organism: Hordeum vulgare

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, in presence of 2.5 mM 3-phosphoglycerate

proof_lines: pH 8.0, in absence of 3-phosphoglycerate


enzyme_display_name: glucose-1-phosphate adenylyltransferase

organism: Lens culinaris

substrate_name: alpha-D-glucose 1-phosphate

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines:
pH 7.4, 37°C, long day photoperiod
pH 7.4, 37°C, short day photoperiod

enzyme: glucose-1-phosphate adenylyltransferase

substrate: alpha-D-glucose 1-phosphate

source: brenda


organism: Mycolicibacterium smegmatis

substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


organism: Escherichia coli

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

mutation_type: substitution


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: pH 7.0, 37°C, mutant enzyme P295E, in the presence of a saturating concentration of fructose 1,6-bisphosphate

substrate: Unknown


organism: Solanum tuberosum

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: mutation P52L, large subunit, plus mutation R350K, small subunit, 37°C, pH 7.0


proof_lines: mutation P52L, large subunit, plus mutation P112L, small subunit, 37°C, pH 7.0


assay_conditions_summary: cofactor ATP


proof_lines: mutation P52L, large subunit, 37°C, pH 7.0


organism: Salmonella enterica subsp. enterica serovar Typhimurium

assay_conditions_summary: pH 8.4; 310.15 K; cofactor ATP

proof_lines: pH 8.4, 37°C, influence of activators on Km

proof_lines: pH 8.0, 37°C, strain JP102, kinetic study

proof_lines: pH 8.0, 37°C, strain LT-2, kinetic study


organism: Serratia liquefaciens


organism: Serratia marcescens

proof_lines:
pH 8.0, 37°C, strain ATCC 15365
pH 8.0, 37°C, strain ATCC 274


organism: Solanum lycopersicum

proof_lines: pH 7.4, 37°C, leaf enzyme, in presence of 3-phosphoglycerate

proof_lines: pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S

proof_lines: pH 7.4, 37°C, fruit enzyme, in presence of 3-phosphoglycerate


substrate_name: ADP alpha-D-glucoside; Diphosphate

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

proof_lines: chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate

proof_lines: chimeric enzyme, pH 7.4, 37°C, presence of phosphate

substrate: ADP alpha-D-glucoside; Diphosphate


proof_lines: mutation D157L, large subunit, plus D143N, small subunit


proof_lines: mutation K41R/T51K, large subunit, plus D143N, small subunit


proof_lines: oxidized wild-type, pH 7.4, 37°C, presence of phosphate

proof_lines: reduced wild-type, pH 7.4, 37°C, presence of phosphate


proof_lines: pH 7.4, 37°C, mutant Mos(1-198), in absence of 3-phosphoglycerate

proof_lines: pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate

proof_lines: pH 7.4, 37°C, mutant Mos(1-376), in absence of 3-phosphoglycerate


proof_lines: mutation T51K, large subunit, plus D143N, small subunit


assay_conditions_summary: 310.15 K; cofactor ATP


proof_lines: mutation P52L, large subunit, plus mutation L46F, small subunit, 37°C, pH 7.0


organism: Nitrosomonas europaea

proof_lines:
pH 8.0, 37°C, presence of Mg2+
pH 8.0, 37°C, presence of Mn2+
pH 8.0, 37°C, presence of Co2+


organism: Oryza sativa

proof_lines: pH 8.0, in presence of 5 mM 3-phosphoglycerate

proof_lines: pH 8.0, in presence of 0.5 mM 3-phosphoglycerate

proof_lines: pH 8.0, in presence of 1 mM 3-phosphoglycerate


proof_lines: S0.5 value, large subunit mutant T139I with wild-type small subunit, 37°C, pH 7.0

proof_lines: S0.5 value, wild-type small subunit alone, 37°C, pH 7.0


organism: Rhodobacter capsulatus


organism: Rhodococcus jostii

proof_lines: hyperbolic behavior, Hill coefficient 1.3, presence of mannose 6-phosphate, pH 8.0, 37°C

proof_lines: hyperbolic behavior, Hill coefficient 1.1, presence of glucose 6-phosphate, pH 8.0, 37°C

proof_lines: hyperbolic behavior, Hill coefficient 0.7, presence of fructose 6-phosphate, pH 8.0, 37°C


organism: Rhodocyclus tenuis

proof_lines:
in absence of pyruvate
in presence of 0.05 mM pyruvate
in presence of 1 mM pyruvate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Zea mays

proof_lines: mutant BT2/E438Q, 15 mM 3-phosphoglycerate


proof_lines: mutant BT2/C382F, 15 mM 3-phosphoglycerate


proof_lines: wild-type, pH 7.4, 37°C, presence of phosphate


organism: Synechocystis sp.

proof_lines: pH 7.0, 37°C, in absence of 3-phosphoglycerate

proof_lines: pH 7.0, 37°C, in presence of 2.5 mM 3-phosphoglycerate


organism: Thermus caldophilus

assay_conditions_summary: pH 7.6; 348.15 K; cofactor ATP


organism: Triticum aestivum

assay_conditions_summary: pH 8

proof_lines: pH 8.0, in absence of 0.25 mM 3-phosphoglycerate

proof_lines: leaf enzyme in absence of 3-phosphoglycerate

proof_lines: endosperm enzyme in absence of 3-phosphoglycerate


substrate_name: Diphosphate; ADP alpha-D-glucoside

proof_lines: chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate

proof_lines: chimeric enzyme, pH 7.4, 37°C, presence of phosphate

substrate: Diphosphate; ADP alpha-D-glucoside


proof_lines: mutant BT2/S163F, 15 mM 3-phosphoglycerate


proof_lines:
pH 7.4, 37°C, mutant BT2-TI
pH 7.4, 37°C, mutant MP-TI
pH 7.4, 37°C, mutant MP


proof_lines: mutant BT2/V227R, 15 mM 3-phosphoglycerate


proof_lines: mutant BT2/D368S, 15 mM 3-phosphoglycerate


proof_lines: mutant BT2/M172T, 15 mM 3-phosphoglycerate


proof_lines: large subunit mutant D161G, 37°C, pH 7.4

proof_lines: large subunit mutant D161G, presence of 3-phosphoglycerate, 37°C, pH 7.4


proof_lines: mutant BT2/P372A, 15 mM 3-phosphoglycerate


proof_lines: large subunit mutant E38K/G101N, pH 7.5, 37°C


proof_lines: large subunit mutant G101N, pH 7.5, 37°C


proof_lines: mutation P52L, large subunit, plus mutation P308L, small subunit, 37°C, pH 7.0


proof_lines: mutation K41R, large subunit, plus D143N, small subunit


enzyme_display_name: beta-galactosidase

organism: Arthrobacter sp.

substrate_name: lactose

proof_lines:
at 10°C
at 20°C
at 5°C

enzyme: beta-galactosidase

substrate: lactose


proof_lines: 15°C, recombinant mutant BgaS7, i.e. E229D/V405A


proof_lines: 15°C, recombinant mutant BgaS6, i.e.E229D/V405A/G803D


organism: Aspergillus aculeatus


organism: Aspergillus carbonarius


organism: Aspergillus niger

proof_lines: enzyme immobilized on sucrose-polycarolein


substrate_name: 2-nitrophenyl beta-D-galactopyranoside

substrate: 2-nitrophenyl beta-D-galactopyranoside


organism: Aspergillus oryzae

substrate_name: 2-nitrophenyl beta-D-galactoside

substrate: 2-nitrophenyl beta-D-galactoside


assay_conditions_summary: pH 4.5; 333.15 K; buffer mixture

proof_lines:
pH 4.5, 60°C
cross-linked enzyme, pH 4.5, 37°C
adsorbed enzyme, pH 4.5, 37°C


organism: Solanum tuberosum


organism: Spinacia oleracea

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

proof_lines: pH 7.3, 37°C, in presence of 1 mM 3-phosphoglycerate

proof_lines: pH 7.3, 37°C, in absence of 3-phosphoglycerate


organism: Streptococcus mutans

proof_lines: S0.5 value, Hill coefficient 1.2, GlgC/GlgD complex, pH 8.0, 37°C

proof_lines: S0.5 value, Hill coefficient 1.5, subunit GlgC in presence of fructose 1,6-bisphosphate, pH 8.0, 37°C

proof_lines: S0.5 value, Hill coefficient 3.7, GlgC/GlgD complex, pH 8.0, 37°C


organism: Streptomyces coelicolor

substrate_name: diphosphate

substrate: diphosphate


organism: Synechococcus sp.


organism: Bispora sp.

assay_conditions_summary: pH 1.5; buffer glycine-HCl


organism: Bos taurus


organism: Caldariella acidophila

substrate_name: 4-nitrophenyl beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


organism: Caldicellulosiruptor saccharolyticus


organism: Averrhoa carambola

substrate_name: nitrophenyl beta-D-galactoside

proof_lines:
37°C, pH 4.1,beta-galactosidase IV
37°C, pH 4.1,beta-galactosidase III
37°C, pH 4.1,beta-galactosidase II

substrate: nitrophenyl beta-D-galactoside


organism: Bacillus sp. (in: firmicutes)

proof_lines:
pH 7.6 enzyme
pH 10.2 enzyme


organism: Bacteroides polypragmatus

substrate_name: o-nitrophenyl-beta-D-galactoside

substrate: o-nitrophenyl-beta-D-galactoside


organism: Bifidobacterium bifidum

substrate_name: p-nitrophenyl-beta-D-galactoside

proof_lines: hydrolysis transgalactosylation

substrate: p-nitrophenyl-beta-D-galactoside


organism: Bifidobacterium longum


organism: Bifidobacterium longum subsp. infantis

substrate_name: o-nitrophenyl beta-D-galactopyranoside

substrate: o-nitrophenyl beta-D-galactopyranoside


organism: Zea mays


proof_lines: mutant BT2/H149S, 15 mM 3-phosphoglycerate


proof_lines: mutant BT2/C114A, 15 mM 3-phosphoglycerate


proof_lines: mutant BT2/C424V, 15 mM 3-phosphoglycerate


proof_lines: large subunit mutant Q96G/D161G/A443R, 37°C, pH 7.4

proof_lines: large subunit mutant Q96G/D161G/A443R, presence of 3-phosphoglycerate, 37°C, pH 7.4


organism: Achatina achatina


organism: Escherichia coli


assay_conditions_summary: pH 7; 298.15 K; buffer 30 mM TES

proof_lines: mutant enzyme H418F, in 30 mM TES buffer, 10 mM Mg2+, 150 mM Na+, pH 7.0 at 25°C


