substrate_name: succinate semialdehyde

smiles: O=CCCC(=O)O

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (succinate semialdehyde) / fixed substrate alanine, column kcat s^-1, raw cell 10.8, normalized 10.8 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (succinate semialdehyde) / fixed substrate alanine, column Km mM, raw cell 0.014+/-0.002, normalized 0.014 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (succinate semialdehyde) / fixed substrate alanine, column kcat/Km s^-1 mM^-1, raw cell 770, normalized 770 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.8 normalized_unit=s^-1; Km normalized_value=0.014 normalized_unit=mM; kcat/Km normalized_value=770 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.8 raw_unit=s^-1 raw_cell=10.8; Km raw_value=0.014+/-0.002 raw_unit=mM raw_cell=0.014+/-0.002; kcat/Km raw_value=770 raw_unit=s^-1*mM^-1 raw_cell=770

substrate: succinate semialdehyde


enzyme_display_name: glucokinase

organism: Aeropyrum pernix

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 6.2; 363.15 K; cofactor ATP

column_label: Table 3 row 2-Deoxyglucose lists Apparent K_m 330 uM, kcat 30 s^-1, kcat/K_m 0.09 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.33 normalized_unit=mM; kcat normalized_value=30 normalized_unit=s^-1; kcat/Km normalized_value=90.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=330 raw_unit=uM; kcat raw_value=30 raw_unit=s^-1; kcat/Km raw_value=0.09 raw_unit=uM^-1 s^-1

table_label: Table 3. Substrate specificity of the GIK from A. pernix with alternate substrates

data_origin: experimental

enzyme: glucokinase

status: corrected

source: oed


substrate_name: D-Fructose

column_label: Table 3 row Fructose lists Apparent K_m 150 uM, kcat 10 s^-1, kcat/K_m 0.07 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.15 normalized_unit=mM; kcat normalized_value=10 normalized_unit=s^-1; kcat/Km normalized_value=70.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=150 raw_unit=uM; kcat raw_value=10 raw_unit=s^-1; kcat/Km raw_value=0.07 raw_unit=uM^-1 s^-1

row_label: Fructose

substrate: D-Fructose


substrate_name: D-Glucosamine

verification_status: verified

column_label: Table 3 row Glucosamine lists Apparent K_m 60 uM, kcat 18 s^-1, kcat/K_m 0.30 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.06 normalized_unit=mM; kcat normalized_value=18 normalized_unit=s^-1; kcat/Km normalized_value=300.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=60 raw_unit=uM; kcat raw_value=18 raw_unit=s^-1; kcat/Km raw_value=0.30 raw_unit=uM^-1 s^-1

row_label: Glucosamine

substrate: D-Glucosamine

status: verified


substrate_name: D-Glucose

column_label: Table 3 row Glucose lists Apparent K_m 44 uM, kcat 23 s^-1, kcat/K_m 0.53 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.044 normalized_unit=mM; kcat normalized_value=23 normalized_unit=s^-1; kcat/Km normalized_value=530.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=44 raw_unit=uM; kcat raw_value=23 raw_unit=s^-1; kcat/Km raw_value=0.53 raw_unit=uM^-1 s^-1

row_label: Glucose

substrate: D-Glucose


substrate_name: D-Mannose

column_label: Table 3 row Mannose lists Apparent K_m 110 uM, kcat 13 s^-1, kcat/K_m 0.12 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.11 normalized_unit=mM; kcat normalized_value=13 normalized_unit=s^-1; kcat/Km normalized_value=120.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=110 raw_unit=uM; kcat raw_value=13 raw_unit=s^-1; kcat/Km raw_value=0.12 raw_unit=uM^-1 s^-1

row_label: Mannose

substrate: D-Mannose


organism: Methylotuvimicrobium alcaliphilum

substrate_name: ATP

source_db: brenda

assay_conditions_summary: pH 9.5; cofactor ATP

column_label: Table 1, row group ATP, metric rows Km app (mM), kcat ATP (1/min), and kcat/Km ATP (1/min mM), column Methylomicrobium alcaliphilum

raw_value_unit_evidence: ATP row: Km app 0.37 +/- 0.06 mM; kcat ATP 15463 1/min; kcat/Km ATP 41792 1/min mM

row_label: ATP

table_label: Table 1 Some properties of the recombinant Glk from M. alcaliphilum 20Z

substrate: ATP

source: brenda


substrate_name: D-glucose

column_label: Table 1, row group Glucose, metric rows Km app (mM), kcat glucose (1/min), and kcat/Km glucose (1/min mM), column Methylomicrobium alcaliphilum

raw_value_unit_evidence: Glucose row: Km app 0.32 +/- 0.05 mM; kcat glucose 15169 1/min; kcat/Km glucose 47403 1/min mM

substrate: D-glucose


substrate_name: D-glucosamine

column_label: Table 1, row group Glucosamine, metric rows Km app (mM), kcat glucosamine (1/min), and kcat/Km glucosamine (1/min mM), column Methylomicrobium alcaliphilum

raw_value_unit_evidence: Glucosamine row: Km app 1.1 +/- 0.2 mM; kcat glucosamine 17612 1/min; kcat/Km glucosamine 16011 1/min mM

substrate: D-glucosamine


assay_conditions_summary: pH 9.5; 303.15 K; cofactor ATP


organism: Mycobacterium tuberculosis

substrate_name: CTP

verification_status: unverified

kcat_over_km_origin: calculated

assay_conditions_summary: pH 8.6; 303.15 K; cofactor ATP

substrate: CTP

status: unverified


substrate_name: dATP

substrate: dATP


substrate_name: GTP

substrate: GTP


substrate_name: UTP

substrate: UTP


enzyme_display_name: hexokinase

organism: Thermoproteus tenax

substrate_name: D-mannose

kcat_display: Not reported

kcat_over_km_display: Not reported

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

column_label: Table II row T. tenax (50 deg C); Mannose Km column; units mM

raw_value_unit_evidence: Mannose Km 0.043 mM

row_label: T. tenax (50 deg C)

table_label: Table II

enzyme: hexokinase

substrate: D-mannose


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

column_label: Table II row T. tenax (50 deg C); 2-Deoxyglucose Km column; units mM

raw_value_unit_evidence: 2-Deoxyglucose Km 0.187 mM


assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table II row T. tenax (50 deg C); ATP Km column; units mM

raw_value_unit_evidence: ATP Km 0.29 mM


substrate_name: D-fructose

column_label: Table II row T. tenax (50 deg C); Fructose Km column; units mM

raw_value_unit_evidence: Fructose Km 0.734 mM

substrate: D-fructose


enzyme_display_name: pyridoxamine--pyruvate transaminase

organism: Rhizobium loti

substrate_name: Pyridoxamine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E68A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: pyridoxamine--pyruvate transaminase

substrate: Pyridoxamine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E68G with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R336A to reconstruct the assayed variant sequence.


substrate_name: Pyridoxamine phosphate

substrate: Pyridoxamine phosphate


organism: Rattus norvegicus

substrate_name: L-kynurenine

source_db: uniprot

proof_lines:
L-kynurenine
kynurenic acid
KAT activity

substrate: L-kynurenine

source: uniprot


proof_lines:
L-kynurenine
KAT activity
3-hydroxy-L-kynurenine not preserved


proof_lines:
L-kynurenine
KAT activity
2-oxoglutarate not preserved


substrate_name: L-glutamate

smiles: C(CC(=O)O)C(C(=O)O)N

proof_lines:
L-kynurenine
KAT activity
L-glutamate not preserved

substrate: L-glutamate


organism: Escherichia coli (strain K12)

substrate_name: KAPA

smiles: CC(C(=O)CCCCCC(=O)O)N

substrate: KAPA


substrate_name: pyridoxamine phosphate (PMP)

substrate: pyridoxamine phosphate (PMP)


substrate_name: pyridoxal phosphate (PLP)

substrate: pyridoxal phosphate (PLP)


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R391A to reconstruct the assayed variant sequence.

smiles: CC(N)C(=O)CCCCCC(=O)O

proof_lines:
7,8-diaminopelargonic acid synthase
R391A mutation
KAPA


substrate_name: S-Adenosyl-L-methionine

substrate: S-Adenosyl-L-methionine


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


organism: Psychrobacter cryohalolentis

smiles: CC(=O)C(C)=O


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


enzyme_display_name: Hexokinase

organism: Brugia malayi

substrate_name: glucose

assay_conditions_summary: cofactor ATP

column_label: PubMed abstract gives Km values for glucose, fructose and ATP as 0.035+/-0.005, 75+/-0.3 and 1.09+/-0.5 mM, respectively; glucose maps to 0.035 mM.

raw_value_unit_evidence: Km raw_value=0.035+/-0.005 raw_unit=mM

row_label: BmHk recombinant hexokinase kinetic characterization; substrate glucose

table_label: PMID 18499511 PubMed abstract

enzyme: Hexokinase

substrate: glucose


substrate_name: fructose

column_label: PubMed abstract gives Km values for glucose, fructose and ATP as 0.035+/-0.005, 75+/-0.3 and 1.09+/-0.5 mM, respectively; fructose maps to 75 mM.

raw_value_unit_evidence: Km raw_value=75+/-0.3 raw_unit=mM

row_label: BmHk recombinant hexokinase kinetic characterization; substrate fructose

substrate: fructose


substrate_name: ATP

column_label: PubMed abstract gives Km values for glucose, fructose and ATP as 0.035+/-0.005, 75+/-0.3 and 1.09+/-0.5 mM, respectively; ATP maps to 1.09 mM.

raw_value_unit_evidence: Km raw_value=1.09+/-0.5 raw_unit=mM

row_label: BmHk recombinant hexokinase kinetic characterization; substrate ATP

substrate: ATP


enzyme_display_name: Kynurenine--oxoglutarate transaminase 1

substrate_name: L-kynurenine (with 2-oxoglutarate as cosubstrate)

enzyme: Kynurenine--oxoglutarate transaminase 1


substrate_name: pyruvate

substrate: pyruvate


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A456V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: glucokinase A456V mouse


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K414E to reconstruct the assayed variant sequence.

proof_lines: glucokinase K414E mouse


proof_lines:
glucokinase
wild type enzyme
A456V


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


substrate_name: D-glucose; D-mannose

proof_lines:
Schizosaccharomyces pombe hexokinase 1
glucose affinity
2-deoxyglucose

substrate: D-glucose; D-mannose


substrate_name: D-glucose

substrate: D-glucose


organism: Arabidopsis thaliana

substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: tyrosine

proof_lines: TAA1 L-tyrosine L-Trp

substrate: tyrosine


substrate_name: phenylalanine

proof_lines: TAA1 L-phenylalanine L-Trp

substrate: phenylalanine


enzyme_display_name: fructokinase

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

enzyme: fructokinase


substrate_name: D-Fructose

column_label: Table 2 columns kcat (s^-1), Km,sugar (M), and kcat/Km,sugar (M^-1 s^-1).

normalized_value_unit_evidence: kcat 14 s^-1; Km 1.3 mM; kcat/Km,sugar 11 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row YajF / D-fructose: kcat 14 s^-1; Km,sugar 1.3 x 10^-3 M; kcat/Km,sugar 1.1 x 10^4 M^-1 s^-1.

row_label: YajF / D-fructose

table_label: Table 2, kinetic parameters for carbohydrate phosphorylation

substrate: D-Fructose


substrate_name: D-Glucose

normalized_value_unit_evidence: kcat 12 s^-1; Km 59 mM; kcat/Km,sugar 0.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row YajF / D-glucose: kcat 12 s^-1; Km,sugar 5.9 x 10^-2 M; kcat/Km,sugar 2.0 x 10^2 M^-1 s^-1.

