organism: Synechocystis sp. PCC 6803 / Kazusa

proof_lines: recombinant full-length CcaA274 enzyme, pH 7.5, 25°C, CO2 hydration reaction

proof_lines: recombinant full-length CcaA274 enzyme, pH 9.5, 25°C, CO2 hydration reaction


enzyme_display_name: carbonic anhydrase

organism: Tectona grandis

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.

enzyme: carbonic anhydrase

source: brenda


organism: Thalassiosira pseudonana

km_display: Not reported

proof_lines: pH 7.9, temperature not specified in the publication, the activities depended on culture conditions, ranging between 80/sec and 200/sec


organism: Thermovibrio ammonificans


organism: Trachurus trachurus

substrate_name: Unknown

ki_unit: mM

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Trematomus bernacchii


organism: Mus musculus

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


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8.3; 293.15 K; buffer 20 mM Tris-HCl

proof_lines: at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl

proof_lines: isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl


organism: Mytilus galloprovincialis

proof_lines: CO2 hydration, pH 8.3, 22°C, native enzyme

proof_lines: CO2 hydration, pH 8.3, 22°C, recombinant enzyme


organism: Nakaseomyces glabratus

substrate_name: histamine

assay_conditions_summary: pH 8.3; 298.15 K; buffer 20 mM Tris

proof_lines: at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine

substrate: histamine


organism: Neisseria gonorrhoeae


proof_lines:
pH 6.7, 25°C
purified recombinant enzyme


organism: Plasmodium falciparum

mutation_signature: truncated form PfCA1 / truncated form PfCA1

mutation_type: truncation

proof_lines: pH 7.5, 22°C, truncated form PfCA1, CO2 hydration reaction


organism: Populus tremula

assay_conditions_summary: pH 6.6; buffer and pH 8

proof_lines:
pH 6.6, MES buffer
pH 8.8, TAPS buffer


organism: Porphyromonas gingivalis

proof_lines: pH 8.3, 22°C, recombinant His-tagged enzyme


organism: Pseudoalteromonas haloplanktis ANT/505

proof_lines: pH 8.3, 20°C, inhibition of CO2 hydration activity


organism: Python bivittatus

proof_lines: pH not specified in the publication, 4°C, assay using the delta pH method


organism: Rattus norvegicus

proof_lines: 25°C, pH 7.0, low activity carbonic anhydrase

proof_lines: 0°C, pH 7.0, high activity carbonic anhydrase


organism: Methanosarcina thermophila

mutation_type: substitution

proof_lines: pH 7.5, 25°C, variant E62H, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E89A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84Y, 50 mM MOPS buffer


proof_lines: pH 7.5, 37°C, variant R59M, without guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59M, 100 mM guanidine hydrochloride


proof_lines: pH 7.5, 25°C, variant E84S, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84S and E84Y, 50 mM MOPS buffer


organism: Trichomonas vaginalis

proof_lines:
at pH 7.5 and 20°C
at pH 7.5 and 25°C
Ki above 0.01 mM, at pH 7.5 and 20°C


organism: Trypanosoma cruzi


organism: Vibrio cholerae serotype O1


organism: Struthio camelus


organism: Sulfurihydrogenibium azorense

proof_lines: pH 7.5, 20°C, recombinant His-tagged enzyme


organism: Sulfurihydrogenibium sp. YO3AOP1


organism: Sulfurihydrogenibium yellowstonense


organism: Sus scrofa


organism: Synechocystis sp. PCC 6803 / Kazusa

mutation_signature: recombinant truncated CcaA220 enzyme / CO2 hydration reaction recombinant truncated CcaA220 enzyme

proof_lines: recombinant truncated CcaA220 enzyme, pH 9.5, 25°C, CO2 hydration reaction


organism: Rhodospirillum rubrum


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8.3; 293.15 K; buffer and 20 mM NaClO4

proof_lines: at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-

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


organism: Salmo labrax

proof_lines: pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity


organism: Salmo trutta Labrax Coruhensis


organism: Sander vitreus


organism: Sordaria macrospora

proof_lines:
20°C, pH 8.3
value above, 20°C, pH 8.3


enzyme_display_name: beta-lactamase

organism: Bacillus cereus

substrate_name: Nitrocefin

source_db: oed

protein_accession_database: UniProt

enzyme: beta-lactamase

substrate: Nitrocefin

source: oed


organism: Citrobacter freundii

substrate_name: Cephalothin

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

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

substrate: Cephalothin


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


organism: Enterobacter aerogenes


organism: Escherichia coli

substrate_name: piperacillin

verification_status: corrected

kcat_over_km_origin: calculated

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

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

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

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

row_label: Piperacillin / TEMpUC19

data_origin: experimental

substrate: piperacillin

status: corrected


substrate_name: Penicillin G

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R164N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: Penicillin G

status: unverified


substrate_name: Ceftazidime

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

substrate: Ceftazidime


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: Cephalosporin C

verification_status: verified

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

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

row_label: Cephalosporin C / TEMpUC19

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

substrate: Cephalosporin C

status: verified


substrate_name: Ampicillin

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P62593 and applied mutation signature R164S with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 295.15 K; buffer full are run in 100 mM sodium phosphate

column_label: Table II (Kinetics parameters of TEMpUC19 and mutant derivatives), substrate block 'Ampicillin', b-lactamase row 'R164S'; column 'kcat (s^-1)' = 15; column 'Km (uM)' = 37; column 'kcat/Km (M^-1 s^-1)' = 4.2 x 10^5.

normalized_value_unit_evidence: kcat: printed Table II cell 15 in a column headed kcat (s^-1); s^-1 is already the canonical unit, so no unit conversion applies and the value is 15 s^(-1). Km: printed Table II cell 37 in a column headed Km (uM); 1 uM is 1/1000 mM, so 37 / 1000 = 0.037 mM. kcat/Km: printed Table II cell 4.2 x 10^5 in a column headed kcat/Km (M^-1 s^-1), that is 420000 s^(-1)*M^(-1); 1 M^(-1) is 1/1000 mM^(-1), so 420000 / 1000 = 420 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, substrate block Ampicillin, b-lactamase row R164S: kcat = 15 s^-1; Km = 37 uM; printed kcat/Km = 4.2 x 10^5 M^-1 s^-1. The number printed after the plus-or-minus glyph beside each cell is the fit error and is not an exported metric.

table_label: Table II: Kinetics parameters of TEMpUC19 and mutant derivatives (J. Biol. Chem. 1999, 274(33):23052-23060). Printed column heads: Substrate; b-Lactamase; kcat (s^-1); Km (uM); kcat/Km (M^-1 s^-1)

substrate: Ampicillin


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


organism: Klebsiella pneumoniae

substrate_name: H2O; Ampicillin

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

substrate: H2O; Ampicillin


organism: Kluyvera ascorbata

substrate_name: H2O; Nitrocefin

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

substrate: H2O; Nitrocefin


organism: Nocardia asteroides

substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


organism: Serratia marcescens

substrate_name: ampicillin

assay_conditions_summary: pH 7; 303.15 K; buffer and temperature fragments

proof_lines: at 30°C in 50 mM sodium phosphate buffer (pH 7.0)

substrate: ampicillin


organism: Bacillus licheniformis

substrate_name: Penicillin V; H2O

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

substrate: Penicillin V; H2O


organism: Stenotrophomonas maltophilia

substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S224D

substrate: Nitrocefin; H2O


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


substrate_name: Biapenem

substrate: Biapenem


organism: Pseudomonas aeruginosa

substrate_name: amoxicillin (at pH 7.0 and 37 degrees Celsius)

source_db: uniprot

source: uniprot


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


organism: Pseudomonas fluorescens

substrate_name: nitrocefin

substrate: nitrocefin


organism: Chryseobacterium indologenes

substrate_name: cefazolin

assay_conditions_summary: pH 6.5; buffer condition (not an identity anchor

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

substrate: cefazolin


substrate_name: Ampicillin; H2O / Carbenicillin; H2O / H2O; Penicillin G / Oxacillin; H2O / Cephaloridin; H2O / Substituted beta-amino acid

sequence_source: UniProtKB/Swiss-Prot P14488


substrate_name: H2O; 6-Aminopenicillanate

substrate: H2O; 6-Aminopenicillanate


enzyme_display_name: Metallo-beta-lactamase type 2

organism: Bacteroides fragilis

substrate_name: mixed substrate rows

enzyme: Metallo-beta-lactamase type 2

substrate: mixed substrate rows


organism: Klebsiella oxytoca

substrate_name: Penicillin G


substrate_name: H2O; Imipenem

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L209F to reconstruct the assayed variant sequence.

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

substrate: H2O; Imipenem


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


substrate_name: penicillin G

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

substrate: penicillin G


substrate_name: imipenem

source_db: skid

source_license: CC BY-NC-ND 4.0

substrate: imipenem

source: skid


organism: Morganella morganii

substrate_name: Ampicillin/imipenem/cephalothin bundle

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

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

substrate: Ampicillin/imipenem/cephalothin bundle


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


assay_conditions_summary: pH 6.5; buffer text (30 mM sodium cacodylate buffer


substrate_name: Imipenem

assay_conditions_summary: pH 7; 298.15 K; buffer / temperature / Km context

proof_lines: Km above 1.0 mM, in 0.01 M phosphate buffer (pH 7.0), at 25°C

substrate: Imipenem


organism: Achromobacter sp. sallbros1

substrate_name: Piperacillin

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

column_label: Table label: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1. Row: Piperacillin. Enzyme column group: TMB-1. Columns read: k cat (s^-1) cell 3.3, K m (uM) cell 72, k cat / K m (s^-1/uM) cell 0.046. metric: kcat; raw value: 3.3; raw unit: s^-1; normalized value: 3.3 s^(-1); metric: Km; raw value: 72; raw unit: uM; normalized value: 0.072 mM; metric: kcat/Km; raw value: 0.046; raw unit: s^-1/uM; normalized value: 46 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified TMB-1 metallo-beta-lactamase; steady-state kinetics were performed at 25 degrees C in a spectrophotometer using 96-well plates; all substrates were tested as duplicates using 50 mM HEPES buffer, pH 7.2, 100 uM ZnCl2, 0.02% NaN3, and 0.1 mg/ml bovine serum albumin as a buffer system. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: TMB-1 columns of Table 2 row Piperacillin: kcat 3.3 s^-1 = 3.3 s^(-1); Km 72 uM = 0.072 mM (1 uM = 0.001 mM); kcat/Km primary cell 0.046 s^-1/uM = 46 s^-1 mM^-1 (1 s^-1/uM = 1000 s^-1 mM^-1). In the table asset the micro sign renders as μ, the superscript minus one as −1, and superscript markers are flattened, so the printed header cells read `k cat (s −1 )`, `K m (μM)` and `k cat / K m (s −1 /μM)`.