proof_lines: wild type enzyme, in 30 mM TES buffer, 145 mM NaCl, pH 7.0 at 25°C

proof_lines: wild type enzyme, in 30 mM TES buffer, 145 mM NaCl, 0.01 mM Mg2+, pH 7.0 at 25°C


proof_lines: mutant enzyme H418N, in 30 mM TES buffer, 0.01 mM Mg2+, 150 mM Na+, pH 7.0 at 25°C

proof_lines: mutant enzyme H418N, in 30 mM TES buffer, 145 mM NaCl, 0.01 mM Mg2+, pH 7.0 at 25°C


organism: Felis catus


organism: Clostridium perfringens

assay_conditions_summary: pH 6; 310.15 K; buffer 20 mM sodium acetate

proof_lines: mutant enzyme D429A, in 20 mM sodium acetate buffer at pH 6.0, 37°C


organism: Corynebacterium murisepticum


organism: Enterobacter cloacae


organism: Erythrina variegata


assay_conditions_summary: pH 7.3; 298.15 K; buffer containing 1 mM MgCl2, 145 mM NaCl and 4 mM dithiothreitol at pH 7

proof_lines:
dimeric enzyme, 25°C
tetrameric enzyme, 25°C
native enzyme


proof_lines: mutant enzyme H418E, in 30 mM TES buffer, 0.01 mM Mg2+, 150 mM Na+, pH 7.0 at 25°C

proof_lines: mutant enzyme H418E, in 30 mM TES buffer, 145 mM NaCl, 0.01 mM Mg2+, pH 7.0 at 25°C


organism: Geobacillus stearothermophilus


organism: Haloferax volcanii

proof_lines: pH 7.2, 22°C, the enzyme also shows beta-fucosidase activity


organism: Hamamotoa singularis


organism: Heyndrickxia coagulans

proof_lines:
at 55°C
at 30°C


organism: Homo sapiens

proof_lines: fibroblast enzyme of GM1 gangliosidosis heterozygotes

proof_lines: leukocyte enzyme of GM1 gangliosidosis heterozygotes


organism: Hymenaea courbaril


organism: Irpex lacteus


organism: Kluyveromyces lactis


organism: Kluyveromyces marxianus

assay_conditions_summary: pH 6.8; 298.15 K; buffer containing 1 mM MgCl2, 145 mM NaCl and 4 mM dithiothreitol at pH 6

proof_lines:
dimeric enzyme, 25°C
pH 6.8, 37°C
pH 6.8


organism: Kluyveromyces sp.

proof_lines: free enzyme, substrate is milk, pH 7.5, 41°C

proof_lines: immobilized enzyme MP-MCC-Gal, substrate is milk, pH 7.5, 41°C

proof_lines: immobilized enzyme Fe-ALK-Gal, pH 7.5, 41°C


organism: Lacticaseibacillus casei


organism: Lactiplantibacillus pentosus


organism: Lactiplantibacillus plantarum


organism: Lactobacillus delbrueckii


organism: Lactobacillus helveticus


organism: Lactococcus lactis subsp. lactis

substrate_name: o-Nitrophenyl-beta-D-galactoside; H2O

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

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Lac- Gal d

substrate: o-Nitrophenyl-beta-D-galactoside; H2O


organism: Lathyrus oleraceus

proof_lines: in 50 mM sodium acetate-acetic acid, pH 4.0, at 37°C

proof_lines: enzyme immobilized on Amberlite MB-150 beads


organism: Limosilactobacillus reuteri

proof_lines:
pH 6.5, 30°C, strain L103
pH 6.5, 30°C, strain L461
recombinant enzyme, pH 6.5, 30°C


organism: Caldicellulosiruptor saccharolyticus


proof_lines:
at pH 6.0 and 80°C
at 80°C and pH 6.0


organism: Clostridium perfringens

assay_conditions_summary: pH 6; 310.15 K; buffer acetate

proof_lines: mutant enzyme E467A, in 20 mM sodium acetate buffer at pH 6.0, 37°C


proof_lines: mutant enzyme E354A, in 20 mM sodium acetate buffer at pH 6.0, 37°C


proof_lines: wild type enzyme, in 20 mM sodium acetate buffer at pH 6.0, 37°C


organism: Macrotyloma geocarpum


organism: Marchantia polymorpha

substrate_name: p-nitrophenyl beta-D-galactopyranoside

substrate: p-nitrophenyl beta-D-galactopyranoside


organism: Mus musculus

proof_lines:
without inhibitor
in presence of inhibitor


organism: Neurospora crassa

proof_lines: beta-D-galactoside galactohydrolase pH 4.2

proof_lines: beta-D-galactoside galactohydrolase pH 4.5


organism: Niallia circulans


organism: Oreochromis niloticus


organism: Oryctolagus cuniculus

substrate_name: p-Nitrophenyl-beta-D-galactoside; H2O

substrate: p-Nitrophenyl-beta-D-galactoside; H2O


organism: Paecilomyces variotii


organism: Paenibacillus macerans


organism: Papiliotrema laurentii


organism: Penicillium canescens

proof_lines:
dimeric enzyme, 25°C
tetrameric enzyme, 25°C


organism: Penicillium chrysogenum


organism: Penicillium citrinum


organism: Penicillium multicolor


organism: Petunia x hybrida

proof_lines:
enzyme form H4
enzyme form H3
enzyme form H1


organism: Phaseolus vulgaris


organism: Planococcus sp. (in: firmicutes)


organism: Priestia megaterium


organism: Lactiplantibacillus plantarum WCFS1

proof_lines:
at pH 7.5 and 55°C
at pH 7.0 and 60°C


organism: Lactobacillus acidophilus


organism: Lactobacillus crispatus


organism: Lactobacillus delbrueckii


assay_conditions_summary: pH 6.5; 318.15 K; buffer HEPES

proof_lines: mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C


proof_lines: wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C


organism: Prunus persica


organism: Pseudarthrobacter oxydans

substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


organism: Pseudoalteromonas haloplanktis


organism: Putranjiva roxburghii

proof_lines:
pH 4.6, 37°C, recombinant enzyme
pH 4.6, 37°C, native enzyme


organism: Pyrococcus furiosus


organism: Raphanus sativus


organism: Saccharolobus solfataricus

proof_lines:
30°C, pH 6.5, wild-type enzyme
pH 6.5, 75°C, wild-type enzyme
pH 6.5, 65°C, wild-type enzyme


proof_lines: pH 7.5, 80°C, recombinant mutant enzyme F441Y


organism: Saccharomyces fragilis

proof_lines: enzyme immobilized on sucrose-polyacrolein


organism: Saccharopolyspora rectivirgula


organism: Rattus norvegicus

substrate_name: H2O; p-Nitrophenyl-beta-D-galactoside

assay_conditions_summary: pH 3; buffer presence of 50 mM glycine/HCl

proof_lines:
enzyme from corpus region
enzyme from cauda region
enzyme from caput region

substrate: H2O; p-Nitrophenyl-beta-D-galactoside


organism: Rhizomucor sp.


proof_lines:
pH 6.5, 30°C
pH 6.5, 75°C
at 75°C and pH 6.5


proof_lines: pH 6.5, 65°C, mutant enzyme delVal484-His489


organism: Torulopsis sphaerica


organism: Trametes cinnabarina


organism: Treponema phagedenis


organism: uncultured microorganism

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

proof_lines: pH 6.0, 60°C, additive: 25 mM cellobiose

proof_lines: pH 6.0, 60°C, additive: 250 mM D-galactose

substrate: 4-nitrophenyl beta-D-glucopyranoside


organism: uncultured soil bacterium

proof_lines:
pH 7, 5°C
pH 7, 10°C
pH 7, 20°C


organism: Vigna radiata

substrate_name: Unknown

proof_lines:
beta-galactosidase II
beta-galactosidase I
beta-galactosidase III

substrate: Unknown


organism: Sterigmatomyces elviae


organism: Streptococcus pneumoniae


organism: Streptococcus sp.


organism: Streptococcus thermophilus

proof_lines: in presence of 0.25 mM Mg2+, 50 mM K+ and 50 mM Na+

proof_lines: in presence of 0.25 mM Mg2+ and 50 mM Na+


organism: Tenebrio molitor

proof_lines: hydrolysis of 4-methylumbelliferyl beta-D-galactoside

proof_lines: hydrolysis of p-nitrophenyl beta-D-galactoside

proof_lines: hydrolysis of 4-methylumbellipheryl beta-D-galactoside


organism: Thermoanaerobacter sp.


proof_lines:
at 25°C, in presence of 10 mM Mg2+
at 50°C, in presence of 10 mM Mg2+


organism: Thermomyces dupontii

proof_lines: immobilized enzyme, 2-nitrophenyl beta-D-galactoside, pH 6.5, 40°C


organism: Thermomyces lanuginosus

substrate_name: methyl-beta-D-galactoside

proof_lines: pH and temperature not specified in the publication

substrate: methyl-beta-D-galactoside


organism: Thermotoga maritima


organism: Thermus aquaticus

proof_lines: calculated from glucose liberated from lactose

proof_lines: calculated from disappearance from lactose


organism: Thermus sp.

substrate_name: lactose

proof_lines: at 70°C and pH 6.5, using 4-nitrophenyl-beta-D-galactopyranoside as substrate

substrate: lactose


organism: Wickerhamiella versatilis


organism: Xanthomonas phaseoli pv. manihotis

proof_lines: pH 7.0, 30°C, mutant E184A, glycohydrolase activity


proof_lines: pH 7.0, 30°C, wild-type enzyme, glycohydrolase activity


organism: Zea mays

substrate_name: alpha-D-glucose 1-phosphate

proof_lines: mutant BT2/A508S, 15 mM 3-phosphoglycerate

substrate: alpha-D-glucose 1-phosphate


substrate_name: ATP

substrate: ATP


proof_lines: mutant BT2/T361C, 15 mM 3-phosphoglycerate


proof_lines: mutant BT2/Q213H, 15 mM 3-phosphoglycerate


proof_lines: mutant BT2/V502T, 15 mM 3-phosphoglycerate


enzyme_display_name: beta-lactamase

organism: Chryseobacterium indologenes

substrate_name: cefazolin

assay_conditions_summary: pH 6.5; buffer and ZnSO4 conditions

proof_lines: in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4

enzyme: beta-lactamase

substrate: cefazolin


organism: Actinomyces viscosus


organism: Alicyclobacillus acidocaldarius


proof_lines:
pH 6.0, 65°C
strain HM-1
strain 11-1O


organism: Arthrobacter psychrolactophilus


organism: Pseudomonas putida

substrate_name: carbenicillin

assay_conditions_summary: buffer HEPES

proof_lines: enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin

proof_lines: inhibitor binding constant (Ki) using 10 microM nitrocefin as indicator substrate

substrate: carbenicillin


enzyme_display_name: beta-N-acetylhexosaminidase

organism: Ostrinia furnacalis

source_db: oed

protein_accession_database: UniProt

enzyme: beta-N-acetylhexosaminidase

source: oed


substrate_name: chitobiose

source_db: skid

source_license: CC BY-NC-ND 4.0

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

substrate: chitobiose

source: skid


organism: Rattus norvegicus


organism: Saccharolobus solfataricus


organism: Stackebrandtia nassauensis


organism: Streptococcus pneumoniae


organism: Clostridium paraputrificum

sequence_variant_note: Mutation signature E293Q matches the mutant residue at offset +0 and the reference residue at offset +13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant E293Q