row_label: YajF / D-glucose

substrate: D-Glucose


enzyme_display_name: Fructokinase

organism: Fusobacterium mortiferum

sequence: MIIGAVEAGGTKFVDGVGNEKGEIFER

wild_type_sequence: MIIGAVEAGGTKFVDGVGNEKGEIFER

enzyme: Fructokinase


substrate_name: magnesium

smiles: [Mg]

proof_lines:
Fusobacterium mortiferum
ATP-dependent fructokinase
fructokinase

substrate: magnesium


organism: Bacillus subtilis

substrate_name: L-lysine

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

smiles: C(CCN)CC(C(=O)O)N

proof_lines:
pH 8.3, 37°C
Raw SKiD Env: Temp=37°C, pH=8.3

source_databases_merged: brenda skid

substrate: L-lysine


smiles: CC(C(=O)CCCCCC(=O)[O-])N


assay_conditions_summary: pH 7


substrate_name: L-glutamate

substrate: L-glutamate


enzyme_display_name: UniProt P12995

substrate_name: S-adenosyl-L-methionine

source_db: skid

sequence_source: multiple

assay_conditions_summary: pH 9

source_databases_merged: skid uniprot

enzyme: UniProt P12995

substrate: S-adenosyl-L-methionine

source: skid


organism: Shigella dysenteriae

column_label: Table 3. Kinetic parameters; row VioA D7 / dTDP-D-Glc4O; column kcat /s; metric kcat; normalized value 0.74 s^-1 | Table 3. Kinetic parameters; row VioA D7 / dTDP-D-Glc4O; column Km (uM); metric km; normalized value 0.98 mM | Table 3. Kinetic parameters; row VioA D7 / dTDP-D-Glc4O; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 0.7551020408163265 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.74 normalized_unit=s^-1; km normalized_value=0.98 normalized_unit=mM; kcat_over_km normalized_value=0.7551020408163265 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.74 raw_unit=s^-1; km raw_value=980 raw_unit=uM; kcat_over_km raw_value=0.74/0.98 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells

row_label: VioA D7 / dTDP-D-Glc4O

table_label: Table 3. Kinetic parameters


column_label: Table 3. Kinetic parameters; row VioA O7 / dTDP-D-Glc4O; column kcat /s; metric kcat; normalized value 5.66 s^-1 | Table 3. Kinetic parameters; row VioA O7 / dTDP-D-Glc4O; column Km (uM); metric km; normalized value 0.0458 mM | Table 3. Kinetic parameters; row VioA O7 / dTDP-D-Glc4O; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 123.58078602620087 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=5.66 normalized_unit=s^-1; km normalized_value=0.0458 normalized_unit=mM; kcat_over_km normalized_value=123.58078602620087 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=5.66 raw_unit=s^-1; km raw_value=45.8 raw_unit=uM; kcat_over_km raw_value=5.66/0.0458 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells

row_label: VioA O7 / dTDP-D-Glc4O


enzyme_display_name: N-acetylglucosamine kinase 1

organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: N-acetylglucosamine (GlcNAc)

smiles: CC(=O)NC(C=O)C(C(C(CO)O)O)O

column_label: Results prose for CaNAG5/CaNag5p; metric Km with GlcNAc

normalized_value_unit_evidence: normalized: Km=0.3755 mM

raw_value_unit_evidence: paper page 4 text: the Km value of CaNag5p with GlcNAc was 375.5 uM

row_label: CaNag5p / GlcNAc

table_label: Results prose plus Fig. 6 context

enzyme: N-acetylglucosamine kinase 1

substrate: N-acetylglucosamine (GlcNAc)


substrate_name: glucose


enzyme_display_name: O-ureido-L-serine synthase

organism: Streptomyces lavendulae

substrate_name: Hydroxyurea

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature Y97F to reconstruct the assayed variant sequence.

smiles: NC(=O)NO

enzyme: O-ureido-L-serine synthase

substrate: Hydroxyurea


substrate_name: hydrogen sulfide

smiles: S

proof_lines:
sulfide
hydroxyurea
O-acetylserine sulfhydrylase

substrate: hydrogen sulfide


organism: Schistosoma mansoni

assay_conditions_summary: pH 8.5; cofactor ATP


substrate_name: ATP


enzyme_display_name: Glucokinase

organism: Bacillus subtilis (strain 168)

column_label: Abstract reports K(m) values for ATP and glucose of 0.77 and 0.24 mM respectively.

raw_value_unit_evidence: Km raw_value=0.77 mM raw_unit=mM

row_label: Bacillus subtilis glucose kinase / ATP

table_label: PubMed XML abstract PMID 9620975

enzyme: Glucokinase


raw_value_unit_evidence: Km raw_value=0.24 mM raw_unit=mM

row_label: Bacillus subtilis glucose kinase / glucose

substrate: glucose


organism: Homo sapiens


substrate: ATP


smiles: C(=O)(N)NO

assay_conditions_summary: pH 8; 303.15 K; buffer 250 mM potassium phosphate

column_label: Table 1 (Kinetic parameters of DcsD), 2nd substrate row Hydroxyurea, product column L-OUS; column Mean Kmapp (mM) = 9.0; column Mean kcatapp (s^-1) = 11; column Mean kcat/Km (M^-1 s^-1) = 1,200; column Mean kcat/Km for L-OAS (M^-1 s^-1) = 150.

normalized_value_unit_evidence: Km: printed Table 1 cell 9.0 mM; the column head prints mM, so no unit conversion applies and the value carried here is 9.0 mM. kcat: printed Table 1 cell 11 s^-1; the column head prints s^-1, so no unit conversion applies and the value carried here is 11.0 s^(-1). kcat/Km: printed Table 1 cell 1.2 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 1.2 s^-1 mM^-1. Quotient disclosure for this cell group: 11 / 9.0 = 1.2222222222222223 s^-1 mM^-1, and the printed efficiency cell is that same quotient carried to the two significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, 2nd substrate row Hydroxyurea, product L-OUS: apparent Km = 9.0 mM; apparent kcat = 11 s^-1; printed kcat/Km = 1.2 x 10^3 M^-1 s^-1 (the cell prints 1,200 with a printed standard deviation of 300).

table_label: Table 1: Kinetic parameters of DcsD (Antimicrobial Agents and Chemotherapy 2013, volume 57, number 6, pages 2603-2612); printed columns Mean Kmapp (mM), Mean kcatapp (s^-1), Mean kcat/Km (M^-1 s^-1) and Mean kcat/Km for L-OAS (M^-1 s^-1)


row_label: Table 1, 2nd substrate row Hydroxyurea, product L-OUS


substrate_name: D-Glucosamine

substrate: D-Glucosamine


organism: Methylomonas methanica

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

column_label: Table 2 columns Parameter/Substrate/Values ATP-Glk: substrate ATP cells under Km app, kcat substrate, and kcat/Km

raw_value_unit_evidence: Table 2 ATP row: Km app 0.078 +/- 0.0056 mM; kcat substrate 7.55 1/min; kcat/Km 96.85 1/min mM

row_label: ATP-Glk; substrate ATP

table_label: Table 2. Kinetic parameters of ATP- and polyphosphate-dependent glucokinases from Methylomonas sp. 12


column_label: Table 2 columns Parameter/Substrate/Values ATP-Glk: substrate Glucose cells under Km app, kcat substrate, and kcat/Km

raw_value_unit_evidence: Table 2 Glucose row: Km app 0.08 +/- 0.007 mM; kcat substrate 6.57 1/min; kcat/Km 82.09 1/min mM

row_label: ATP-Glk; substrate Glucose


organism: Mycobacterium tuberculosis


organism: Methylotuvimicrobium alcaliphilum

substrate_name: D-fructose

assay_conditions_summary: pH 9; cofactor ATP

proof_lines: ATP-dependent phosphorylation of fructose

proof_lines: apparent K(m) values for fructose and ATP

substrate: D-fructose


organism: Escherichia coli

assay_conditions_summary: pH 7.6; 298.15 K; buffer a 0.3-0.5 M Tris-HCl; cofactor ATP

normalized_value_unit_evidence: Glk / D-glucose column of Table 2: kcat 410 s^-1 = 410.0 s^(-1); Km,ATP 2.6 × 10-4 M = 0.00026 M = 0.26 mM (1 M = 1000 mM); kcat/Km derived 410 s^-1 / 0.26 mM = 1576.923076923077 s^-1 mM^-1. In the flattened text the multiplication sign renders as × and superscript exponents are flattened, so `7.6 × 10-5` is the paper's 7.6 x 10^-5, `5.4 × 106` is the paper's 5.4 x 10^6, and the unit labels `kcat (s-1)` and `kcat/Km,sugar (M-1 s-1)` are the paper's kcat (s^-1) and kcat/Km,sugar (M^-1 s^-1). Table 2 is transposed: parameters are rows and enzyme/substrate pairs are columns, in the order Glk / D-glucose, YcfX / D-glucose, NanK / D-glucose, NanK / N-acetyl-D-mannosamine, YajF / D-glucose, YajF / D-fructose.

raw_value_unit_evidence: Table 2: Kinetic Parameters for the Phosphorylation of Carbohydrates by Glk, YcfX, NanK, and YajFa | column header rows: `Glk YcfX NanK YajF` over `parameter D-glucose D-glucose D-glucose N-acetyl-D-mannosamine D-glucose D-fructose` | metric rows quoted in the captured segment: `kcat (s-1) 410 9.2 9.1 83 12 14`, `Km,sugar (M) 7.6 × 10-5 3.8 × 10-3 1.8 × 10-2 3.1 × 10-4 5.9 × 10-2 1.3 × 10-3`, `Km,ATP (M) 2.6 × 10-4 3.4 × 10-3 2.9 × 10-3 5.1 × 10-4 1.2 × 10-2 1.8 × 10-3`, `kcat/Km,sugar (M-1 s-1) 5.4 × 106 2.4 × 103 5.1 × 102 2.7 × 105 2.0 × 102 1.1 × 104` | Glk / D-glucose column cells read: kcat = 410 s^-1; Km,ATP = 2.6 × 10-4 M; no kcat/Km,ATP cell is printed

row_label: Glk | D-glucose reaction | ATP (Km,ATP)


raw_value_unit_evidence: Table 2 row Glk / D-glucose: kcat 410 s^-1; Km,sugar 7.6 x 10^-5 M; kcat/Km,sugar 5.4 x 10^6 M^-1 s^-1.

row_label: Glk / D-glucose


organism: Naegleria fowleri

assay_conditions_summary: pH 7.4; 295.15 K; cofactor ATP

proof_lines:
pH 7.4, 22°C
Raw SKiD Env: Temp=22°C, pH=7.4


substrate_name: D-glucose

substrate: D-glucose


organism: Oryza sativa subsp. japonica

substrate_name: fructose

substrate: fructose


enzyme_display_name: tryptophan-phenylpyruvate transaminase

organism: Aspergillus nidulans

substrate_name: phenylpyruvate

enzyme: tryptophan-phenylpyruvate transaminase

substrate: phenylpyruvate


enzyme_display_name: GDP-perosamine synthase

organism: Caulobacter vibrioides

assay_conditions_summary: pH 7.5; 295.15 K; buffer C pH 7

column_label: Table 3 row GDP-4-keto-6-deoxymannose reaction reports Km sugar, kcat, and kcat/Km sugar in separate metric-labeled columns.

