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


enzyme_display_name: galactokinase

organism: Homo sapiens

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

enzyme: galactokinase

status: unverified

source: oed


substrate_name: D-Galactosamine

verification_status: corrected

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

status: corrected


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 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


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 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.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

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

source_db: skid

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

sequence_source: multiple

proof_lines: ATP galactokinase

source_databases_merged: skid uniprot

enzyme: UniProt P51570

substrate: D-talose

source: skid


substrate_name: ATP

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

substrate: 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_accession and applied mutation signature H44Y to reconstruct the assayed variant sequence.

proof_lines:
human galactokinase
ATP-first binding
ordered ternary complex


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


substrate_name: D-Galactose

proof_lines: galactokinase first committed step in galactose catabolism

substrate: D-Galactose


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.


substrate_name: alpha-D-galactose

substrate: alpha-D-galactose


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


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


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


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


enzyme_display_name: ATP-dependent 6-phosphofructokinase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: fructose 6-phosphate

source_db: uniprot

verification_status: verified

kcat_display: Not reported

kcat_over_km_display: Not reported

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

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.

enzyme: ATP-dependent 6-phosphofructokinase

substrate: fructose 6-phosphate

status: verified

source: uniprot


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


enzyme_display_name: ATP-dependent 6-phosphofructokinase isozyme 2

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


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

enzyme: ATP-dependent 6-phosphofructokinase isozyme 2


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

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_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

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

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


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


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.


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


substrate_name: ATP


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

substrate_name: alpha-D-galactose

source_db: brenda

assay_conditions_summary: pH 9

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

source: brenda


assay_conditions_summary: pH 9; cofactor ATP

proof_lines:
broad substrate tolerance
catalyse 1-phosphorylation of galactose

substrate: ATP


substrate: alpha-D-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

table_label: Main article kinetic prose


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


enzyme_display_name: L-Rhamnulokinase

organism: Escherichia coli (strain K12)

substrate_name: L-rhamnulose

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

assay_conditions_summary: pH 8.5; cofactor ATP

enzyme: L-Rhamnulokinase

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


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


organism: Dictyostelium discoideum

proof_lines: phosphofructokinase MgATP


substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


organism: Thermotoga maritima

assay_conditions_summary: pH 7.8; cofactor ATP

source_databases_merged: brenda uniprot


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


column_label: Table 1 columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 M^-1); row PfkA E.co PFK / ATP / F6P.

normalized_value_unit_evidence: kcat 1.2 s^-1; Km 0.065 mM; kcat/Km 19 x 10^3 s^-1 M^-1 = 19 s^-1 mM^-1, consistent with expected 18.46153846153846 by displayed rounding of kcat/Km.

raw_value_unit_evidence: Table 1 row PfkA E.co PFK / ATP / F6P: Km = 0.065 mM; kcat = 1.2 s^-1; kcat/Km = 19 x 10^3 s^-1 M^-1.

row_label: PfkA E.co PFK; ATP; F6P


organism: Komagataella pastoris


enzyme_display_name: UniProt P06999

assay_conditions_summary: pH 8.2; 301.15 K; cofactor ATP

column_label: Table 1 row K_M ATP, uM reports Control = 8 +/- 3.

raw_value_unit_evidence: Km raw_value=8 uncertainty=+/-3 raw_unit=uM

row_label: Control / K_M ATP

table_label: PMC3699746 Table 1, Effect of KCl on the kinetic parameters of Pfk-2

enzyme: UniProt P06999


assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP

proof_lines:
Pfk-2
MgATP
KM ATP


organism: Lactococcus lactis subsp. lactis

normalized_value_unit_evidence: Km normalized_value=0.18 normalized_unit=mM from 0.18 mM.

raw_value_unit_evidence: Michaelis constants prose reports Km values for MgATP and Fru-6-P as 0.18 mM and 0.25 mM, respectively; MgATP maps to the ATP row. Raw value 0.18 mM.

row_label: MgATP

table_label: Michaelis Constants prose


assay_conditions_summary: cofactor NADH

normalized_value_unit_evidence: Km normalized_value=0.25 normalized_unit=mM from 0.25 mM.

raw_value_unit_evidence: Michaelis constants prose reports Km values for MgATP and Fru-6-P as 0.18 mM and 0.25 mM, respectively; Fru-6-P maps to 0.25 mM. Raw value 0.25 mM.


organism: Lactobacillus delbrueckii subsp. bulgaricus

assay_conditions_summary: pH 6; cofactor ATP


organism: Streptomyces coelicolor


assay_conditions_summary: pH 7.4; cofactor ATP

column_label: Table 1 row ATP; columns Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1)

raw_value_unit_evidence: ATP row: Km 0.035 plus/minus 0.004 mM; kcat 1.350 plus/minus 0.033 s^-1; kcat/Km 38.90 s^-1 mM^-1

row_label: Substrate ATP

table_label: Table 1. Kinetic parameters for ScGalK


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

column_label: Table 1 row Gal; columns Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1)

raw_value_unit_evidence: Gal row: Km 0.627 plus/minus 0.061 mM; kcat 1.350 plus/minus 0.044 s^-1; kcat/Km 2.15 s^-1 mM^-1

row_label: Substrate Gal


assay_conditions_summary: pH 7; cofactor ATP


assay_conditions_summary: pH 7; cofactor ADP


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines:
Trypanosoma brucei
phosphofructokinase
ATP


substrate_name: Fructose 6-phosphate

substrate: Fructose 6-phosphate


enzyme_display_name: ATP-dependent 6-phosphofructokinase 1

organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

assay_conditions_summary: cofactor ATP

proof_lines:
Thermus thermophilus
phosphofructokinase
ATP

enzyme: ATP-dependent 6-phosphofructokinase 1


proof_lines:
Thermus thermophilus
phosphofructokinase
fructose 6-phosphate


organism: Mycobacterium sp.

column_label: Abstract reports apparent Michaelis constants for galactose and ATP as 1.0 mM and 0.29 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.29 mM raw_unit=mM

row_label: Mycobacterium galactokinase / ATP

table_label: PubMed XML abstract PMID 6189374


substrate_name: D-galactose

raw_value_unit_evidence: Km raw_value=1.0 mM raw_unit=mM

row_label: Mycobacterium galactokinase / D-galactose

substrate: D-galactose


enzyme_display_name: Galactokinase

organism: Arabidopsis thaliana

enzyme: Galactokinase


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

substrate_name: D-galactose (at 50 degrees Celsius)

substrate: D-galactose (at 50 degrees Celsius)


substrate_name: ATP (at 50 degrees Celsius)

substrate: ATP (at 50 degrees Celsius)


enzyme_display_name: glucosamine kinase

organism: Vibrio cholerae serotype O1

substrate_name: D-glucosamine

assay_conditions_summary: pH 7

enzyme: glucosamine kinase

substrate: D-glucosamine


organism: Amycolatopsis methanolica

assay_conditions_summary: pH 7.5; cofactor ATP

normalized_value_unit_evidence: Km 0.6 mM.

raw_value_unit_evidence: Table 4 row ATP: Kapp 0.6 mM with table uncertainty 0.1 mM; prose identifies this as the apparent Km for ATP.

row_label: ATP; PPi absent; F-6-P fixed at 10 mM

table_label: Table 4. Kinetics of the ATP-PFK enzyme from A. methanolica WVI and effects of PPi on affinities for substrates F-6-P and ATP


organism: Bacillus sp. (in: firmicutes)


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: Leishmania donovani


organism: Oceanimonas doudoroffii

assay_conditions_summary: pH 8; cofactor ATP


organism: Escherichia coli (strain K12)


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

substrate_name: fructose 1,6-bisphosphate (at 75 degrees Celsius)


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Schizosaccharomyces pombe

substrate_name: ATP

assay_conditions_summary: pH 7.2; cofactor ATP


organism: Trypanosoma cruzi (strain CL Brener)


enzyme_display_name: Glucosamine kinase

organism: Streptacidiphilus jiangxiensis

substrate_name: glucosamine

enzyme: Glucosamine kinase

substrate: glucosamine


organism: Schistosoma mansoni


organism: Homo sapiens

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


substrate_name: D-galactosamine

substrate: D-galactosamine


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: pH 7.5, 37°C, mutant enzyme Y379W, cosubstrate: D-galactosamine

proof_lines: pH 7.5, 37°C, mutant enzyme Y379W, cosubstrate: 2-deoxy-D-galactose

proof_lines: pH 7.5, 37°C, mutant enzyme Y379W, cosubstrate: alpha-D-galactose


substrate_name: D-talose

substrate: D-talose


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-talose

proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-galactosamine

proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: alpha-D-galactose

substrate: ATP


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-galactosamine

proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: 2-deoxy-D-galactose

proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: alpha-D-galactose


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


proof_lines: pH 7.5, 37°C, mutant enzyme M180V, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V, cosubstrate: alpha-D-galactose


substrate_name: alpha-D-galactose

substrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/A334S/D268E/R336Q/G373S, cosubstrate: alpha-D-galactose