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-N-acetylhexosaminidase(Enzyme) mutant E121A


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


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant D274N


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant D229N


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant D303N


sequence_variant_note: Mutation signature D119N matches the mutant residue at offset +0 and the reference residue at offset -8; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant D119N


organism: Enterococcus faecalis

verification_status: unverified

status: unverified


organism: Cellulomonas fimi


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant D329N


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant E121Q


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant D229A


organism: Homo sapiens


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


organism: Lactobacillus casei


organism: Mus musculus


organism: Paenibacillus sp. TS12


proof_lines:
pH 6.0, 37°C, wild-type isozyme Hex1
pH 6.0, 37°C, wild-type isozyme Hex2


organism: Akkermansia muciniphila


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant D326A His6-tagged


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant E327A His6-tagged


organism: Aspergillus versicolor

data_origin: experimental


organism: Bifidobacterium longum


organism: Caenorhabditis elegans


organism: Mycobacterium tuberculosis

sequence_source: UniProt reviewed canonical sequence for L7N6B0


organism: Ostrinia furnacalis

sequence_source: UniProt reviewed canonical sequence for Q06GJ0


kcat_over_km_origin: calculated

sequence_source: Reconstructed from UniProt Q06GJ0 canonical sequence


sequence_variant_note: Mutation signature V327G matches the mutant residue at offset +0 and the reference residue at offset -12; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DRL6 and applied mutation signature Y914F to reconstruct the assayed variant sequence.

column_label: TABLE 3: Kinetic constants of different constructs of StrH and mutants towards pNp-NAG and NAG-beta(1,2)-Man (J. Biol. Chem. 2011, volume 286, number 50, pages 43004-43012); pNp-NAG panel; enzyme row 'Y914F'; column 'Km (uM)' = 950; column 'kcat (s^-1)' = 4.7; column 'kcat/Km (x10^-3 s^-1 uM^-1)' = 5.0.

normalized_value_unit_evidence: Km: printed cell 950 uM; 950 / 1000 = 0.9500000000000001 mM. kcat: printed cell 4.7 s^-1; the printed unit is already s^-1, so no unit conversion applies; the normalized value is 4.7 s^(-1). kcat/Km: printed cell 5.0 x 10^-3 s^-1 uM^-1 (the column head prints the x10^-3 decade); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 5.0 x 10^-3 x 1000 = 5.0 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 3, pNp-NAG panel, enzyme row 'Y914F': Km (uM) cell 950; kcat (s^-1) cell 4.7; kcat/Km (x10^-3 s^-1 uM^-1) cell 5.0.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DRL6 and applied mutation signature W443F to reconstruct the assayed variant sequence.

column_label: TABLE 3: Kinetic constants of different constructs of StrH and mutants towards pNp-NAG and NAG-beta(1,2)-Man (J. Biol. Chem. 2011, volume 286, number 50, pages 43004-43012); pNp-NAG panel; enzyme row 'W443F'; column 'Km (uM)' = 1120; column 'kcat (s^-1)' = 0.11; column 'kcat/Km (x10^-3 s^-1 uM^-1)' = 0.09.

normalized_value_unit_evidence: Km: printed cell 1120 uM; 1120 / 1000 = 1.12 mM. kcat: printed cell 0.11 s^-1; the printed unit is already s^-1, so no unit conversion applies; the normalized value is 0.11 s^(-1). kcat/Km: printed cell 0.09 x 10^-3 s^-1 uM^-1 (the column head prints the x10^-3 decade); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.09 x 10^-3 x 1000 = 0.09 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 3, pNp-NAG panel, enzyme row 'W443F': Km (uM) cell 1120; kcat (s^-1) cell 0.11; kcat/Km (x10^-3 s^-1 uM^-1) cell 0.09.


sequence_source: UniProtKB Q8DRL6 canonical sequence


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DRL6 and applied mutation signature W876F to reconstruct the assayed variant sequence.

column_label: TABLE 3: Kinetic constants of different constructs of StrH and mutants towards pNp-NAG and NAG-beta(1,2)-Man (J. Biol. Chem. 2011, volume 286, number 50, pages 43004-43012); pNp-NAG panel; enzyme row 'W876F'; column 'Km (uM)' = 1292; column 'kcat (s^-1)' = 0.98; column 'kcat/Km (x10^-3 s^-1 uM^-1)' = 0.75.

normalized_value_unit_evidence: Km: printed cell 1292 uM; 1292 / 1000 = 1.292 mM. kcat: printed cell 0.98 s^-1; the printed unit is already s^-1, so no unit conversion applies; the normalized value is 0.98 s^(-1). kcat/Km: printed cell 0.75 x 10^-3 s^-1 uM^-1 (the column head prints the x10^-3 decade); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.75 x 10^-3 x 1000 = 0.75 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 3, pNp-NAG panel, enzyme row 'W876F': Km (uM) cell 1292; kcat (s^-1) cell 0.98; kcat/Km (x10^-3 s^-1 uM^-1) cell 0.75.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DRL6 and applied mutation signature W876A to reconstruct the assayed variant sequence.

column_label: TABLE 3: Kinetic constants of different constructs of StrH and mutants towards pNp-NAG and NAG-beta(1,2)-Man (J. Biol. Chem. 2011, volume 286, number 50, pages 43004-43012); NAG-beta(1,2)-Man panel; enzyme row 'W876A'; column 'Km (mM)' = 1.51; column 'kcat (min^-1)' = 0.54; column 'kcat/Km (min^-1 mM^-1)' = 0.36.

normalized_value_unit_evidence: Km: printed cell 1.51 mM; the printed unit is already mM, so no unit conversion applies; the normalized value is 1.51 mM. kcat: printed cell 0.54 min^-1; 0.54 / 60 = 0.009000000000000001 s^(-1). kcat/Km: printed cell 0.36 min^-1 mM^-1; 0.36 / 60 = 0.006 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 3, NAG-beta(1,2)-Man panel, enzyme row 'W876A': Km (mM) cell 1.51; kcat (min^-1) cell 0.54; kcat/Km (min^-1 mM^-1) cell 0.36.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DRL6 and applied mutation signature E361A to reconstruct the assayed variant sequence.

column_label: TABLE 2: Kinetic constants of different constructs of StrH towards pNp-NAG (J. Biol. Chem. 2011, volume 286, number 50, pages 43004-43012); pNp-NAG panel; enzyme row 'E361A'; column 'Km (uM)' = 900; column 'kcat (s^-1)' = 0.4; column 'kcat/Km (x10^-3 s^-1 uM^-1)' = 0.4.

normalized_value_unit_evidence: Km: printed cell 900 uM; 900 / 1000 = 0.9 mM. kcat: printed cell 0.4 s^-1; the printed unit is already s^-1, so no unit conversion applies; the normalized value is 0.4 s^(-1). kcat/Km: printed cell 0.4 x 10^-3 s^-1 uM^-1 (the column head prints the x10^-3 decade); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.4 x 10^-3 x 1000 = 0.4 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, pNp-NAG panel, enzyme row 'E361A': Km (uM) cell 900; kcat (s^-1) cell 0.4; kcat/Km (x10^-3 s^-1 uM^-1) cell 0.4.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DRL6 and applied mutation signature Y914A to reconstruct the assayed variant sequence.

column_label: TABLE 3: Kinetic constants of different constructs of StrH and mutants towards pNp-NAG and NAG-beta(1,2)-Man (J. Biol. Chem. 2011, volume 286, number 50, pages 43004-43012); pNp-NAG panel; enzyme row 'Y914A'; column 'Km (uM)' = 1560; column 'kcat (s^-1)' = 0.033; column 'kcat/Km (x10^-3 s^-1 uM^-1)' = 0.022.

normalized_value_unit_evidence: Km: printed cell 1560 uM; 1560 / 1000 = 1.56 mM. kcat: printed cell 0.033 s^-1; the printed unit is already s^-1, so no unit conversion applies; the normalized value is 0.033 s^(-1). kcat/Km: printed cell 0.022 x 10^-3 s^-1 uM^-1 (the column head prints the x10^-3 decade); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.022 x 10^-3 x 1000 = 0.022 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 3, pNp-NAG panel, enzyme row 'Y914A': Km (uM) cell 1560; kcat (s^-1) cell 0.033; kcat/Km (x10^-3 s^-1 uM^-1) cell 0.022.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DRL6 and applied mutation signature W443A/W876A to reconstruct the assayed variant sequence.

column_label: TABLE 3: Kinetic constants of different constructs of StrH and mutants towards pNp-NAG and NAG-beta(1,2)-Man (J. Biol. Chem. 2011, volume 286, number 50, pages 43004-43012); NAG-beta(1,2)-Man panel; enzyme row 'W443A/W876A'; column 'Km (mM)' = 1.30; column 'kcat (min^-1)' = 0.58; column 'kcat/Km (min^-1 mM^-1)' = 0.44.

normalized_value_unit_evidence: Km: printed cell 1.30 mM; the printed unit is already mM, so no unit conversion applies; the normalized value is 1.3 mM. kcat: printed cell 0.58 min^-1; 0.58 / 60 = 0.009666666666666665 s^(-1). kcat/Km: printed cell 0.44 min^-1 mM^-1; 0.44 / 60 = 0.007333333333333333 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 3, NAG-beta(1,2)-Man panel, enzyme row 'W443A/W876A': Km (mM) cell 1.30; kcat (min^-1) cell 0.58; kcat/Km (min^-1 mM^-1) cell 0.44.


organism: Dictyostelium discoideum

proof_lines: extract of wild type strain, purified major and minor isozyme


organism: Capsicum annuum

proof_lines:
pH 6.0, 37°C
isoenzyme II
isoenzyme I


proof_lines: with 0.01% bovine or human serum albumin


organism: Solanum lycopersicum

proof_lines:
isoenzyme II
isoenzyme I


organism: Streptococcus pneumoniae

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8DRL6 canonical sequence reconstructed from stated mutation signature and applied mutation signature Y482F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DRL6 and applied mutation signature W443A to reconstruct the assayed variant sequence.