normalized_value_unit_evidence: Km 0.013 mM; kcat 2.7 s^-1; kcat/Km 210000 M^-1 s^-1 = 210 s^-1*mM^-1, consistent with expected 207.6923076923077 by rounding/uncertainty.

row_label: GDP-4-keto-6-deoxymannose reaction

table_label: PMC HTML Table 3, Kinetic Parameters for C. crescentus GDP-perosamine Synthase

enzyme: GDP-perosamine synthase


organism: Bifidobacterium longum


enzyme_display_name: Putrescine aminotransferase

organism: Escherichia coli (strain K12)

substrate_name: putrescine

smiles: C(CCN)CN

column_label: Abstract reports that the first enzyme showed an apparent Km for putrescine of 22.5 microM.

raw_value_unit_evidence: Km raw_value=22.5 microM raw_unit=microM

row_label: putrescine-alpha-ketoglutarate transaminase / putrescine

table_label: PubMed XML abstract PMID 3510672

enzyme: Putrescine aminotransferase

substrate: putrescine


enzyme_display_name: UDP-N-acetylbacillosamine transaminase

organism: Campylobacter jejuni subsp. jejuni

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

enzyme: UDP-N-acetylbacillosamine transaminase


substrate_name: L-tryptophan

proof_lines:
L-tryptophan aminotransferase
KM 0.198 mM
kcat 0.0032 s^-1

source_databases_merged: brenda uniprot

substrate: L-tryptophan


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: KAPA (at pH 8.6 and at 37 degrees Celsius)


substrate_name: sinefungin (at pH 8.5 at room temperature)

column_label: Prose reports Km_app and kmax values for sinefungin as 0.7 +/- 0.2 mM and 0.009/sec; required metric km.

normalized_value_unit_evidence: 0.7 mM = 0.7 mM for required km.

raw_value_unit_evidence: Km_app for sinefungin = 0.7 +/- 0.2 mM; kmax = 0.009/sec.

row_label: Mtb DAPAS / sinefungin half-reaction

table_label: PMC3503319 Results prose, spectroscopic studies of Mtb DAPAS


organism: Botrytis cinerea


organism: Toxoplasma gondii

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Aspergillus niger


enzyme_display_name: UniProt P9WQ81

column_label: Prose reports Mtb DAPAS kcat 1 +/- 0.2/min and SAM Km 750 +/- 200 uM; required metrics kcat and km.

normalized_value_unit_evidence: 1 per min = 0.0167 s^-1; 750 uM = 0.75 mM. Staged 0.78 mM is within the reported +/- 200 uM uncertainty but the paper nominal value is 0.75 mM.

raw_value_unit_evidence: kcat for Mtb DAPAS = 1 +/- 0.2 per min; Km for amino donor SAM = 750 +/- 200 uM.

row_label: Mtb DAPAS / SAM amino donor

table_label: PMC3503319 Results/Introduction prose, Mtb DAPAS kinetics

enzyme: UniProt P9WQ81


substrate_name: SAM (at pH 8.5 at room temperature)

column_label: Prose reports equivalent values for SAM as 0.45 +/- 0.2 mM and 0.012/sec; required metric km.

normalized_value_unit_evidence: 0.45 mM = 0.45 mM for required km.

raw_value_unit_evidence: Equivalent values for SAM: Km_app = 0.45 +/- 0.2 mM and kmax = 0.012/sec.

row_label: Mtb DAPAS / SAM half-reaction

substrate: SAM (at pH 8.5 at room temperature)


organism: Leishmania major

column_label: Official ScienceDirect HTML Table 2 row L. major His-tagged GlcK; ATP Km column and kcat column.

normalized_value_unit_evidence: kcat=316.7 s^-1, rounds to 317 s^-1; ATP kcat/Km=316.7/0.35=904.8 s^-1 mM^-1, matching 905.714 using rounded kcat

row_label: L. major His-tagged GlcK

table_label: Table 2. Kinetic characteristics of Trypanosoma cruzi and Leishmania major recombinant glucokinases


organism: Pyrobaculum calidifontis

assay_conditions_summary: pH 8.5; 323.15 K; cofactor ATP

column_label: Kinetic parameters section, glucose experiment, printed Km/kcat/catalytic-efficiency values; Table 1, P. calidifontis row, Km towards glucose column.

raw_value_unit_evidence: Kinetic parameters prose: glucose Km 660 +/- 7 uM; kcat 289 s^-1; catalytic efficiency 437 mM^-1 s^-1. Table 1 P. calidifontis row: glucose Km 0.66 mM.

row_label: Pcal_1032 / D-glucose

table_label: Kinetic parameters section and Table 1


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y214C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


organism: Trypanosoma cruzi

assay_conditions_summary: pH 7.3; 353.15 K; cofactor ATP

column_label: Official ScienceDirect HTML Table 2 row T. cruzi His-tagged GlcK; ATP Km column and kcat column.

row_label: T. cruzi His-tagged GlcK


organism: Oryza sativa subsp. indica


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

assay_conditions_summary: pH 7.3; cofactor ATP

column_label: Table 1 reports Apparent Km (mM) for 2-deoxyglucose as 1.1 for ATP-GLK from T. maritima.

raw_value_unit_evidence: 1.1 under Apparent Km (mM) for 2-deoxyglucose

row_label: Apparent Km (mM); 2-deoxyglucose

table_label: Table 1, Biochemical and kinetic properties of ATP-GLK from T. maritima


enzyme_display_name: Peroxisomal bifunctional enzyme

assay_conditions_summary: cofactor CoA

proof_lines: Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids

enzyme: Peroxisomal bifunctional enzyme


assay_conditions_summary: pH 8.5; cofactor CoA

column_label: Results prose lines 260-266 and Fig. 4; protein LBP; substrate C16:1-CoA ((2E)-hexadecenoyl-CoA); metric apparent Km; raw value 10.4 uM; normalized Km=0.0104 mM.

raw_value_unit_evidence: Results text reports LBP apparent Km 10.4 uM for C16:1-CoA (Fig. 4).

table_label: PMID 15060085, Results prose and Fig. 4: kinetic analysis of human DBP and LBP


organism: Saccharomyces cerevisiae

substrate_name: D-Glucose

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

column_label: Table 2; reaction HXK; isoenzyme Hxk1p; parameter kcat value 10.2 s^-1; parameter Kglc value 0.15 mM; kcat/Km computed from those explicit cells

normalized_value_unit_evidence: kcat normalized_value=10.2 normalized_unit=s^-1; Km normalized_value=0.15 normalized_unit=mM; kcat/Km normalized_value=68.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.2 raw_unit=s^-1; Km raw_value=0.15 raw_unit=mM; kcat/Km computed from explicit Table 2 cells 10.2/0.15 raw_unit=s^-1*mM^-1

row_label: HXK / Hxk1p / Kglc

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

substrate: D-Glucose


column_label: Table 2; reaction HXK; isoenzyme Hxk2p; parameter kcat value 63.1 s^-1; parameter Kglc value 0.2 mM; kcat/Km computed from those explicit cells

normalized_value_unit_evidence: kcat normalized_value=63.1 normalized_unit=s^-1; Km normalized_value=0.2 normalized_unit=mM; kcat/Km normalized_value=315.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=63.1 raw_unit=s^-1; Km raw_value=0.2 raw_unit=mM; kcat/Km computed from explicit Table 2 cells 63.1/0.2 raw_unit=s^-1*mM^-1

row_label: HXK / Hxk2p / Kglc


enzyme_display_name: acetoacetyl-CoA reductase

substrate_name: acetoacetyl-CoA

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

column_label: Table 2, row Acetoacetyl-CoA, columns Km, kcat, kcat/Km; unit header row: Km uM; kcat min^-1; kcat/Km uM^-1 min^-1

normalized_value_unit_evidence: Km normalized_value=0.0634 normalized_unit=mM; kcat normalized_value=0.008333333333333333333333333333 normalized_unit=s^-1; kcat_over_km normalized_value=0.1666666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Table 2 (Reductive reactions), row Acetoacetyl-CoA: Km 63.4 +/- 7.4 uM; kcat 0.5 +/- 0.1 min^-1; kcat/Km 0.01 uM^-1 min^-1

row_label: Acetoacetyl-CoA

table_label: Table 2

enzyme: acetoacetyl-CoA reductase

substrate: acetoacetyl-CoA


organism: Escherichia coli

substrate_name: isopentenyl diphosphate

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

smiles: CC(=C)CCOP(=O)(O)OP(=O)(O)O

substrate: isopentenyl diphosphate


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


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


enzyme_display_name: glucokinase

column_label: Table 2; reaction HXK; isoenzyme Glk1p; parameter kcat value 0.0721 s^-1; parameter Kglc value 0.0106 mM; kcat/Km computed from those explicit cells

normalized_value_unit_evidence: kcat normalized_value=0.0721 normalized_unit=s^-1; Km normalized_value=0.0106 normalized_unit=mM; kcat/Km normalized_value=6.80188679245283 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.0721 raw_unit=s^-1; Km raw_value=0.0106 raw_unit=mM; kcat/Km computed from explicit Table 2 cells 0.0721/0.0106 raw_unit=s^-1*mM^-1

row_label: HXK / Glk1p / Kglc

enzyme: glucokinase


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


smiles: C(CC(=O)O)CN


enzyme_display_name: hexokinase

assay_conditions_summary: pH 7.1; cofactor ATP

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant T65I

enzyme: hexokinase


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M298K


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K140E


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S263P


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y215A


assay_conditions_summary: pH 7.1; 303.15 K; cofactor ATP

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V62M

proof_lines: mutant enzyme V62M, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol

proof_lines: mutant enzyme V62M, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant P417R


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant 454-Ala

proof_lines: pH 8.0, mutant enzyme Q466_H467insHMNLAEQ


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant E442K


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S64P


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S64Y


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214A


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214C


substrate_name: S-adenosyl-L-methionine

assay_conditions_summary: pH 9

substrate: S-adenosyl-L-methionine


proof_lines: pH 9.0, recombinant wild-type enzyme and mutant R253K


enzyme_display_name: glutamine-phenylpyruvate transaminase

organism: Rattus norvegicus

proof_lines: pH 7.0, 30°C, L-glutamine as amino group donor

enzyme: glutamine-phenylpyruvate transaminase


substrate_name: L-phenylalanine

substrate: L-phenylalanine


proof_lines: pH 8.5, 37°C, L-phenylalanine as amino group donor


substrate_name: glyoxalate

substrate: glyoxalate


substrate_name: L-methionine

smiles: CSCCC(C(=O)O)N

proof_lines:
pH 7.0, 30°C
pH 8.5, 37°C, phenylpyruvate

substrate: L-methionine


substrate_name: L-ethionine

smiles: CCSCCC(C(=O)O)N

substrate: L-ethionine


substrate_name: L-S-methylcysteine

smiles: CSCC(C(=O)O)N

substrate: L-S-methylcysteine


smiles: CCCC(=O)C(=O)O


smiles: CCC(=O)C(=O)O


substrate_name: pyruvate

substrate: pyruvate


substrate_name: D-fructose 6-phosphate

proof_lines: mutant enzyme W74L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C

substrate: D-fructose 6-phosphate


proof_lines: mutant enzyme W74A, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C


substrate_name: L-gamma-glutamyl-p-nitroanilide

substrate: L-gamma-glutamyl-p-nitroanilide


proof_lines: mutant enzyme V605L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C


proof_lines: mutant enzyme A602L, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C


substrate_name: L-glutamine

smiles: C(CC(=O)N)C(C(=O)O)N

substrate: L-glutamine


proof_lines: wild type enzyme, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C


proof_lines: mutant enzyme W74F, in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 50 mM KCl, at 37°C