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


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/A334S, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/A334S/G373S, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/A334S/D268E/G373S, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/A334S


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/A334S/G373S


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/M180V/A334S/D268E/G373S


proof_lines: pH 7.5, 37°C, mutant enzyme R366Q, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme G373S, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme M185L/Y379W, cosubstrate: alpha-D-galactose

proof_lines: pH 7.5, 37°C, mutant enzyme M185L/Y379W, cosubstrate: D-galactosamine


proof_lines: pH 7.5, 37°C, mutant enzyme M60V/A334S, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme D268E, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme A334S, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme M60V, cosubstrate: alpha-D-galactose


proof_lines: pH 7.5, 37°C, mutant enzyme M185L, cosubstrate: alpha-D-galactose

proof_lines: pH 7.5, 37°C, mutant enzyme M185L, cosubstrate: 2-deoxy-D-galactose


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


km_display: Not reported


proof_lines:
pH 8, 37°C, mutant enzyme A198V
mutant enzyme A198V


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: mutant enzyme N341A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme N341A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme N341A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme S377A/K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme S377A/K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme S377A/K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme H242A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme H242A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme H242A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme N341A/R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme N341A/R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme N341A/R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme S377A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme S377A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme S377A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme R246A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme R246A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme R246A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


substrate_name: ADP

ki_unit: mM

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

proof_lines: mutant enzyme N341A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

substrate: ADP


proof_lines: mutant enzyme S377A/K678A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme K678A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: wild type enzyme, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme N341A/R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme S377A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme H242A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: mutant enzyme K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


organism: Saccharomyces cerevisiae

substrate_name: D-glucose

substrate: D-glucose


assay_conditions_summary: 303.15 K; cofactor ATP

proof_lines: in the presence of 2-deoxy-D-galactose as a substrate, at 30°C, wild type enzyme

proof_lines: in the presence of D-galactose as a substrate, wild type enzyme

proof_lines: in the presence of D-glucose as a substrate, at 30°C, wild type enzyme


enzyme_display_name: hexokinase

organism: Rattus norvegicus

proof_lines: recombinant wild-type hexokinase I, D84A, D84E and D84K mutants

enzyme: hexokinase


substrate_name: Unknown

substrate: Unknown


proof_lines:
recombinant D84A mutant hexokinase I
HK I+ and its D84A mutant
D84A mutant of HK I


organism: Geobacillus stearothermophilus

substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


proof_lines: pH 7.5, 37°C, wild-type enzyme, cosubstrate: D-galactosamine


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


organism: Cucumis sativus

substrate_name: GTP

proof_lines:
pH 7.2, 25°C, cytosolic PFK
pH 8.0, 25°C, cytosolic PFK
pH 7.2, 25°C, plastid PFK

substrate: GTP


substrate_name: ITP

proof_lines: pH 8.0, 25°C, pH 7.2, 25°C, cytosolic PFK

substrate: ITP


assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines:
pH 7.2, 25°C, cytosolic PFK
pH 7.2, 25°C, plastid PFK
pH 8.0, 25°C, cytosolic PFK


substrate_name: UTP

proof_lines:
pH 7.2, 25°C, cytosolic PFK
pH 8.0, 25°C, plastid PFK
pH 8.0, 25°C, cytosolic PFK

substrate: UTP


substrate_name: CTP

proof_lines:
pH 8.0, 25°C, cytosolic PFK
pH 7.2, 25°C, plastid PFK
pH 7.2, 25°C, cytosolic PFK

substrate: CTP


smiles: C(C(C(C(C(C=O)F)O)O)O)O


smiles: C(C(C(C(C(C=O)O)O)O)S)O


substrate_name: D-mannosamine

substrate: D-mannosamine


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


organism: Escherichia coli


substrate_name: D-galactose

substrate: D-galactose


assay_conditions_summary: pH 8


proof_lines: pH 8.0, mutant enzyme Q466_H467insHMNLAEQ

proof_lines: nonaggregating interface mutant hexokinase I, pH 7.8


proof_lines:
pH 8.0, wild-type enzyme
wild type hexokinase II
wild-type hexokinase I, pH 7.8


organism: Lactococcus lactis


assay_conditions_summary: pH 8; 297.15 K; cofactor ATP


organism: Oryctolagus cuniculus

substrate_name: ATP; D-Glucose

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

proof_lines: erythrocyte enzyme, mixed inhibitor versus MgATP2-

proof_lines: erythrocyte enzyme, mixed inhibitor versus glucose

substrate: ATP; D-Glucose


proof_lines:
reticulocyte hexokinase Ia
at 37°C, pH 8.1
erythrocyte enzyme


proof_lines:
hexokinase Ia
erythrocyte enzyme
hexokinase Ib


proof_lines:
MgITP2-, erythrocyte enzyme
MgITP2-, hexokinase Ib
MgITP2-, at 37°C, pH 8.1


substrate_name: D-fructose

proof_lines:
hexokinase Ia
at 37°C, pH 8.1
erythrocyte enzyme

substrate: D-fructose


enzyme_display_name: fructokinase

organism: Solanum lycopersicum

proof_lines:
FKI, pH 8, 25°C
pH 7.5
FKII, pH 8, 25°C

enzyme: fructokinase


substrate_name: ATP

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
FKI, pH 8, 25°C
recombinant enzyme, pH 8, 25°C
FKII, pH 8, 25°C


proof_lines:
recombinant enzyme, pH 8, 25°C
FKI, pH 8, 25°C
FKII, pH 8, 25°C


proof_lines:
FKI, pH 8, 25°C
FKII, pH 8, 25°C
recombinant enzyme, pH 8, 25°C


proof_lines:
at 3 mM fructose, pH 8, 25°C
at 0.5 mM fructose, pH 8, 25°C


organism: Arabidopsis thaliana

substrate_name: S-adenosyl-L-methionine

proof_lines: mutant F326Y, K0.5 value, Hill coefficient 1.23, pH 8.6, 37°C

substrate: S-adenosyl-L-methionine


proof_lines: wild-type, K0.5 value, Hill coefficient 1.34, pH 8.6, 37°C


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

proof_lines: mutant F326Y, K0.5 value, Hill coefficient 1.36, pH 8.6, 37°C


proof_lines: wild-type, K0.5 value, Hill coefficient 1.29, pH 8.6, 37°C


enzyme_display_name: glutamine-phenylpyruvate transaminase

organism: Bos taurus

substrate_name: S-aminomethyl-L-cysteine

enzyme: glutamine-phenylpyruvate transaminase

substrate: S-aminomethyl-L-cysteine


substrate_name: cystine

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

substrate: cystine


substrate_name: L-cystathionine

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

substrate: L-cystathionine


substrate_name: L-Lanthionine

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

substrate: L-Lanthionine


organism: Musa acuminata

assay_conditions_summary: pH 7.3; 298.15 K; cofactor ATP

proof_lines:
pH 7.3, 25°C, PFK II
pH 8.0, 25°C, PFK I

substrate: ATP


organism: Brugia malayi

substrate_name: D-glucose

substrate: D-glucose


substrate_name: Unknown

substrate: Unknown


substrate_name: ATP; D-Galactose

substrate: ATP; D-Galactose


proof_lines:
wild-type, 37°C
wild-type


organism: Aspergillus niger


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


substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


enzyme_display_name: rhamnulokinase

substrate_name: L-rhamnulose

enzyme: rhamnulokinase

substrate: L-rhamnulose


substrate_name: L-xylulose

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

substrate: L-xylulose


substrate_name: L-Fructose

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

substrate: L-Fructose


substrate_name: D-psicose

substrate: D-psicose


enzyme_display_name: galactokinase

substrate_name: D-galactose

enzyme: galactokinase

substrate: D-galactose


substrate_name: ITP

substrate: ITP


substrate_name: GTP

substrate: GTP


substrate_name: UTP

substrate: UTP


substrate_name: CTP

substrate: CTP


proof_lines:
hexokinase I, at 37°C, pH 8.1
hexokinase Ib, at 37°C, pH 7.2
hexokinase Ia, at 37°C, pH 7.2


enzyme_display_name: ribulokinase

organism: Anoxybacillus kestanbolensis

substrate_name: D-ribulose

enzyme: ribulokinase

substrate: D-ribulose


enzyme_display_name: xylulokinase

organism: Saccharococcus caldoxylosilyticus

substrate_name: xylulose

enzyme: xylulokinase

substrate: xylulose


enzyme_display_name: UniProt P09099

substrate_name: ATP

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P09099


enzyme_display_name: UniProt Q9TVW2

organism: Toxoplasma gondii

enzyme: UniProt Q9TVW2


substrate_name: adenosine

substrate: adenosine


enzyme_display_name: salicylate 1-monooxygenase

organism: Pseudomonas sp.

