: Cephaloridine


substrate_name: aztreonam

substrate: aztreonam


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K104E


substrate_name: cefotaxime

column_label: Table 2 wild-type NDM-1 columns Km (uM), Kcat (s^-1), and Kcat/Km (uM^-1 s^-1) for Cefotaxime.

normalized_value_unit_evidence: kcat=84.84 s^-1; Km=0.03194 mM; Kcat/Km=2631 s^-1*mM^-1; package kcat/Km 2651.25 is consistent with displayed-value rounding.

row_label: Wild type NDM-1 / Cefotaxime

substrate: cefotaxime


substrate_name: Imipenem

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q123A to reconstruct the assayed variant sequence.

column_label: Table 2 NDM-1Q123A mutant columns Km (uM), Kcat (s^-1), and Kcat/Km (uM^-1 s^-1) for Imipenem.

normalized_value_unit_evidence: kcat=678.2 s^-1; Km=0.02488 mM; Kcat/Km=27250 s^-1*mM^-1; package kcat/Km 27128.0 is consistent with displayed-value rounding.

row_label: NDM-1Q123A mutant / Imipenem

substrate: Imipenem


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1(R974) S238G/E240

substrate: Nitrocefin; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant M69V


substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant M69I


organism: Pseudomonas aeruginosa

substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: H2O; Imipenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant IMP-1 W64A

substrate: H2O; Imipenem


substrate_name: cephaloridin

substrate: cephaloridin


substrate_name: Imipenem; H2O

mutation_type: deletion

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant IMP-1 delta 61-66

substrate: Imipenem; H2O


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: Cefuroxime

substrate: Cefuroxime


substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S164R

substrate: H2O; Nitrocefin


substrate_name: Ceftazidime

substrate: Ceftazidime


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant P51L


substrate_name: carbenicillin

substrate: carbenicillin


column_label: PMC Table 2, Aztreonam: Km 50 uM = 0.05 mM; kcat 5.3 s^-1; printed kcat/Km 1.1 × 10^5 M^-1 s^-1 = 110 s^-1 mM^-1. Current 105.99999999999999 is the exact quotient of the same row's printed kcat and Km cells; the separately printed efficiency is retained without forcing literal equality.

normalized_value_unit_evidence: The same Table 2 row normalizes to kcat=5.3 s^-1 and Km=0.05 mM. Their stored-precision quotient is 5.3 / 0.05 = 105.99999999999999 s^-1 mM^-1. The independently printed efficiency 1.1 × 10^5 M^-1 s^-1 normalizes separately to 110 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=50 raw_unit=uM; kcat raw_value=5.3 raw_unit=s^-1; printed kcat/Km raw_value=1.1 × 10^5 raw_unit=M^-1 s^-1

row_label: Aztreonam

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


substrate_name: Ampicillin

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

normalized_value_unit_evidence: Km normalized=0.0055 mM; kcat normalized=18 s^-1; kcat/Km normalized=3300 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Ampicillin: Km=5.5 uM; kcat=18 s^-1; kcat/Km=3.3 x 10^6 M^-1 s^-1.

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

substrate: Ampicillin


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

normalized_value_unit_evidence: Km normalized=0.0062 mM; kcat normalized=39 s^-1; kcat/Km normalized=6300 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Benzylpenicillin: Km=6.2 uM; kcat=39 s^-1; kcat/Km=6.3 x 10^6 M^-1 s^-1.