raw_value_unit_evidence: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1 | enzyme column group header row of Table 2: TMB-1 DIM-1 a GIM-1 b; metric header row: k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) | row: Piperacillin 3.3 72 0.046 NR NR NR 6.9 69 0.1 | TMB-1 cells read: k cat = 3.3 s^-1; K m = 72 uM; k cat / K m = 0.046 s^-1/uM

row_label: TMB-1 | Piperacillin

substrate: Piperacillin


substrate_name: Cefoxitin

column_label: Table label: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1. Row: Cefoxitin. Enzyme column group: TMB-1. Columns read: k cat (s^-1) cell 0.3, K m (uM) cell 69, k cat / K m (s^-1/uM) cell 0.004. metric: kcat; raw value: 0.3; raw unit: s^-1; normalized value: 0.3 s^(-1); metric: Km; raw value: 69; raw unit: uM; normalized value: 0.069 mM; metric: kcat/Km; raw value: 0.004; raw unit: s^-1/uM; normalized value: 4 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified TMB-1 metallo-beta-lactamase; steady-state kinetics were performed at 25 degrees C in a spectrophotometer using 96-well plates; all substrates were tested as duplicates using 50 mM HEPES buffer, pH 7.2, 100 uM ZnCl2, 0.02% NaN3, and 0.1 mg/ml bovine serum albumin as a buffer system. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: TMB-1 columns of Table 2 row Cefoxitin: kcat 0.3 s^-1 = 0.3 s^(-1); Km 69 uM = 0.069 mM (1 uM = 0.001 mM); kcat/Km primary cell 0.004 s^-1/uM = 4 s^-1 mM^-1 (1 s^-1/uM = 1000 s^-1 mM^-1). In the table asset the micro sign renders as μ, the superscript minus one as −1, and superscript markers are flattened, so the printed header cells read `k cat (s −1 )`, `K m (μM)` and `k cat / K m (s −1 /μM)`.

raw_value_unit_evidence: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1 | enzyme column group header row of Table 2: TMB-1 DIM-1 a GIM-1 b; metric header row: k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) | row: Cefoxitin 0.3 69 0.004 8 20 0.4 8.3 206 0.04 | TMB-1 cells read: k cat = 0.3 s^-1; K m = 69 uM; k cat / K m = 0.004 s^-1/uM

row_label: TMB-1 | Cefoxitin

substrate: Cefoxitin


substrate_name: Ceftazidime

column_label: Table label: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1. Row: Ceftazidime. Enzyme column group: TMB-1. Columns read: k cat (s^-1) cell 0.07, K m (uM) cell 31, k cat / K m (s^-1/uM) cell 0.002. metric: kcat; raw value: 0.07; raw unit: s^-1; normalized value: 0.07 s^(-1); metric: Km; raw value: 31; raw unit: uM; normalized value: 0.031 mM; metric: kcat/Km; raw value: 0.002; raw unit: s^-1/uM; normalized value: 2 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified TMB-1 metallo-beta-lactamase; steady-state kinetics were performed at 25 degrees C in a spectrophotometer using 96-well plates; all substrates were tested as duplicates using 50 mM HEPES buffer, pH 7.2, 100 uM ZnCl2, 0.02% NaN3, and 0.1 mg/ml bovine serum albumin as a buffer system. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: TMB-1 columns of Table 2 row Ceftazidime: kcat 0.07 s^-1 = 0.07 s^(-1); Km 31 uM = 0.031 mM (1 uM = 0.001 mM); kcat/Km primary cell 0.002 s^-1/uM = 2 s^-1 mM^-1 (1 s^-1/uM = 1000 s^-1 mM^-1). In the table asset the micro sign renders as μ, the superscript minus one as −1, and superscript markers are flattened, so the printed header cells read `k cat (s −1 )`, `K m (μM)` and `k cat / K m (s −1 /μM)`.

raw_value_unit_evidence: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1 | enzyme column group header row of Table 2: TMB-1 DIM-1 a GIM-1 b; metric header row: k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) | row: Ceftazidime 0.07 31 0.002 3 50 0.06 18 31 0.58 | TMB-1 cells read: k cat = 0.07 s^-1; K m = 31 uM; k cat / K m = 0.002 s^-1/uM

row_label: TMB-1 | Ceftazidime

substrate: Ceftazidime


substrate_name: Meropenem

column_label: Table label: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1. Row: Meropenem. Enzyme column group: TMB-1. Columns read: k cat (s^-1) cell 1.4, K m (uM) cell 75, k cat / K m (s^-1/uM) cell 0.019. metric: kcat; raw value: 1.4; raw unit: s^-1; normalized value: 1.4 s^(-1); metric: Km; raw value: 75; raw unit: uM; normalized value: 0.075 mM; metric: kcat/Km; raw value: 0.019; raw unit: s^-1/uM; normalized value: 19 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified TMB-1 metallo-beta-lactamase; steady-state kinetics were performed at 25 degrees C in a spectrophotometer using 96-well plates; all substrates were tested as duplicates using 50 mM HEPES buffer, pH 7.2, 100 uM ZnCl2, 0.02% NaN3, and 0.1 mg/ml bovine serum albumin as a buffer system. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: TMB-1 columns of Table 2 row Meropenem: kcat 1.4 s^-1 = 1.4 s^(-1); Km 75 uM = 0.075 mM (1 uM = 0.001 mM); kcat/Km primary cell 0.019 s^-1/uM = 19 s^-1 mM^-1 (1 s^-1/uM = 1000 s^-1 mM^-1). In the table asset the micro sign renders as μ, the superscript minus one as −1, and superscript markers are flattened, so the printed header cells read `k cat (s −1 )`, `K m (μM)` and `k cat / K m (s −1 /μM)`.

raw_value_unit_evidence: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1 | enzyme column group header row of Table 2: TMB-1 DIM-1 a GIM-1 b; metric header row: k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) | row: Meropenem 1.4 75 0.019 50 10 5 2.7 25 0.108 | TMB-1 cells read: k cat = 1.4 s^-1; K m = 75 uM; k cat / K m = 0.019 s^-1/uM

row_label: TMB-1 | Meropenem

substrate: Meropenem


substrate_name: Ertapenem

column_label: Table label: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1. Row: Ertapenem. Enzyme column group: TMB-1. Columns read: k cat (s^-1) cell 0.4, K m (uM) cell 31, k cat / K m (s^-1/uM) cell 0.013. metric: kcat; raw value: 0.4; raw unit: s^-1; normalized value: 0.4 s^(-1); metric: Km; raw value: 31; raw unit: uM; normalized value: 0.031 mM; metric: kcat/Km; raw value: 0.013; raw unit: s^-1/uM; normalized value: 13 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified TMB-1 metallo-beta-lactamase; steady-state kinetics were performed at 25 degrees C in a spectrophotometer using 96-well plates; all substrates were tested as duplicates using 50 mM HEPES buffer, pH 7.2, 100 uM ZnCl2, 0.02% NaN3, and 0.1 mg/ml bovine serum albumin as a buffer system. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: TMB-1 columns of Table 2 row Ertapenem: kcat 0.4 s^-1 = 0.4 s^(-1); Km 31 uM = 0.031 mM (1 uM = 0.001 mM); kcat/Km primary cell 0.013 s^-1/uM = 13 s^-1 mM^-1 (1 s^-1/uM = 1000 s^-1 mM^-1). In the table asset the micro sign renders as μ, the superscript minus one as −1, and superscript markers are flattened, so the printed header cells read `k cat (s −1 )`, `K m (μM)` and `k cat / K m (s −1 /μM)`.

raw_value_unit_evidence: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1 | enzyme column group header row of Table 2: TMB-1 DIM-1 a GIM-1 b; metric header row: k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) | row: Ertapenem 0.4 31 0.013 NR NR NR NR NR NR | TMB-1 cells read: k cat = 0.4 s^-1; K m = 31 uM; k cat / K m = 0.013 s^-1/uM

row_label: TMB-1 | Ertapenem

substrate: Ertapenem


substrate_name: Cefuroxime

column_label: Table label: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1. Row: Cefuroxime. Enzyme column group: TMB-1. Columns read: k cat (s^-1) cell 0.1, K m (uM) cell 9, k cat / K m (s^-1/uM) cell 0.011. metric: kcat; raw value: 0.1; raw unit: s^-1; normalized value: 0.1 s^(-1); metric: Km; raw value: 9; raw unit: uM; normalized value: 0.009 mM; metric: kcat/Km; raw value: 0.011; raw unit: s^-1/uM; normalized value: 11 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified TMB-1 metallo-beta-lactamase; steady-state kinetics were performed at 25 degrees C in a spectrophotometer using 96-well plates; all substrates were tested as duplicates using 50 mM HEPES buffer, pH 7.2, 100 uM ZnCl2, 0.02% NaN3, and 0.1 mg/ml bovine serum albumin as a buffer system. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: TMB-1 columns of Table 2 row Cefuroxime: kcat 0.1 s^-1 = 0.1 s^(-1); Km 9 uM = 0.009 mM (1 uM = 0.001 mM); kcat/Km primary cell 0.011 s^-1/uM = 11 s^-1 mM^-1 (1 s^-1/uM = 1000 s^-1 mM^-1). In the table asset the micro sign renders as μ, the superscript minus one as −1, and superscript markers are flattened, so the printed header cells read `k cat (s −1 )`, `K m (μM)` and `k cat / K m (s −1 /μM)`.