assay_conditions_summary: cofactor NADH

enzyme: salicylate 1-monooxygenase


substrate_name: p-Aminosalicylate

substrate: p-Aminosalicylate


organism: Mycobacterium tuberculosis

substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


substrate_name: geranyl diphosphate

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

substrate: geranyl diphosphate


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

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


substrate_name: isopentenyl diphosphate

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

substrate: isopentenyl diphosphate


enzyme_display_name: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]


enzyme: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]


enzyme_display_name: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]

proof_lines: pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)

proof_lines: pH 8.0, 30°C, cosubstrate: farnesyl diphosphate, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)


proof_lines: pH 8.0, 30°C, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus), truncated from of At-SPS2 (At-SPS2DELTA, in whic

enzyme: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]


proof_lines: pH 8.0, 30°C, truncated from of At-SPS2 (At-SPS2DELTA, in which the 30 N-terminal residues of the putative signal-peptide are removed and, instead the His6 tag is attached to the N-terminus)


proof_lines: pH 8.0, 30°C, cosubstrate: farnesyl diphosphate

proof_lines: pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate


substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


organism: Sus scrofa


assay_conditions_summary: pH 8.5; 298.15 K; buffer 50 mM potassium diphosphate

proof_lines: at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol

proof_lines: in potassium diphosphate buffer (pH 8.5)


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


organism: Ascaris suum

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-fructose

substrate: D-fructose


organism: Solanum tuberosum


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: D-amino-acid transaminase

organism: Lysinibacillus sphaericus

substrate_name: D-alanine

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

proof_lines: pH 8.0, 37°C, cosubstrate 2-oxobutanoate

proof_lines: pH 8.0, 37°C, cosubstrate 2-oxoglutarate

enzyme: D-amino-acid transaminase

substrate: D-alanine


proof_lines:
cosubstrate D-alanine
pH 8.0, 37°C


substrate_name: beta-chloro-D-alanine

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

substrate: beta-chloro-D-alanine


organism: Bifidobacterium bifidum

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


substrate_name: D-galactose

substrate: D-galactose


enzyme_display_name: thymidine kinase

organism: Chlamydomonas reinhardtii

substrate_name: thymidine

enzyme: thymidine kinase

substrate: thymidine


enzyme_display_name: UniProt Q0H0H6

organism: Bacillus cereus

enzyme: UniProt Q0H0H6


enzyme_display_name: UniProt O43252

organism: Homo sapiens

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt O43252


substrate_name: adenosine 5'-phosphosulfate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=30°C, pH=8

substrate: adenosine 5'-phosphosulfate


enzyme_display_name: UniProt Q12657

organism: Penicillium chrysogenum

enzyme: UniProt Q12657


substrate_name: 3'-phosphoadenosine 5'-phosphosulfate

substrate: 3'-phosphoadenosine 5'-phosphosulfate


substrate_name: ATP


enzyme_display_name: UniProt Q59263

organism: Corynebacterium ammoniagenes

substrate_name: riboflavin

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=37°C, pH=7

enzyme: UniProt Q59263

substrate: riboflavin


enzyme_display_name: UniProt Q969G6

enzyme: UniProt Q969G6


substrate_name: GTP

substrate: GTP


assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP


proof_lines:
pH 7.8, 30°C
pH 7.8, 30°C, at 0.1 mM ATP
pH 7.8, 30°C, at 0.5 mM ATP


organism: Escherichia coli

substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


proof_lines:
pH 8.0, 8.5°C, wild-type PFK
pH 8.5, 30°C, wild-type PFK


substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

proof_lines: pH 7.2, 30°C, cosubstrate gamma-thio-ATP

proof_lines: in the presence of 0.5 mM MgATP2-, at pH 8.2 and 25°C

substrate: D-fructose 6-phosphate


assay_conditions_summary: pH 8.2; 278.15 K; cofactor ATP

proof_lines:
pH 8.2, 5°C
pH 7.2, 30°C, cosubstrate ATP
pH 8.2, 15°C


proof_lines: pH 7.2, 30°C, cosubstrate fructose 1-phosphate


proof_lines:
pH 8.5, 37°C
native enzyme


substrate_name: pyridoxamine 5'-phosphate

substrate: pyridoxamine 5'-phosphate


substrate_name: pyridoxal 5'-phosphate

substrate: pyridoxal 5'-phosphate


proof_lines: at pH 7.5, temperature not specified in the publication


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

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


substrate_name: isopentenyl diphosphate

proof_lines: with (2R,6E)-farnesyl diphosphate as cosubstrate, at pH 7.5, temperature not specified in the publication

proof_lines: with (2E,6E)-8-O-(N-methyl-2-aminobenzoyl)-3,7-dimethyl-2,6-octandien-1-diphosphate as cosubstrate, at pH 7.5, temperature not specified in the publication

proof_lines: with dimethylallyl diphosphate as cosubstrate, at pH 7.5 and 30°C

substrate: isopentenyl diphosphate


enzyme_display_name: hexokinase

substrate_name: D-glucose

proof_lines: mutant enzyme W167F, in 25 mM HEPES (pH 7.4), at 37°C

enzyme: hexokinase

substrate: D-glucose


proof_lines: mutant enzyme W257F, in 25 mM HEPES (pH 7.4), at 37°C


proof_lines: mutant enzyme W99F, in 25 mM HEPES (pH 7.4), at 37°C


mutation_signature: truncated enzyme with removed helix alpha13 truncated enzyme with removed helix alpha13

mutation_type: truncation


assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines: co-substrate: ATP, wild-type in the presence of 20-30% glycerol, pH and temperature not specified in the publication


proof_lines: glucokinase with C-terminal 5 alanine addition

proof_lines: glucokinase with C-terminal 10 alanine addition

proof_lines: recombinant hexokinase I expressed in Escherichia coli


mutation_signature: a truncate HK I form lacking the first 11 amino acids named HK-11aa / a truncate HK I form lacking the first 11 amino acids named HK-11aa

proof_lines: recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37°C, pH 7.2


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: MgATP2-, recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37°C, pH 7.2

substrate: ATP


substrate_name: Unknown

substrate: Unknown


substrate_name: L-gamma-glutamyl-p-nitroanilide

proof_lines: both wild-type and mutant S243E, 37°C, pH 7.5

substrate: L-gamma-glutamyl-p-nitroanilide


organism: Pseudomonas putida

substrate_name: o-Nitrophenol

substrate: o-Nitrophenol


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


smiles: O=O

proof_lines:
cosubstrate o-nitrophenol
cosubstrates salicylate and NADH


enzyme_display_name: GDP-perosamine synthase

organism: Caulobacter vibrioides

enzyme: GDP-perosamine synthase


substrate_name: L-glutamate

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

proof_lines: pH 7.5, 22°C, cosubstrate: GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose

proof_lines: pH 7.5, 22°C, cosubstrate: GDP-4-dehydro-6-deoxy-D-mannose

substrate: L-glutamate


enzyme_display_name: UniProt P76015

substrate_name: dihydroxyacetone

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

enzyme: UniProt P76015

substrate: dihydroxyacetone


enzyme_display_name: glycerol kinase

organism: Cellulomonas sp.

substrate_name: glycerol

smiles: C(C(CO)O)O

enzyme: glycerol kinase

substrate: glycerol


enzyme_display_name: UniProt Q8IDI4

organism: Plasmodium falciparum

enzyme: UniProt Q8IDI4


substrate_name: ATP


enzyme_display_name: UniProt Q8DPI4

organism: Streptococcus pneumoniae

substrate_name: choline

smiles: C[N+](C)(C)CCO

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=25°C, pH=8

enzyme: UniProt Q8DPI4

substrate: choline


enzyme_display_name: UniProt Q9Y259

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

enzyme: UniProt Q9Y259


enzyme_display_name: UniProt P9WPA7

organism: Mycobacterium tuberculosis

substrate_name: pantothenol

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

enzyme: UniProt P9WPA7

substrate: pantothenol


substrate_name: pantothenate

smiles: CC(C)(CO)C(C(=O)NCCC(=O)[O-])O

substrate: pantothenate


enzyme_display_name: UniProt O00764

substrate_name: pyridoxine

proof_lines:
Raw SKiD Env: Temp=-----, pH=6.2
Raw SKiD Env: Temp=37°C, pH=7.3
Raw SKiD Env: Temp=37°C, pH=6.2

enzyme: UniProt O00764

substrate: pyridoxine


proof_lines:
Raw SKiD Env: Temp=-----, pH=6.2
Raw SKiD Env: Temp=37°C, pH=6.2


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.3
Raw SKiD Env: Temp=-----, pH=-----


substrate_name: pyridoxamine

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.3
Raw SKiD Env: Temp=-----, pH=6.2
Raw SKiD Env: Temp=37°C, pH=6.2

substrate: pyridoxamine


substrate_name: ginkgotoxin

substrate: ginkgotoxin


enzyme_display_name: pyridoxal kinase

organism: Bombyx mori

enzyme: pyridoxal kinase


substrate_name: pyridoxal

substrate: pyridoxal


organism: Triticum aestivum

assay_conditions_summary: pH 7.9; cofactor ATP


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: galactokinase

organism: Sus scrofa

assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines:
pH 7.8
ATP in form of MgATP2-