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

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

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


substrate_name: piperacillin

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

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

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

row_label: piperacillin

substrate: piperacillin


substrate_name: H2O; Carbenicillin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant R234K

substrate: H2O; Carbenicillin


substrate_name: ceftriaxone

column_label: Table 2 row Ceftriaxone, columns kcat (s^-1), Km (microM), and kcat/Km (mM^-1 s^-1), raw cells 25, 30, and 820, normalized to 25 s^(-1), 0.03 mM, and 820 s^(-1)*mM^(-1)

normalized_value_unit_evidence: kcat normalized_value=25 normalized_unit=s^(-1); Km normalized_value=0.03 normalized_unit=mM; kcat/Km normalized_value=820 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=25 raw_unit=s^-1 raw_cell=25; Km raw_value=30 microM raw_unit=microM raw_cell=30; kcat/Km raw_value=820 mM^-1 s^-1 raw_unit=mM^-1 s^-1 raw_cell=820

row_label: ceftriaxone

table_label: Table 2. Kinetic parameters of purified beta-lactamase BEL-1

substrate: ceftriaxone


substrate_name: Ticarcillin

column_label: Table 2; row Ticarcillin; column kcat: raw 6 s^-1; normalized 6 s^-1; column Km: raw 8 uM; normalized 0.008 mM; column kcat/Km: raw 750 mM^-1 s^-1; normalized 750 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Ticarcillin gives kcat 6 s^-1; Km 8 uM; kcat/Km 750 mM^-1 s^-1.

table_label: PMID 16127048, Table 2: kinetic parameters of purified beta-lactamase BEL-1

substrate: Ticarcillin


column_label: Table 2; row Benzylpenicillin; column kcat: raw 3 s^-1; normalized 3 s^-1; column Km: raw 20 uM; normalized 0.02 mM; column kcat/Km: raw 150 mM^-1 s^-1; normalized 150 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Benzylpenicillin gives kcat 3 s^-1; Km 20 uM; kcat/Km 150 mM^-1 s^-1.


substrate_name: cefotaxime

column_label: Table 2; row Cefotaxime; column kcat: raw 30 s^-1; normalized 30 s^-1; column Km: raw 250 uM; normalized 0.25 mM; column kcat/Km: raw 120 mM^-1 s^-1; normalized 120 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Cefotaxime gives kcat 30 s^-1; Km 250 uM; kcat/Km 120 mM^-1 s^-1.

row_label: Cefotaxime

substrate: cefotaxime


substrate_name: Cefsulodin

column_label: Table 2, Cefsulodine row, kcat column 25 s^-1, Km column 150 uM, kcat/Km column 170 mM^-1 s^-1.

normalized_value_unit_evidence: kcat=25 s^-1; Km=0.15 mM; printed kcat/Km=170 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Cefsulodine row: kcat 25 s^-1; Km 150 uM; kcat/Km 170 mM^-1 s^-1.

row_label: Cefsulodine

table_label: Table 2. Kinetic parameters of BEL-1

substrate: Cefsulodin


substrate_name: aztreonam

column_label: Table 2; row Aztreonam; column kcat: raw 10 s^-1; normalized 10 s^-1; column Km: raw 100 uM; normalized 0.1 mM; column kcat/Km: raw 100 mM^-1 s^-1; normalized 100 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Aztreonam gives kcat 10 s^-1; Km 100 uM; kcat/Km 100 mM^-1 s^-1.

substrate: aztreonam


column_label: Table 2 row Piperacillin, columns kcat (s^-1), Km (microM), and kcat/Km (mM^-1 s^-1), raw cells 2, 15, and 130, normalized to 2 s^(-1), 0.015 mM, and 130 s^(-1)*mM^(-1)

normalized_value_unit_evidence: kcat normalized_value=2 normalized_unit=s^(-1); Km normalized_value=0.015 normalized_unit=mM; kcat/Km normalized_value=130 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=2 raw_unit=s^-1 raw_cell=2; Km raw_value=15 microM raw_unit=microM raw_cell=15; kcat/Km raw_value=130 mM^-1 s^-1 raw_unit=mM^-1 s^-1 raw_cell=130


substrate_name: amoxicillin

column_label: Table 2 row Amoxicillin, columns kcat (s^-1), Km (microM), and kcat/Km (mM^-1 s^-1), raw cells 10, 30, and 330, normalized to 10 s^(-1), 0.03 mM, and 330 s^(-1)*mM^(-1)