raw_value_unit_evidence: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1 | enzyme column group header row of Table 2: TMB-1 DIM-1 a GIM-1 b; metric header row: k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) | row: Cefuroxime 0.1 9 0.011 NR NR NR 5.9 7 0.843 | TMB-1 cells read: k cat = 0.1 s^-1; K m = 9 uM; k cat / K m = 0.011 s^-1/uM

row_label: TMB-1 | Cefuroxime

substrate: Cefuroxime


substrate_name: Ampicillin

column_label: Table label: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1. Row: Ampicillin. Enzyme column group: TMB-1. Columns read: k cat (s^-1) cell 3.3, K m (uM) cell 27, k cat / K m (s^-1/uM) cell 0.122. metric: kcat; raw value: 3.3; raw unit: s^-1; normalized value: 3.3 s^(-1); metric: Km; raw value: 27; raw unit: uM; normalized value: 0.027 mM; metric: kcat/Km; raw value: 0.122; raw unit: s^-1/uM; normalized value: 122 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified TMB-1 metallo-beta-lactamase; steady-state kinetics were performed at 25 degrees C in a spectrophotometer using 96-well plates; all substrates were tested as duplicates using 50 mM HEPES buffer, pH 7.2, 100 uM ZnCl2, 0.02% NaN3, and 0.1 mg/ml bovine serum albumin as a buffer system. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: TMB-1 columns of Table 2 row Ampicillin: kcat 3.3 s^-1 = 3.3 s^(-1); Km 27 uM = 0.027 mM (1 uM = 0.001 mM); kcat/Km primary cell 0.122 s^-1/uM = 122 s^-1 mM^-1 (1 s^-1/uM = 1000 s^-1 mM^-1). In the table asset the micro sign renders as μ, the superscript minus one as −1, and superscript markers are flattened, so the printed header cells read `k cat (s −1 )`, `K m (μM)` and `k cat / K m (s −1 /μM)`.

raw_value_unit_evidence: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1 | enzyme column group header row of Table 2: TMB-1 DIM-1 a GIM-1 b; metric header row: k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) | row: Ampicillin 3.3 27 0.122 20 110 0.182 3.3 20 0.165 | TMB-1 cells read: k cat = 3.3 s^-1; K m = 27 uM; k cat / K m = 0.122 s^-1/uM

row_label: TMB-1 | Ampicillin

substrate: Ampicillin


organism: Aeromonas hydrophila

substrate_name: H2O; HRE-664; H2O; HRE-664; Substituted beta-amino acid; H2O; CP-65207; CP-65207; H2O; CGP-31608A; CGP-31608A; H2O; Sulbenicillin; Sulbenicillin; H2O; Piperacillin; Piperacillin

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


organism: Aliivibrio salmonicida

column_label: Table 1 (Comparison of kcat, KM and catalytic efficiency for ALI-1, IMP-1 and VIM-2), row 'Imipenem', ALI-1 columns: 'kcat (s^-1)' = 8.0; 'KM (uM)' = 933; 'kcat/KM (uM^-1 s^-1)' = 0.0085. The Km and efficiency column headers are printed with the Greek letter mu for micromolar; pdftotext renders that glyph as a plain 'm', so the printed text shows 'KM (mM)' and 'kcat/KM (mM^-1 s^-1)', but the true printed unit, confirmed against a rendered page image, is micromolar (uM / uM^-1 s^-1).

normalized_value_unit_evidence: kcat: printed Table 1 cell 8.0 s^-1; already in s^-1, no conversion needed; normalized value 8.0 s^(-1). Km: printed Table 1 cell 933 uM; 933 / 1000 = 0.933 mM; normalized value 0.933 mM. kcat/Km: printed Table 1 cell 0.0085 uM^-1 s^-1 (same micromolar unit); 0.0085 * 1000 = 8.5 s^-1 mM^-1. This printed efficiency cell is the paper's own independently fitted value for this row and condition, carried forward as-is; it is a separate figure from the quotient of the row's own kcat and Km cells (8.0 / 0.933 = 8.5744908896034 s^-1 mM^-1).

raw_value_unit_evidence: Table 1, ALI-1 columns, row 'Imipenem': kcat = 8.0 s^-1; KM = 933 (column head prints the Greek mu for micromolar, rendered here as 'm'; true unit uM); printed kcat/KM = 0.0085 uM^-1 s^-1 (same micromolar-based ratio unit).

row_label: Table 1, row 'Imipenem' (ALI-1 columns)

table_label: Table 1: Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-1 and VIM-2 (J Antimicrob Chemother 2015, 70(3):766-772)


enzyme_display_name: Beta-lactamase

organism: Citrobacter diversus

substrate_name: Cephalosporin C

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

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

row_label: Form I; Cephalosporin C

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

enzyme: Beta-lactamase

substrate: Cephalosporin C


organism: Escherichia coli

substrate_name: H2O; Cephalosporin C

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

substrate: H2O; Cephalosporin C


organism: Klebsiella pneumoniae

substrate_name: ceftaxidime

substrate: ceftaxidime


substrate_name: temocillin

substrate: temocillin


organism: Klebsiella pneumoniae subsp. ozaenae

substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


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


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

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


organism: Kluyvera ascorbata

substrate_name: Nitrocefin

substrate: Nitrocefin


organism: Serratia fonticola

sequence_source: UniProtKB unreviewed entry Q9RMI1

column_label: Official PMC Table 1 row Nitrocefin Sfh-I columns: kcat=0.06 +/- 0.003 s^-1, Km=106 +/- 13.4 uM, kcat/Km=5.7 x 10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat 0.06 s^-1; Km 0.106 mM; primary table kcat/Km 0.57 s^-1 mM^-1. Exported kcat/Km 0.5660377358490566 s^-1 mM^-1 is consistent with table significant-figure rounding/computation from displayed kcat and Km.

row_label: Nitrocefin

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


substrate_name: H2O; Biapenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120C

substrate: H2O; Biapenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120S


substrate_name: cefazolin

assay_conditions_summary: pH 6.5; buffer note

substrate: cefazolin


organism: Treponema pallidum

substrate_name: Cloxacillin

substrate: Cloxacillin


substrate_name: carbenicillin

substrate: carbenicillin


substrate_name: cefotaxime

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

substrate: cefotaxime


substrate_name: Penicillin G

substrate: Penicillin G


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


organism: Enterobacter cloacae

substrate_name: Penicillin G / Amoxicillin / Ticarcillin / Cephalothin / Cefotaxime


substrate_name: Ampicillin

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


substrate_name: H2O; Ampicillin

substrate: H2O; Ampicillin


organism: Proteus mirabilis


organism: Providencia stuartii


organism: Pseudomonas aeruginosa

substrate_name: H2O; Carbenicillin

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

substrate: H2O; Carbenicillin


substrate_name: Imipenem

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

substrate: Imipenem


mutation_type: deletion

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


organism: Serratia marcescens

substrate_name: Cephaloridine; H2O

substrate: Cephaloridine; H2O


organism: Brachyspira pilosicoli

assay_conditions_summary: pH 7; 298.15 K; buffer note

proof_lines: at 25°C in 100 mM sodium phosphate (pH 7.0)


organism: Psychrobacter immobilis

substrate_name: ampicillin

assay_conditions_summary: pH 7; 303.15 K; buffer sodium phosphate

proof_lines: at 30°C in 50mM sodium phosphate buffer (pH 7.0)

substrate: ampicillin


substrate_name: Ampicillin / Penicillin G / Oxacillin

substrate: Ampicillin / Penicillin G / Oxacillin


substrate_name: nitrocefin

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

table_label: Table 3

substrate: nitrocefin


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: Bacillus licheniformis


organism: Citrobacter freundii

substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


organism: Enterobacter aerogenes


substrate_name: Cephalosporin C

substrate: Cephalosporin C


substrate_name: cefepime

substrate: cefepime


substrate_name: Aztreonam; H2O

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

substrate: Aztreonam; H2O


substrate_name: 6-beta-Iodopenicillanic acid; H2O

sequence_variant_note: Mutation signature T316V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

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

substrate: 6-beta-Iodopenicillanic acid; H2O


substrate_name: Cefuroxime; H2O

substrate: Cefuroxime; H2O


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


substrate_name: Ampicillin; H2O

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

substrate: Ampicillin; H2O


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


substrate_name: Cephalothin; H2O

substrate: Cephalothin; H2O


sequence_variant_note: Mutation signature K161A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

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


substrate_name: H2O; Cephalothin

sequence_variant_note: Mutation signature K161E could not be applied safely because the resolved sequence does not match the expected reference residue(s).

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

substrate: H2O; Cephalothin


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N167A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

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


sequence_variant_note: Mutation signature N167D matches the mutant residue at offset -7 and the reference residue at offset -6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

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


substrate_name: ceftazidime

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

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

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

row_label: VIM-1 / Ceftazidime

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

substrate: ceftazidime


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

assay_conditions_summary: pH 7

proof_lines: kcat is 123 sec(-1) with imipenem as substrate (at pH 7.4 and 30 degrees Celsius) (PubMed:15788415). kcat is 127 sec(-1) with imipenem as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:10898670). kcat is 162 sec(-1) with ampicillin as


organism: Streptomyces cacaoi

substrate_name: benzylpenicillin

substrate: benzylpenicillin


organism: Streptomyces sp.