enzyme: galactokinase


substrate_name: D-galactose

substrate: D-galactose


substrate_name: Unknown


organism: Saccharomyces cerevisiae

substrate_name: L-glutamine

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

proof_lines: co-substrate: D-fructose 6-phosphate, pH 7.0, 37°C

substrate: L-glutamine


proof_lines:
co-substrate: L-glutamine, pH 7.0, 37°C
pH 7.0, 37°C


substrate: Unknown


enzyme_display_name: fructokinase

organism: Arabidopsis thaliana

substrate_name: D-fructose

proof_lines: pH 7.5, temperature not specified in the publication, FRK7

proof_lines: pH 7.5, temperature not specified in the publication, FRK5

proof_lines: pH 7.5, temperature not specified in the publication, FRK2

enzyme: fructokinase

substrate: D-fructose


assay_conditions_summary: pH 7.5; cofactor ATP

substrate: ATP


organism: Anguilla anguilla


organism: Rana catesbeiana

substrate_name: ATP; D-Glucose

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

substrate: ATP; D-Glucose


organism: Bacillus thuringiensis


organism: Bos taurus

substrate_name: D-glucose

proof_lines: pH 7.2, 37°C, recombinant catalytic C-terminal domain

proof_lines: pH 7.2, 37°C, recombinant full length enzyme

substrate: D-glucose


smiles: C(C(C(C(C(C=O)F)O)O)O)O

proof_lines:
HK I, at 25°C, pH 7.4
at 37°C, pH 7.4


organism: Bifidobacterium longum subsp. infantis

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


enzyme_display_name: homoserine kinase

organism: Rhodospirillum rubrum

enzyme: homoserine kinase


substrate_name: L-homoserine

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

substrate: L-homoserine


enzyme_display_name: pyruvate kinase

organism: Periplaneta americana

substrate_name: phosphoenolpyruvate

enzyme: pyruvate kinase

substrate: phosphoenolpyruvate


organism: Thermoplasma acidophilum


organism: Brassica juncea

substrate_name: ADP

substrate: ADP


enzyme_display_name: UniProt P30615

organism: Trypanosoma brucei brucei

enzyme: UniProt P30615


enzyme_display_name: UniProt C6KTA4

organism: Plasmodium falciparum

enzyme: UniProt C6KTA4


enzyme_display_name: UniProt P30613

organism: Homo sapiens

enzyme: UniProt P30613


enzyme_display_name: UniProt Q27686

organism: Leishmania mexicana

enzyme: UniProt Q27686


enzyme_display_name: hexokinase

substrate_name: 2-Deoxyglucose; ATP

proof_lines: pH 7.2, 37°C, recombinant catalytic C-terminal domain, versus MgATP2-

proof_lines: pH 7.2, 37°C, recombinant full length enzyme, versus MgATP2-

enzyme: hexokinase

substrate: 2-Deoxyglucose; ATP


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


substrate_name: alpha-ketoglutarate

substrate: alpha-ketoglutarate


organism: Citrus x paradisi

substrate_name: ATP


proof_lines:
pH 7.5, theoretical value
pH 7.5


organism: Cyprinus carpio


organism: Clostridium pasteurianum

assay_conditions_summary: pH 8; 301.15 K; cofactor ATP


organism: Escherichia coli

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

proof_lines:
pH 9, 25°C, R391A mutant
pH 9, 25°C, R391A murant
value above 2, pH 9, 25°C, R391A mutant


proof_lines:
pH 9, 25°C, wild-type enzyme
pH 9.0, recombinant wild-type enzyme


substrate_name: L-glutamate

proof_lines: calorimetric determination, pH 7.2, 25°C

substrate: L-glutamate


proof_lines: calorimetric determination, pH 7.2, 37°C


enzyme_display_name: UniProt Q5SKR5

organism: Thermus thermophilus

substrate_name: cytidine

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=25°C, pH=7.2

enzyme: UniProt Q5SKR5

substrate: cytidine


substrate_name: uridine

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.2
Raw SKiD Env: Temp=25°C, pH=8

substrate: uridine


enzyme_display_name: UniProt Q9BZX2

enzyme: UniProt Q9BZX2


enzyme_display_name: UniProt P55882

organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=25°C, pH=7

enzyme: UniProt P55882


enzyme_display_name: UniProt Q6GEY3

organism: Staphylococcus aureus

enzyme: UniProt Q6GEY3


enzyme_display_name: fucokinase

organism: Bacteroides fragilis

substrate_name: L-galactose

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

enzyme: fucokinase

substrate: L-galactose


enzyme_display_name: diamine transaminase

enzyme: diamine transaminase


substrate_name: pyruvate

substrate: pyruvate


substrate_name: K+

substrate: K+


assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

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

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


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: succinyldiaminopimelate transaminase

enzyme: succinyldiaminopimelate transaminase


substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


proof_lines: pH 8.5, 30°C, D127/R252Q double mutant PFK


enzyme_display_name: glucokinase

enzyme: glucokinase


assay_conditions_summary: pH 7.65; cofactor ATP


enzyme_display_name: UniProt Q2G159

substrate_name: N-acetyl-D-glucosamine

enzyme: UniProt Q2G159

substrate: N-acetyl-D-glucosamine


substrate: ATP


enzyme_display_name: UniProt Q9Y223

enzyme: UniProt Q9Y223


organism: Escherichia coli K-12

proof_lines:
recombinant NanK, pH 7.6, 25°C
recombinant YcfX, pH 7.6, 25°C
recombinant Glk, pH 7.6, 25°C


proof_lines:
recombinant Glk, pH 7.6, 25°C
recombinant YajF, pH 7.6, 25°C
recombinant NanK, pH 7.6, 25°C


enzyme_display_name: gluconokinase

substrate_name: D-gluconate

proof_lines:
25°C, pH 7
25°C, pH 8, gene gntU

enzyme: gluconokinase

substrate: D-gluconate


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


substrate_name: isopentenyl diphosphate

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

substrate: isopentenyl diphosphate


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

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


substrate_name: Unknown

substrate: Unknown


organism: Gallus gallus

substrate_name: L-glutamine

substrate: L-glutamine


proof_lines:
wild-type enzyme
30°C, pH 7.5, wild-type


substrate_name: D-glucose

assay_conditions_summary: pH 7.1; cofactor ATP

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

substrate: D-glucose


substrate_name: beta-D-glucose

assay_conditions_summary: cofactor ATP

proof_lines: co-substrate: ATP, mutant W167F/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W167F/W257F, pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W167F/W257F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

substrate: beta-D-glucose


substrate_name: ATP

proof_lines: mutant W167F/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: mutant W167F/W257F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: mutant W167F/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication


organism: Aquarana catesbeiana


enzyme_display_name: Phosphatidylinositol 4-kinase type 2-alpha

organism: Rattus norvegicus


enzyme_display_name: galactokinase

assay_conditions_summary: 310.15 K; cofactor ATP

enzyme: galactokinase


proof_lines: pH 8, 37°C, uncompetitive inhibition constant with respect to galactose

proof_lines: pH 8, 37°C, uncompetitive inhibition constant with respect to ATP


substrate_name: D-glucosamine

proof_lines:
hexokinases Ib and Ic, at 37°C, pH 7.2
hexokinase I, at 37°C, pH 8.1
hexokinase Ia, at 37°C, pH 7.2

substrate: D-glucosamine


substrate_name: D-fructose

proof_lines: hexokinases Ia, Ib and Ic, at 37°C, pH 7.2

substrate: D-fructose


enzyme_display_name: fructokinase

organism: Lactococcus lactis

enzyme: fructokinase


assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: pH 7.2, temperature not specified in the publication


proof_lines:
ATP in form of MgATP2-
pH 7.5


enzyme_display_name: shikimate kinase

organism: Vigna mungo

substrate_name: shikimate

enzyme: shikimate kinase

substrate: shikimate


enzyme_display_name: UniProt A0A0M3KL09

organism: Acinetobacter baumannii

enzyme: UniProt A0A0M3KL09


enzyme_display_name: UniProt P0A6D7

enzyme: UniProt P0A6D7


enzyme_display_name: UniProt P56073

organism: Helicobacter pylori

enzyme: UniProt P56073


enzyme_display_name: UniProt P27707

organism: Homo sapiens

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

enzyme: UniProt P27707


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.5


substrate_name: UTP

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.6

substrate: UTP


substrate_name: thymidine

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.5

substrate: thymidine


enzyme_display_name: acetoacetyl-CoA reductase

organism: Methylorubrum extorquens

substrate_name: acetoacetyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: acetoacetyl-CoA reductase

substrate: acetoacetyl-CoA


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: 4-hydroxybenzoate geranyltransferase

organism: Lithospermum erythrorhizon

substrate_name: geranyl diphosphate

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

proof_lines:
pH 7.8, 37°C
recombinant enzyme, pH 7.0-7.5, 45°C

enzyme: 4-hydroxybenzoate geranyltransferase

substrate: geranyl diphosphate


organism: Mycobacterium tuberculosis

substrate_name: sinefungin

proof_lines: pH 7.5, temperature not specified in the publication

substrate: sinefungin


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: hexokinase

organism: Oryctolagus cuniculus

proof_lines:
at 37°C, pH 8.1
hexokinase Ia
hexokinase Ib

enzyme: hexokinase


organism: Methylomonas methanica


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: ATP


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 8
ATP in form of MgATP2-


organism: Pseudomonas fluorescens


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


organism: Pseudomonas aeruginosa


enzyme_display_name: beta-alanine-pyruvate transaminase

substrate_name: beta-Alanine

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

enzyme: beta-alanine-pyruvate transaminase

substrate: beta-Alanine


substrate_name: pyruvate

substrate: pyruvate


organism: Mus musculus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


enzyme_display_name: salicylate 1-monooxygenase

organism: Pseudomonas sp.