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: ATP


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


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: ketohexokinase

organism: Bos taurus

proof_lines:
25°C, pH 7
25°C, pH 7.5, MgATP2-: 4mM

enzyme: ketohexokinase


substrate_name: L-ribulose

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

substrate: L-ribulose


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


substrate_name: D-xylose

substrate: D-xylose


substrate_name: D-sedoheptulose

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

substrate: D-sedoheptulose


substrate_name: D-ribono-gamma-lactone

substrate: D-ribono-gamma-lactone


mutation_signature: deletion mutant lacking residues 68-71

mutation_type: deletion

proof_lines: deletion mutant lacking residues 68-71, pH 7.6, 25°C

proof_lines: deletion mutant lacking residues 68-71, K0.5 value, Hill coefficient 1.2, pH 7.6, 25°C


mutation_signature: deletion mutant lacking residues 66-71

proof_lines: deletion mutant lacking residues 66-71, pH 7.6, 25°C

proof_lines: deletion mutant lacking residues 66-71, K0.5 value, Hill coefficient 1.2, pH 7.6, 25°C


mutation_signature: deletion mutant lacking residues 67-71

proof_lines: deletion mutant lacking residues 67-71, pH 7.6, 25°C

proof_lines: deletion mutant lacking residues 67-71, K0.5 value, Hill coefficient 1.1, pH 7.6, 25°C


mutation_signature: deletion mutant lacking residues 70-71

proof_lines: deletion mutant lacking residues 70-71, pH 7.6, 25°C

proof_lines: deletion mutant lacking residues 70-71, K0.5 value, Hill coefficient 1.3, pH 7.6, 25°C


mutation_signature: deletion mutant lacking residue 71

proof_lines: deletion mutant lacking residue 71, pH 7.6, 25°C

proof_lines: deletion mutant lacking residue 71, K0.5 value, Hill coefficient 1.5, pH 7.6, 25°C


assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


assay_conditions_summary: cofactor ATP


proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V62M

proof_lines: mutant enzyme V62M, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol


organism: Sus scrofa

substrate_name: 4-(aminomethyl)furan-3-carboxylic acid

substrate: 4-(aminomethyl)furan-3-carboxylic acid


substrate_name: 4-(aminomethyl)furan-2-carboxylic acid

substrate: 4-(aminomethyl)furan-2-carboxylic acid


substrate_name: 5-(aminomethyl)furan-2-carboxylic acid

substrate: 5-(aminomethyl)furan-2-carboxylic acid


organism: Cupriavidus necator

substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: D-hydroxybutyryl-CoA

substrate: D-hydroxybutyryl-CoA


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


enzyme_display_name: UniProt P51570

substrate_name: D-galactosamine

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P51570

substrate: D-galactosamine


enzyme_display_name: UniProt Q9R7D7

organism: Lactococcus lactis

substrate_name: alpha-D-galactose

enzyme: UniProt Q9R7D7

substrate: alpha-D-galactose


enzyme_display_name: UniProt Q7WT42

organism: Arthrobacter sp.

substrate_name: D-glucose

assay_conditions_summary: pH 7

enzyme: UniProt Q7WT42

substrate: D-glucose


substrate_name: ATP

substrate: ATP


enzyme_display_name: UniProt P06999

substrate_name: D-fructose 6-phosphate

enzyme: UniProt P06999

substrate: D-fructose 6-phosphate


enzyme_display_name: UniProt P0A796

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.2
Raw SKiD Env: Temp=55°C, pH=7

enzyme: UniProt P0A796


substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


substrate_name: sedoheptulose 7-phosphate

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

substrate: sedoheptulose 7-phosphate


enzyme_display_name: UniProt Q2FXM8

organism: Staphylococcus aureus

enzyme: UniProt Q2FXM8


enzyme_display_name: UniProt P00512

organism: Geobacillus stearothermophilus

enzyme: UniProt P00512


substrate_name: ITP

substrate: ITP


substrate_name: GTP

substrate: GTP


substrate_name: CTP

substrate: CTP


substrate_name: UTP

substrate: UTP


enzyme_display_name: UniProt Q01813

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.1
Raw SKiD Env: Temp=25°C, pH=7.2

enzyme: UniProt Q01813


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


enzyme_display_name: ATP-dependent 6-phosphofructokinase

organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)

enzyme: ATP-dependent 6-phosphofructokinase


substrate_name: ATP; D-Glucose

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

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

proof_lines: uncomplexed, hexokinase III, at 30°C, pH 7.2

substrate: ATP; D-Glucose


substrate_name: D-mannose

proof_lines:
hexokinase III, at 30°C, pH 8.1
hexokinase II, at 30°C, pH 8.1
hexokinase IV

substrate: D-mannose


substrate_name: D-glucosamine

substrate: D-glucosamine


assay_conditions_summary: pH 8.1; 303.15 K; cofactor ATP

proof_lines: uncomplexed ATP4-, hexokinase III, at 30°C, pH 7.2


substrate_name: D-fructose

substrate: D-fructose


organism: Mus musculus

substrate_name: D-Fructose 6-phosphate; ATP

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

substrate: D-Fructose 6-phosphate; ATP


organism: Pichia pastoris


substrate_name: ATP; D-Fructose 6-phosphate

substrate: ATP; D-Fructose 6-phosphate


organism: Desulfurococcus amylolyticus


assay_conditions_summary: pH 6; 323.15 K; cofactor ATP


substrate_name: ADP

assay_conditions_summary: pH 6; 358.15 K; cofactor ATP

substrate: ADP


substrate_name: D-fructose 1,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


organism: Helianthus annuus


substrate_name: ATP

assay_conditions_summary: pH 7.6; 295.15 K; cofactor ATP

substrate: ATP


organism: Homo sapiens


organism: Kluyveromyces lactis


enzyme_display_name: galactokinase

organism: Vicia faba

substrate_name: ATP; D-Galactose

assay_conditions_summary: pH 7.3; 298.15 K; cofactor ATP

proof_lines: pH 7.3, 25°C, competitive inhibition with galactose as the variable substrate

proof_lines: pH 7.3, 25°C, non-competitive with respect to ATP

proof_lines: non-competitive with respect to galactose

enzyme: galactokinase

substrate: ATP; D-Galactose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-galactosamine

substrate: D-galactosamine


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Auxenochlorella pyrenoidosa

assay_conditions_summary: pH 7.7; cofactor ATP


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


organism: Thermococcus kodakarensis

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ADP


substrate_name: D-glucose

substrate: D-glucose


substrate_name: AMP

substrate: AMP


organism: Bombus atratus


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


enzyme_display_name: mannokinase

organism: Streptomyces violaceoruber

enzyme: mannokinase


substrate_name: mannoheptulose

substrate: mannoheptulose


substrate_name: D-mannosamine

substrate: D-mannosamine


substrate_name: Unknown

substrate: Unknown


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

assay_conditions_summary: pH 7.1; cofactor ATP

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant 454-Ala

proof_lines: pH 8.0, mutant enzyme Q466_H467insHMNLAEQ


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A208G to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

column_label: Table 2 columns Mutant and Km ATP (mM), row A208G; kinetic determinations section defines ATP affinity assay.

table_label: Table 2 Kinetic parameters of mutated forms of glucokinase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A460R to reconstruct the assayed variant sequence.

column_label: Table 2 columns Mutant and Km ATP (mM), row A460R; kinetic determinations section defines ATP affinity assay.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K459L to reconstruct the assayed variant sequence.

column_label: Table 2 columns Mutant and Km ATP (mM), row K459L; kinetic determinations section defines ATP affinity assay.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C457V to reconstruct the assayed variant sequence.

column_label: Table 2 columns Mutant and Km ATP (mM), row C457V; kinetic determinations section defines ATP affinity assay.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K458R to reconstruct the assayed variant sequence.

column_label: Table 2 columns Mutant and Km ATP (mM), row K458R; kinetic determinations section defines ATP affinity assay.


organism: Streptomyces sp.

substrate_name: D-mannose

assay_conditions_summary: pH 8.4; 310.15 K; cofactor ADP

substrate: D-mannose


assay_conditions_summary: pH 8.4; 310.15 K; cofactor ATP

proof_lines:
pH 8.4, 37°C
ATP in form of MgATP2-


proof_lines: pH 8.4, 37°C, competitive versus MgAtP2-

proof_lines: pH 8.4, 37°C, noncompetitive versus mannose

proof_lines: pH 8.4, 37°C, noncompetitive versus MgATP2-


organism: Dunaliella marina


assay_conditions_summary: pH 7; cofactor ATP


organism: Haloferax volcanii

assay_conditions_summary: pH 8; 315.15 K; cofactor ATP


organism: Arthrobacter sp.

substrate_name: Hexametaphosphate

substrate: Hexametaphosphate


substrate_name: D-glucose / D-mannose

substrate: D-glucose / D-mannose


organism: Leuconostoc mesenteroides


substrate_name: D-fructose

substrate: D-fructose


organism: Austromegabalanus psittacus


organism: Tetrahymena thermophila

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Blastocladiella emersonii

substrate_name: ATP; D-Fructose 6-phosphate

substrate: ATP; D-Fructose 6-phosphate


organism: Selenastrum minutum


organism: Trachemys scripta


assay_conditions_summary: pH 7; 279.15 K; cofactor ATP

proof_lines: pH 7.0, 20°C, normoxic and anoxic animals


proof_lines:
pH 7.0, 6°C, normoxic animals
pH 7.0, 6°C, anoxic animals
pH 7.0, 20°C, anoxic animals


organism: Monoraphidium minutum

assay_conditions_summary: pH 7.25; 298.15 K; cofactor ATP


organism: Bacillus methanolicus

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

assay_conditions_summary: pH 9; cofactor ATP

proof_lines:
strain PB1, Pfk2, pH 9.0, 30°C
strain MGA3, Pfk2, pH 9.0, 30°C


proof_lines:
strain MGA3, Pfk2, pH 9.0, 30°C
strain PB1, Pfk2, pH 9.0, 30°C


organism: Pseudomonas doudoroffii


organism: Zapus hudsonius


enzyme_display_name: Galactokinase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: alpha-D-galactose

proof_lines: kcat is 11.7 sec(-1) for alpha-D-galactose and 8.7 sec(-1) for ATP utilization.

enzyme: Galactokinase

substrate: alpha-D-galactose


substrate_name: ATP

substrate: ATP


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E190Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.2; cofactor ATP

proof_lines: mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication

proof_lines: mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R171E with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


organism: Escherichia coli (strain K12)

column_label: Article text line 64 reports Km for galactose 2.1 mM; reference note line 196 describes the galactose Km assay setup.

normalized_value_unit_evidence: Km=2.1 mM

raw_value_unit_evidence: Km for galactose 2.1 mM

row_label: galactose

table_label: Main article kinetic prose


column_label: Article text line 70 maps compound 2 to 2-deoxy-D-galactose; line 76 reports compound 2 Km 3.6 mM.

normalized_value_unit_evidence: Km=3.6 mM

raw_value_unit_evidence: Km for compound 2 is 3.6 mM

row_label: compound 2; 2-deoxy-D-galactose


column_label: Article text line 70 maps compound 3 to 2-amino-deoxy-D-galactose; line 76 reports compound 3 Km 2.9 mM.