organism: synthetic construct

substrate_name: cephalothin

substrate: cephalothin


organism: Yersinia enterocolitica

substrate_name: cefalotin

substrate: cefalotin


organism: Yersinia ruckeri

substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Cephaloridine

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

substrate: Cephaloridine


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant A164S


organism: Citrobacter diversus

substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


organism: Morganella morganii

substrate_name: H2O; Ampicillin

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

substrate: H2O; Ampicillin


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


organism: Nocardia asteroides


organism: Nocardia farcinica

substrate_name: Nitrocefin

unit: Mswedgeone

substrate: Nitrocefin


organism: Ochrobactrum anthropi

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


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


organism: Proteus mirabilis


enzyme_display_name: pyruvate kinase

organism: Homo sapiens

substrate_name: ADP

enzyme: pyruvate kinase

substrate: ADP


substrate_name: Pyruvate; ATP

substrate: Pyruvate; ATP


organism: Lactococcus lactis subsp. cremoris

substrate_name: ADP; Phosphoenolpyruvate

substrate: ADP; Phosphoenolpyruvate


organism: Corynebacterium glutamicum


organism: Escherichia coli

substrate_name: Phosphoenolpyruvate; ADP

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K382Q

substrate: Phosphoenolpyruvate; ADP


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R431E


sequence_source: UniProt REST canonical sequence for P0AD61

assay_conditions_summary: cofactor ATP


organism: Lactococcus lactis subsp. lactis


organism: Leishmania mexicana


organism: Mus musculus

substrate_name: ATP; Pyruvate

substrate: ATP; Pyruvate


organism: Oryctolagus cuniculus


organism: Plasmodium falciparum


organism: Ustilago maydis


organism: Zymomonas mobilis


enzyme_display_name: purine-nucleoside phosphorylase

substrate_name: Inosine

enzyme: purine-nucleoside phosphorylase

substrate: Inosine


sequence_source: UniProt REST canonical sequence for P00491


organism: Bos taurus

substrate_name: Phosphate; Inosine

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

substrate: Phosphate; Inosine


organism: Cellulomonas sp.


substrate_name: guanosine

substrate: guanosine


substrate_name: adenosine

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=6.5

substrate: adenosine


organism: Helicobacter pylori


substrate_name: phosphate

smiles: O=P(O)(O)O

substrate: phosphate


substrate_name: Phosphate; Adenosine

substrate: Phosphate; Adenosine


substrate_name: Phosphate

substrate: Phosphate


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant R84A


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant F200A


substrate_name: Hypoxanthine

substrate: Hypoxanthine


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant K244A


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant E89A


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant H257A


substrate_name: Inosine; Phosphate

proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant T242A

substrate: Inosine; Phosphate


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant Y88F


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant S33A


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant F159A


organism: Aeropyrum pernix


organism: Aneurinibacillus migulanus

column_label: Table 2 row Inosine; columns Km (mol/L), Kcat (s^-1), and Kcat/Km (s^-1 M^-1) report 5.30 x 10^-3, 6.38 x 10^4, and 1.21 x 10^7.

normalized_value_unit_evidence: Km normalized_value=5.3 normalized_unit=mM; kcat normalized_value=63800 normalized_unit=s^-1; kcat/Km normalized_value=12100 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=5.30 x 10^-3 raw_unit=mol/L; kcat raw_value=6.38 x 10^4 raw_unit=s^-1; kcat/Km raw_value=1.21 x 10^7 raw_unit=s^-1 M^-1

row_label: Inosine

table_label: Table 2: Kinetic parameters for AmPNP with various purine nucleosides


column_label: Table 2 row Guanosine; columns Km (mol/L), Kcat (s^-1), and Kcat/Km (s^-1 M^-1) report 1.16 x 10^-3, 1.84 x 10^4, and 1.58 x 10^7.

normalized_value_unit_evidence: Km normalized_value=1.16 normalized_unit=mM; kcat normalized_value=18400 normalized_unit=s^-1; kcat/Km normalized_value=15800 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=1.16 x 10^-3 raw_unit=mol/L; kcat raw_value=1.84 x 10^4 raw_unit=s^-1; kcat/Km raw_value=1.58 x 10^7 raw_unit=s^-1 M^-1

row_label: Guanosine


column_label: Table 2 row Adenosine; columns Km (mol/L), Kcat (s^-1), and Kcat/Km (s^-1 M^-1) report 1.45 x 10^-3, 1.43 x 10^1, and 9.92 x 10^3.

normalized_value_unit_evidence: Km normalized_value=1.45 normalized_unit=mM; kcat normalized_value=14.3 normalized_unit=s^-1; kcat/Km normalized_value=9.92 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=1.45 x 10^-3 raw_unit=mol/L; kcat raw_value=1.43 x 10^1 raw_unit=s^-1; kcat/Km raw_value=9.92 x 10^3 raw_unit=s^-1 M^-1

row_label: Adenosine


organism: Anopheles gambiae


organism: Bacillus subtilis


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant V181D


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant M183L


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


organism: Pseudoalteromonas sp.


organism: Homo sapiens


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant M219A


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant E201A


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant H86A


proof_lines: SABIO-RK modifier species: purine-nucleoside phosphorylase(Enzyme) mutant N243A


organism: Kluyveromyces lactis


substrate_name: Xanthosine

substrate: Xanthosine


organism: Pyrococcus furiosus

substrate_name: Adenosine; Phosphate

substrate: Adenosine; Phosphate


organism: Salmonella typhimurium


organism: Thermus thermophilus


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=25°C, pH=7.4


enzyme_display_name: fructose-bisphosphate aldolase

organism: Bacillus methanolicus

substrate_name: glycerone phosphate

smiles: O=C(CO)COP(=O)(O)O

enzyme: fructose-bisphosphate aldolase

substrate: glycerone phosphate


substrate_name: D-Fructose 1,6-bisphosphate

substrate: D-Fructose 1,6-bisphosphate


substrate_name: D-Glyceraldehyde 3-phosphate

substrate: D-Glyceraldehyde 3-phosphate


substrate_name: D-fructose 1,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


organism: Cyanophora paradoxa


organism: Escherichia coli


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant S61T


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant Q59A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant K325A


organism: Drosophila melanogaster


organism: Edwardsiella ictaluri


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant 1-44F2

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant 2-15B2

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant 3-4C10


organism: Entamoeba histolytica

substrate_name: Glycerone phosphate; D-Glyceraldehyde 3-phosphate


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant Q59A/F67H


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant G64T


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant Q59A/S61T/D288A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant S61A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant S61T/G64T/F67H


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant N35A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant E174A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant E181A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant D329A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant N286A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant N286D


organism: Anoxybacillus gonensis

assay_conditions_summary: pH 8.5; buffer 50 mM Tris-HCl

column_label: Enzyme kinetics section and Fig. 9, metric labels Km and Vmax, row/segment A. gonensis G2 FBP aldolase toward FBP, cells 567 uM and 2.4 uM min^-1 mg protein^-1.

raw_value_unit_evidence: Enzyme kinetics prose/Fig. 9 reports Km = 567 uM and Vmax = 2.4 uM min^-1 mg protein^-1 for A. gonensis G2 FBP aldolase toward FBP.

row_label: A. gonensis G2 FBP aldolase toward FBP

table_label: Enzyme kinetics prose and Fig. 9 Lineweaver-Burk plot


organism: Arabidopsis thaliana


substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant F67H


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant Q59A/G64T/F67H


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant D109A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant D288A


organism: Euglena gracilis


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant D144A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant D290A


enzyme_display_name: uridine phosphorylase

column_label: PMC3346467 HTML lines 1814-1843 define Table 5 columns and units; lines 1860-1863 give row dGuo under TtPNPI: Km 1.01 +/- 0.03 mM, kcat 830 +/- 6 s^-1, kcat/Km 822.53.

normalized_value_unit_evidence: Km 1.01 mM; kcat 830 s^-1; kcat/Km 822.53 s^-1*mM^-1 from the primary Table 5 dGuo row. Exported kcat/Km is 821.7821782178218 s^-1*mM^-1 and does not exactly equal the primary paper value.

raw_value_unit_evidence: Table 5 dGuo row under TtPNPI: Km 1.01 +/- 0.03 mM; kcat 830 +/- 6 s^-1; kcat/Km 822.53.

row_label: dGuo under TtPNPI

table_label: Table 5: Kinetic parameters of NPs

enzyme: uridine phosphorylase


substrate_name: Inosine

column_label: PMC3346467 HTML lines 1814-1843 define Table 5 columns and units; lines 1872-1875 give row Ino under TtPNPI: Km 2.08 +/- 0.02 mM, kcat 173 +/- 2 s^-1, kcat/Km 83.20.

normalized_value_unit_evidence: Km 2.08 mM; kcat 173 s^-1; kcat/Km 83.20 s^-1*mM^-1 from the primary Table 5 Ino row. Exported kcat/Km is 83.17307692307692 s^-1*mM^-1 and does not exactly equal the primary paper value.

raw_value_unit_evidence: Table 5 Ino row under TtPNPI: Km 2.08 +/- 0.02 mM; kcat 173 +/- 2 s^-1; kcat/Km 83.20.

row_label: Ino under TtPNPI


organism: Toxoplasma gondii


substrate_name: D-Fructose 1-phosphate

substrate: D-Fructose 1-phosphate


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant aldolase B L256P


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant aldolase B W147R


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant aldolase B R303W


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant LOOP (G176A, G179A, G180A, G184A)


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant E182A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant H142A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant C112A


sequence_source: UniProt REST canonical sequence for P0A991

column_label: Table 3; Class I FBP aldolase row; FBP plus citrate columns; Km (mM) and kcat (min^-1) columns; kcat converted from min^-1 to s^-1. kcat/Km is calculated from the same table row where required.

raw_value_unit_evidence: Table 3 Class I FBP aldolase row; FBP plus citrate columns: Km 0.07 +/- 0.012 mM; kcat 190 +/- 9.5 min^-1.

table_label: PMID 9531482 / DOI 10.1042/bj3310437, Table 3: FBP-cleavage kinetics of the wild-type and mutant E. coli FBP aldolases


column_label: Table 3; Class I FBP aldolase row; F1P minus citrate columns; Km (mM) and kcat (min^-1) columns; kcat converted from min^-1 to s^-1. kcat/Km is calculated from the same table row where required.

raw_value_unit_evidence: Table 3 Class I FBP aldolase row; F1P minus citrate columns: Km 33 +/- 6 mM; kcat 7 +/- 0.8 min^-1.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt REST canonical sequence for P0A991 and explicit K239A mutagenesis annotation and applied mutation signature K239A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant K239A


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt REST canonical sequence for P0A991 and explicit K237A mutagenesis annotation and applied mutation signature K237A to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProt REST canonical sequence for P0A991 and explicit K239A mutagenesis annotation


sequence_source: Reconstructed from UniProt REST canonical sequence for P0A991 and explicit K237A mutagenesis annotation

assay_conditions_summary: pH 8

column_label: Table 3 FBP plus citrate columns Km (mM) and kcat (min^-1); this SABIO row only requires kcat and Km.