substrate_name: o-Nitrophenol

assay_conditions_summary: cofactor NADH

enzyme: salicylate 1-monooxygenase

substrate: o-Nitrophenol


assay_conditions_summary: cofactor NADPH


organism: Pseudomonas putida

substrate_name: salicylate

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines:
native enzyme
cosubstrate NADH
modified enzyme

substrate: salicylate


substrate_name: NADH

proof_lines:
native enzyme
modified enzyme
cosubstrate salicylaldehyde

substrate: NADH


assay_conditions_summary: pH 8; 310.15 K; cofactor NADH

proof_lines:
pH 8.0, 37°C
cosubstrate NADH


proof_lines:
pH 8.0, 37°C
cosubstrate NADH
enzyme form NahU


enzyme_display_name: Beta-glucoside kinase

organism: Klebsiella pneumoniae

substrate_name: n-octyl-beta-D-glucopyranoside

enzyme: Beta-glucoside kinase

substrate: n-octyl-beta-D-glucopyranoside


substrate_name: salicin

substrate: salicin


substrate_name: arbutin

substrate: arbutin


substrate_name: cellobiose

substrate: cellobiose


substrate_name: amygdalin

substrate: amygdalin


substrate_name: gentiobiose

substrate: gentiobiose


substrate_name: laminaribiose

substrate: laminaribiose


substrate_name: phenyl-beta-D-glucopyranoside

substrate: phenyl-beta-D-glucopyranoside


substrate_name: cellobiitol

substrate: cellobiitol


substrate_name: isopropyl-beta-D-thioglucopyranoside

substrate: isopropyl-beta-D-thioglucopyranoside


substrate_name: methyl-beta-D-glucopyranoside

substrate: methyl-beta-D-glucopyranoside


substrate_name: sophorose

substrate: sophorose


substrate_name: thiocellobiose

substrate: thiocellobiose


substrate_name: glucose

substrate: glucose


substrate_name: ATP

substrate: ATP


organism: Naegleria fowleri

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


organism: Naegleria gruberi

substrate_name: diphosphate

substrate: diphosphate


organism: Rhodospirillum rubrum

substrate_name: D-fructose 1,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


substrate_name: phosphate

substrate: phosphate


organism: Rattus norvegicus

substrate_name: L-glutamine

substrate: L-glutamine


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: kynurenine-glyoxylate transaminase

substrate_name: glyoxylate

enzyme: kynurenine-glyoxylate transaminase

substrate: glyoxylate


substrate_name: L-kynurenine

substrate: L-kynurenine


assay_conditions_summary: pH 7.6; 318.15 K; cofactor ATP


substrate_name: fructose

substrate: fructose


substrate_name: D-glucose

proof_lines:
hexokinase C
hexokinase III
HK I, at 25°C, pH 7.4

substrate: D-glucose


proof_lines:
hexokinase B
hexokinase II
at 30°C, pH 7.5


enzyme_display_name: glutamine-phenylpyruvate transaminase

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

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

enzyme: glutamine-phenylpyruvate transaminase


substrate_name: alpha-keto-gamma-methiolbutyrate

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

substrate: alpha-keto-gamma-methiolbutyrate


proof_lines:
HK I and its D84A mutant
HK I+ and its D84A mutant


substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


organism: Ricinus communis

proof_lines:
pH 7.0, 25°C, cytosolic PFK
pH 7.0, 25°C, chloroplasr PFK
pH 8.0, 25°C, cytosolic PFK


enzyme_display_name: gluconokinase

organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.6; 303.15 K; cofactor ATP


substrate_name: D-gluconate

substrate: D-gluconate


substrate_name: D-galactose

substrate: D-galactose


organism: Aspergillus niger

substrate_name: beta-D-fructose 6-phosphate

substrate: beta-D-fructose 6-phosphate


enzyme_display_name: UniProt Q16875

organism: Homo sapiens

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

enzyme: UniProt Q16875


substrate_name: D-glucosamine

substrate: D-glucosamine


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: kanamycin kinase

organism: Unknown

source_db: unknown

source_license: see source

enzyme: kanamycin kinase

source: unknown


proof_lines:
pH 7.5, 22°C, soluble enzyme
pH 7.5, 22°C, immobilized enzyme
glucokinase


substrate_name: ATP

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

substrate: ATP


organism: Spinacia oleracea

assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: fructokinase

organism: Saccharum sp.

proof_lines:
isoform FRK2, pH 8.0
isoform FRK1, pH 8.0, 25°C
isoform FRK1, pH 8.0


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
isoform FRK1, pH 8.0, 25°C
isoform FRK2, pH 8.0, 25°C


enzyme_display_name: UniProt O67572

organism: Aquifex aeolicus

enzyme: UniProt O67572


organism: Streptococcus thermophilus

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


enzyme_display_name: galactokinase

organism: Streptococcus pneumoniae

substrate_name: N-acetyl-D-galactosamine

enzyme: galactokinase

substrate: N-acetyl-D-galactosamine


substrate_name: D-glucose / D-galactose

substrate: D-glucose / D-galactose


organism: Staphylococcus aureus


enzyme_display_name: UniProt Q47396

organism: Escherichia coli

enzyme: UniProt Q47396


organism: Sus scrofa

assay_conditions_summary: pH 7; cofactor ATP


assay_conditions_summary: pH 7


proof_lines: C-terminal deletion mutant L307, 1 mM co-substrate


proof_lines: Y306A, C-terminal point mutant, 1 mM co-substrate


proof_lines: C-terminal deletion mutant D299, 1 mM co-substrate


proof_lines: L307A, C-terminal point mutant, 1 mM co-substrate


proof_lines: C-terminal deletion mutant A305, 1 mM co-substrate


proof_lines: C-terminal deletion mutant Y306, 1 mM co-substrate


organism: Thermus thermophilus


organism: Toxoplasma gondii


organism: Trypanosoma cruzi

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: natural and recombinant hexokinase, expressed in Escherichia coli XL-1 Blue, at pH 7.5


proof_lines: varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kis

proof_lines: varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kis

proof_lines: varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kii


enzyme_display_name: UniProt Q58999

organism: Methanocaldococcus jannaschii

proof_lines:
Raw SKiD Env: Temp=40°C, pH=6.5
Raw SKiD Env: Temp=50°C, pH=6.5

enzyme: UniProt Q58999


substrate_name: ADP

substrate: ADP


substrate_name: acetyl-phosphate

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

substrate: acetyl-phosphate


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


enzyme_display_name: UniProt Q8VDL4

organism: Mus musculus

substrate_name: GDP

enzyme: UniProt Q8VDL4

substrate: GDP


substrate_name: ADP with D-glucose as phosphoryl group acceptor


enzyme_display_name: UniProt O67060

enzyme: UniProt O67060


enzyme_display_name: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]

substrate_name: isopentenyl diphosphate

proof_lines: pH 8.5, 37°C, enzyme released from microsomes

substrate: isopentenyl diphosphate


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

enzyme: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]

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


organism: Vigna mungo

assay_conditions_summary: cofactor ATP


enzyme_display_name: hexokinase

organism: Trypanosoma brucei

substrate_name: D-glucose

proof_lines: pH and temperature not specified in the publication

substrate: D-glucose


organism: Zea mays

enzyme: fructokinase


assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


enzyme_display_name: UniProt Q01415

organism: Homo sapiens

substrate_name: N-acetyl-alpha-D-glucosamine

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=8

enzyme: UniProt Q01415

substrate: N-acetyl-alpha-D-glucosamine


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=8


enzyme_display_name: UniProt Q93YN9

organism: Arabidopsis thaliana

enzyme: UniProt Q93YN9


enzyme_display_name: UniProt O80568

enzyme: UniProt O80568


organism: Xenopus laevis

proof_lines: enzyme isolated from dehydrated frogs, pH 8.0, 22°C

enzyme: hexokinase


assay_conditions_summary: pH 8; 295.15 K; cofactor ATP


enzyme_display_name: UniProt Q9I5Q5

organism: Pseudomonas aeruginosa

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

enzyme: UniProt Q9I5Q5


organism: Ascaris suum

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ATP


enzyme_display_name: UniProt Q9NWW6

substrate_name: cytidine

enzyme: UniProt Q9NWW6

substrate: cytidine


enzyme_display_name: salicylate 1-monooxygenase

organism: Aspergillus niger

substrate_name: salicylate

enzyme: salicylate 1-monooxygenase

substrate: salicylate


enzyme_display_name: D-amino-acid transaminase

organism: Bacillus subtilis

enzyme: D-amino-acid transaminase


enzyme_display_name: UniProt O68183

organism: Enterococcus casseliflavus

substrate_name: GTP

enzyme: UniProt O68183

substrate: GTP


enzyme_display_name: UniProt P0A0C1

organism: Staphylococcus aureus

substrate_name: kanamycin A

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7
Raw SKiD Env: Temp=37°C, pH=7.5