column_label: TABLE 3: Kinetic constants of different constructs of StrH and mutants towards pNp-NAG and NAG-beta(1,2)-Man (J. Biol. Chem. 2011, volume 286, number 50, pages 43004-43012); NAG-beta(1,2)-Man panel; enzyme row 'W443A'; column 'Km (mM)' = 1.34; column 'kcat (min^-1)' = 0.52; column 'kcat/Km (min^-1 mM^-1)' = 0.39.

normalized_value_unit_evidence: Km: printed cell 1.34 mM; the printed unit is already mM, so no unit conversion applies; the normalized value is 1.34 mM. kcat: printed cell 0.52 min^-1; 0.52 / 60 = 0.008666666666666666 s^(-1). kcat/Km: printed cell 0.39 min^-1 mM^-1; 0.39 / 60 = 0.0065 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 3, NAG-beta(1,2)-Man panel, enzyme row 'W443A': Km (mM) cell 1.34; kcat (min^-1) cell 0.52; kcat/Km (min^-1 mM^-1) cell 0.39.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8DRL6 canonical sequence reconstructed from stated mutation signature and applied mutation signature W876A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8DRL6 and applied mutation signature C469Y to reconstruct the assayed variant sequence.

column_label: TABLE 2: Kinetic constants of different constructs of StrH towards pNp-NAG (J. Biol. Chem. 2011, volume 286, number 50, pages 43004-43012); pNp-NAG panel; enzyme row 'C469Y'; column 'Km (uM)' = 650; column 'kcat (s^-1)' = 5.1; column 'kcat/Km (x10^-3 s^-1 uM^-1)' = 7.8.

normalized_value_unit_evidence: Km: printed cell 650 uM; 650 / 1000 = 0.65 mM. kcat: printed cell 5.1 s^-1; the printed unit is already s^-1, so no unit conversion applies; the normalized value is 5.1 s^(-1). kcat/Km: printed cell 7.8 x 10^-3 s^-1 uM^-1 (the column head prints the x10^-3 decade); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 7.8 x 10^-3 x 1000 = 7.8 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, pNp-NAG panel, enzyme row 'C469Y': Km (uM) cell 650; kcat (s^-1) cell 5.1; kcat/Km (x10^-3 s^-1 uM^-1) cell 7.8.


organism: Thermotoga maritima MSB8

sequence_source: UniProtKB Q9WZR6 canonical sequence

column_label: ScienceDirect rendered article Table 2, NagA row pNPGlcNAc3: Km column 0.29 +/- 0.05 mM; kcat column 146.7 s^-1; kcat/Km column 505.7 mM^-1 s^-1.

normalized_value_unit_evidence: Km=0.29 mM; kcat=146.7 s^-1; kcat_over_km=505.8620689655172 s^-1*mM^-1 calculated from 146.7/0.29 and consistent with table 505.7 after rounding.

row_label: NagA / pNPGlcNAc3

table_label: Table 2. Kinetic parameters of NagA and CbsA with p-nitrophenyl N-acetyl beta-D-glucosaminide


column_label: ScienceDirect rendered article Table 2, NagA row pNPGlcNAc: Km column 0.28 +/- 0.04 mM; kcat column 246.2 s^-1; kcat/Km column 879.3 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.28 normalized_unit=mM; kcat normalized_value=246.2 normalized_unit=s^-1; kcat_over_km normalized_value=879.3 normalized_unit=s^-1*mM^-1.

row_label: NagA / pNPGlcNAc


source_db: uniprot

source: uniprot


organism: Palythoa caribaeorum

substrate_name: pNP-GlcNAc

sequence: GKSSSRPLGDATLGDLDFDIEVTQDYWDDLAR

wild_type_sequence: GKSSSRPLGDATLGDLDFDIEVTQDYWDDLAR

substrate: pNP-GlcNAc


organism: Vibrio furnissii


substrate_name: 4-methylumbelliferone-N-acetylglucosamine (at pH 4-4.5)

assay_conditions_summary: pH 4

proof_lines: 4-methylumbelliferone-N-acetylglucosamine (MU-(GlcNAc)1) is a GlcNAc2 analog.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.02 sec(-1) with 4MU-GlcNAc as substrate.


substrate_name: GlcNAc-beta-1,4-GlcNAc (at pH 6.8 and 25 degrees Celsius)

proof_lines: kcat is 934 sec(-1) with GlcNAc-beta-1,4-GlcNAc as substrate. kcat is 708 sec(-1) with p-nitrophenyl-beta-GlcNAc as substrate. kcat is 766 sec(-1) with p-nitrophenyl-beta-GalNAc as substrate (PubMed:18959754). kcat is 434.7 sec(-1) with 4MU


organism: Aeromonas hydrophila

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


organism: Aggregatibacter actinomycetemcomitans

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


proof_lines: presence of GDP, mutant E649A, pH 8, 37°C


proof_lines: presence of GDP, mutant Y327F/Y331F, pH 8, 37°C


proof_lines: mutant D412A, pH not specified in the publication, temperature not specified in the publication


proof_lines: presence of GDP, mutant Y550A, pH 8, 37°C


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: wild-type, pH not specified in the publication, temperature not specified in the publication


proof_lines: presence of GDP, mutant R292A, pH 8, 37°C


proof_lines:
isoform Am2301, at pH 5.0 and 37°C
isoform Am2446, at pH 6.5 and 37°C


organism: Arabidopsis thaliana

substrate_name: pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)


substrate: pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)


organism: Aspergillus oryzae

substrate_name: 4-nitrophenyl-2-acetamido-2-deoxyglucopyranoside with native glycosylated enzyme


organism: Lupinus albus

sequence: VDSEDLIEAFKIYVEDDNEHLQGSVD

wild_type_sequence: VDSEDLIEAFKIYVEDDNEHLQGSVD


organism: Akkermansia muciniphila

proof_lines: presence of GDP, mutant R256A, pH 8, 37°C


proof_lines: presence of GDP, mutant P595A/H597A, pH 8, 37°C


proof_lines: mutant E413A, pH not specified in the publication, temperature not specified in the publication


organism: Aspergillus niger

proof_lines:
in D2O, pD 7.0
in D2O, pD 4.6


organism: Caldicellulosiruptor acetigenus

assay_conditions_summary: pH 5

proof_lines: pH 5, temperature not specified in the publication


organism: Callithrix jacchus


organism: Canavalia ensiformis


organism: Canavalia sp.


organism: Carica papaya


organism: Cellulomonas fimi

proof_lines: 50 mM sodium phosphate buffer (pH 7.08) at 25°C


organism: Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc)

substrate_name: pNP-beta-GlcNAc (at pH 7.0 and 37 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: kcat is 1.01 sec(-1) and kcat/KM is 34.34 mM(-1)sec(-1) with pNP-beta-GlcNAc as substrate.


substrate_name: pNP-beta-GlcNAc (at pH 8.0 and 37 degrees Celsius)

assay_conditions_summary: pH 8

proof_lines: kcat is 5.57 sec(-1) and kcat/KM is 202.45 mM(-1)sec(-1) with pNP-beta-GlcNAc as substrate.


substrate_name: pNP-GlcNAc (at pH 7.0 and 37 degrees Celsius)

proof_lines: kcat is 51.39 sec(-1) and kcat/KM is 1.73 M(-1)sec(-1) with pNP-GlcNAc as substrate.


proof_lines: There is a 4-fold greater activity on 4'-nitrophenyl beta-N-acetyl-D-glucosaminide than on 4'-nitrophenyl beta-N-acetyl-D-galactosaminide.


proof_lines: The catalytic efficiencies against 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 4'-nitrophenyl beta-D-glucopyranoside are similar.


organism: Homo sapiens

proof_lines: kcat is 79.3 min(-1), 30.4 min(-1), 122 min(-1) and 92.4 min(-1) for PNP-GalNAc, PNP-GlcNAc, 3F4NP-GalNAc and 3F4NP-GlcNAc, respectively.


organism: Chitinibacter sp. GC72


organism: Citrullus lanatus


organism: Cupiennius salei


organism: Curvibacter putative symbiont of Hydra magnipapillata

proof_lines: pH not specified in the publication, temperature not specified in the publication


organism: Dictyostelium discoideum


organism: Escherichia coli


organism: Gallus gallus


organism: Geobacillus stearothermophilus

substrate_name: 4-nitrophenyl N,N'-diacetylchitobioside

substrate: 4-nitrophenyl N,N'-diacetylchitobioside


organism: Glycine max


organism: Halocynthia roretzi


organism: Helicella ericetorum


proof_lines:
wild type enzyme, at pH 7.4 and 37°C
wild-type enzyme


organism: Limulus polyphemus

proof_lines:
passing through enzyme
adherent enzyme


organism: Lupinus luteus


organism: Mizuhopecten yessoensis


organism: Mucor fragilis


organism: Mus musculus


organism: Octopus vulgaris

substrate_name: phenyl-N-acetyl-beta-D-glucosaminide

substrate: phenyl-N-acetyl-beta-D-glucosaminide


organism: Oryctolagus cuniculus


organism: Oryza sativa


organism: Ostrinia furnacalis


organism: Thermotoga maritima MSB8

column_label: ScienceDirect rendered article Table 2, NagA row pNPGlcNAc2: Km column 0.37 +/- 0.07 mM; kcat column 199.0 s^-1; kcat/Km column 538.0 mM^-1 s^-1.

normalized_value_unit_evidence: Km=0.37 mM; kcat=199.0 s^-1; kcat_over_km=537.8378378378378 s^-1*mM^-1 calculated from 199.0/0.37 and consistent with table 538.0 after rounding.