normalized_value_unit_evidence: Km 0.06 mM and kcat 0.008666667 s^-1 after dividing min^-1 by 60.

raw_value_unit_evidence: Table 3 row K237A mutant Class I FBP aldolase, FBP plus citrate columns report Km 0.06 +/- 0.02 mM and kcat 0.52 +/- 0.004 min^-1.

row_label: K237A mutant Class I FBP aldolase

table_label: Table 3: FBP-cleavage kinetics of the wild-type and mutant E. coli FBP aldolases


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


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


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant Y363S


organism: Lactococcus lactis subsp. cremoris


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q354E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3; row Q354E; FBP Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 3 values: Km=0.0091 mM; kcat=0.57 s^-1; printed kcat/Km=64 s^-1 mM^-1; exported kcat/Km=63.333333333333336 s^-1 mM^-1.

row_label: Q354E / FBP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P05062 and applied mutation signature N334K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3; row N334K; FBP Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 3 values: Km=0.0324 mM; kcat=0.19 s^-1; printed kcat/Km=6 s^-1 mM^-1; exported kcat/Km=5.9375 s^-1 mM^-1.

row_label: N334K / FBP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W147R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P05062 and applied mutation signature L256P with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3; row L256P; F1P Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 3 values: Km=1.73 mM; kcat=0.38 s^-1; printed kcat/Km=0.23 s^-1 mM^-1; exported kcat/Km=0.21965317919075145 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R303W with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3; row R303W; FBP Km, kcat, and kcat/Km columns; footnote says data from reference 8.

normalized_value_unit_evidence: normalized Table 3 values: Km=1.6 mM; kcat=0.08 s^-1; printed kcat/Km=0.052 s^-1 mM^-1; exported kcat/Km=0.049999999999999996 s^-1 mM^-1.

row_label: R303W / FBP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N334K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: ScienceDirect HTML Table 3 lists row N334K with Km FBP 32.4+/-2.0 uM and kcat FBP 0.19+/-0.05 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0324 normalized_unit=mM; kcat normalized_value=0.19 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=32.4+/-2.0 raw_unit=uM; kcat raw_value=0.19+/-0.05 raw_unit=s^-1

table_label: Table 3. Kinetic parameters of various recombinant human aldolase B mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R303Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: ScienceDirect HTML Table 3 lists row R303Q with Km FBP 147+/-15 uM and kcat FBP 0.39+/-0.04 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.147 normalized_unit=mM; kcat normalized_value=0.39 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=147+/-15 raw_unit=uM; kcat raw_value=0.39+/-0.04 raw_unit=s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P05062 and applied mutation signature R303Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3; row R303Q; F1P Km, kcat, and kcat/Km columns; footnote says data from reference 8.

normalized_value_unit_evidence: normalized Table 3 values: Km=57.5 mM; kcat=0.15 s^-1; printed kcat/Km=0.0026 s^-1 mM^-1; exported kcat/Km=0.002608695652173913 s^-1 mM^-1.


organism: Oryctolagus cuniculus

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant E189Q


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant E187A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant S271A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant K107M


organism: Lampetra japonica


organism: Leishmania mexicana


organism: Magnaporthe grisea 70-15


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D276A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WQA3 and applied mutation signature E169A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 295.15 K; cofactor NADH

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row E169A; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 0.40; column 'Km (uM)' = 18; column 'kcat/Km (uM-1 min-1)' = 0.017.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row E169A: kcat = 0.40 min^-1; Km = 18 uM; printed kcat/Km = 0.017 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row E169A

table_label: Table 2: Kinetic Parameters for MtFBA, panel A: Fructose 1,6-bisphosphate (H2O) (Biochemistry 2013, 52(5):912-925, author manuscript page 28)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WQA3 and applied mutation signature E168A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row E168A; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 160; column 'Km (uM)' = 30; column 'kcat/Km (uM-1 min-1)' = 5.3.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row E168A: kcat = 160 min^-1; Km = 30 uM; printed kcat/Km = 5.3 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row E168A


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

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row wt; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 720; column 'Km (uM)' = 40; column 'kcat/Km (uM-1 min-1)' = 18.

normalized_value_unit_evidence: Km: printed Table 2 panel A cell 40 uM; 1 uM is 1/1000 mM, so 40 / 1000 = 0.04 mM. kcat: printed Table 2 panel A cell 720 min^-1; the printed turnover column is per MINUTE, so 720 / 60 = 12.0 s^(-1). kcat/Km: printed Table 2 panel A cell 18 uM^-1 min^-1; 1 uM^-1 min^-1 is (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 18 x 16.666666666666668 = 300.0 s^(-1)*mM^(-1). Each of the three converted cells equals the value the catalog already carries.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row wt: kcat = 720 min^-1; Km = 40 uM; printed kcat/Km = 18 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row wt


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C72A/C239A/C289A/C338A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant C72A / C239A / C289A / C338A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E187Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant E187Q


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E189A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant E189A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant AB_NP (Y58F, V113A, H156Q, I182L, P262A, A296K, Y327F)


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant gBi (C239A, C289A)


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant AB_TSP (S38T, I39M, A40G, S45R, K311A, S353T, E354Q, I358T, S359A, H361Y)


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant AB_P (S38T, I39M, A40G, S45R, Q60E, P71Q, R91K, G102I, K311A, L320K, S353T, E354Q, I358T, S359A, H361Y)


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant Ald337 (pPB14 in pTYB1)

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant pQ125D

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant pD128N


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant AB_NPS (V113A, H156Q, P262A, A296K)


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant AB_NPB (Y58F, I182L, Y327F)


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant AB_DSP (Q60E, P71Q, R91K, G102I, L320K)


substrate_name: beta-D-Fructose 1,6-bisphosphate

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant D33S

substrate: beta-D-Fructose 1,6-bisphosphate


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant D33E


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant pD128N/R258Q


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant pQ125D/E224A


organism: Pisum sativum

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


organism: Giardia intestinalis


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


organism: Giardia lamblia


column_label: PMID 17166851 Expression and Characterization of glFBPA prose: kcat = 3.55 +/- 0.05 s^-1, Km = 1.7 +/- 0.1 uM, kcat/Km = 2.1 x 10^6 s^-1 M^-1.

row_label: glFBPA-catalyzed cleavage of FBP


organism: Halothece sp. PCC 7418

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.


organism: Helicobacter pylori


organism: Homo sapiens

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant aldolase B A337V


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant aldolase B A149P


column_label: PMID 16901716 kinetic characterization prose, FBP cleavage row/context, Km and kcat values.

raw_value_unit_evidence: Kinetic characterization prose reports Km = 51 +/- 1 uM and kcat = 45.7 +/- 0.4 s^-1.

row_label: recombinant Magnaporthe grisea FBA / fructose 1,6-bisphosphate

table_label: Kinetic characterization prose


organism: Methanocaldococcus jannaschii


organism: Mus musculus


proof_lines:
Raw SKiD Env: Temp=28°C, pH=7.3
Raw SKiD Env: Temp=22°C, pH=7.8
Raw SKiD Env: Temp=-----, pH=-----


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WQA3 and applied mutation signature G167A/G166A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row G167A, G166A; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 6.6; column 'Km (uM)' = 21; column 'kcat/Km (uM-1 min-1)' = 0.32.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row G167A, G166A: kcat = 6.6 min^-1; Km = 21 uM; printed kcat/Km = 0.32 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row G167A, G166A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WQA3 and applied mutation signature G167A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row G167A; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 10; column 'Km (uM)' = 21; column 'kcat/Km (uM-1 min-1)' = 0.48.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row G167A: kcat = 10 min^-1; Km = 21 uM; printed kcat/Km = 0.48 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row G167A


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


proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.6
Raw SKiD Env: Temp=30°C, pH=-----
Raw SKiD Env: Temp=-----, pH=-----


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant D33A


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant aldolase B Q354E


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant AP

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant Val337


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


proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant isozyme A Gly346->Ser

proof_lines: SABIO-RK modifier species: fructose-bisphosphate aldolase(Enzyme) mutant isozyme A Gln206->Lys


organism: Plasmodium falciparum


organism: Pyrococcus furiosus


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

column_label: Table 2; isoenzyme block FBA / Fba1p; row "FBA | Fba1p | kcat | 4.14 | 1.5 |  | s−1" column Value raw value 4.14 with column Unit s−1; row "FBA | Fba1p | Kf16bp | 0.451 | 5.3 | 0.3 | mM" column Value raw value 0.451 with column Unit mM. Both cells sit in the same Fba1p isoenzyme block of Table 2, so the kcat and Km cells are one tuple.

normalized_value_unit_evidence: kcat 4.14 s-1 normalizes to 4.14 s^-1. Kf16bp 0.451 mM normalizes to 0.451 mM. kcat/Km is not printed in Table 2, so paper kcat/Km = paper kcat / paper Km = 4.14 / 0.451 = 9.179600886917958 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 line "FBA | Fba1p | kcat | 4.14 | 1.5 |  | s−1" gives kcat 4.14 s−1. Table 2 line "FBA | Fba1p | Kf16bp | 0.451 | 5.3 | 0.3 | mM" gives Kf16bp 0.451 mM. Table 2 prints no kcat/Km or catalytic-efficiency column.

row_label: FBA / Fba1p

table_label: Table 2. Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]


organism: Spinacia oleracea


organism: Trypanosoma brucei


organism: Zea mays


organism: Sulfolobus solfataricus

substrate_name: D-Glyceraldehyde 3-phosphate; Glycerone phosphate


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; 321.15 K; cofactor NADPH

column_label: Table 1 (Activities of wild type and mutants of ST0318), FBPA (anabolic direction) block, row 'Wild type'; column 'kcat (s^-1)' = 0.91; column 'Km (mM)' = 0.19; column 'kcat/Km (s^-1 mM^-1)' = 4.7. The kcat and Km cells also print the standard deviations 0.04 and 0.02, which the export does not carry.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.91 s^-1; already in s^-1, so no unit conversion applies; the value carried forward is 0.91 s^(-1). Km: printed Table 1 cell 0.19 mM; already in mM, so no unit conversion applies; the value carried forward is 0.19 mM. kcat/Km: printed Table 1 cell 4.7 s^-1 mM^-1; already in s^-1 mM^-1, so no unit conversion applies; the value carried forward is 4.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, FBPA (anabolic direction) block, row 'Wild type': kcat = 0.91 s^-1; Km = 0.19 mM; printed kcat/Km = 4.7 s^-1 mM^-1.