normalized_value_unit_evidence: kcat normalized_value=10 normalized_unit=s^(-1); Km normalized_value=0.03 normalized_unit=mM; kcat/Km normalized_value=330 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=10 raw_unit=s^-1 raw_cell=10; Km raw_value=30 microM raw_unit=microM raw_cell=30; kcat/Km raw_value=330 mM^-1 s^-1 raw_unit=mM^-1 s^-1 raw_cell=330

row_label: amoxicillin

substrate: amoxicillin


sequence_source: UniProt REST

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

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

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

row_label: Cefuroxime | VIM-13

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


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

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

row_label: Piperacillin | VIM-13


substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


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

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

row_label: Ampicillin | VIM-13


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

row_label: Cefotaxime | VIM-13


substrate_name: Imipenem

column_label: Table 4, substrate row Imipenem, enzyme column VIM-13: kcat cell 54 +/- 17 s^-1, Km cell 18.5 +/- 2.2 uM, kcat/Km cell 2.92E6 M^-1 s^-1. The exported kcat 54 s^-1 and Km 0.018 mM select the VIM-13 column of the Imipenem row uniquely: the other enzyme column of that row prints different cells.

row_label: Imipenem | VIM-13

substrate: Imipenem


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

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

row_label: Cefotaxime | VIM-1


substrate_name: Penicillin G

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

row_label: Penicillin G | VIM-1

substrate: Penicillin G


substrate_name: cefoxitin

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

normalized_value_unit_evidence: Table 1 row Cefoxitin, IMP-13 normalized: kcat 35 s^-1; Km 0.012 mM; kcat/Km 2900 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Cefoxitin, IMP-13 columns: kcat 35 ± 1 s^-1; Km 12 ± 2 uM; kcat/Km 2.9 uM^-1 s^-1.

row_label: Cefoxitin

substrate: cefoxitin


substrate_name: cephalotin

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

normalized_value_unit_evidence: Table 1 row Cephalotin, IMP-13 normalized: kcat 25 s^-1; Km 0.031 mM; kcat/Km 810 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Cephalotin, IMP-13 columns: kcat 25 ± 1 s^-1; Km 31 ± 6 uM; kcat/Km 0.81 uM^-1 s^-1.

row_label: Cephalotin

substrate: cephalotin


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

normalized_value_unit_evidence: Table 1 row Piperacillin, IMP-13 normalized: kcat 280 s^-1; Km 0.15 mM; kcat/Km 1900 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Piperacillin, IMP-13 columns: kcat 280 ± 40 s^-1; Km 150 ± 23 uM; kcat/Km 1.9 uM^-1 s^-1.

row_label: Piperacillin


substrate_name: meropenem

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

normalized_value_unit_evidence: Table 1 row Meropenem, IMP-13 normalized: kcat 1.4 s^-1; Km 0.01 mM; kcat/Km 140 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Meropenem, IMP-13 columns: kcat 1.4 ± 0.1 s^-1; Km 10 ± 2 uM; kcat/Km 0.14 uM^-1 s^-1.

row_label: Meropenem

substrate: meropenem


substrate_name: ertapenem

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

normalized_value_unit_evidence: Table 1 row Ertapenem, IMP-13 normalized: kcat 1.8 s^-1; Km 0.0008 mM; kcat/Km 2200 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Ertapenem, IMP-13 columns: kcat 1.8 ± 0.1 s^-1; Km 0.8 ± 0.1 uM; kcat/Km 2.2 uM^-1 s^-1.

row_label: Ertapenem

substrate: ertapenem


substrate_name: ticarcillin

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

normalized_value_unit_evidence: Table 1 row Ticarcillin, IMP-13 normalized: kcat 220 s^-1; Km 0.13 mM; kcat/Km 1800 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Ticarcillin, IMP-13 columns: kcat 220 ± 30 s^-1; Km 130 ± 20 uM; kcat/Km 1.8 uM^-1 s^-1.