row_label: NagA / pNPGlcNAc2


organism: uncultured Actinomycetales bacterium


organism: uncultured Bacteroidetes bacterium


organism: Vibrio furnissii


organism: Bacillus subtilis


organism: Bacteroides thetaiotaomicron

substrate_name: Unknown

proof_lines: substrate concentration 0.5 mM, two enzyme concentrations of 0.04 and 0.012 micrograms per microliter


organism: Bipolaris sorokiniana


organism: Bombyx mori

proof_lines:
Ex 2
Ex 1


organism: Bos taurus

proof_lines:
form B, pH 4.55
form A, pH 4.55
form B, pH 5.5


organism: Brassica oleracea


organism: Homo sapiens

substrate_name: complex of GM2 activator protein and GM2 ganglioside


organism: Hordeum vulgare


organism: Hydra vulgaris


organism: Lactococcus lactis


organism: Lathyrus oleraceus

proof_lines: beta-NAHA-IA beta-NAHA-IB beta-NAHA-II


organism: Leishmania major


organism: Stackebrandtia nassauensis


organism: Streptococcus pneumoniae


organism: Rhinella arenarum


organism: Saccharolobus solfataricus


organism: Salinivibrio costicola

substrate_name: p-nitrophenyl N,N'-diacetylchitobiose

proof_lines: Chi-I Chi-II

substrate: p-nitrophenyl N,N'-diacetylchitobiose


organism: Sclerotinia fructigena

substrate_name: N,N-diacetylchitobiose

substrate: N,N-diacetylchitobiose


organism: Spodoptera frugiperda

proof_lines:
product MGn-2-aminopyridine
product GnM-2-aminopyridine


organism: Stachybotrys elegans


proof_lines: construct of StrH covering GH20-1, the linker and GH20-2, pH 7.5, 37°C


organism: Ostrinia furnacalis

proof_lines:
pH 4.0, 25°C
at pH 6.5 and 30°C
pH 6, 30°C


organism: Ovis aries


organism: Palythoa caribaeorum


organism: Penaeus japonicus


organism: Penicillium oxalicum


organism: Phycomyces blakesleeanus


organism: Prunus serotina


organism: Rattus norvegicus

proof_lines:
caput, Hex B
caput, Hex A
caudal, Hex B


organism: Trichomonas vaginalis


organism: Trigonella foenum-graecum

proof_lines:
form IV
form I
form III


organism: Triticum aestivum


organism: Tritrichomonas suis


organism: uncultured Actinomycetales bacterium


organism: uncultured Bacteroidota bacterium


organism: Verruciconidia persicina


organism: Vibrio furnissii


organism: Streptomyces sp.


organism: Sus scrofa

proof_lines: PI PII


organism: Thermotoga maritima MSB8


organism: Streptococcus pneumoniae


organism: Streptomyces plicatus


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant D246N SpHex-MBP


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant R162H SpHex-MBP


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant E314Q SpHex-MBP


organism: Aspergillus versicolor


organism: Bacillus pumilus


organism: Bacillus sp. (in: firmicutes)


organism: Bacillus subtilis

proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant D232G


proof_lines: SABIO-RK modifier species: beta-N-acetylhexosaminidase(Enzyme) mutant H234G


organism: Thermotoga neapolitana


organism: Trametes cinnabarina


organism: Tremella fuciformis


organism: Trichinella spiralis

substrate_name: N-acetyl-beta-D-glucosamine

substrate: N-acetyl-beta-D-glucosamine


organism: Trichoderma harzianum

substrate_name: p-nitrophenyl-N-acetylglucosaminide

proof_lines: in presence of 200 mM heptakis-(2,6-di-O-methyl)-beta-cyclodextrin

substrate: p-nitrophenyl-N-acetylglucosaminide


organism: Trichoderma virens


organism: Acinetobacter baumannii

substrate_name: Imipenem; cephaloridine; Cloxacillin; Oxacillin


organism: Bacteroides fragilis

substrate_name: Penicillin G; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C155V CcrA1

substrate: Penicillin G; H2O


organism: Escherichia coli

substrate_name: Cephalosporin C; H2O

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

substrate: Cephalosporin C; H2O


substrate_name: H2O; Ampicillin

substrate: H2O; Ampicillin


substrate_name: ceftazidime; Imipenem; nitrocefin

substrate: ceftazidime; Imipenem; nitrocefin


substrate_name: cefalotin; cefotaxime

substrate: cefalotin; cefotaxime


substrate_name: cefoxitin; doripenem; cefalotin; meropenem; ampicillin; nitrocefin; ceftazidime; Imipenem


substrate_name: nitrocefin; cefoxitin; ceftazidime; doripenem; meropenem; ampicillin; Imipenem; cefalotin


organism: Fluoribacter gormanii

substrate_name: Imipenem

substrate: Imipenem


substrate_name: Cefuroxime

substrate: Cefuroxime


substrate_name: cefotaxime

substrate: cefotaxime


organism: Klebsiella pneumoniae

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


organism: Mycobacterium tuberculosis

substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


organism: Stenotrophomonas maltophilia

substrate_name: Nitrocefin

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

substrate: Nitrocefin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant I164A


organism: Pseudomonas aeruginosa

substrate_name: ampicillin (at 37 degrees Celsius and pH 7.5)


organism: Pseudomonas fluorescens

substrate_name: nitrocefin

substrate: nitrocefin


organism: Chryseobacterium indologenes

substrate_name: benzylpenicillin (at pH 7.0 and 30 degrees Celsius)


substrate_name: ampicillin

substrate: ampicillin


organism: Homo sapiens

substrate_name: palmitoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: palmitoyl-CoA


substrate_name: cloxacillin (at pH 7.0 and 30 degrees Celsius)

proof_lines: kcat is 577 sec(-1) with oxacillin as substrate (in the presence of 0.02 M NaHCO3) (PubMed:20086146). kcat is 357 sec(-1) with ampicillin as substrate (in the presence of 0.02 M NaHCO3) (PubMed:20086146). kcat is 16 sec(-1) with cephaloridi


organism: Aeromonas hydrophila

substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: Cephaloridine

substrate: Cephaloridine


substrate_name: biapenem

substrate: biapenem


substrate_name: H2O; Imipenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant R121H

substrate: H2O; Imipenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N116H/R121H/N220G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N116H/N220G


organism: Achromobacter sp. sallbros1

column_label: Table 2 'Table 2: Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1'; row Imipenem; TMB-1 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Imipenem, TMB-1 normalized: kcat 1.7 s^-1; Km 0.2 mM; kcat/Km 9 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Imipenem, TMB-1 columns: kcat 1.7 s^-1; Km 200 uM; kcat/Km 0.009 s^-1/uM.

row_label: Imipenem


substrate_name: piperacillin

column_label: Table 2 'Table 2: Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1'; row Piperacillin; TMB-1 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Piperacillin, TMB-1 normalized: kcat 3.3 s^-1; Km 0.072 mM; kcat/Km 46 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Piperacillin, TMB-1 columns: kcat 3.3 s^-1; Km 72 uM; kcat/Km 0.046 s^-1/uM.

row_label: Piperacillin

substrate: piperacillin


substrate_name: cefoxitin

column_label: Table 2 'Table 2: Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1'; row Cefoxitin; TMB-1 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Cefoxitin, TMB-1 normalized: kcat 0.3 s^-1; Km 0.069 mM; kcat/Km 4 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Cefoxitin, TMB-1 columns: kcat 0.3 s^-1; Km 69 uM; kcat/Km 0.004 s^-1/uM.

row_label: Cefoxitin

substrate: cefoxitin


substrate_name: ceftazidime

column_label: Table 2 'Table 2: Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1'; row Ceftazidime; TMB-1 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Ceftazidime, TMB-1 normalized: kcat 0.07 s^-1; Km 0.031 mM; kcat/Km 2 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Ceftazidime, TMB-1 columns: kcat 0.07 s^-1; Km 31 uM; kcat/Km 0.002 s^-1/uM.

row_label: Ceftazidime

substrate: ceftazidime


substrate_name: meropenem

column_label: Table 2 'Table 2: Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1'; row Meropenem; TMB-1 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Meropenem, TMB-1 normalized: kcat 1.4 s^-1; Km 0.075 mM; kcat/Km 19 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Meropenem, TMB-1 columns: kcat 1.4 s^-1; Km 75 uM; kcat/Km 0.019 s^-1/uM.

row_label: Meropenem

substrate: meropenem


substrate_name: ertapenem

column_label: Table 2 'Table 2: Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1'; row Ertapenem; TMB-1 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Ertapenem, TMB-1 normalized: kcat 0.4 s^-1; Km 0.031 mM; kcat/Km 13 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Ertapenem, TMB-1 columns: kcat 0.4 s^-1; Km 31 uM; kcat/Km 0.013 s^-1/uM.

row_label: Ertapenem

substrate: ertapenem


substrate_name: cefuroxime

column_label: Table 2 'Table 2: Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1'; row Cefuroxime; TMB-1 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Cefuroxime, TMB-1 normalized: kcat 0.1 s^-1; Km 0.009 mM; kcat/Km 11 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Cefuroxime, TMB-1 columns: kcat 0.1 s^-1; Km 9 uM; kcat/Km 0.011 s^-1/uM.

row_label: Cefuroxime

substrate: cefuroxime


column_label: Table 2 'Table 2: Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1'; row Ampicillin; TMB-1 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Ampicillin, TMB-1 normalized: kcat 3.3 s^-1; Km 0.027 mM; kcat/Km 122 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Ampicillin, TMB-1 columns: kcat 3.3 s^-1; Km 27 uM; kcat/Km 0.122 s^-1/uM.

row_label: Ampicillin


organism: Aeromonas enteropelogenes

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Ampicillin; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 0.63, 0.72, 8.8 × 10^5

row_label: TRU-1 / Ampicillin


substrate_name: cefpirome

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Cefpirome; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 23, 85, 2.7 × 10^5

raw_value_unit_evidence: TRU-1 / Cefpirome: kcat=23 s^-1; Km=85 uM; kcat/Km=2.7 × 10^5 M^-1 s^-1

row_label: TRU-1 / Cefpirome

substrate: cefpirome


substrate_name: cefazolin

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Cefazolin (vo); TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 0.55, 120, 4.6 × 10^3

row_label: TRU-1 / Cefazolin (vo)

substrate: cefazolin


substrate_name: cefepime

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Cefepime; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 9.4, 360, 2.6 × 10^4

row_label: TRU-1 / Cefepime

substrate: cefepime


substrate_name: ceftriaxone

verification_status: verified

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Ceftriaxone; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 0.042, 6, 7.0 × 10^3

raw_value_unit_evidence: TRU-1 / Ceftriaxone: kcat=0.042 s^-1; Km=6 uM; kcat/Km=7.0 × 10^3 M^-1 s^-1

row_label: TRU-1 / Ceftriaxone

substrate: ceftriaxone

status: verified


column_label: PMID 15588826 DOI 10.1016/j.jmb.2004.10.070 Table 1; row Wild-type; biapenem columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 wild-type CphA biapenem: kcat 300 s^-1; Km 166 uM; kcat/Km 1.8 x 10^6 M^-1 s^-1.