table_label: Table 1: Activities of wild type and mutants of ST0318 (Nature 2011, 478:538-541)


row_label: Table 1, FBPA (anabolic direction) block, row 'Wild type'


organism: Synechocystis sp.


organism: Escherichia coli (strain K12)

substrate_name: phosphate (at 25 degrees Celsius and pH 7)


substrate_name: xanthosine (at pH 7.0)

substrate: xanthosine (at pH 7.0)


organism: Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34)

substrate_name: guanosine

substrate: guanosine


substrate_name: adenosine (for adenosine phosphorylase activity)


substrate_name: L-citrulline

substrate: L-citrulline


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: phosphate (at pH 7.1)

substrate: phosphate (at pH 7.1)


organism: Homo sapiens

substrate_name: phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0)

assay_conditions_summary: cofactor ADP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: phosphoenolpyruvate (with magnesium as divalent cation)


organism: Arabidopsis thaliana

substrate_name: fructose 1,6-bisphosphate

substrate: fructose 1,6-bisphosphate


substrate_name: fructose-bisphosphate for the cleavage reaction


organism: Caenorhabditis elegans

substrate_name: beta-D-fructose 1,6-bisphosphate

substrate: beta-D-fructose 1,6-bisphosphate


substrate_name: FBP

substrate: FBP


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

substrate_name: D-fructose 1,6-bisphosphate


substrate_name: fructose 1,6-bisphosphate (at 30 degrees Celsius)


organism: Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBP phosphatase activity, at 48 degrees Celsius)


organism: Oryctolagus cuniculus

substrate_name: fructose-l-phosphate

substrate: fructose-l-phosphate


organism: Plasmodium falciparum (isolate K1 / Thailand)

substrate_name: fructose 1,6-bisphosphate (at pH 7.3 and with native protein)


organism: Thermococcus kodakaraensis

substrate_name: D-Fructose 1,6-bisphosphate


organism: Thermoproteus tenax


organism: Thermus aquaticus


organism: Toxoplasma gondii


organism: Triticum aestivum


organism: Trypanosoma brucei

substrate_name: glycerone phosphate


substrate_name: D-Glyceraldehyde 3-phosphate


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: inosine

proof_lines: kcat is 84 sec(-1) with inosine as substrate (PubMed:17419725). kcat is 150 sec(-1) with inosine as substrate (PubMed:21683167). kcat is 28 sec(-1) with guanosine as substrate (PubMed:17419725). kcat is 0.15 sec(-1) with adenosine as substr

substrate: inosine


organism: Unknown prokaryotic organism

substrate_name: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (at pH 4.5 and 40 degrees Celsius)

proof_lines: kcat is 18 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 660 sec(-1) with syringaldazine as substrate. kcat is 1175 sec(-1) with 2,6-dimethoxyphenol as substrate (at pH 4.5 and 40 degrees Celsius).


organism: Anopheles gambiae

substrate_name: inosine (at 25 degrees Celsius and pH 7.4)

proof_lines: kcat is 41 sec(-1) with inosine as substrate (PubMed:17918964). kcat is 1 sec(-1) with guanosine as substrate (PubMed:17918964). kcat is 54 sec(-1) with 2-deoxyinosine as substrate (PubMed:17918964). kcat is 5.4 sec(-1) with 2-deoxyguanosin


organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

proof_lines: kcat is 13000 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 33300 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).

substrate: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (at pH 4.5 and 40 degrees Celsius)


organism: Escherichia coli (strain K12)

proof_lines: kcat is 1450 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 21720 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).


organism: Homo sapiens

substrate_name: inosine (at 30 degrees Celsius and pH 7)

proof_lines: kcat is 57 sec(-1) with inosine as substrate (PubMed:9305964). kcat is 47 sec(-1) with inosine as substrate (PubMed:23438750). kcat is 70 sec(-1) with hypoxanthine as substrate (PubMed:9305964). kcat is 28 sec(-1) with guanosine as substrat


organism: Plasmodium falciparum

proof_lines: kcat is 0.34 sec(-1) with inosine as substrate (PubMed:11707439). kcat is 0.14 sec(-1) with guanosine as substrate (PubMed:11707439). kcat is 0.64 sec(-1) with 2'-deoxyinosine as substrate (PubMed:11707439). kcat is 0.2 sec(-1) with 2'-deox

proof_lines: kcat is 1.7 sec(-1) with inosine as substrate (PubMed:14982926, PubMed:24416224). kcat is 2.63 sec(-1) with inosine as substrate (PubMed:29440412). kcat is 1.1 sec(-1) with guanosine as substrate (PubMed:19575810). kcat is 1.5 sec(-1) with


organism: Plasmodium vivax (strain Salvador I)

proof_lines: kcat is 1.2 sec(-1) with inosine as substrate (PubMed:19575810). kcat is 0.7 sec(-1) with guanosine as substrate (PubMed:19575810). kcat is 5.6 sec(-1) with 2'-deoxyinosine as substrate (PubMed:19575810). kcat is 0.7 sec(-1) with 2'-deoxygu


organism: Aeropyrum pernix

substrate_name: adenosine

substrate: adenosine


organism: Agaricus bisporus var. burnettii

substrate_name: Inosine

substrate: Inosine


organism: Aneurinibacillus migulanus


substrate_name: guanosine


organism: Bacillus cereus

proof_lines:
enzyme from vegetative cells
enzyme from spores


organism: Bacillus subtilis

proof_lines: isoform of 702 amino acids, pH 7.0, 37°C

proof_lines: isoform of 816 amino acids, pH 7.0, 37°C


organism: Bos taurus

proof_lines: about, pH 6.5, 25°C, recombinant mutant N243D

proof_lines: above, pH 6.5, 25°C, recombinant mutant N243D


organism: Cellulomonas sp.

proof_lines: 25°C, pH 7.0, cosubstrate: 7-methylguanosine


organism: Cricetulus griseus

substrate_name: hypoxanthine

substrate: hypoxanthine


organism: Enterobacter cloacae

substrate_name: phosphate

substrate: phosphate


organism: Escherichia coli

substrate_name: Inosine; Phosphate

proof_lines:
pH 7.4, 25°C
reaction with 7-methylinosine
37°C

substrate: Inosine; Phosphate


proof_lines: about, pH 6.5, 25°C, recombinant wild-type enzyme


organism: Cenarchaeum symbiosum (strain A)

proof_lines: The aldolase reaction is a classic case for a fully reversible enzymatic reaction but here, the KM values for the substrate for the aldol condensation and the aldol cleavage differ by a factor of 1000, and the intrinsic phosphatase activity

substrate: D-fructose 1,6-bisphosphate (when assaying the FBP phosphatase activity, at 48 degrees Celsius)


proof_lines: The catalytic efficiency measured with fructose-1,6-bisphosphate as substrate is 1440-fold higher than that with tagatose-1,6-bisphosphate.


organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6)

substrate_name: fructose 1,6-bisphosphate (at pH 7.5 and 25 degrees Celsius)

proof_lines: kcat is 3.55 sec(-1) with fructose 1,6-bisphosphate as substrate (at pH 7.5 and 25 degrees Celsius) (PubMed:17166851). kcat is 4.3 sec(-1) with fructose 1,6-bisphosphate as substrate (PubMed:31409864).


organism: Geobacillus stearothermophilus


organism: Halalkalibacterium halodurans


organism: Helicobacter pylori

proof_lines:
pH 7.0, 25°C, with 7-methylguanosine
pH 7.0, 25°C
pH 7.0, 25°C, with guanosine


organism: Homo sapiens


proof_lines: reaction with inosine, mutant enzyme S33A


proof_lines: reaction with inosine, mutant enzyme T242A


proof_lines: reaction with inosine, mutant enzyme Y88F


proof_lines: reaction with inosine, mutant enzyme K244A


substrate_name: Methylthioinosine

proof_lines:
pH 7.5, 25°C
25°C, pH 7.4
recombinant erythrocyte enzyme

substrate: Methylthioinosine


proof_lines: reaction with inosine, mutant enzyme N243A


proof_lines: reaction with inosine, mutant enzyme M219A


substrate_name: Unknown

proof_lines: 25°C, pH 7.4, mutant enzyme H257G, measured in slow-onset tight-binding phase

substrate: Unknown


proof_lines: reaction with inosine, mutant enzyme F200A


proof_lines:
wild-type, pH 7.0, 25°C
pH 7.4, 25°C, wild-type heavy PNP
pH 7.4, 25°C, wild-type light PNP


proof_lines: 25°C, pH 7.4, mutant enzyme H257F, measured in slow-onset tight-binding phase


proof_lines: reaction with inosine, mutant enzyme R84A


proof_lines: reaction with inosine, mutant enzyme E89A


proof_lines: 25°C, pH 7.4, mutant enzyme H257D, measured in slow-onset tight-binding phase


proof_lines: reaction with inosine, mutant enzyme H86A


substrate_name: Phosphate; Inosine

proof_lines:
pH 7.4, 25°C
reaction with hypoxanthine
reaction with ribose 1-phosphate

substrate: Phosphate; Inosine


proof_lines: mutant F200W, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant F159W, pH not specified in the publication, temperature not specified in the publication


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

proof_lines: pH 6.5, 25°C, recombinant wild-type enzyme


organism: Kluyveromyces lactis


substrate_name: Xanthosine

proof_lines: recombinant wild-type enzyme, pH 7.0, 25°C

substrate: Xanthosine


organism: Mesomycoplasma hyorhinis


organism: Mus musculus

proof_lines:
mutant enzyme N243D, pH 7.0
mutant enzyme N243D, pH 6.0
mutant enzyme N243D, pH 6.0 ot pH 7.0


proof_lines: mutant enzyme N243D/K244Q, with adenosine as substrate


assay_conditions_summary: pH 6

proof_lines: wild-type enzyme, with inosine as substrate


organism: Plasmodium berghei (strain Anka)

proof_lines: kcat is 66 min(-1) with fructose-1-phosphate as substrate (PubMed:1625704). kcat is 164 min(-1) with fructose-1,6- bisphosphate as substrate (PubMed:1625704).