normalized_value_unit_evidence: Km=2.9 mM

raw_value_unit_evidence: Km for compound 3 is 2.9 mM

row_label: compound 3; 2-amino-deoxy-D-galactose


column_label: Article text line 64 reports Km for ATP 2.5 mM; reference note line 196 describes the ATP Km assay setup.

normalized_value_unit_evidence: Km=2.5 mM

raw_value_unit_evidence: Km for ATP 2.5 mM

row_label: ATP


organism: Klebsiella aerogenes

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

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, 25, at a Mg2+/ATP ratio of 1.4/1

proof_lines: pH 8.0, 25, at a Mg2+/ATP ratio of 0.7/1


enzyme_display_name: glucosamine kinase

organism: Mycolicibacterium smegmatis

substrate_name: D-glucosamine

proof_lines: pH and temperature not specified in the publication

enzyme: glucosamine kinase

substrate: D-glucosamine


organism: Trypanosoma brucei

assay_conditions_summary: pH 6.7; cofactor ATP

proof_lines: pH 6.7, 37°C, at 0.25 mM fructose 6-phosphate

proof_lines: pH 6.7, 37°C, at 0.4 mM fructose 6-phosphate

proof_lines: pH 6.7, 37°C, at 0.75 mM fructose 6-phosphate


organism: Pyrococcus horikoshii

substrate_name: D-galactose

assay_conditions_summary: pH 7.5; 323.00 K; cofactor ATP

proof_lines:
in 50 mM HEPES-NaOH pH 7.5, at 50°C
kcat is 0.91 sec(-1).

substrate: D-galactose


organism: Streptacidiphilus jiangxiensis


organism: Aeropyrum pernix

substrate_name: D-Fructose 6-phosphate; ATP

substrate: D-Fructose 6-phosphate; ATP


organism: Amycolatopsis methanolica


organism: Aspergillus niger


organism: Bacillus macquariensis


organism: Dictyostelium discoideum


organism: Fasciola hepatica

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 8

proof_lines:
pH 8.0, phosphorylated PFK
pH 8.0, native PFK

substrate: D-fructose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D127S with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


organism: Lactobacillus delbrueckii subsp. bulgaricus


organism: Lactobacillus plantarum


organism: Lactococcus lactis subsp. lactis


organism: Leishmania donovani


organism: Oryctolagus cuniculus


organism: Rattus norvegicus


enzyme_display_name: Gluconokinase

organism: Gluconobacter oxydans (strain 621H)

substrate_name: gluconate

enzyme: Gluconokinase

substrate: gluconate


organism: Saccharomyces cerevisiae


organism: Schistosoma mansoni


organism: Schizosaccharomyces pombe


organism: Spinacia oleracea


organism: Homo sapiens

substrate_name: ATP; D-Galactose

substrate: ATP; D-Galactose


organism: Escherichia coli


organism: Geobacillus stearothermophilus


enzyme_display_name: ATP-dependent 6-phosphofructokinase isozyme 2

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


enzyme_display_name: ATP-dependent 6-phosphofructokinase 2

organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

enzyme: ATP-dependent 6-phosphofructokinase 2


organism: Ustilago maydis


organism: Arabidopsis thaliana


substrate_name: D-Galactose; ATP

proof_lines: kcat is 108 min(-1), 30 min(-1) and 11.7 min(-1) with D-galactose, 2-deoxy-D-galactose, and D-galactosamine as substrate, respectively.

substrate: D-Galactose; ATP


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


organism: Vibrio cholerae

substrate_name: D-Glucosamine; ATP

substrate: D-Glucosamine; ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51570 and applied mutation signature M185L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

column_label: Table 4: Kinetic parameters of selected variants with substrates other than galactose (ChemBioChem 2018, 19(10):1088-1095), Table 4, sugar 2-deoxy-D-galactose block, entry number 14, variant M185L; column 'KM SUGAR (uM)' = 7400; column 'KCAT (S-1)' = 0.4; column 'KCAT /KM SUGAR (MM-1S-1)' = 0.06.

normalized_value_unit_evidence: Km: printed cell 7400 uM; 1 uM is 0.001 mM, so 7400 / 1000 = 7.4 mM. kcat: printed cell 0.4 s^-1; this is already the canonical kcat unit and no unit conversion applies, so the canonical value is 0.4 s^(-1). kcat/Km: printed cell 0.06 mM^-1 s^-1; mM^-1 s^-1 is the canonical efficiency unit written in the other order and no unit conversion applies, so the canonical value is 0.06 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Table 4, sugar 2-deoxy-D-galactose block, entry number 14, variant M185L: printed KM SUGAR (uM) cell 7400; printed KCAT (S-1) cell 0.4; printed KCAT /KM SUGAR (MM-1S-1) cell 0.06.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51570 and applied mutation signature M60V/M180V/D268E/A334S/R366Q/G373S/Y379W to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic parameters of selected variants with substrates other than galactose (ChemBioChem 2018, 19(10):1088-1095), Table 4, sugar 2-deoxy-D-galactose block, entry number 17, variant M60V/M180V/D268E/A334S/R366Q/G373S/Y379W; column 'KM SUGAR (uM)' = 2000; column 'KCAT (S-1)' = 6.8; column 'KCAT /KM SUGAR (MM-1S-1)' = 3.1.

normalized_value_unit_evidence: Km: printed cell 2000 uM; 1 uM is 0.001 mM, so 2000 / 1000 = 2.0 mM. kcat: printed cell 6.8 s^-1; this is already the canonical kcat unit and no unit conversion applies, so the canonical value is 6.8 s^(-1). kcat/Km: printed cell 3.1 mM^-1 s^-1; mM^-1 s^-1 is the canonical efficiency unit written in the other order and no unit conversion applies, so the canonical value is 3.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Table 4, sugar 2-deoxy-D-galactose block, entry number 17, variant M60V/M180V/D268E/A334S/R366Q/G373S/Y379W: printed KM SUGAR (uM) cell 2000; printed KCAT (S-1) cell 6.8; printed KCAT /KM SUGAR (MM-1S-1) cell 3.1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51570 and applied mutation signature Y379W to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic parameters of selected variants with substrates other than galactose (ChemBioChem 2018, 19(10):1088-1095), Table 4, sugar 2-deoxy-D-galactose block, entry number 15, variant Y379W; column 'KM SUGAR (uM)' = 2200; column 'KCAT (S-1)' = 0.8; column 'KCAT /KM SUGAR (MM-1S-1)' = 0.39.

normalized_value_unit_evidence: Km: printed cell 2200 uM; 1 uM is 0.001 mM, so 2200 / 1000 = 2.2 mM. kcat: printed cell 0.8 s^-1; this is already the canonical kcat unit and no unit conversion applies, so the canonical value is 0.8 s^(-1). kcat/Km: printed cell 0.39 mM^-1 s^-1; mM^-1 s^-1 is the canonical efficiency unit written in the other order and no unit conversion applies, so the canonical value is 0.39 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Table 4, sugar 2-deoxy-D-galactose block, entry number 15, variant Y379W: printed KM SUGAR (uM) cell 2200; printed KCAT (S-1) cell 0.8; printed KCAT /KM SUGAR (MM-1S-1) cell 0.39.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A334S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51570 and applied mutation signature D268E to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of consensus variants of human galactokinase (ChemBioChem 2018, 19(10):1088-1095), Table 1, entry number 4, variant D268E, galactose columns; column 'Km, Gal (uM)' = 580; column 'kcat (s-1)' = 3.2; column 'kcat /Km,Gal (mM-1s-1)' = 6.0.

normalized_value_unit_evidence: Km: printed cell 580 uM; 1 uM is 0.001 mM, so 580 / 1000 = 0.58 mM. kcat: printed cell 3.2 s^-1; this is already the canonical kcat unit and no unit conversion applies, so the canonical value is 3.2 s^(-1). kcat/Km: printed cell 6.0 mM^-1 s^-1; mM^-1 s^-1 is the canonical efficiency unit written in the other order and no unit conversion applies, so the canonical value is 6.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Table 1, entry number 4, variant D268E, galactose columns: printed Km, Gal (uM) cell 580; printed kcat (s-1) cell 3.2; printed kcat /Km,Gal (mM-1s-1) cell 6.0.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature G373S to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 7 row G373S; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=2.4 s^-1; Km=0.09 mM; kcat/Km=25 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 7 row G373S: kcat=2.4 s^-1; Km,Gal=90 uM; kcat/Km,Gal=25 mM^-1 s^-1.

row_label: entry 7 / G373S

table_label: Table 1


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M180V to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 3 row M180V; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=1 s^-1; Km=0.099 mM; kcat/Km=10.1 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 3 row M180V: kcat=1 s^-1; Km,Gal=99 uM; kcat/Km,Gal=10.1 mM^-1 s^-1.

row_label: entry 3 / M180V


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M185L to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 14 row M185L; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=8.1 s^-1; Km=1.19 mM; kcat/Km=8 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 14 row M185L: kcat=8.1 s^-1; Km,Gal=1190 uM; kcat/Km,Gal=8 mM^-1 s^-1.

row_label: entry 14 / M185L


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M185L/Y379W to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 16 row M185L/Y379W; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=2.5 s^-1; Km=1.12 mM; kcat/Km=2.4 s^-1 mM^-1.


organism: Bacillus licheniformis

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ATP


organism: Fasciola hepatica

proof_lines:
pH 8.0, native PFK
pH 8.0, phosphorylated PFK


organism: Gallus gallus


organism: Lactobacillus acidophilus


organism: Mus musculus


organism: Streptococcus thermophilus

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


organism: Streptomyces coelicolor


organism: Thermotoga maritima


organism: Trypanosoma brucei brucei


organism: Trypanosoma cruzi


enzyme_display_name: L-Rhamnulokinase

organism: Escherichia coli (strain K12)

substrate_name: beta-L-fructose (at pH 8)

enzyme: L-Rhamnulokinase

substrate: beta-L-fructose (at pH 8)


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature Y379W to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 15 row Y379W; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=6.8 s^-1; Km=1.32 mM; kcat/Km=5.2 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 15 row Y379W: kcat=6.8 s^-1; Km,Gal=1320 uM; kcat/Km,Gal=5.2 mM^-1 s^-1.

row_label: entry 15 / Y379W


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature A334S to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 5 row A334S; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 5 row A334S: kcat=4.3 s^-1; Km,ATP=7.9 uM; kcat/Km,ATP=550 mM^-1 s^-1.

row_label: entry 5 / A334S


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature D268E to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 4 row D268E; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

normalized_value_unit_evidence: normalized: kcat=3.2 s^-1; Km=0.013 mM; kcat/Km=240 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 4 row D268E: kcat=3.2 s^-1; Km,ATP=13 uM; kcat/Km,ATP=240 mM^-1 s^-1.

row_label: entry 4 / D268E


column_label: PMID 29505688 Table 1; entry 7 row G373S; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

normalized_value_unit_evidence: normalized: kcat=2.4 s^-1; Km=0.013 mM; kcat/Km=190 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 7 row G373S: kcat=2.4 s^-1; Km,ATP=13 uM; kcat/Km,ATP=190 mM^-1 s^-1.


column_label: PMID 29505688 Table 1; entry 3 row M180V; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

normalized_value_unit_evidence: normalized: kcat=1 s^-1; Km=0.0054 mM; kcat/Km=185 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 3 row M180V: kcat=1 s^-1; Km,ATP=5.4 uM; kcat/Km,ATP=185 mM^-1 s^-1.