row_label: Wild-type / Biapenem

table_label: Table 1. Kinetic parameters of the wild type and selected mutants of CphA


substrate_name: Imipenem

substrate: Imipenem


column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Cefoxitin; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 0.88, 0.025, 3.5 × 10^7

row_label: TRU-1 / Cefoxitin


substrate_name: penicillin G

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Penicillin G; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 27, 2, 1.4 × 10^7

raw_value_unit_evidence: TRU-1 / Penicillin G: kcat=27 s^-1; Km=2 uM; kcat/Km=1.4 × 10^7 M^-1 s^-1

row_label: TRU-1 / Penicillin G

substrate: penicillin G


substrate_name: cefotaxime

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Cefotaxime; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 0.015, 0.0009, 1.7 × 10^7

row_label: TRU-1 / Cefotaxime

substrate: cefotaxime


column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Ceftazidime; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 0.11, 0.12, 9.2 × 10^5

row_label: TRU-1 / Ceftazidime


column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Piperacillin; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 0.54, 0.2, 2.7 × 10^6

raw_value_unit_evidence: TRU-1 / Piperacillin: kcat=0.54 s^-1; Km=0.2 uM; kcat/Km=2.7 × 10^6 M^-1 s^-1

row_label: TRU-1 / Piperacillin


substrate_name: cephalothin

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Cephalothin; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 470, 45, 1.0 × 10^7

raw_value_unit_evidence: TRU-1 / Cephalothin: kcat=470 s^-1; Km=45 uM; kcat/Km=1.0 × 10^7 M^-1 s^-1

row_label: TRU-1 / Cephalothin

substrate: cephalothin


substrate_name: cephalexin

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Cephalexin; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 160, 17, 9.3 × 10^6

raw_value_unit_evidence: TRU-1 / Cephalexin: kcat=160 s^-1; Km=17 uM; kcat/Km=9.3 × 10^6 M^-1 s^-1

row_label: TRU-1 / Cephalexin

substrate: cephalexin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N220G


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Cephaloridine

substrate: Cephaloridine


substrate_name: Nitrocefin

substrate: Nitrocefin


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

column_label: Table 3. Kinetic parameters of metallo-beta-lactamases with benzylpenicillin and imipenem after purification; row Penicillin G (A. hydrophila AE036 column group); A. hydrophila AE036 column group (the leftmost of the three enzyme column groups): column Km (uM) raw cell 680; column kcat (s^-1) raw cell 5; column kcat/Km (M^-1 s^-1) printed cell 7.35 x 10^3 M^-1 s^-1 = 7.35 s^-1 mM^-1.

normalized_value_unit_evidence: kcat 5 s^-1 = 5.0 s^-1. Km 680 uM = 680/1000 = 0.68 mM. The table prints kcat/Km as 7.35 x 10^3 M^-1 s^-1 = 7.35 s^-1 mM^-1; the exact quotient of the same two printed cells is 5.0 / 0.68 = 7.352941176470588 s^-1 mM^-1, and the printed cell is that quotient rounded to the three significant figures the table carries, so the printed ratio and the exported ratio are the same measurement at two precisions.

raw_value_unit_evidence: Table 3. Kinetic parameters of metallo-beta-lactamases with benzylpenicillin and imipenem after purification, row Penicillin G (A. hydrophila AE036 column group): Km column cell 680 uM; kcat column cell 5 s^-1; kcat/Km column cell 7.35 x 10^3 M^-1 s^-1 = 7.35 s^-1 mM^-1.


substrate_name: tazobactam

column_label: Table label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonama. Row: Tazobactam. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 440 ± 10, kcat (s^-1) cell 0.65, kcat/Km (M^-1 s^-1) cell 1.50 x 10^3 M^-1 s^-1. Km 440 ± 10 uM normalizes to 0.44 mM and equals the exported km; kcat 0.65 s^-1 equals the exported kcat; the exported kcat_over_km 1.4772727272727273 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 1.50 x 10^3 M^-1 s^-1 = 1.50 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 6 row Tazobactam: Km 440 ± 10 uM = 0.44 mM; kcat 0.65 s^-1 = 0.65 s^-1; kcat/Km taken as the quotient of those two printed cells, 0.65 s^-1 / 0.44 mM = 1.4772727272727273 s^-1 mM^-1. The table also prints a rounded kcat/Km cell, 1.50 x 10^3 M^-1 s^-1 = 1.50 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)` and `1.50 3 103` is `1.50 x 10^3`.

raw_value_unit_evidence: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonama | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Tazobactam 440 6 10 0.65 1.50 3 103 420 6 10 6.5 1.55 3 104 190 6 5 270.0 1.40 3 106

row_label: A. hydrophila AE036 | Tazobactam

substrate: tazobactam


substrate_name: Epicillin

column_label: Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins; row Epicillin (A. hydrophila AE036 column group); A. hydrophila AE036 column group (the leftmost of the three enzyme column groups): column Km (uM) raw cell 300; column kcat (s^-1) raw cell 0.6; column kcat/Km (M^-1 s^-1) printed cell 2.00 x 10^3 M^-1 s^-1 = 2.0 s^-1 mM^-1.

normalized_value_unit_evidence: kcat 0.6 s^-1 = 0.6 s^-1. Km 300 uM = 300/1000 = 0.3 mM. The table prints kcat/Km as 2.00 x 10^3 M^-1 s^-1 = 2.0 s^-1 mM^-1; the exact quotient of the same two printed cells is 0.6 / 0.3 = 2.0 s^-1 mM^-1, and the printed cell is that quotient rounded to the three significant figures the table carries, so the printed ratio and the exported ratio are the same measurement at two precisions.

raw_value_unit_evidence: Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins, row Epicillin (A. hydrophila AE036 column group): Km column cell 300 uM; kcat column cell 0.6 s^-1; kcat/Km column cell 2.00 x 10^3 M^-1 s^-1 = 2.0 s^-1 mM^-1.

substrate: Epicillin


column_label: Table label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonama. Row: HRE-664. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 140 ± 10, kcat (s^-1) cell 10.0, kcat/Km (M^-1 s^-1) cell 7.15 x 10^4 M^-1 s^-1. Km 140 ± 10 uM normalizes to 0.14 mM and equals the exported km; kcat 10.0 s^-1 equals the exported kcat; the exported kcat_over_km 71.42857142857142 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 7.15 x 10^4 M^-1 s^-1 = 71.5 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 6 row HRE-664: Km 140 ± 10 uM = 0.14 mM; kcat 10.0 s^-1 = 10.0 s^-1; kcat/Km taken as the quotient of those two printed cells, 10.0 s^-1 / 0.14 mM = 71.42857142857142 s^-1 mM^-1. The table also prints a rounded kcat/Km cell, 7.15 x 10^4 M^-1 s^-1 = 71.5 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)` and `1.50 3 103` is `1.50 x 10^3`.

raw_value_unit_evidence: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonama | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: HRE-664 140 6 10 10.0 7.15 3 104 25 6 2 10.0 4.00 3 105 20 6 2 1.5 7.50 3 104

row_label: A. hydrophila AE036 | HRE-664


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


substrate_name: Meropenem

column_label: Table label: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibioticsa. Row: Meropenem. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 250 ± 5, kcat (s^-1) cell 440, kcat/Km (M^-1 s^-1) cell 1.75 x 10^6 M^-1 s^-1. Km 250 ± 5 uM normalizes to 0.25 mM and equals the exported km; kcat 440 s^-1 equals the exported kcat; the exported kcat_over_km 1760.0 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 1.75 x 10^6 M^-1 s^-1 = 1750 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 7 row Meropenem: Km 250 ± 5 uM = 0.25 mM; kcat 440 s^-1 = 440.0 s^-1; kcat/Km taken as the quotient of those two printed cells, 440 s^-1 / 0.25 mM = 1760.0 s^-1 mM^-1. The table also prints a rounded kcat/Km cell, 1.75 x 10^6 M^-1 s^-1 = 1750 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)` and `1.50 3 103` is `1.50 x 10^3`.

raw_value_unit_evidence: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibioticsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Meropenem 250 6 5 440 1.75 3 106 400 6 20 580 1.45 3 106 10 6 1b 45 4.50 3 106

row_label: A. hydrophila AE036 | Meropenem

substrate: Meropenem


substrate_name: Temocillin

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Temocillin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 65 ± 5, kcat (s^-1) cell 1.75, kcat/Km (M^-1 s^-1) cell 2.70 x 10^4 M^-1 s^-1. Km 65 ± 5 uM normalizes to 0.065 mM and equals the exported km; kcat 1.75 s^-1 equals the exported kcat; the exported kcat_over_km 26.923076923076923 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 2.70 x 10^4 M^-1 s^-1 = 27.0 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 4 row Temocillin: Km 65 ± 5 uM = 0.065 mM; kcat 1.75 s^-1 = 1.75 s^-1; kcat/Km taken as the quotient of those two printed cells, 1.75 s^-1 / 0.065 mM = 26.923076923076923 s^-1 mM^-1. The table also prints a rounded kcat/Km cell, 2.70 x 10^4 M^-1 s^-1 = 27.0 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)` and `1.50 3 103` is `1.50 x 10^3`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Temocillin 65 6 5 1.75 2.70 3 104 — — — 155 6 5 135 1.20 3 106

row_label: A. hydrophila AE036 | Temocillin

substrate: Temocillin


substrate_name: Ticarcillin

column_label: Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins; row Ticarcillin (A. hydrophila AE036 column group); A. hydrophila AE036 column group (the leftmost of the three enzyme column groups): column Km (uM) raw cell 250; column kcat (s^-1) raw cell 3.5; column kcat/Km (M^-1 s^-1) printed cell 1.40 x 10^4 M^-1 s^-1 = 14.0 s^-1 mM^-1.

normalized_value_unit_evidence: kcat 3.5 s^-1 = 3.5 s^-1. Km 250 uM = 250/1000 = 0.25 mM. The table prints kcat/Km as 1.40 x 10^4 M^-1 s^-1 = 14.0 s^-1 mM^-1; the exact quotient of the same two printed cells is 3.5 / 0.25 = 14.0 s^-1 mM^-1, and the printed cell is that quotient rounded to the three significant figures the table carries, so the printed ratio and the exported ratio are the same measurement at two precisions.

raw_value_unit_evidence: Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins, row Ticarcillin (A. hydrophila AE036 column group): Km column cell 250 uM; kcat column cell 3.5 s^-1; kcat/Km column cell 1.40 x 10^4 M^-1 s^-1 = 14.0 s^-1 mM^-1.

substrate: Ticarcillin


substrate_name: Oxacillin

substrate: Oxacillin


substrate_name: azlocillin

column_label: Table 4: Kinetic parameters of metallo-beta-lactamases with penicillins; organism block A. hydrophila AE036; row Azlocillin; Km raw 90 uM normalized 0.09 mM; kcat raw 0.18 s^-1 normalized 0.18 s^-1; kcat/Km raw 2000.0 M^-1 s^-1 normalized 2 s^-1 mM^-1.