enzyme: UniProt P0A0C1

substrate: kanamycin A


substrate_name: tobramycin

substrate: tobramycin


substrate_name: kanamycin B

substrate: kanamycin B


enzyme_display_name: UniProt P96762

organism: Enterococcus gallinarum

enzyme: UniProt P96762


substrate_name: ATP

substrate: ATP


enzyme_display_name: glycerate 2-kinase

organism: Picrophilus oshimae

substrate_name: (R)-glycerate

enzyme: glycerate 2-kinase

substrate: (R)-glycerate


assay_conditions_summary: pH 7.3; 333.15 K; cofactor ATP


enzyme_display_name: aminoglycoside 2''-phosphotransferase

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F95Y with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

enzyme: aminoglycoside 2''-phosphotransferase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F95M with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

column_label: Table 2 (Steady state kinetic parameters for APH(2'')-IVa), Protein row 'Wild type', NTP row 'ATP'; column 'kcat (s^-1)' = 4.37; column 'Km (uM)' = 69; column 'kcat/Km (M^-1 s^-1)' = 6.3 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.37 s^-1; already in s^-1, no unit conversion applies; the paper value is 4.37 s^(-1). Km: printed Table 2 cell 69 uM; 69 / 1000 = 0.069 mM. kcat/Km: printed Table 2 cell 6.3 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 63000 / 1000 = 63.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Protein row 'Wild type', NTP row 'ATP': kcat = 4.37 s^-1; Km = 69 uM; printed kcat/Km = 6.3 x 10^4 M^-1 s^-1.

table_label: Table 2: Steady state kinetic parameters for APH(2'')-IVa (J. Biol. Chem. 2012, 287(16):13094-13102)


column_label: Table 2 (Steady state kinetic parameters for APH(2'')-IVa), Protein row 'Wild type', NTP row 'GTP'; column 'kcat (s^-1)' = 5.03; column 'Km (uM)' = 168; column 'kcat/Km (M^-1 s^-1)' = 3.0 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.03 s^-1; already in s^-1, no unit conversion applies; the paper value is 5.03 s^(-1). Km: printed Table 2 cell 168 uM; 168 / 1000 = 0.168 mM. kcat/Km: printed Table 2 cell 3.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 30000 / 1000 = 30.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Protein row 'Wild type', NTP row 'GTP': kcat = 5.03 s^-1; Km = 168 uM; printed kcat/Km = 3.0 x 10^4 M^-1 s^-1.


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


sequence_variant_note: Mutation signature Y92A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant Y92A, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: fructoselysine 6-kinase

substrate_name: fructosyl-L-valine

enzyme: fructoselysine 6-kinase

substrate: fructosyl-L-valine


substrate_name: fructosylglycine

smiles: C(C(C(C(C(=O)CNCC(=O)O)O)O)O)O

substrate: fructosylglycine


enzyme_display_name: cytidine kinase

organism: Schistosoma mansoni

assay_conditions_summary: pH 7.4; 313.15 K; cofactor ATP

enzyme: cytidine kinase


enzyme_display_name: farnesol kinase

organism: Rattus norvegicus

smiles: CC(=CCCC(=CCCC(=CCO)C)C)C

enzyme: farnesol kinase


enzyme_display_name: mevalonate 3-kinase

organism: Unknown

substrate_name: Unknown

enzyme: mevalonate 3-kinase

substrate: Unknown


organism: Streptococcus pyogenes

substrate_name: Protein N-phosphohistidine; D-Mannose

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

substrate: Protein N-phosphohistidine; D-Mannose


enzyme_display_name: inositol phosphorylceramide synthase

organism: Candida albicans

proof_lines:
CHAPS-washed membranes, pH 7.5, 23°C
pH 7.0, 23°C

enzyme: inositol phosphorylceramide synthase


organism: Phaseolus vulgaris


substrate_name: Protein N-phosphohistidine; Maltotriose

substrate: Protein N-phosphohistidine; Maltotriose


enzyme_display_name: D-threonate 4-kinase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

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

enzyme: D-threonate 4-kinase


substrate_name: D-threonate

substrate: D-threonate


enzyme_display_name: Nucleoside kinase

organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: guanosine (at pH 8.0 and 22 degrees Celsius)

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: kcat is 0.072 sec(-1) with ATP and guanosine as substrates. kcat is 0.16 sec(-1) with ATP and inosine as substrates. kcat is 0.064 sec(-1) with ATP and cytidine as substrates. kcat is 0.084 sec(-1) with ATP and adenosine as substrates. kcat

enzyme: Nucleoside kinase


substrate_name: inosine (at pH 8.0 and 22 degrees Celsius)


substrate_name: cytidine (at pH 8.0 and 22 degrees Celsius)


substrate_name: adenosine (at pH 8.0 and 22 degrees Celsius)


substrate_name: ATP (at pH 8.0 and 22 degrees Celsius)

substrate: ATP (at pH 8.0 and 22 degrees Celsius)


substrate_name: GTP (at pH 8.0 and 22 degrees Celsius)

substrate: GTP (at pH 8.0 and 22 degrees Celsius)


enzyme_display_name: D-erythronate 4-kinase

organism: Heliomicrobium modesticaldum

enzyme: D-erythronate 4-kinase


enzyme_display_name: Autoinducer-2 kinase

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

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

enzyme: Autoinducer-2 kinase


enzyme_display_name: C7-cyclitol 7-kinase

organism: Streptomyces hygroscopicus subsp. jinggangensis

substrate_name: valienone

proof_lines: kcat is 7.3 sec(-1) for validone as substrate. kcat is 3.5 sec(-1) for valienone as substrate.

enzyme: C7-cyclitol 7-kinase

substrate: valienone


substrate_name: validone

substrate: validone


organism: Thermococcus kodakarensis

proof_lines: kcat is 280 sec(-1) with cytidine as substrate. kcat is 226 sec(-1) with deoxycytidine as substrate. kcat is 222 sec(-1) with ATP as substrate.


substrate_name: cytidine

substrate: cytidine


enzyme_display_name: ATP-dependent L-serine kinase SbnI

organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: ATP

proof_lines: kcat is 3.9 min(-1) with ATP as substrate. kcat is 14.3 min(-1) with L-serine as substrate.

enzyme: ATP-dependent L-serine kinase SbnI


substrate_name: L-serine

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

substrate: L-serine


enzyme_display_name: cytidine diphosphoramidate kinase

organism: Campylobacter jejuni subsp. jejuni serotype O:2

substrate_name: CDP-methyl phosphonate

column_label: Table 1. Kinetic Constants of Cj1415 at 25 C, pH 8.0; row CDP-Me (5); kcat column (s^-1) = 1.4 +/- 0.1 s^-1; kcat/Km column (M^-1 s^-1), normalized to s^-1 mM^-1 by dividing by 1000 = 1700 +/- 400 M^-1 s^-1; Km column (mM) = 0.8 +/- 0.2 mM

normalized_value_unit_evidence: kcat 1.4 s^-1; kcat_over_km 1.7 s^-1 mM^-1; km 0.8 mM

row_label: CDP-Me (5)

enzyme: cytidine diphosphoramidate kinase

substrate: CDP-methyl phosphonate


substrate_name: cytidine 5'-diphosphoramidate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S85A to reconstruct the assayed variant sequence.

substrate: cytidine 5'-diphosphoramidate


column_label: Table 1. Kinetic Constants of Cj1415 at 25 C, pH 8.0; row CDP-NH2 (1); kcat column (s^-1) = 2.2 +/- 0.3 s^-1; kcat/Km column (M^-1 s^-1), normalized to s^-1 mM^-1 by dividing by 1000 = 20000 +/- 3300 M^-1 s^-1; Km column (mM) = 0.11 +/- 0.01 mM

normalized_value_unit_evidence: kcat 2.2 s^-1; kcat_over_km 20 s^-1 mM^-1; km 0.11 mM

row_label: CDP-NH2 (1)


column_label: Table 1. Kinetic Constants of Cj1415 at 25 C, pH 8.0; row ATP; kcat column (s^-1) = 2.2 +/- 0.3 s^-1; kcat/Km column (M^-1 s^-1), normalized to s^-1 mM^-1 by dividing by 1000 = 1500 +/- 200 M^-1 s^-1; Km column (mM) = 1.5 +/- 0.1 mM

normalized_value_unit_evidence: kcat 2.2 s^-1; kcat_over_km 1.5 s^-1 mM^-1; km 1.5 mM

row_label: ATP


enzyme_display_name: D-threonate kinase

proof_lines: kcat is 22 sec(-1) with D-threonate as substrate. kcat is 4.0 sec(-1) with 4-hydroxy-L-threonine as substrate.