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 80 degrees Celsius)

proof_lines: kcat is 2.5 sec(-1) for the FBPase activity (at 80 degrees Celsius) (PubMed:15274916). kcat is 0.62 sec(-1) for the FBPase activity (at 48 degrees Celsius). kcat is 0.91 sec(-1) for the FBP aldolase activity in the anabolic direction (at 48


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 95 degrees Celsius)

proof_lines: kcat is 17 sec(-1) for the FBPase activity (at 95 degrees Celsius). kcat is 7 sec(-1) for the FBPase activity (at 85 degrees Celsius). kcat is 2.9 sec(-1) for the FBPase activity (at 37 degrees Celsius).


organism: Thermococcus onnurineus (strain NA1)

substrate_name: FBP

proof_lines: kcat is 14.84 sec(-1) for the FBPase activity (at 95 degrees Celsius).


organism: Toxoplasma gondii

proof_lines: kcat is 7.09 sec(-1) with fructose-1,6- bisphosphate as substrate.


organism: Plasmodium falciparum

proof_lines: mutant enzyme V73I, at pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme V66I, at pH 7.4, temperature not specified in the publication


organism: Plasmodium lophurae


organism: Plasmodium yoelii


organism: Proteus vulgaris

proof_lines:
reaction with inosine
reaction with guanosine


organism: Pseudoalteromonas sp.


organism: Pyrococcus furiosus

substrate: guanosine


organism: Rattus norvegicus


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: deoxyinosine

proof_lines:
reaction with inosine
reaction with adenine

substrate: deoxyinosine


organism: Schistosoma mansoni

proof_lines: free enzyme, at pH 7.4, temperature not specified in the publication

proof_lines: immobilized enzyme, at pH 7.4, temperature not specified in the publication


organism: Serratia marcescens


organism: Thermus thermophilus

proof_lines: wild type hexameric enzyme, at pH 8.0 and 70°C

proof_lines: wild type trimeric enzyme, at pH 8.0 and 70°C


proof_lines: mutant hexameric enzyme N204D, at pH 8.0 and 70°C


proof_lines: mutant trimeric enzyme A196E/D238N, at pH 8.0 and 70°C


organism: Homo sapiens

proof_lines: reaction with inosine, mutant enzyme E201A


proof_lines: reaction with inosine, mutant enzyme F159A


proof_lines:
pH 7.4, 25°C, mutant F159Y heavy PNP
pH 7.4, 25°C, mutant F159Y light PNP


organism: Mycobacterium smegmatis

substrate_name: Phosphate; Adenosine

substrate: Phosphate; Adenosine


organism: Mycobacterium tuberculosis

proof_lines:
cosubstrate guanosine, pH 7.0, 25°C
pH 7.0, 25°C
pH 7.5, 37°C


organism: Oryctolagus cuniculus

substrate_name: Phosphate; Deoxyguanosine

substrate: Phosphate; Deoxyguanosine


organism: Pectobacterium carotovorum


proof_lines: mutant enzyme Y160F, at pH 7.4, temperature not specified in the publication


proof_lines: native enzyme subunits fused with subunits of mutant enzyme M183L, at pH 7.4 and 25°C


proof_lines: reaction with inosine, mutant enzyme H257A


organism: Hyalomma dromedarii


organism: Klebsiella aerogenes


organism: Kluyveromyces lactis


organism: Toxoplasma gondii

proof_lines: pH 7.4, temperature not specified in the publication


organism: Trichomonas vaginalis

substrate_name: p-nitrophenyl beta-D-ribofuranoside

substrate: p-nitrophenyl beta-D-ribofuranoside


organism: Acanthocardia tuberculata

substrate_name: IDP

substrate: IDP


organism: Archaeoglobus fulgidus

substrate_name: ADP

proof_lines: 50°C, pH not specified in the publication

substrate: ADP


organism: Bacillus licheniformis

substrate_name: phosphoenolpyruvate

proof_lines: pH 7.1, 30°C, in the presence of Mg2+, 7fold lower in the presence of Mn2+

substrate: phosphoenolpyruvate


organism: Saccharomyces cerevisiae

substrate_name: ADP; Phosphoenolpyruvate

proof_lines:
cosubstrate phosphoenolpyruvate
pH 6.2, 30°C

substrate: ADP; Phosphoenolpyruvate


organism: Selenomonas ruminantium


organism: Sus scrofa

proof_lines:
bound enzyme
solubilized enzyme
at 25°C


organism: Plasmodium falciparum

substrate_name: uridine

proof_lines: native enzyme subunits fused with the same peptide linker, at pH 7.4 and 25°C

substrate: uridine


proof_lines: mutant enzyme V66I/Y73I/Y160F, at pH 7.4, temperature not specified in the publication


proof_lines: wild type enzyme, at pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme V66I/V73I, at pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme V66I/Y160F, at pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme V73I/Y160F, at pH 7.4, temperature not specified in the publication


enzyme_display_name: fructose-bisphosphatase

organism: Corynebacterium glutamicum

substrate_name: Fructose 1,6-bisphosphate

enzyme: fructose-bisphosphatase

substrate: Fructose 1,6-bisphosphate


organism: Escherichia coli

substrate_name: Fructose 1,6-bisphosphate; H2O

proof_lines:
Raw SKiD Env: Temp=37°C, pH=9
Raw SKiD Env: Temp=-----, pH=7.7

substrate: Fructose 1,6-bisphosphate; H2O


substrate_name: H2O; Fructose 1,6-bisphosphate

substrate: H2O; Fructose 1,6-bisphosphate


substrate_name: D-Fructose 1,6-bisphosphate

substrate: D-Fructose 1,6-bisphosphate


proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=22°C, pH=7.5


organism: Gallus gallus

substrate_name: H2O; D-Fructose 1,6-bisphosphate

substrate: H2O; D-Fructose 1,6-bisphosphate


organism: Oryctolagus cuniculus


substrate_name: D-Fructose 1,6-bisphosphate; H2O

substrate: D-Fructose 1,6-bisphosphate; H2O


organism: Pisum sativum


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant chimeric HL1: NH2-half from Homo sapiens (P09467), COOH-half from Pisum sativum

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant chimeric HL2: NH2- and COOH-half from Homo sapiens (P09467), 170 loop from Pisum sativum

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant chimeric BV2: NH2- and COOH-half from Beta vulgaris (Q42649), 170 loop from Pisum sativum


organism: Pyrococcus furiosus

substrate_name: D-fructose 1,6-bisphosphate

proof_lines:
Raw SKiD Env: Temp=22°C, pH=8
Raw SKiD Env: Temp=50°C, pH=8

substrate: D-fructose 1,6-bisphosphate


organism: Rattus norvegicus


sequence_source: UniProtKB reviewed (Swiss-Prot)


organism: Bacillus methanolicus

sequence_source: UniProtKB unreviewed (TrEMBL)


organism: Bacillus subtilis

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant YwjI


organism: Bos taurus


organism: Homo sapiens

sequence_source: UniProtKB REST FASTA O00757

column_label: Table 1 row Wild-type muscle reports kcat 23.4 +/- 0.7 and Km,F1,6-P2 1.3 +/- 0.3 microM.

normalized_value_unit_evidence: kcat normalized_value=23.4 normalized_unit=s^-1; Km normalized_value=0.0013 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=23.4 +/- 0.7 raw_unit=s^-1; Km raw_value=1.3 +/- 0.3 raw_unit=microM

row_label: Wild-type muscle FBPase

table_label: ScienceDirect full text Table 1


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant T177M/Q179C


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant K20E/T177M/Q179C


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant K20E


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----


organism: Leishmania major


organism: Methanocaldococcus jannaschii


organism: Saccharomyces cerevisiae


organism: Spinacia oleracea

sequence_source: UniProtKB P22418 canonical sequence; reconstructed from mature-chain C179S

sequence_variant_note: Mutation signature C179S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant C179S not-activated (oxidized)

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant C179S activated (reduced)


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant C155/174S not-activated (oxidized)

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant C155/179S not-activated (oxidized)

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant C174/179S not-activated (oxidized)


sequence_source: UniProtKB P22418 canonical sequence; reconstructed from mature-chain C174S

sequence_variant_note: Mutation signature C174S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant C174S not-activated (oxidized)

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant C174S activated (reduced)


sequence_source: UniProtKB P22418 canonical sequence; reconstructed from mature-chain C155S

sequence_variant_note: Mutation signature C155S matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant C155S not-activated (oxidized)

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant C155S activated (reduced)


sequence_source: UniProtKB P22418 canonical sequence


substrate_name: Fructose 6-phosphate

substrate: Fructose 6-phosphate


column_label: PMC HTML Table 2 row MJ0109 / FBP columns Km (mM), kcat (s^-1), and kcat/Km; table footnote reports means +/- SD for three determinations.

row_label: MJ0109 / FBP

table_label: Table 2. Kinetic constants for phosphatase activities


organism: Mycobacterium tuberculosis

proof_lines:
Raw SKiD Env: Temp=22°C, pH=8
Raw SKiD Env: Temp=37°C, pH=-----


organism: Oncorhynchus mykiss


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant E69Q


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Q69E


column_label: PMID 17350621 Table 2, N-FBPase row, Km F1,6P2 column = 2.1 uM.

raw_value_unit_evidence: N-FBPase Km F1,6P2 = 2.1 uM; S.E.M. 0.2 uM.