row_label: A. hydrophila AE036 / Azlocillin

substrate: azlocillin


substrate_name: Sulbenicillin

column_label: Table 4: Kinetic parameters of metallo-beta-lactamases with penicillins; organism block A. hydrophila AE036; row Sulbenicillin; Km raw 230 uM normalized 0.23 mM; kcat raw 0.5 s^-1 normalized 0.5 s^-1; kcat/Km raw 2100.0 M^-1 s^-1 normalized 2.1 s^-1 mM^-1.

row_label: A. hydrophila AE036 / Sulbenicillin

substrate: Sulbenicillin


substrate_name: Cefsulodin

column_label: Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cefsulodin / A. hydrophila AE036, column A. hydrophila AE036; Km uM, raw cell 130 +/- 10, normalized 0.13 mM; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cefsulodin / A. hydrophila AE036, column A. hydrophila AE036; kcat s^-1, raw cell 0.05, normalized 0.05 s^-1; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cefsulodin / A. hydrophila AE036, column A. hydrophila AE036; kcat/Km M^-1 s^-1, raw cell 3.50 x 10^2, normalized 0.35 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.13 normalized_unit=mM; kcat normalized_value=0.05 normalized_unit=s^-1; kcat/Km normalized_value=0.35 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=130 +/- 10 raw_unit=uM raw_cell=130 +/- 10; kcat raw_value=0.05 raw_unit=s^-1 raw_cell=0.05; kcat/Km raw_value=3.50 x 10^2 raw_unit=M^-1*s^-1 raw_cell=3.50 x 10^2

row_label: Cefsulodin / A. hydrophila AE036

substrate: Cefsulodin


substrate_name: piperacillin

column_label: Table 4: Kinetic parameters of metallo-beta-lactamases with penicillins; organism block A. hydrophila AE036; row Piperacillin; Km raw 55 uM normalized 0.055 mM; kcat raw 0.43 s^-1 normalized 0.43 s^-1; kcat/Km raw 7800.0 M^-1 s^-1 normalized 7.8 s^-1 mM^-1.

row_label: A. hydrophila AE036 / Piperacillin

substrate: piperacillin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Asparenomycin A

column_label: Table 7. Kinetic parameters of metallo-beta-lactamases with carbapenem antibiotics row Asparenomycin A / A. hydrophila AE036, column A. hydrophila AE036; Km uM, raw cell 170 +/- 5, normalized 0.17 mM; Table 7. Kinetic parameters of metallo-beta-lactamases with carbapenem antibiotics row Asparenomycin A / A. hydrophila AE036, column A. hydrophila AE036; kcat s^-1, raw cell 475, normalized 475 s^-1; Table 7. Kinetic parameters of metallo-beta-lactamases with carbapenem antibiotics row Asparenomycin A / A. hydrophila AE036, column A. hydrophila AE036; kcat/Km M^-1 s^-1, raw cell 2.80 x 10^6, normalized 2800 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.17 normalized_unit=mM; kcat normalized_value=475 normalized_unit=s^-1; kcat/Km normalized_value=2800 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=170 +/- 5 raw_unit=uM raw_cell=170 +/- 5; kcat raw_value=475 raw_unit=s^-1 raw_cell=475; kcat/Km raw_value=2.80 x 10^6 raw_unit=M^-1*s^-1 raw_cell=2.80 x 10^6

row_label: Asparenomycin A / A. hydrophila AE036

substrate: Asparenomycin A


substrate_name: carbenicillin

column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label carbenicillin; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: carbenicillin

table_label: Table 3

substrate: carbenicillin


substrate_name: H2O; Ampicillin

substrate: H2O; Ampicillin


substrate_name: cefotaxime

column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label cefotaxime; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: cefotaxime

substrate: cefotaxime


column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label nitrocefin; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: nitrocefin


substrate_name: cephalexin

column_label: PMC1132494 scanned page 154 Table 3; organism/enzyme column Aeromonas hydrophila A2 enzyme; row cephalexin; Km column=230 +/- 20 uM; kcat column=0.65 s^-1; kcat/Km column=2.90 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: normalized km=0.23 mM; export km=0.23 mM; normalized kcat=0.65 s^-1; export kcat=0.65 s^-1; normalized kcat_over_km=2.9 s^-1 mM^-1; export kcat_over_km=2.82608695652174 s^-1 mM^-1

raw_value_unit_evidence: Table 3 Aeromonas hydrophila A2 enzyme / cephalexin; Km = 230 +/- 20 uM; kcat = 0.65 s^-1; kcat/Km = 2.90 x 10^3 M^-1 s^-1

table_label: PMC1132494 scanned page 154 Table 3

substrate: cephalexin


substrate_name: Cefuroxime

column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label cefuroxime; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: cefuroxime

substrate: Cefuroxime


substrate_name: Cephaloglycin

column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label cephaloglycin; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: cephaloglycin

substrate: Cephaloglycin


organism: Aliivibrio salmonicida

substrate_name: cefuroxime

column_label: Table 1 row Cefuroxime; ALI-1 kcat = 11 +/- 3; ALI-1 KM = 68 +/- 30; ALI-1 kcat/KM = 0.16.

raw_value_unit_evidence: ALI-1 columns report kcat 11 +/- 3 s^-1; KM 68 +/- 30 uM; kcat/KM 0.16 1/uM*s.

row_label: Cefuroxime

table_label: Table 1. Comparison of kcat, KM and catalytic efficiency for ALI-1, IMP-1 and VIM-2.

substrate: cefuroxime


substrate_name: Talampicillin

column_label: Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Talampicillin / A. hydrophila AE036, column A. hydrophila AE036; Km uM, raw cell 90 +/- 10, normalized 0.09 mM; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Talampicillin / A. hydrophila AE036, column A. hydrophila AE036; kcat s^-1, raw cell 0.04, normalized 0.04 s^-1; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Talampicillin / A. hydrophila AE036, column A. hydrophila AE036; kcat/Km M^-1 s^-1, raw cell 5.00 x 10^2, normalized 0.5 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.09 normalized_unit=mM; kcat normalized_value=0.04 normalized_unit=s^-1; kcat/Km normalized_value=0.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=90 +/- 10 raw_unit=uM raw_cell=90 +/- 10; kcat raw_value=0.04 raw_unit=s^-1 raw_cell=0.04; kcat/Km raw_value=5.00 x 10^2 raw_unit=M^-1*s^-1 raw_cell=5.00 x 10^2

row_label: Talampicillin / A. hydrophila AE036

substrate: Talampicillin


column_label: Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row CGP-31523A / A. hydrophila AE036, column A. hydrophila AE036; Km uM, raw cell 75 +/- 5, normalized 0.075 mM; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row CGP-31523A / A. hydrophila AE036, column A. hydrophila AE036; kcat s^-1, raw cell 0.05, normalized 0.05 s^-1; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row CGP-31523A / A. hydrophila AE036, column A. hydrophila AE036; kcat/Km M^-1 s^-1, raw cell 6.00 x 10^2, normalized 0.6 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.075 normalized_unit=mM; kcat normalized_value=0.05 normalized_unit=s^-1; kcat/Km normalized_value=0.6 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=75 +/- 5 raw_unit=uM raw_cell=75 +/- 5; kcat raw_value=0.05 raw_unit=s^-1 raw_cell=0.05; kcat/Km raw_value=6.00 x 10^2 raw_unit=M^-1*s^-1 raw_cell=6.00 x 10^2

row_label: CGP-31523A / A. hydrophila AE036


substrate_name: 6-beta-Iodopenicillanic acid

column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label 6-beta-Iodopenicillanic acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: 6-beta-Iodopenicillanic acid

substrate: 6-beta-Iodopenicillanic acid


substrate_name: Sulbactam

column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label Sulbactam; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: Sulbactam

substrate: Sulbactam


column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label Imipenem; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: Imipenem


substrate_name: cephaloridin

column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label cephaloridin; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: cephaloridin

substrate: cephaloridin


substrate_name: Oxacillin

column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label Oxacillin; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: Oxacillin

substrate: Oxacillin


substrate_name: Penicillin G

column_label: Table 3 scanned page 154; enzyme block Aeromonas hydrophila A2 enzyme; row label Penicillin G; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; A. hydrophila experiments at 30 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: Penicillin G

substrate: Penicillin G


organism: Bacillus cereus

substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H196S

substrate: H2O; Penicillin G


substrate_name: Nitrocefin

substrate: Nitrocefin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H116S


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H263S


substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120N; fusion protein to glutathione-S-transferase

substrate: H2O; Nitrocefin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: cefoxitin

row_label: Cefoxitin

substrate: cefoxitin


substrate_name: ceftazidime

column_label: Table 1 row Ceftazidime; ALI-1 kcat = 0.09 +/- 0.03; ALI-1 KM = 37 +/- 12; ALI-1 kcat/KM = 0.0024.

row_label: Ceftazidime

substrate: ceftazidime


substrate_name: cefepime

row_label: Cefepime

substrate: cefepime


substrate_name: meropenem

column_label: Table 1 row Meropenem; ALI-1 kcat = 13 +/- 5; ALI-1 KM = 142 +/- 100; ALI-1 kcat/KM = 0.094.

raw_value_unit_evidence: ALI-1 columns report kcat 13 +/- 5 s^-1; KM 142 +/- 100 uM; kcat/KM 0.094 1/uM*s.

row_label: Meropenem

substrate: meropenem


substrate_name: nitrocefin

column_label: Table 1 row Nitrocefin; ALI-1 kcat = 6.3 +/- 0.6; ALI-1 KM = 6 +/- 3; ALI-1 kcat/KM = 1.0.

raw_value_unit_evidence: ALI-1 columns report kcat 6.3 +/- 0.6 s^-1; KM 6 +/- 3 uM; kcat/KM 1.0 1/uM*s.

row_label: Nitrocefin

substrate: nitrocefin


substrate_name: ertapenem

substrate: ertapenem


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

column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'H116S', benzylpenicillin column group; column 'Km (uM)' = 530; column 'kcat (s^-1)' = 47; column 'kcat/Km (M^-1 s^-1)' = 89000.

normalized_value_unit_evidence: Km: printed Table 3 cell 530 uM; 530 / 1000 = 0.53 mM; the paper value is 0.53 mM and the exported value is 0.53 mM. kcat: printed Table 3 cell 47 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 47.0 s^(-1) and the exported value is 47.0 s^(-1). kcat/Km: printed Table 3 cell 89000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 89000 / 1000 = 89.0 s^-1 mM^-1; the paper value is 89.0 s^(-1)*mM^(-1); the exported value is 88.67924528301886 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme row 'H116S', benzylpenicillin column group: Km = 530 uM; kcat = 47 s^-1; printed kcat/Km = 89000 M^-1 s^-1.