enzyme: D-threonate kinase


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: MurNAc (at pH 7.6 and 25 degrees Celsius)

proof_lines: kcat is 5.15 sec(-1) for MurNAc phosphorylation. kcat is 6.64 sec(-1) for GlcNAc phosphorylation (at pH 7.6 and 25 degrees Celsius).


substrate_name: GlcNAc(at pH 7.6 and 25 degrees Celsius)


substrate_name: ATP(at pH 7.6 and 25 degrees Celsius)

assay_conditions_summary: pH 7.6; cofactor ATP

substrate: ATP(at pH 7.6 and 25 degrees Celsius)


enzyme_display_name: GTP-dependent dephospho-CoA kinase

assay_conditions_summary: pH 8; cofactor CoA

column_label: Table 1 columns Substrate, Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1); row Dephospho-CoA under T. kodakarensis

normalized_value_unit_evidence: Km 0.14 mM; kcat 5.57 s^-1; kcat/Km paper cell 40.4 s^-1 mM^-1 (sheet ratio 39.785714285714285 comes from rounded kcat/Km)

raw_value_unit_evidence: Dephospho-CoA row: Km 0.14 +/- 0.02 mM; kcat 5.57 s^-1; kcat/Km 40.4 s^-1 mM^-1

row_label: T. kodakarensis / Dephospho-CoA

table_label: PMC6650551 Table 1 - Kinetic parameters of DPCK toward dephospho-CoA and GTP

enzyme: GTP-dependent dephospho-CoA kinase


substrate_name: GTP

column_label: Table 1 columns Substrate, Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1); row GTP under T. kodakarensis

normalized_value_unit_evidence: Km 0.26 mM; kcat 6.68 s^-1; kcat/Km 25.7 s^-1 mM^-1 (sheet ratio 25.69230769230769 is the same to paper precision)

row_label: T. kodakarensis / GTP

substrate: GTP


enzyme_display_name: Cytidine diphosphoramidate kinase

organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: cytidine diphosphoramidate

column_label: Table 1. Kinetic Constants of Cj1415 at 25 C, pH 8.0; row CDP-NH2 (1); Km column (mM) = 0.11 +/- 0.01 mM

normalized_value_unit_evidence: km 0.11 mM

enzyme: Cytidine diphosphoramidate kinase

substrate: cytidine diphosphoramidate


column_label: Table 1. Kinetic Constants of Cj1415 at 25 C, pH 8.0; row ATP; Km column (mM) = 1.5 +/- 0.1 mM

normalized_value_unit_evidence: km 1.5 mM

substrate: ATP


substrate_name: CDP

column_label: Table 1. Kinetic Constants of Cj1415 at 25 C, pH 8.0; row CDP (3); Km column (mM) = 4.2 +/- 0.7 mM

normalized_value_unit_evidence: km 4.2 mM

row_label: CDP (3)

substrate: CDP


substrate_name: CDP-methyl phosphate

column_label: Table 1. Kinetic Constants of Cj1415 at 25 C, pH 8.0; row CDP-OMe (4); Km column (mM) = 1.4 +/- 0.2 mM

normalized_value_unit_evidence: km 1.4 mM

row_label: CDP-OMe (4)

substrate: CDP-methyl phosphate


column_label: Table 1. Kinetic Constants of Cj1415 at 25 C, pH 8.0; row CDP-Me (5); Km column (mM) = 0.8 +/- 0.2 mM

normalized_value_unit_evidence: km 0.8 mM


substrate_name: uridine diphosphoramidate

column_label: Table 1. Kinetic Constants of Cj1415 at 25 C, pH 8.0; row UDP-NH2 (6); Km column (mM) = 21 +/- 3 mM

normalized_value_unit_evidence: km 21 mM

row_label: UDP-NH2 (6)

substrate: uridine diphosphoramidate


enzyme_display_name: Cytidine kinase

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

substrate_name: deoxycytidine

enzyme: Cytidine kinase

substrate: deoxycytidine


enzyme_display_name: acetate kinase

organism: Acetivibrio thermocellus

substrate_name: acetate

enzyme: acetate kinase

substrate: acetate


enzyme_display_name: UniProt A8BB85

organism: Giardia intestinalis

substrate_name: Carbamate

enzyme: UniProt A8BB85

substrate: Carbamate


substrate_name: ADP

substrate: ADP


substrate_name: Carbamoyl phosphate

substrate: Carbamoyl phosphate


substrate_name: ATP


enzyme_display_name: UniProt P00560

organism: Saccharomyces cerevisiae

enzyme: UniProt P00560


enzyme_display_name: UniProt A8JC04

organism: Chlamydomonas reinhardtii

enzyme: UniProt A8JC04


enzyme_display_name: UniProt P07378

organism: Trypanosoma brucei brucei

enzyme: UniProt P07378


enzyme_display_name: UniProt P09403

organism: Thermus thermophilus

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

enzyme: UniProt P09403


enzyme_display_name: UniProt P00558

organism: Homo sapiens P00558 GenBank

enzyme: UniProt P00558


substrate_name: 2-deoxy-alpha-D-ribose 1-phosphate

assay_conditions_summary: cofactor ADP

proof_lines: presence of Mg2+, pH and temperature not specified in the publication

proof_lines: presence of Mg2+, pH not specified in the publication, temperature not specified in the publication

proof_lines: kcat is 485 sec(-1) with ribose 1-phosphate as substrate. kcat is 73 sec(-1) with deoxyribose 1-phosphate as substrate. kcat is 612 sec(-1) with ADP as substrate. kcat is 189 sec(-1) with GDP as substrate.

substrate: 2-deoxy-alpha-D-ribose 1-phosphate


substrate_name: GDP

substrate: GDP


substrate_name: alpha-D-ribose 1-phosphate

substrate: alpha-D-ribose 1-phosphate


proof_lines: depending on the presence of Ca2+, pH and temperature not specified in the publication


enzyme_display_name: D-erythrulose 4-kinase

organism: Mycolicibacterium smegmatis

substrate_name: dihydroxyacetone

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

proof_lines: pH and temperature not specified in the publication

proof_lines: kcat is 2.88 sec(-1) with D-erythrulose as substrate. kcat is 0.091 sec(-1) with L-erythrulose as substrate. kcat is 0.063 sec(-1) with dihydroxyacetone as substrate.

enzyme: D-erythrulose 4-kinase

substrate: dihydroxyacetone


substrate_name: D-erythrulose

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

substrate: D-erythrulose


enzyme_display_name: UniProt Q01217

enzyme: UniProt Q01217


substrate_name: N-acetyl-L-glutamate

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

substrate: N-acetyl-L-glutamate


enzyme_display_name: UniProt Q9SCL7

organism: Arabidopsis thaliana

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt Q9SCL7


enzyme_display_name: aminoglycoside 2''-phosphotransferase

organism: Campylobacter jejuni

substrate_name: tobramycin

enzyme: aminoglycoside 2''-phosphotransferase

substrate: tobramycin


organism: Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)

substrate_name: D-threonate

proof_lines: kcat is 120 sec(-1) with D-threonate as substrate. kcat is 170 sec(-1) with 4-hydroxy-L-threonine as substrate.

substrate: D-threonate


enzyme_display_name: L-erythrulose 1-kinase

proof_lines: kcat is 1.79 sec(-1) with L-erythrulose as substrate. kcat is 1.60 sec(-1) with D-erythrulose as substrate. kcat is 2.12 sec(-1) with dihydroxyacetone as substrate.

enzyme: L-erythrulose 1-kinase


enzyme_display_name: UniProt O06961

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: UTP

enzyme: UniProt O06961

substrate: UTP


substrate_name: CTP

substrate: CTP


substrate_name: Butyrate

smiles: CCCC(=O)[O-]

substrate: Butyrate


substrate_name: GTP

substrate: GTP


enzyme_display_name: UniProt P12277

organism: Homo sapiens

substrate_name: N-ethylglycocyamine

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

enzyme: UniProt P12277

substrate: N-ethylglycocyamine


substrate_name: Creatine

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

substrate: Creatine


substrate_name: cyclocreatine

substrate: cyclocreatine


enzyme_display_name: UniProt P00563

organism: Oryctolagus cuniculus

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=25°C, pH=-----

enzyme: UniProt P00563

substrate: ATP


proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=-----, pH=-----


enzyme_display_name: UniProt P06732

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=25Â°C, pH=-----

enzyme: UniProt P06732


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


enzyme_display_name: L-erythrulose kinase

substrate_name: L-erythrulose

proof_lines: kcat is 2.76 sec(-1) with L-erythrulose as substrate. kcat is 0.72 sec(-1) with D-erythrulose as substrate. kcat is 1.34 sec(-1) with dihydroxyacetone as substrate.

enzyme: L-erythrulose kinase

substrate: L-erythrulose


column_label: Supplementary Table 5. Kinetic parameters for kinase activity of Q6D8V6; row/segment Q6D8V6/ECA0866; Dihydroxyacetone; column/metric KM (mM)

raw_value_unit_evidence: Supplementary Table 5 reports KM 0.015 +/- 0.005 mM for Q6D8V6/ECA0866 with dihydroxyacetone.