row_label: N-FBPase native rabbit muscle FBPase

table_label: Table 2: kinetic properties of native rabbit muscle FBPase and modified/recombinant FBPases


organism: Sus scrofa


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R22A


sequence_source: UniProtKB P00636 canonical sequence

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


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Glu29GLn

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Glu29Gln


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Thr31Val


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R243A


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Leu54Ala


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 7.8; 321.15 K; cofactor NADPH

column_label: Table 1 (Activities of wild type and mutants of ST0318), FBPase block, row 'Wild type'; column 'kcat (s^-1)' = 0.62; column 'Km (mM)' = 0.027; column 'kcat/Km (s^-1 mM^-1)' = 23. The kcat and Km cells also print the standard deviations 0.02 and 0.003, which the export does not carry.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.62 s^-1; already in s^-1, so no unit conversion applies; the value carried forward is 0.62 s^(-1). Km: printed Table 1 cell 0.027 mM; already in mM, so no unit conversion applies; the value carried forward is 0.027 mM. kcat/Km: the printed Table 1 cell 23 s^-1 mM^-1 is the rounded rendering of the exact same-row quotient 0.62 / 0.027 = 22.962962962962962 s^(-1)*mM^(-1), and that exact quotient is the value carried forward.

raw_value_unit_evidence: Table 1, FBPase block, row 'Wild type': kcat = 0.62 s^-1; Km = 0.027 mM; printed kcat/Km = 23 s^-1 mM^-1.

row_label: Table 1, FBPase block, row 'Wild type'


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Tyr57Trp


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Glu-tagged

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Glu97->Ala(1 3)

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp118->Ala(1 3)


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant T27A


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant E192A


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant E192Q


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant D187A


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Lys71Ala


organism: Synechocystis sp.


organism: Thermotoga maritima


organism: Vigna radiata

proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R30T/D32E/F33L


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R30T/D32E


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant M251L


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant D32E


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant D32E/D33L


proof_lines:
wild-type liver isoenzyme enzyme
wild-type liver enzyme, pH 7.5, 37°C
wild-type, pH 7.0, 37°C


substrate_name: fructose 1,6-diphosphate

proof_lines:
alkaline isoenzyme
neutral isoenzyme
pH 7.5, 30°C, recombinant enzyme

substrate: fructose 1,6-diphosphate


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp74Glu


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asn64Ala


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp74Ala


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asn64Gln


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp68Glu


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant Asp74Asn


organism: Synechococcus elongatus

substrate_name: H2O; beta-D-Fructose 1,6-bisphosphate

substrate: H2O; beta-D-Fructose 1,6-bisphosphate


organism: Euglena gracilis

proof_lines: isozyme EgFBPaseI, pH 8.0, temperature not specified in the publication

proof_lines: pH and temperature not specified in the publication

proof_lines: isozyme EgFBPaseII, pH 8.0, temperature not specified in the publication


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R15A


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R22K


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant E19Q


proof_lines: SABIO-RK modifier species: fructose-bisphosphatase(Enzyme) mutant R22M


organism: Synechococcus sp.

proof_lines:
isoenzyme F-II
isoenzyme F-I


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

substrate_name: inositol-1-phosphate (at 85 degrees Celsius)

proof_lines: kcat is 2.5 sec(-1) for IMPase activity (at 85 degrees Celsius) and 2.7 sec(-1) for FBPase activity (at 85 degrees Celsius).


organism: Cenarchaeum symbiosum (strain A)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBP phosphatase activity, at 48 degrees Celsius)

proof_lines: The aldolase reaction is a classic case for a fully reversible enzymatic reaction but here, the KM values for the substrate for the aldol condensation and the aldol cleavage differ by a factor of 1000, and the intrinsic phosphatase activity


organism: Escherichia coli (strain K12)

substrate_name: fructose 1,6-bisphosphate (at pH 7.7 and room temperature)

proof_lines: The catalytic efficiency of GlpX is 3-fold higher than that of YggF, the other FBPase class 2 in E.coli.


substrate_name: fructose 1,6-bisphosphate

proof_lines: The catalytic efficiency of YggF is 3-fold lower than that of GlpX, the other FBPase class 2 in E.coli.

substrate: fructose 1,6-bisphosphate


organism: Homo sapiens

proof_lines: The kinetic constants are determined for the recombinant enzyme expressed in E.coli.


substrate_name: fructose 1,6-biphosphate

substrate: fructose 1,6-biphosphate


organism: Rhodococcus opacus

substrate_name: sedoheptulose 1,7-diphosphate

substrate: sedoheptulose 1,7-diphosphate


organism: Archaeoglobus fulgidus


organism: Bacillus methanolicus


organism: Bacillus subtilis

proof_lines: in presence of 0.01 mM phosphoenolpyruvate


organism: Blastocladiella emersonii


organism: Bombus atratus


organism: Bombus terrestris

proof_lines: activated by Mg2+, at 22°C or activated by Mn2+ at 17°C


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

proof_lines: kcat is 4.2 sec(-1) for IMPase activity (at 85 degrees Celsius) and 7.0 sec(-1) for FBPase activity (at 85 degrees Celsius).

substrate: inositol-1-phosphate (at 85 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


substrate_name: 3'-phosphoadenosine 5'-phosphate (at pH 9.0 and 30 degrees Celsius)

proof_lines: The second-order rate constant for PAP was determined to be over 3 orders of magnitude greater than those determined for IMP and FBP.


substrate_name: p-nitrophenyl phosphate (at pH 5.5 and 37 degrees Celsius)

proof_lines: kcat is 0.00071 sec(-1) for phosphoglycerate mutase activity (PubMed:16672613). The enzyme's FBPase activity does not follow Michaelis-Menten kinetics but follows allosteric sigmoidal kinetics that show lower affinity for FBP compared with


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 80 degrees Celsius)

proof_lines: kcat is 2.5 sec(-1) for the FBPase activity (at 80 degrees Celsius) (PubMed:15274916). kcat is 0.62 sec(-1) for the FBPase activity (at 48 degrees Celsius). kcat is 0.91 sec(-1) for the FBP aldolase activity in the anabolic direction (at 48


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 95 degrees Celsius)

proof_lines: kcat is 17 sec(-1) for the FBPase activity (at 95 degrees Celsius). kcat is 7 sec(-1) for the FBPase activity (at 85 degrees Celsius). kcat is 2.9 sec(-1) for the FBPase activity (at 37 degrees Celsius).


organism: Bos taurus

proof_lines:
pH 7.5, lung
pH 7.5, lung enzyme in presence of AMP


organism: Campylobacter jejuni serotype O:2


organism: Candidatus Cenarchaeum symbiosum

proof_lines: pH not specified in the publication, 40°C


organism: Citrus x paradisi


organism: Clonorchis sinensis


organism: Corynebacterium glutamicum


organism: Cyberlindnera jadinii


organism: Escherichia coli


proof_lines: 22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+


organism: Homo sapiens


mutation_signature: Δ4


proof_lines: liver enzyme mutant E20K/M177T/C179Q, pH 7.5, 37°C


mutation_signature: Δ6


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: fructose 1,6-bisphosphate (at 85 degrees Celsius)


organism: Sus scrofa

column_label: Table I row KmF16P2 (uM); column Wild type; substrate fructose 1,6-bisphosphate/F16P2.

raw_value_unit_evidence: Table I row KmF16P2 (uM), column Wild type: 1.2 +/- 0.05 uM.

row_label: KmF16P2 (uM)

table_label: Table I. Kinetic parameters for wild-type and Leu54 FBPases


organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

substrate_name: fructose-1,6-bisphosphate (at pH 8)

substrate: fructose-1,6-bisphosphate (at pH 8)


substrate_name: fructose 1,6-bisphosphate (at pH 8)

substrate: fructose 1,6-bisphosphate (at pH 8)


proof_lines:
wild-type
pH 9.0, 37°C, wild-type
wild-type, 22°C, pH 7.5


substrate_name: D-fructose 1,6-bisphosphate


organism: Francisella tularensis

proof_lines: recombinant mutant T89S, pH and temperature not specified in the publication


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


organism: Gallus gallus


organism: Lactobacillus delbrueckii subsp. lactis

substrate_name: beta-D-glucose 1,6-bisphosphate

proof_lines: wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C

substrate: beta-D-glucose 1,6-bisphosphate


proof_lines: mutant enzyme K76A, in 50 mM K+HEPES pH 7.0 at 25°C


proof_lines: mutant enzyme H20N, in 50 mM K+HEPES pH 7.0 at 25°C


organism: Lathyrus oleraceus


proof_lines: pH 8.0, 26-27°C, recombinant nontreated mutant C173S/C178S

proof_lines: pH 8.0, 26-27°C, recombinant S-nitrosoglutathione-treated mutant C173S/C178S


proof_lines:
pH 6.6, 25°C, native enzyme
pH 6.6, 25°C, Trombin treated enzyme
pH 6.6, 25°C, recombinant enzyme


organism: Leishmania major


organism: Malus domestica

substrate_name: D-Fructose 1,6-bisphosphate; H2O


organism: Methanocaldococcus jannaschii

proof_lines: pH and temperature not specified in the publication


organism: Mus musculus

substrate_name: fructose 1,6-diphosphate


mutation_signature: Δ8


proof_lines: liver enzyme mutant M177T/C179Q, pH 7.5, 37°C


mutation_signature: Δ5


proof_lines: muscle enzyme mutant K20E/T177M/Q179C, pH 7.5, 37°C


proof_lines: mutant Y57W, pH 7.0, 37°C, Hill-coefficient 2.0

proof_lines: mutant Y57W, pH 7.0, 37°C, Hill-coefficient 1.84


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme K274L


organism: Mustela vison

substrate_name: H2O; Fructose 1,6-bisphosphate


organism: Mycobacterium tuberculosis


proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme


organism: Mycolicibacterium smegmatis

substrate_name: D-fructose 1,6-diphosphate

substrate: D-fructose 1,6-diphosphate


organism: Neisseria meningitidis


organism: Pisum sativum


organism: Ptyas dhumnades

proof_lines:
pH 7.5, 30°C, recombinant enzyme
pH 7.5, 30°C, chimeric enzyme


organism: Pyrobaculum calidifontis

proof_lines:
recombinant enzyme, pH 8.0, 55°C
pH 8.0, 25°C


organism: Pyrococcus furiosus


organism: Rattus norvegicus

substrate_name: H2O; D-Fructose 1,6-bisphosphate