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


substrate_name: cefotaxime

sequence_source: UniProtKB P04190 canonical sequence

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

substrate: cefotaxime


sequence_source: Reconstructed from UniProtKB P04190 canonical sequence and mutation signature

sequence_variant_note: Mutation signature D120S matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature D120E matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120E; fusion protein to glutathione-S-transferase


sequence_variant_note: Mutation signature D120Q matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature D120N matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120Q; fusion protein to glutathione-S-transferase


column_label: Official Cell full text Table 2 row Cefoxitin under BcII columns gives Km 240 +/- 33 uM, kcat 0.34 +/- 0.01 s^-1, and kcat/Km 0.0014 in 10^6 M^-1 s^-1 units.

normalized_value_unit_evidence: Km normalized_value=0.24 normalized_unit=mM from 240 uM / 1000; kcat normalized_value=0.34 normalized_unit=s^-1; kcat/Km normalized_value=1.4166666666666667 normalized_unit=s^-1*mM^-1 from 0.34 / 0.24, consistent with table rounded 0.0014 x 10^6 M^-1 s^-1.

row_label: BcII / Cefoxitin

table_label: Table 2: Molecular Mass, Zinc Content, and Kinetic Constants at 30C for Various Substrates of BcII, BcII DeltaIMP, and BcII DeltaIMP W64A


substrate_name: Cephapirin

column_label: Table III Cephapirin row, experimental kcat and Km columns and their same-row quotient.

raw_value_unit_evidence: Table III Cephapirin row: kcat 101 +/- 4 s^-1; Km 27.7 +/- 0.4 uM.

row_label: Cephapirin; experimental kcat and Km columns

table_label: Table III: Steady state kinetic parameters at 15 C

substrate: Cephapirin


substrate_name: H2O; Cefotaxime

substrate: H2O; Cefotaxime


substrate_name: Penicillin G; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H118S

substrate: Penicillin G; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C221S


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N233Y


substrate_name: Imipenem; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C221A

substrate: Imipenem; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K73R


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K73R, E166D


sequence_source: UniProtKB reviewed (Swiss-Prot) P00809 canonical sequence

assay_conditions_summary: pH 7; 293.15 K; buffer containing 0

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

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

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

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


substrate_name: Cephalosporin C

substrate: Cephalosporin C


substrate_name: carbenicillin

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

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

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

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

substrate: carbenicillin


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: Nitrocefin

substrate: Nitrocefin


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

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

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D120N to reconstruct the assayed variant sequence.


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant BcII delta IMP

substrate: Nitrocefin; H2O


substrate_name: cephaloridin

substrate: cephaloridin


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


substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E166D

substrate: H2O; Nitrocefin


column_label: Table 6: Kinetic parameters of metallo-beta-lactamases with penems, tazobactam (YTR-830), and carumonam; organism block B. cereus 5/B/6; row HRE-664; Km raw 25 uM normalized 0.025 mM; kcat raw 10.0 s^-1 normalized 10 s^-1; kcat/Km raw 400000.0 M^-1 s^-1 normalized 400 s^-1 mM^-1.

row_label: B. cereus 5/B/6 / HRE-664


substrate_name: tazobactam

column_label: Table 6. Kinetic parameters of metallo-beta-lactamases with penems, tazobactam (YTR-830), and carumonam row Tazobactam / B. cereus 5/B/6, column B. cereus 5/B/6; Km uM, raw cell 420 +/- 10, normalized 0.42 mM; Table 6. Kinetic parameters of metallo-beta-lactamases with penems, tazobactam (YTR-830), and carumonam row Tazobactam / B. cereus 5/B/6, column B. cereus 5/B/6; kcat s^-1, raw cell 6.5, normalized 6.5 s^-1; Table 6. Kinetic parameters of metallo-beta-lactamases with penems, tazobactam (YTR-830), and carumonam row Tazobactam / B. cereus 5/B/6, column B. cereus 5/B/6; kcat/Km M^-1 s^-1, raw cell 1.55 x 10^4, normalized 15.5 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.42 normalized_unit=mM; kcat normalized_value=6.5 normalized_unit=s^-1; kcat/Km normalized_value=15.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=420 +/- 10 raw_unit=uM raw_cell=420 +/- 10; kcat raw_value=6.5 raw_unit=s^-1 raw_cell=6.5; kcat/Km raw_value=1.55 x 10^4 raw_unit=M^-1*s^-1 raw_cell=1.55 x 10^4

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

substrate: tazobactam


substrate_name: Cephradine

column_label: Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cephradine / B. cereus 5/B/6, column B. cereus 5/B/6; Km uM, raw cell 930 +/- 20, normalized 0.93 mM; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cephradine / B. cereus 5/B/6, column B. cereus 5/B/6; kcat s^-1, raw cell 12.5, normalized 12.5 s^-1; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cephradine / B. cereus 5/B/6, column B. cereus 5/B/6; kcat/Km M^-1 s^-1, raw cell 1.30 x 10^4, normalized 13 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.93 normalized_unit=mM; kcat normalized_value=12.5 normalized_unit=s^-1; kcat/Km normalized_value=13 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=930 +/- 20 raw_unit=uM raw_cell=930 +/- 20; kcat raw_value=12.5 raw_unit=s^-1 raw_cell=12.5; kcat/Km raw_value=1.30 x 10^4 raw_unit=M^-1*s^-1 raw_cell=1.30 x 10^4

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

substrate: Cephradine


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

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


substrate_name: azlocillin

column_label: Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Azlocillin / B. cereus 5/B/6, column B. cereus 5/B/6; Km uM, raw cell 170 +/- 10, normalized 0.17 mM; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Azlocillin / B. cereus 5/B/6, column B. cereus 5/B/6; kcat s^-1, raw cell 205, normalized 205 s^-1; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Azlocillin / B. cereus 5/B/6, column B. cereus 5/B/6; kcat/Km M^-1 s^-1, raw cell 1.20 x 10^6, normalized 1200 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.17 normalized_unit=mM; kcat normalized_value=205 normalized_unit=s^-1; kcat/Km normalized_value=1200 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=170 +/- 10 raw_unit=uM raw_cell=170 +/- 10; kcat raw_value=205 raw_unit=s^-1 raw_cell=205; kcat/Km raw_value=1.20 x 10^6 raw_unit=M^-1*s^-1 raw_cell=1.20 x 10^6

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

substrate: azlocillin


substrate_name: Penicillin V

substrate: Penicillin V


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E166Cmc


substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E166A

substrate: H2O; Penicillin G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E166C


substrate_name: cefotaxime

substrate: cefotaxime


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120S; fusion protein to glutathione-S-transferase


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Cephaloridine

substrate: Cephaloridine


substrate_name: Penicillin G; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C155V CcrA1

substrate: Penicillin G; H2O


substrate_name: Cefsulodin

column_label: Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cefsulodin / B. cereus 5/B/6, column B. cereus 5/B/6; Km uM, raw cell 230 +/- 20, normalized 0.23 mM; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cefsulodin / B. cereus 5/B/6, column B. cereus 5/B/6; kcat s^-1, raw cell 12.5, normalized 12.5 s^-1; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cefsulodin / B. cereus 5/B/6, column B. cereus 5/B/6; kcat/Km M^-1 s^-1, raw cell 5.40 x 10^4, normalized 54 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.23 normalized_unit=mM; kcat normalized_value=12.5 normalized_unit=s^-1; kcat/Km normalized_value=54 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=230 +/- 20 raw_unit=uM raw_cell=230 +/- 20; kcat raw_value=12.5 raw_unit=s^-1 raw_cell=12.5; kcat/Km raw_value=5.40 x 10^4 raw_unit=M^-1*s^-1 raw_cell=5.40 x 10^4

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

substrate: Cefsulodin


substrate_name: Meropenem

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

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

substrate: Meropenem


substrate_name: piperacillin

column_label: Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Piperacillin / B. cereus 5/B/6, column B. cereus 5/B/6; Km uM, raw cell 450 +/- 10, normalized 0.45 mM; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Piperacillin / B. cereus 5/B/6, column B. cereus 5/B/6; kcat s^-1, raw cell 75, normalized 75 s^-1; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Piperacillin / B. cereus 5/B/6, column B. cereus 5/B/6; kcat/Km M^-1 s^-1, raw cell 1.70 x 10^5, normalized 170 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.45 normalized_unit=mM; kcat normalized_value=75 normalized_unit=s^-1; kcat/Km normalized_value=170 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=450 +/- 10 raw_unit=uM raw_cell=450 +/- 10; kcat raw_value=75 raw_unit=s^-1 raw_cell=75; kcat/Km raw_value=1.70 x 10^5 raw_unit=M^-1*s^-1 raw_cell=1.70 x 10^5

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

substrate: piperacillin


substrate_name: Asparenomycin A

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

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

substrate: Asparenomycin A


substrate_name: Epicillin

column_label: Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Epicillin / B. cereus 5/B/6, column B. cereus 5/B/6; Km uM, raw cell 550 +/- 10, normalized 0.55 mM; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Epicillin / B. cereus 5/B/6, column B. cereus 5/B/6; kcat s^-1, raw cell 160, normalized 160 s^-1; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Epicillin / B. cereus 5/B/6, column B. cereus 5/B/6; kcat/Km M^-1 s^-1, raw cell 2.90 x 10^5, normalized 290 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.55 normalized_unit=mM; kcat normalized_value=160 normalized_unit=s^-1; kcat/Km normalized_value=290 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=550 +/- 10 raw_unit=uM raw_cell=550 +/- 10; kcat raw_value=160 raw_unit=s^-1 raw_cell=160; kcat/Km raw_value=2.90 x 10^5 raw_unit=M^-1*s^-1 raw_cell=2.90 x 10^5

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

substrate: Epicillin


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

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

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

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

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


substrate_name: H2O; 6-Aminopenicillanate

substrate: H2O; 6-Aminopenicillanate


substrate_name: Penicillin G

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

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

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

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

substrate: Penicillin G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D103N CcrA3


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H99N CcrA3


substrate_name: Sulbactam

substrate: Sulbactam


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: 6-beta-Iodopenicillanic acid

substrate: 6-beta-Iodopenicillanic acid


substrate_name: cephalexin

substrate: cephalexin


substrate_name: Cephaloglycin

substrate: Cephaloglycin


substrate_name: Cefuroxime

substrate: Cefuroxime


organism: Bacillus licheniformis

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

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

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

row_label: wild type; ampicillin (III)

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


substrate_name: H2O; Penicillin V

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K234E

substrate: H2O; Penicillin V


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

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

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

row_label: wild type; nitrocefin (IV)


substrate_name: Penicillin V

substrate: Penicillin V


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K234A


substrate_name: Penicillin V; H2O

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----

substrate: Penicillin V; H2O


substrate_name: amoxicillin

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

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

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

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

row_label: Amoxicillin

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

substrate: amoxicillin