row_label: Q6D8V6/ECA0866; Dihydroxyacetone


enzyme_display_name: D-threonate kinase

organism: Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)

proof_lines: kcat is 41 sec(-1) with D-threonate as substrate. kcat is 28 sec(-1) with 4-hydroxy-L-threonine as substrate.

enzyme: D-threonate kinase


enzyme_display_name: D-erythronate kinase

organism: Heliobacterium modesticaldum (strain ATCC 51547 / Ice1)

substrate_name: D-erythronate

proof_lines: kcat is 16 sec(-1) with D-erythronate as substrate. kcat is 12 sec(-1) with D-threonate as substrate. kcat is 41 sec(-1) with 4-hydroxy-L-threonine as substrate.

enzyme: D-erythronate kinase

substrate: D-erythronate


column_label: Table S2; row B0TBI9 (HmDenK) / 4-Hydroxy-L-threonine; KM (mM) column cell 44; populated export metric Km=44 mM

normalized_value_unit_evidence: Km=44 mM

raw_value_unit_evidence: B0TBI9 (HmDenK) / 4-Hydroxy-L-threonine: KM=44 mM in Supplementary Table S2

row_label: B0TBI9 (HmDenK) / 4-Hydroxy-L-threonine

table_label: Table S2. Kinetic parameters for PdxA2-DUF1537 proteins


enzyme_display_name: L-serine kinase (ADP)

organism: Thermococcus kodakarensis

substrate_name: ADP

assay_conditions_summary: pH 7.5; 358.15 K; cofactor ADP

proof_lines: kcat is 218 sec(-1) with serine as substrate. kcat is 204 sec(-1) with ADP as substrate.

source_databases_merged: brenda skid uniprot

enzyme: L-serine kinase (ADP)

substrate: ADP


substrate_name: L-serine

substrate: L-serine


enzyme_display_name: D-threonate 4-kinase

organism: Cupriavidus necator

assay_conditions_summary: pH 8

proof_lines: kcat is 45 sec(-1) with D-threonate as substrate. kcat is 27 sec(-1) with 4-hydroxy-L-threonine as substrate.

enzyme: D-threonate 4-kinase


substrate_name: Unknown

substrate: Unknown


organism: Enterococcus casseliflavus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, recombinant enzyme, versus kanamycin

proof_lines: pH 7.5, 25°C, recombinant enzyme, versus ATP


enzyme_display_name: ADP-dependent ribose-1-phosphate kinase

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

proof_lines: kcat is 485 sec(-1) with ribose 1-phosphate as substrate. kcat is 73 sec(-1) with deoxyribose 1-phosphate as substrate. kcat is 612 sec(-1) with ADP as substrate. kcat is 189 sec(-1) with GDP as substrate.

enzyme: ADP-dependent ribose-1-phosphate kinase


enzyme_display_name: Nucleoside kinase

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

enzyme: Nucleoside kinase


enzyme_display_name: Cytidine kinase

proof_lines: kcat is 280 sec(-1) with cytidine as substrate. kcat is 226 sec(-1) with deoxycytidine as substrate. kcat is 222 sec(-1) with ATP as substrate.

enzyme: Cytidine kinase


enzyme_display_name: cytidine diphosphoramidate kinase

substrate_name: ATP; Cytidine diphosphoramidate

proof_lines: kcat is 2.2 sec(-1) with cytidine diphosphoramidate as substrate. kcat is 2.2 sec(-1) with 2'-deoxycytidine diphosphoramidate as substrate. kcat is 0.64 sec(-1) with CDP as substrate. kcat is 0.65 sec(-1) with CDP-methyl phosphate as substr

enzyme: cytidine diphosphoramidate kinase

substrate: ATP; Cytidine diphosphoramidate


organism: Campylobacter jejuni subsp. jejuni serotype O:2

substrate_name: 2'-deoxycytidine 5'-diphosphoramidate

substrate: 2'-deoxycytidine 5'-diphosphoramidate


enzyme_display_name: ATP-dependent L-serine kinase

organism: Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)

proof_lines: kcat is 57.0 sec(-1) with serine as substrate. kcat is 78.4 sec(-1) with ATP as substrate. kcat is 60.9 sec(-1) with UTP as substrate. kcat is 130 sec(-1) with triphosphate as substrate.

enzyme: ATP-dependent L-serine kinase


enzyme_display_name: GTP-dependent dephospho-CoA kinase

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 5.57 sec(-1) with dephospho-CoA as substrate (PubMed:31337720). kcat is 6.68 sec(-1) with GTP as substrate (PubMed:31337720).

enzyme: GTP-dependent dephospho-CoA kinase


enzyme_display_name: UniProt A0A0A7CK57

organism: Daphnia magna

substrate_name: ATP

enzyme: UniProt A0A0A7CK57


substrate_name: L-arginine

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

substrate: L-arginine


enzyme_display_name: UniProt O15992

organism: Anthopleura japonica

enzyme: UniProt O15992


substrate_name: L-Arg

substrate: L-Arg


enzyme_display_name: UniProt O96507

organism: Trypanosoma cruzi

enzyme: UniProt O96507


enzyme_display_name: PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component

organism: Escherichia coli (strain K12)

substrate_name: mannosyl-D-glycerate

column_label: PMID 14645248 Figure 2B caption/prose, MG uptake by MG-induced MC4100 cells, Km = 10 uM.

raw_value_unit_evidence: Figure 2B caption/prose reports a Km of 10 uM for [14C]MG uptake.

row_label: MG-induced MC4100 cells / [14C]MG uptake

table_label: Figure 2B caption/prose

substrate: mannosyl-D-glycerate


organism: Klebsiella pneumoniae

substrate_name: L-Sorbose; Protein N-phosphohistidine

substrate: L-Sorbose; Protein N-phosphohistidine


organism: Staphylococcus aureus


organism: Bacillus subtilis

substrate_name: Maltose; Protein N-phosphohistidine

substrate: Maltose; Protein N-phosphohistidine


enzyme_display_name: L-erythrulose 1-kinase

organism: Pectobacterium atrosepticum

substrate_name: L-Erythrulose; ATP

enzyme: L-erythrulose 1-kinase

substrate: L-Erythrulose; ATP


enzyme_display_name: erythritol kinase (D-erythritol 1-phosphate-forming)

organism: Brucella abortus

substrate_name: Erythritol; ATP

substrate: Erythritol; ATP


enzyme_display_name: aminoglycoside 2''-phosphotransferase

organism: Campylobacter jejuni

substrate_name: tobramycin

enzyme: aminoglycoside 2''-phosphotransferase

substrate: tobramycin


substrate_name: sisomicin

assay_conditions_summary: pH 7; 295.15 K; cofactor NADH

column_label: Table 2. Steady-state kinetic parameters for aminoglycosides and nucleotides row sisomicin / APH(2"-If), column APH(2"-If); kcat s^-1, raw cell 17 +/- 1, normalized 17 s^-1; Table 2. Steady-state kinetic parameters for aminoglycosides and nucleotides row sisomicin / APH(2"-If), column APH(2"-If); Km uM, raw cell 1.6 +/- 0.3, normalized 0.0016 mM; Table 2. Steady-state kinetic parameters for aminoglycosides and nucleotides row sisomicin / APH(2"-If), column APH(2"-If); kcat/Km M^-1 s^-1, raw cell (1.1 +/- 0.2) x 10^7, normalized 11000 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=17 normalized_unit=s^-1; Km normalized_value=0.0016 normalized_unit=mM; kcat/Km normalized_value=11000 normalized_unit=s^-1*mM^-1

row_label: sisomicin / APH(2"-If)

substrate: sisomicin


substrate_name: netilmicin

substrate: netilmicin


enzyme_display_name: fructoselysine 6-kinase

substrate_name: ATP; epsilon-Fructoselysine

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

enzyme: fructoselysine 6-kinase

substrate: ATP; epsilon-Fructoselysine


organism: Escherichia coli

substrate_name: epsilon-Fructoselysine; ATP

substrate: epsilon-Fructoselysine; ATP


enzyme_display_name: L-serine kinase (ATP)

substrate_name: ATP; L-Serine

enzyme: L-serine kinase (ATP)

substrate: ATP; L-Serine


substrate_name: L-Serine; ATP

substrate: L-Serine; ATP


enzyme_display_name: inositol phosphorylceramide synthase

organism: Saccharomyces cerevisiae

enzyme: inositol phosphorylceramide synthase


column_label: Table 1. MIC data, steady-state kinetic parameters, and dissociation constants for AAC(6')-Ie/APH(2'')-Ia; row/segment 4,6-disubstituted / Netilmicin; kcat column (s^-1) = 6.5 +/- 0.1 s^-1; kcat/Km column (M^-1 s^-1), normalized to s^-1 mM^-1 by dividing by 1000 = (1.6 +/- 0.2) x 10^7 M^-1 s^-1; Km column (uM), normalized to mM by dividing by 1000 = 0.41 +/- 0.05 uM

row_label: 4,6-disubstituted / Netilmicin