row_label: Ticarcillin

substrate: ticarcillin


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

normalized_value_unit_evidence: Table 1 row Cefotaxime, IMP-13 normalized: kcat 33 s^-1; Km 0.021 mM; kcat/Km 1600 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Cefotaxime, IMP-13 columns: kcat 33 ± 2 s^-1; Km 21 ± 2 uM; kcat/Km 1.6 uM^-1 s^-1.


substrate_name: cefepime

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

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

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

row_label: Cefepime

substrate: cefepime


column_label: Table 4; row Cefepime; enzyme column VIM-13; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 61 +/- 21, Km 1,870 +/- 569, kcat/Km 3.3E4

normalized_value_unit_evidence: kcat=61 s^-1; Km=1.87 mM; kcat/Km=33 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-13 / Cefepime


column_label: Table 4; row Penicillin G; enzyme column VIM-13; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 757 +/- 146, Km 1,127 +/- 172, kcat/Km 6.7E5

normalized_value_unit_evidence: kcat=757 s^-1; Km=1.127 mM; kcat/Km=670 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-13 / Penicillin G


substrate_name: piperacillin

column_label: Table 4; row Piperacillin; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 374 +/- 107, Km 1,377 +/- 340, kcat/Km 2.7E5

normalized_value_unit_evidence: kcat=374 s^-1; Km=1.377 mM; kcat/Km=270 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Piperacillin

substrate: piperacillin


substrate_name: Cephalothin

column_label: Table 4; row Cephalothin; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 449 +/- 133, Km 135 +/- 29, kcat/Km 3.3E6

normalized_value_unit_evidence: kcat=449 s^-1; Km=0.135 mM; kcat/Km=3300 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Cephalothin

substrate: Cephalothin


substrate_name: Ceftazidime

column_label: Table 4; row Ceftazidime; enzyme column VIM-13; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 10 +/- 1, Km 509 +/- 120, kcat/Km 1.9E4

normalized_value_unit_evidence: kcat=10 s^-1; Km=0.509 mM; kcat/Km=19 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-13 / Ceftazidime

substrate: Ceftazidime


substrate_name: Ampicillin

column_label: Table 4; row Ampicillin; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 307 +/- 67, Km 1,737 +/- 376, kcat/Km 1.8E5

normalized_value_unit_evidence: kcat=307 s^-1; Km=1.737 mM; kcat/Km=180 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Ampicillin

substrate: Ampicillin


column_label: Table 4; row Ceftazidime; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 42 +/- 9.6, Km 1,132 +/- 320, kcat/Km 3.7E4

normalized_value_unit_evidence: kcat=42 s^-1; Km=1.132 mM; kcat/Km=37 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Ceftazidime


substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


column_label: Table 2, TEM-89 enzyme block; row Cephalothin; column k cat (s^-1) cell 5; column K m (uM) cell 79; column k cat / K m (uM^-1 s^-1) cell 0.06.

normalized_value_unit_evidence: kcat 5 s^-1 = 5.0 s^(-1). Km 79 uM = 79 / 1000 = 0.079 mM. kcat/Km is recorded as the quotient of this row's own two printed cells: 5 s^-1 / 0.079 mM = 63.291139240506325 s^-1 mM^-1. Table 2 prints the ratio cell only to two significant figures (0.06 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 Cephalothin, TEM-89 enzyme block: kcat column cell 5 s^-1; Km column cell 79 uM; kcat/Km column cell 0.06 uM^-1 s^-1.

row_label: Cephalothin


column_label: Table 2, TEM-89 enzyme block; row Amoxicillin; column k cat (s^-1) cell 50; column K m (uM) cell 28; column k cat / K m (uM^-1 s^-1) cell 1.79.

normalized_value_unit_evidence: kcat 50 s^-1 = 50.0 s^(-1). Km 28 uM = 28 / 1000 = 0.028 mM. kcat/Km is recorded as the quotient of this row's own two printed cells: 50 s^-1 / 0.028 mM = 1785.7142857142858 s^-1 mM^-1. Table 2 prints the ratio cell only to two significant figures (1.79 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-89 enzyme block: kcat column cell 50 s^-1; Km column cell 28 uM; kcat/Km column cell 1.79 uM^-1 s^-1.