column_label: PMID 29505688 Table 1; entry 14 row M185L; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 14 row M185L: kcat=8.1 s^-1; Km,ATP=34.5 uM; kcat/Km,ATP=236 mM^-1 s^-1.


column_label: PMID 29505688 Table 1; entry 16 row M185L/Y379W; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M60V to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 2 row M60V; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

normalized_value_unit_evidence: normalized: kcat=4.8 s^-1; Km=0.018 mM; kcat/Km=270 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 2 row M60V: kcat=4.8 s^-1; Km,ATP=18 uM; kcat/Km,ATP=270 mM^-1 s^-1.

row_label: entry 2 / M60V


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M60V/A334S to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 9 row M60V/A334S; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 9 row M60V/A334S: kcat=2.6 s^-1; Km,ATP=4.2 uM; kcat/Km,ATP=620 mM^-1 s^-1.

row_label: entry 9 / M60V/A334S


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M60V/M180V to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 8 row M60V/M180V; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 8 row M60V/M180V: kcat=1.5 s^-1; Km,ATP=1 uM; kcat/Km,ATP=1430 mM^-1 s^-1.

row_label: entry 8 / M60V/M180V


column_label: PMID 29505688 Table 1; entry 2 row M60V; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=4.8 s^-1; Km=0.22 mM; kcat/Km=21.8 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 2 row M60V: kcat=4.8 s^-1; Km,Gal=220 uM; kcat/Km,Gal=21.8 mM^-1 s^-1.


column_label: PMID 29505688 Table 1; entry 9 row M60V/A334S; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=2.6 s^-1; Km=0.48 mM; kcat/Km=5.4 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 9 row M60V/A334S: kcat=2.6 s^-1; Km,Gal=480 uM; kcat/Km,Gal=5.4 mM^-1 s^-1.


column_label: PMID 29505688 Table 1; entry 8 row M60V/M180V; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=1.5 s^-1; Km=0.19 mM; kcat/Km=8.8 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 8 row M60V/M180V: kcat=1.5 s^-1; Km,Gal=190 uM; kcat/Km,Gal=8.8 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M60V/M180V/A334S to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 10 row M60V/M180V/A334S; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=1.7 s^-1; Km=0.078 mM; kcat/Km=20 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 10 row M60V/M180V/A334S: kcat=1.7 s^-1; Km,Gal=78 uM; kcat/Km,Gal=20 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M60V/M180V/A334S/D268E/G373S to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 12 row M60V/M180V/A334S/D268E/G373S; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=1.7 s^-1; Km=0.27 mM; kcat/Km=6.3 s^-1 mM^-1.


sequence_variant_note: Mutation signature M60V/M180V/A334S/D268E/R336Q/G373S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M60V/M180V/A334S/G373S to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 11 row M60V/M180V/A334S/G373S; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=1.7 s^-1; Km=0.23 mM; kcat/Km=7.3 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M60V/M180V/D268E/A334S/R366Q/G373S/Y379W to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 17 row M60V/M180V/D268E/A334S/R366Q/G373S/Y379W; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=5 s^-1; Km=0.31 mM; kcat/Km=16.1 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 18 row M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature R366Q to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 1; entry 6 row R366Q; columns kcat (s^-1), Km,Gal (uM), and kcat/Km,Gal (mM^-1 s^-1); substrate axis alpha-D-galactose.

normalized_value_unit_evidence: normalized: kcat=2.1 s^-1; Km=0.53 mM; kcat/Km=4 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 6 row R366Q: kcat=2.1 s^-1; Km,Gal=530 uM; kcat/Km,Gal=4 mM^-1 s^-1.

row_label: entry 6 / R366Q


column_label: PMID 29505688 Table 1; entry 10 row M60V/M180V/A334S; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.


column_label: PMID 29505688 Table 1; entry 12 row M60V/M180V/A334S/D268E/G373S; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51570 and applied mutation signature M60V/M180V/A334S/D268E/R366Q/G373S to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of consensus variants of human galactokinase (ChemBioChem 2018, 19(10):1088-1095), Table 1, entry number 13, the hexa-variant carrying all six return-to-consensus changes, ATP columns; column 'Km, ATP (uM)' = 3.8; column 'kcat (s-1)' = 1.6; column 'kcat /Km, ATP (mM-1s-1)' = 390.

normalized_value_unit_evidence: Km: printed cell 3.8 uM; 1 uM is 0.001 mM, so 3.8 / 1000 = 0.0038 mM. kcat: printed cell 1.6 s^-1; this is already the canonical kcat unit and no unit conversion applies, so the canonical value is 1.6 s^(-1). kcat/Km: printed cell 390 mM^-1 s^-1; mM^-1 s^-1 is the canonical efficiency unit written in the other order and no unit conversion applies, so the canonical value is 390.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Table 1, entry number 13, the hexa-variant carrying all six return-to-consensus changes, ATP columns: printed Km, ATP (uM) cell 3.8; printed kcat (s-1) cell 1.6; printed kcat /Km, ATP (mM-1s-1) cell 390.


column_label: PMID 29505688 Table 1; entry 11 row M60V/M180V/A334S/G373S; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.


column_label: PMID 29505688 Table 1; entry 17 row M60V/M180V/D268E/A334S/R366Q/G373S/Y379W; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

normalized_value_unit_evidence: normalized: kcat=5 s^-1; Km=0.0081 mM; kcat/Km=550 s^-1 mM^-1.


column_label: PMID 29505688 Table 1; entry 18 row M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.


column_label: PMID 29505688 Table 1; entry 6 row R366Q; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 6 row R366Q: kcat=2.1 s^-1; Km,ATP=7.7 uM; kcat/Km,ATP=270 mM^-1 s^-1.


column_label: PMID 29505688 Table 1; entry 15 row Y379W; columns kcat (s^-1), Km,ATP (uM), and kcat/Km,ATP (mM^-1 s^-1); substrate axis ATP.

raw_value_unit_evidence: PMID 29505688 Table 1 entry 15 row Y379W: kcat=6.8 s^-1; Km,ATP=5 uM; kcat/Km,ATP=1360 mM^-1 s^-1.


substrate_name: D-Talose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M60V/M180V/D268E/A334S/R366Q/G373S/Y379W to reconstruct the assayed variant sequence.

substrate: D-Talose


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


substrate_name: D-Galactosamine

sequence_variant_note: Resolved canonical sequence from uniprotkb:P51570 and applied mutation signature M185L/Y379W to reconstruct the assayed variant sequence.

column_label: PMID 29505688 Table 4; sugar block D-Galactosamine; entry 16 row M185L/Y379W; columns KCAT (S^-1), KM SUGAR (uM), and KCAT/KM SUGAR (mM^-1 s^-1).

normalized_value_unit_evidence: normalized: kcat=25 s^-1; Km=0.27 mM; kcat/Km=91 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 4 sugar block D-Galactosamine, entry 16 row M185L/Y379W: kcat=25 s^-1; Km,sugar=270 uM; kcat/Km,sugar=91 mM^-1 s^-1.

row_label: D-Galactosamine / entry 16 / M185L/Y379W

table_label: Table 4

substrate: D-Galactosamine


column_label: PMID 29505688 Table 4; sugar block D-Galactosamine; entry 17 row M60V/M180V/D268E/A334S/R366Q/G373S/Y379W; columns KCAT (S^-1), KM SUGAR (uM), and KCAT/KM SUGAR (mM^-1 s^-1).

normalized_value_unit_evidence: normalized: kcat=4 s^-1; Km=4.8 mM; kcat/Km=0.9 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 4 sugar block D-Galactosamine, entry 17 row M60V/M180V/D268E/A334S/R366Q/G373S/Y379W: kcat=4 s^-1; Km,sugar=4800 uM; kcat/Km,sugar=0.9 mM^-1 s^-1.

row_label: D-Galactosamine / entry 17 / M60V/M180V/D268E/A334S/R366Q/G373S/Y379W


column_label: PMID 29505688 Table 4; sugar block D-Galactosamine; entry 18 row M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W; columns KCAT (S^-1), KM SUGAR (uM), and KCAT/KM SUGAR (mM^-1 s^-1).

normalized_value_unit_evidence: normalized: kcat=0.3 s^-1; Km=0.62 mM; kcat/Km=0.4 s^-1 mM^-1.

raw_value_unit_evidence: PMID 29505688 Table 4 sugar block D-Galactosamine, entry 18 row M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W: kcat=0.3 s^-1; Km,sugar=620 uM; kcat/Km,sugar=0.4 mM^-1 s^-1.

row_label: D-Galactosamine / entry 18 / M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y379W to reconstruct the assayed variant sequence.

column_label: Table 4; row_label: Wild type / D-Galactosamine; columns kcat (s^-1), Km sugar (uM), kcat/Km sugar (mM^-1 s^-1)

normalized_value_unit_evidence: normalized: kcat=1.7 s^-1; Km=0.71 mM; kcat/Km=2.9 s^-1 mM^-1

raw_value_unit_evidence: paper Table 4 cells for Wild type / D-Galactosamine: kcat=1.7 s^-1; Km=710 uM; kcat/Km=2.9 mM^-1 s^-1

row_label: Wild type / D-Galactosamine


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


enzyme_display_name: UniProt P51570

substrate_name: D-talose

proof_lines: ATP galactokinase

substrate: D-talose


column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row Wild-type; substrate ATP; columns kcat (s^-1), Km,ATP (uM), kcat/Km,ATP (10^5 x L mol^-1 s^-1); normalized cells kcat=8.7 s^-1, Km=0.034 mM, kcat/Km=260.0 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=8.7 normalized_unit=s^-1; Km normalized_value=0.034 normalized_unit=mM; kcat/Km normalized_value=260.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 8.7 +/- 0.5 s^-1; Km,gal 970 +/- 220 uM; Km,ATP 34 +/- 4 uM; kcat/Km,gal 8900 +/- 2900 L mol^-1 s^-1; kcat/Km,ATP 2.6 +/- 0.4 x 10^5 L mol^-1 s^-1; selected substrate ATP uses Km,ATP and kcat/Km,ATP columns.

row_label: Wild-type / ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A198V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row A198V; substrate ATP; columns kcat (s^-1), Km,ATP (uM), kcat/Km,ATP (10^5 x L mol^-1 s^-1); normalized cells kcat=5.9 s^-1, Km=0.026 mM, kcat/Km=230.0 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=5.9 normalized_unit=s^-1; Km normalized_value=0.026 normalized_unit=mM; kcat/Km normalized_value=230.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 5.9 +/- 0.1 s^-1; Km,gal 660 +/- 220 uM; Km,ATP 26 +/- 1 uM; kcat/Km,gal 8500 +/- 4000 L mol^-1 s^-1; kcat/Km,ATP 2.3 +/- 0.2 x 10^5 L mol^-1 s^-1; selected substrate ATP uses Km,ATP and kcat/Km,ATP columns.

row_label: A198V / ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G346S to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row G346S; substrate ATP; columns kcat (s^-1), Km,ATP (uM), kcat/Km,ATP (10^5 x L mol^-1 s^-1); normalized cells kcat=0.4 s^-1, Km=0.005 mM, kcat/Km=87.0 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.4 normalized_unit=s^-1; Km normalized_value=0.005 normalized_unit=mM; kcat/Km normalized_value=87.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 0.4 +/- 0.04 s^-1; Km,gal 1100 +/- 160 uM; Km,ATP 5 +/- 2 uM; kcat/Km,gal 400 +/- 96 L mol^-1 s^-1; kcat/Km,ATP 0.87 +/- 0.37 x 10^5 L mol^-1 s^-1; selected substrate ATP uses Km,ATP and kcat/Km,ATP columns.

row_label: G346S / ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G347S to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row G347S; substrate ATP; columns kcat (s^-1), Km,ATP (uM), kcat/Km,ATP (10^5 x L mol^-1 s^-1); normalized cells kcat=1.1 s^-1, Km=0.089 mM, kcat/Km=12.0 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=1.1 normalized_unit=s^-1; Km normalized_value=0.089 normalized_unit=mM; kcat/Km normalized_value=12.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 1.1 +/- 0.2 s^-1; Km,gal 13000 +/- 2000 uM; Km,ATP 89 +/- 34 uM; kcat/Km,gal 85 +/- 21 L mol^-1 s^-1; kcat/Km,ATP 0.12 +/- 0.07 x 10^5 L mol^-1 s^-1; selected substrate ATP uses Km,ATP and kcat/Km,ATP columns.

row_label: G347S / ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G349S to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row G349S; substrate ATP; columns kcat (s^-1), Km,ATP (uM), kcat/Km,ATP (10^5 x L mol^-1 s^-1); normalized cells kcat=1.8 s^-1, Km=0.039 mM, kcat/Km=46.0 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=1.8 normalized_unit=s^-1; Km normalized_value=0.039 normalized_unit=mM; kcat/Km normalized_value=46.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 1.8 +/- 0.1 s^-1; Km,gal 1700 +/- 480 uM; Km,ATP 39 +/- 4 uM; kcat/Km,gal 1100 +/- 380 L mol^-1 s^-1; kcat/Km,ATP 0.46 +/- 0.07 x 10^5 L mol^-1 s^-1; selected substrate ATP uses Km,ATP and kcat/Km,ATP columns.

row_label: G349S / ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51570 and applied mutation signature H44Y to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants of disease-causing mutations in GALK1 (Eur. J. Biochem. 2003, volume 270, pages 1767-1774); printed column heads Enzyme | kcat (s^-1) | Km,gal (uM) | Km,ATP (uM) | kcat/Km,gal (M^-1 s^-1) | kcat/Km,ATP (10^5 x M^-1 s^-1). Table 1, enzyme row H44Y, ATP tuple; column kcat (s^-1) = 2.0; column Km,ATP (uM) = 130; column kcat/Km,ATP (10^5 x M^-1 s^-1) = 0.15. captured primary segment: H44Y | kcat 2.0 s^-1 | Km,ATP 130 uM | kcat/Km,ATP 0.15 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 2.0 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 2.0 s^(-1). Km: printed Table 1 Km,ATP cell 130 uM; 1 uM is 1/1000 mM, so 130 / 1000 = 0.13 mM. kcat/Km: printed Table 1 kcat/Km,ATP cell 0.15 under the column head kcat/Km,ATP (10^5 x M^-1 s^-1), that is 0.15 x 10^5 M^-1 s^-1 = 15000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 15000 / 1000 = 15.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.0 / 0.13 = 15.384615384615383 s^-1 mM^-1, against the printed efficiency cell 15.0 s^-1 mM^-1, which is that quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 1, enzyme row H44Y, ATP tuple: kcat = 2.0 s^-1; Km,ATP = 130 uM; printed kcat/Km,ATP = 0.15 x 10^5 M^-1 s^-1 (the cell prints 0.15 under the column head kcat/Km,ATP (10^5 x M^-1 s^-1)).

row_label: Table 1, enzyme row H44Y, ATP tuple (kcat, Km,ATP, kcat/Km,ATP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51570 and applied mutation signature R68C to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants of disease-causing mutations in GALK1 (Eur. J. Biochem. 2003, volume 270, pages 1767-1774); printed column heads Enzyme | kcat (s^-1) | Km,gal (uM) | Km,ATP (uM) | kcat/Km,gal (M^-1 s^-1) | kcat/Km,ATP (10^5 x M^-1 s^-1). Table 1, enzyme row R68C, ATP tuple; column kcat (s^-1) = 3.9; column Km,ATP (uM) = 110; column kcat/Km,ATP (10^5 x M^-1 s^-1) = 0.35. captured primary segment: R68C | kcat 3.9 s^-1 | Km,ATP 110 uM | kcat/Km,ATP 0.35 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 3.9 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 3.9 s^(-1). Km: printed Table 1 Km,ATP cell 110 uM; 1 uM is 1/1000 mM, so 110 / 1000 = 0.11 mM. kcat/Km: printed Table 1 kcat/Km,ATP cell 0.35 under the column head kcat/Km,ATP (10^5 x M^-1 s^-1), that is 0.35 x 10^5 M^-1 s^-1 = 35000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 35000 / 1000 = 35.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.9 / 0.11 = 35.45454545454545 s^-1 mM^-1, against the printed efficiency cell 35.0 s^-1 mM^-1, which is that quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 1, enzyme row R68C, ATP tuple: kcat = 3.9 s^-1; Km,ATP = 110 uM; printed kcat/Km,ATP = 0.35 x 10^5 M^-1 s^-1 (the cell prints 0.35 under the column head kcat/Km,ATP (10^5 x M^-1 s^-1)).

row_label: Table 1, enzyme row R68C, ATP tuple (kcat, Km,ATP, kcat/Km,ATP)


substrate_name: D-Galactose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51570 and applied mutation signature A198V to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants of disease-causing mutations in GALK1 (Eur. J. Biochem. 2003, volume 270, pages 1767-1774); printed column heads Enzyme | kcat (s^-1) | Km,gal (uM) | Km,ATP (uM) | kcat/Km,gal (M^-1 s^-1) | kcat/Km,ATP (10^5 x M^-1 s^-1). Table 1, enzyme row A198V, galactose tuple; column kcat (s^-1) = 5.9; column Km,gal (uM) = 660; column kcat/Km,gal (M^-1 s^-1) = 8500. captured primary segment: A198V | kcat 5.9 s^-1 | Km,gal 660 uM | kcat/Km,gal 8500 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 5.9 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 5.9 s^(-1). Km: printed Table 1 Km,gal cell 660 uM; 1 uM is 1/1000 mM, so 660 / 1000 = 0.66 mM. kcat/Km: printed Table 1 kcat/Km,gal cell 8500 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8500 / 1000 = 8.5 s^(-1)*mM^(-1). Quotient disclosure for this row: 5.9 / 0.66 = 8.93939393939394 s^-1 mM^-1, against the printed efficiency cell 8.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme row A198V, galactose tuple: kcat = 5.9 s^-1; Km,gal = 660 uM; printed kcat/Km,gal = 8500 M^-1 s^-1.

row_label: Table 1, enzyme row A198V, galactose tuple (kcat, Km,gal, kcat/Km,gal)

substrate: D-Galactose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51570 and applied mutation signature G346S to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants of disease-causing mutations in GALK1 (Eur. J. Biochem. 2003, volume 270, pages 1767-1774); printed column heads Enzyme | kcat (s^-1) | Km,gal (uM) | Km,ATP (uM) | kcat/Km,gal (M^-1 s^-1) | kcat/Km,ATP (10^5 x M^-1 s^-1). Table 1, enzyme row G346S, galactose tuple; column kcat (s^-1) = 0.4; column Km,gal (uM) = 1100; column kcat/Km,gal (M^-1 s^-1) = 400. captured primary segment: G346S | kcat 0.4 s^-1 | Km,gal 1100 uM | kcat/Km,gal 400 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 0.4 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 0.4 s^(-1). Km: printed Table 1 Km,gal cell 1100 uM; 1 uM is 1/1000 mM, so 1100 / 1000 = 1.1 mM. kcat/Km: printed Table 1 kcat/Km,gal cell 400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 400 / 1000 = 0.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.4 / 1.1 = 0.36363636363636365 s^-1 mM^-1, against the printed efficiency cell 0.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme row G346S, galactose tuple: kcat = 0.4 s^-1; Km,gal = 1100 uM; printed kcat/Km,gal = 400 M^-1 s^-1.

row_label: Table 1, enzyme row G346S, galactose tuple (kcat, Km,gal, kcat/Km,gal)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E244S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E245S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L231S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q242S to reconstruct the assayed variant sequence.


column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row G347S; substrate D-Galactose; columns kcat (s^-1), Km,gal (uM), kcat/Km,gal (L mol^-1 s^-1); normalized cells kcat=1.1 s^-1, Km=13.0 mM, kcat/Km=0.085 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=1.1 normalized_unit=s^-1; Km normalized_value=13.0 normalized_unit=mM; kcat/Km normalized_value=0.085 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 1.1 +/- 0.2 s^-1; Km,gal 13000 +/- 2000 uM; Km,ATP 89 +/- 34 uM; kcat/Km,gal 85 +/- 21 L mol^-1 s^-1; kcat/Km,ATP 0.12 +/- 0.07 x 10^5 L mol^-1 s^-1; selected substrate D-Galactose uses Km,gal and kcat/Km,gal columns.

row_label: G347S / D-Galactose


column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row G349S; substrate D-Galactose; columns kcat (s^-1), Km,gal (uM), kcat/Km,gal (L mol^-1 s^-1); normalized cells kcat=1.8 s^-1, Km=1.7 mM, kcat/Km=1.1 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=1.8 normalized_unit=s^-1; Km normalized_value=1.7 normalized_unit=mM; kcat/Km normalized_value=1.1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 1.8 +/- 0.1 s^-1; Km,gal 1700 +/- 480 uM; Km,ATP 39 +/- 4 uM; kcat/Km,gal 1100 +/- 380 L mol^-1 s^-1; kcat/Km,ATP 0.46 +/- 0.07 x 10^5 L mol^-1 s^-1; selected substrate D-Galactose uses Km,gal and kcat/Km,gal columns.

row_label: G349S / D-Galactose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H44Y to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row H44Y; substrate D-Galactose; columns kcat (s^-1), Km,gal (uM), kcat/Km,gal (L mol^-1 s^-1); normalized cells kcat=2.0 s^-1, Km=7.7 mM, kcat/Km=0.27 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=2.0 normalized_unit=s^-1; Km normalized_value=7.7 normalized_unit=mM; kcat/Km normalized_value=0.27 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 2.0 +/- 0.1 s^-1; Km,gal 7700 +/- 4400 uM; Km,ATP 130 +/- 9 uM; kcat/Km,gal 270 +/- 240 L mol^-1 s^-1; kcat/Km,ATP 0.15 +/- 0.02 x 10^5 L mol^-1 s^-1; selected substrate D-Galactose uses Km,gal and kcat/Km,gal columns.

row_label: H44Y / D-Galactose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R68C to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row R68C; substrate D-Galactose; columns kcat (s^-1), Km,gal (uM), kcat/Km,gal (L mol^-1 s^-1); normalized cells kcat=3.9 s^-1, Km=0.43 mM, kcat/Km=11.0 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=3.9 normalized_unit=s^-1; Km normalized_value=0.43 normalized_unit=mM; kcat/Km normalized_value=11.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 3.9 +/- 0.8 s^-1; Km,gal 430 +/- 150 uM; Km,ATP 110 +/- 35 uM; kcat/Km,gal 11000 +/- 5600 L mol^-1 s^-1; kcat/Km,ATP 0.35 +/- 0.18 x 10^5 L mol^-1 s^-1; selected substrate D-Galactose uses Km,gal and kcat/Km,gal columns.

row_label: R68C / D-Galactose


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

column_label: Table 1. Kinetic parameters of wild-type human galactokinase and disease-causing mutants; row Wild-type; substrate D-Galactose; columns kcat (s^-1), Km,gal (uM), kcat/Km,gal (L mol^-1 s^-1); normalized cells kcat=8.7 s^-1, Km=0.97 mM, kcat/Km=8.9 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=8.7 normalized_unit=s^-1; Km normalized_value=0.97 normalized_unit=mM; kcat/Km normalized_value=8.9 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat 8.7 +/- 0.5 s^-1; Km,gal 970 +/- 220 uM; Km,ATP 34 +/- 4 uM; kcat/Km,gal 8900 +/- 2900 L mol^-1 s^-1; kcat/Km,ATP 2.6 +/- 0.4 x 10^5 L mol^-1 s^-1; selected substrate D-Galactose uses Km,gal and kcat/Km,gal columns.

row_label: Wild-type / D-Galactose


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: fructose 6-phosphate

column_label: Table 1; row Pfk A / F6P; column K1/2 (Km) (mM); raw cell 0.4 ± 0.1; normalized Km 0.4 mM

normalized_value_unit_evidence: Km=0.4 mM

row_label: Pfk A / F6P

table_label: Table 1. Kinetic characteristics of Pfk A and Pfk B in the glycolytic reaction.

substrate: fructose 6-phosphate


assay_conditions_summary: cofactor ATP

column_label: Table 1; row Pfk A / ATP; column K1/2 (Km) (mM); raw cell 1.0 ± 0.2; normalized Km 1.0 mM

normalized_value_unit_evidence: Km=1.0 mM

row_label: Pfk A / ATP


column_label: Table 1; row Pfk B / F6P; column K1/2 (Km) (mM); raw cell 0.04 ± 0.01; normalized Km 0.04 mM

row_label: Pfk B / F6P

enzyme: ATP-dependent 6-phosphofructokinase isozyme 2


column_label: Table 1; row Pfk B / ATP; column K1/2 (Km) (mM); raw cell 0.052 ± 0.005; normalized Km 0.052 mM

row_label: Pfk B / ATP


substrate_name: fructose 1,6-bisphosphate (for gluconeogenic reaction)

column_label: Table 2; row F16bP; column Km (mM); raw cell 17.5 ± 1.5; normalized Km 17.5 mM

table_label: Table 2. Kinetic characteristics of Pfk B in the gluconeogenic reaction.


substrate_name: ADP (for gluconeogenic reaction)

assay_conditions_summary: cofactor ADP

column_label: Table 2; row ADP; column Km (mM); raw cell 12.9 ± 3.0; normalized Km 12.9 mM

row_label: ADP

substrate: ADP (for gluconeogenic reaction)


substrate_name: IDP (for gluconeogenic reaction)

column_label: Table 2; row IDP; column Km (mM); raw cell 0.27 ± 0.05; normalized Km 0.27 mM

row_label: IDP

substrate: IDP (for gluconeogenic reaction)


substrate_name: GDP (for gluconeogenic reaction)

column_label: Table 2; row GDP; column Km (mM); raw cell 0.28 ± 0.03; normalized Km 0.28 mM

row_label: GDP

substrate: GDP (for gluconeogenic reaction)


organism: Geobacillus stearothermophilus

substrate_name: ATP

assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

column_label: Table 2: Alternative Nucleoside Triphosphate Substrates (Biochemistry 1994, 33(11):3424-3431); row ATP; the Michaelis constant 0.07 mM comes from the column Km(NTP) (mM) of that row, whose footnote a states that Fru-6P concentration was kept fixed at 1.0 mM (saturating) for these determinations; the turnover number 112 s-1 comes from the Results text eq 3 fit of the forward reaction, which is the 100 percent reference of the Table 2 column % of kcat(ATP) and is the only forward-reaction turnover number the article prints. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed value 112 s-1; already in s^-1, so no unit conversion applies; the paper value is 112.0 s^(-1). Km: printed cell 0.07 mM; already in mM, so no unit conversion applies; the paper value is 0.07 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the catalog value 1599.9999999999998 s^(-1)*mM^(-1) is not a printed value; it is the quotient 112 / 0.07 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, row ATP: Km = 0.07 mM printed in the column Km(NTP) (mM). Results text, forward reaction fit to eq 3 with A as MgATP and B as Fru-6P: kcat = 112 s-1. No kcat/Km value is printed for this measurement.

row_label: Table 2, row ATP, alternative nucleoside triphosphate substrates, read with the forward-reaction turnover number of the Results text

substrate: ATP


substrate_name: CTP

substrate: CTP


substrate_name: D-Fructose 1,6-bisphosphate

assay_conditions_summary: pH 8.2; 303.15 K; cofactor ADP

column_label: Results text, reverse reaction initial velocity analysis (Biochemistry 1994, 33(11):3424-3431); the paragraph states that the initial velocity data were fit to the equation for a rapid-equilibrium random or ordered bireactant mechanism (eq 3), assuming that A is MgADP and B is Fru-1,6BP, and prints kcat = 3.2 s-1 together with Kb = 0.44 mM, the Michaelis constant of substrate B, which that fit declares to be Fru-1,6BP. The same paragraph prints Ka = 0.11 mM for MgADP and the two dissociation constants Kia and Kib. There is no kcat/Km value.

normalized_value_unit_evidence: kcat: printed value 3.2 s-1; already in s^-1, so no unit conversion applies; the paper value is 3.2 s^(-1). Km: printed value 0.44 mM; already in mM, so no unit conversion applies; the paper value is 0.44 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the catalog value 7.272727272727273 s^(-1)*mM^(-1) is not a printed value; it is the quotient 3.2 / 0.44 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Results text, reverse reaction fit to eq 3 with A as MgADP and B as Fru-1,6BP: kcat = 3.2 s-1 and Kb = 0.44 mM, the Michaelis constant of substrate B, Fru-1,6BP. No kcat/Km value is printed for this measurement.

row_label: Results text, reverse reaction initial velocity fit to eq 3 with A as MgADP and B as Fru-1,6BP

substrate: D-Fructose 1,6-bisphosphate


substrate_name: GTP

substrate: GTP


substrate_name: UTP

substrate: UTP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E43A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E43G to reconstruct the assayed variant sequence.


organism: Thermococcus kodakarensis

substrate_name: ADP

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ADP

substrate: ADP


substrate_name: AMP

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ATP

substrate: AMP


substrate_name: D-fructose 1,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


substrate_name: alpha-D-galactose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E174D to reconstruct the assayed variant sequence.

substrate: alpha-D-galactose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R105M with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R228K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R228M to reconstruct the assayed variant sequence.


enzyme_display_name: ATP-dependent 6-phosphofructokinase subunit alpha

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ATP (without effector)

substrate: ATP (without effector)


substrate_name: fructose 6-phosphate (without effector)

enzyme: ATP-dependent 6-phosphofructokinase subunit alpha

substrate: fructose 6-phosphate (without effector)


enzyme_display_name: ATP-dependent 6-phosphofructokinase subunit beta


enzyme: ATP-dependent 6-phosphofructokinase subunit beta


organism: Leminorella grimontii

assay_conditions_summary: pH 9

proof_lines:
cloned from Leminorella grimontii
catalyse 1-phosphorylation of galactose


assay_conditions_summary: pH 9; cofactor ATP

proof_lines:
broad substrate tolerance
catalyse 1-phosphorylation of galactose


assay_conditions_summary: pH 9; 323.15 K; cofactor ATP


organism: Escherichia coli

column_label: Article text line 70 maps compound 2 to 2-deoxy-D-galactose; line 76 reports compound 2 kcat 30 min^-1 and Km 3.6 mM.

normalized_value_unit_evidence: kcat=0.5 s^-1; Km=3.6 mM; kcat/Km=0.1388888888888889 s^-1 mM^-1 from the same row kcat and Km central values

raw_value_unit_evidence: compound 2: kcat 30 min^-1; Km 3.6 mM

row_label: compound 2; 2-deoxy-D-galactose


column_label: Article text line 70 maps compound 5 to 3-deoxy-D-galactose; line 76 reports compound 5 kcat 5.1 min^-1 and Km 6.4 mM.

normalized_value_unit_evidence: kcat=0.085 s^-1; Km=6.4 mM; kcat/Km=0.01328125 s^-1 mM^-1 from the same row kcat and Km central values

raw_value_unit_evidence: compound 5: kcat 5.1 min^-1; Km 6.4 mM

row_label: compound 5; 3-deoxy-D-galactose


substrate_name: D-Fucose

column_label: Article text line 70 maps compound 11 to 6-deoxy-D-galactose; line 76 reports compound 11 kcat 2.9 min^-1 and Km 4.9 mM.

normalized_value_unit_evidence: kcat=0.048 s^-1 (2.9 min^-1 converted and rounded to expected row precision); Km=4.9 mM; kcat/Km=0.009795918367346938 s^-1 mM^-1 from the same row kcat and Km central values

raw_value_unit_evidence: compound 11: kcat 2.9 min^-1; Km 4.9 mM

row_label: compound 11; 6-deoxy-D-galactose

substrate: D-Fucose


substrate_name: D-Galactosamine

column_label: Article text line 70 maps compound 3 to 2-amino-deoxy-D-galactose; line 76 reports compound 3 kcat 11.7 min^-1 and Km 2.9 mM.

normalized_value_unit_evidence: kcat=0.195 s^-1; Km=2.9 mM; kcat/Km=0.06724137931034484 s^-1 mM^-1 from the same row kcat and Km central values

raw_value_unit_evidence: compound 3: kcat 11.7 min^-1; Km 2.9 mM

row_label: compound 3; 2-amino-deoxy-D-galactose

substrate: D-Galactosamine


substrate_name: L-rhamnulose

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

assay_conditions_summary: pH 8.5; cofactor ATP

substrate: L-rhamnulose


substrate_name: magnesium ion

substrate: magnesium ion


organism: Bacillus licheniformis

substrate_name: D-fructose 6-phosphate

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

assay_conditions_summary: pH 6.8; cofactor ATP

normalized_value_unit_evidence: Km normalized_value=0.05 normalized_unit=mM from 0.05 mM.

raw_value_unit_evidence: Kinetics prose reports apparent Km values for ATP and Fru-6-P as 0.07 and 0.05 mM, respectively; Fru-6-P maps to 0.05 mM. Raw value 0.05 mM.

row_label: Fru-6-P saturation function

table_label: Kinetics of Phosphofructokinase prose

substrate: D-fructose 6-phosphate


substrate_name: ATP

normalized_value_unit_evidence: Km normalized_value=0.07 normalized_unit=mM from 0.07 mM.

raw_value_unit_evidence: Kinetics prose reports apparent Km values for ATP and Fru-6-P as 0.07 and 0.05 mM, respectively; ATP maps to 0.07 mM. Raw value 0.07 mM.

row_label: ATP saturation function

substrate: ATP


organism: Dictyostelium discoideum

proof_lines: phosphofructokinase MgATP


substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


assay_conditions_summary: pH 7.8; cofactor ATP


substrate_name: sedoheptulose 7-phosphate

assay_conditions_summary: pH 7; 328.15 K; cofactor ATP

column_label: Table 1 columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 M^-1); row PfkA E.co PFK / ATP / S7P.

raw_value_unit_evidence: Table 1 row PfkA E.co PFK / ATP / S7P: Km = 2.5 mM; kcat = 0.25 s^-1; kcat/Km = 0.15 x 10^3 s^-1 M^-1.

row_label: PfkA E.co PFK; ATP; S7P

table_label: Table 1: Kinetics of the PFKs tested

substrate: sedoheptulose 7-phosphate