row_label: Amoxicillin


substrate_name: Cephaloridine

column_label: Table 2, TEM-89 enzyme block; row Cephaloridine; column k cat (s^-1) cell 5; column K m (uM) cell 160; column k cat / K m (uM^-1 s^-1) cell 0.03.

normalized_value_unit_evidence: kcat 5 s^-1 = 5.0 s^(-1). Km 160 uM = 160 / 1000 = 0.16 mM. kcat/Km is recorded as the quotient of this row's own two printed cells: 5 s^-1 / 0.16 mM = 31.25 s^-1 mM^-1. Table 2 prints the ratio cell only to two significant figures (0.03 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 Cephaloridine, TEM-89 enzyme block: kcat column cell 5 s^-1; Km column cell 160 uM; kcat/Km column cell 0.03 uM^-1 s^-1.

row_label: Cephaloridine

substrate: Cephaloridine


column_label: PMC Table 2, Cefepime: Km 23 uM = 0.023 mM; kcat 4.4 s^-1; printed kcat/Km 1.9 × 10^5 M^-1 s^-1 = 190 s^-1 mM^-1. Current 191.30434782608697 is the exact quotient of the same row's printed kcat and Km cells; the separately printed efficiency is retained without forcing literal equality.

normalized_value_unit_evidence: The same Table 2 row normalizes to kcat=4.4 s^-1 and Km=0.023 mM. Their stored-precision quotient is 4.4 / 0.023 = 191.30434782608697 s^-1 mM^-1. The independently printed efficiency 1.9 × 10^5 M^-1 s^-1 normalizes separately to 190 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=23 raw_unit=uM; kcat raw_value=4.4 raw_unit=s^-1; printed kcat/Km raw_value=1.9 × 10^5 raw_unit=M^-1 s^-1


substrate_name: cefazolin

column_label: PMC Table 2, Cefazolin: Km 54 uM = 0.054 mM; kcat 13 s^-1; printed kcat/Km 2.4 × 10^5 M^-1 s^-1 = 240 s^-1 mM^-1. Current 240.74074074074073 is the exact quotient of the same row's printed kcat and Km cells; the separately printed efficiency is retained without forcing literal equality.

normalized_value_unit_evidence: The same Table 2 row normalizes to kcat=13 s^-1 and Km=0.054 mM. Their stored-precision quotient is 13 / 0.054 = 240.74074074074073 s^-1 mM^-1. The independently printed efficiency 2.4 × 10^5 M^-1 s^-1 normalizes separately to 240 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=54 raw_unit=uM; kcat raw_value=13 raw_unit=s^-1; printed kcat/Km raw_value=2.4 × 10^5 raw_unit=M^-1 s^-1

row_label: Cefazolin

substrate: cefazolin


substrate_name: cefotaxime

column_label: PMC Table 2, Cefotaxime: Km 53 uM = 0.053 mM; kcat 2.2 s^-1; printed kcat/Km 4.1 × 10^4 M^-1 s^-1 = 41 s^-1 mM^-1. Current 41.509433962264154 is the exact quotient of the same row's printed kcat and Km cells; the separately printed efficiency is retained without forcing literal equality.

normalized_value_unit_evidence: The same Table 2 row normalizes to kcat=2.2 s^-1 and Km=0.053 mM. Their stored-precision quotient is 2.2 / 0.053 = 41.509433962264154 s^-1 mM^-1. The independently printed efficiency 4.1 × 10^4 M^-1 s^-1 normalizes separately to 41 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=53 raw_unit=uM; kcat raw_value=2.2 raw_unit=s^-1; printed kcat/Km raw_value=4.1 × 10^4 raw_unit=M^-1 s^-1

row_label: Cefotaxime

substrate: cefotaxime


substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin