organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

proof_lines: kcat is 1.14 sec(-1) with acetoacetyl-CoA as substrate. kcat is 5.72 sec(-1) with beta-keto-octanoyl-CoA as substrate.

substrate: acetoacetyl-CoA


enzyme_display_name: Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

organism: Sus scrofa

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8; cofactor CoA

column_label: Table 1, row 3-Hydroxybutyryl-CoA, column Apparent Km (uM): 7.2. Shared footnote a states pH 8 forward-direction measurements with L-3-hydroxyacyl-CoA as variable substrate, several fixed NAD+ concentrations, CoASH, and 3-ketoacyl-CoA thiolase.

raw_value_unit_evidence: Apparent Km 7.2 uM.

table_label: Table 1. Kinetic Parameters of Pig Heart 3-Hydroxyacyl-CoA Dehydrogenase

status: verified

source: uniprot


enzyme_display_name: acetoacetyl-CoA reductase

organism: Methylorubrum rhodesianum

substrate_name: L-beta-hydroxybutyryl-CoA

source_db: brenda

verification_status: unverified

assay_conditions_summary: cofactor CoA

enzyme: acetoacetyl-CoA reductase

substrate: L-beta-hydroxybutyryl-CoA

status: unverified

source: brenda


organism: Vitis vinifera

substrate_name: Unknown

km_display: Not reported

substrate: Unknown


enzyme_display_name: UniProt Q0KEY8

organism: Cupriavidus necator

substrate_name: acetoacetyl-CoA

source_db: skid

source_license: CC BY-NC-ND 4.0

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

data_origin: experimental

enzyme: UniProt Q0KEY8

source: skid


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Homo sapiens

substrate_name: 5-alpha-pregnan-20-beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor CoA

proof_lines: kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


organism: Mycobacterium smegmatis

substrate_name: H+; NADPH; Acetoacetyl-CoA

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

sequence_source: multiple

assay_conditions_summary: cofactor NADPH

substrate: H+; NADPH; Acetoacetyl-CoA


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: beta-ketododecanoyl-CoA (at 25 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: kcat is 4.3 sec(-1) with beta-ketododecanoyl-CoA as substrate. kcat is 3.5 sec(-1) with beta-ketooctanoyl-CoA as substrate. kcat is 1.9 sec(-1) with acetoacetyl-CoA as substrate. kcat is 2.6 sec(-1) with NADPH as substrate (PubMed:11932442)


organism: Escherichia coli

substrate_name: trans,trans-Farnesyl diphosphate

source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D215A to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: trans,trans-Farnesyl diphosphate

source: oed


enzyme_display_name: 4-O-dimethylallyl-L-tyrosine synthase

organism: Aspergillus niger

proof_lines:
TyrPT
tyrosine derivatives
Aspergillus niger

enzyme: 4-O-dimethylallyl-L-tyrosine synthase


proof_lines:
4- and 5-methyl-DL-tryptophan
L-tryptophan
TyrPT


substrate_name: alpha-methyl-L-tyrosine

substrate: alpha-methyl-L-tyrosine


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: D-Tyrosine

substrate: D-Tyrosine


substrate_name: Isopentenyl diphosphate

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

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

substrate: Isopentenyl diphosphate


enzyme_display_name: Alanine--glyoxylate aminotransferase 2, mitochondrial

organism: Rattus norvegicus

substrate_name: N(omega),N('omega)-dimethyl-L-arginine (with pyruvate as cosubstrate)


substrate_name: N(omega),N(omega)-dimethyl-L-arginine (with pyruvate as cosubstrate)

verification_status: corrected

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

column_label: Table IV row N^G,N^G-Dimethyl-L-arginine:pyruvate; amino acid Km (mM) column = 9.7 +/- 1.2.

raw_value_unit_evidence: Km raw_value=9.7 +/- 1.2 raw_unit=mM

table_label: Table IV, Kinetic properties of dimethylarginine:pyruvate aminotransferase

enzyme: Alanine--glyoxylate aminotransferase 2, mitochondrial

status: corrected


substrate_name: N(omega)-methyl-L-arginine (with pyruvate as cosubstrate)

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

column_label: Table IV row N^G-Monomethyl-L-arginine:pyruvate; amino acid Km (mM) column = 8.0 +/- 0.9.

raw_value_unit_evidence: Km raw_value=8.0 +/- 0.9 raw_unit=mM


substrate_name: L-ornithine (with pyruvate as cosubstrate)

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

column_label: Table IV row L-Ornithine:pyruvate; amino acid Km (mM) column = 70.0 +/- 1.2.

raw_value_unit_evidence: Km raw_value=70.0 +/- 1.2 raw_unit=mM


substrate_name: L-alanine (with glyoxylate as cosubstrate)

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

column_label: Kinetic Properties prose states: in the transamination between L-alanine and glyoxylate, Km values for L-alanine and glyoxylate were 7.8 and 2.9 mM, respectively.

raw_value_unit_evidence: Km raw_value=7.8 raw_unit=mM

row_label: L-alanine in the L-alanine/glyoxylate substrate pair

table_label: Kinetic Properties prose, page 20940


substrate_name: pyruvate (with L-ornithine as cosubstrate)

column_label: Table IV row L-Ornithine:pyruvate; keto acid Km (mM) column = 4.1 +/- 0.5.

raw_value_unit_evidence: Km raw_value=4.1 +/- 0.5 raw_unit=mM


substrate_name: glyoxylate (with L-alanine as cosubstrate)

raw_value_unit_evidence: Km raw_value=2.9 raw_unit=mM

row_label: glyoxylate in the L-alanine/glyoxylate substrate pair


enzyme_display_name: UniProt P9WFF7

organism: Mycobacterium tuberculosis

substrate_name: isopentenyl diphosphate

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

column_label: Table 2; substrate column IPP; row Kcat (min^-1) raw value 4.8; row Km (uM) raw value 89; row Kcat/Km raw value 5.4 x 10^4 with unit M^-1*min^-1 from Kcat/Km using Km in M

normalized_value_unit_evidence: kcat normalized_value=0.08 normalized_unit=s^-1; Km normalized_value=0.089 normalized_unit=mM; kcat/Km normalized_value=0.9 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.8 raw_unit=min^-1; Km raw_value=89 raw_unit=uM; kcat/Km raw_value=5.4 x 10^4 raw_unit=M^-1*min^-1

row_label: IPP

table_label: Table 2. Calculated kinetic parameters of Rv2361c

source_databases_merged: skid uniprot

enzyme: UniProt P9WFF7

substrate: isopentenyl diphosphate


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

column_label: Table 2; substrate column E,Z-FPP; row Kcat (min^-1) raw value 690; row Km (uM) raw value 290; row Kcat/Km raw value 2.4 x 10^6 with unit M^-1*min^-1 from Kcat/Km using Km in M

normalized_value_unit_evidence: kcat normalized_value=11.5 normalized_unit=s^-1; Km normalized_value=0.29 normalized_unit=mM; kcat/Km normalized_value=40 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=690 raw_unit=min^-1; Km raw_value=290 raw_unit=uM; kcat/Km raw_value=2.4 x 10^6 raw_unit=M^-1*min^-1

row_label: E,Z-FPP

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


substrate_name: geranyl diphosphate

smiles: CC(C)=CCC/C(C)=C/COP(=O)(O)OP(=O)(O)O

column_label: Table 2; substrate column GPP; row Kcat (min^-1) raw value 3.6; row Km (uM) raw value 490; row Kcat/Km raw value 7.4 x 10^3 with unit M^-1*min^-1 from Kcat/Km using Km in M

normalized_value_unit_evidence: kcat normalized_value=0.06 normalized_unit=s^-1; Km normalized_value=0.49 normalized_unit=mM; kcat/Km normalized_value=0.1233333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=3.6 raw_unit=min^-1; Km raw_value=490 raw_unit=uM; kcat/Km raw_value=7.4 x 10^3 raw_unit=M^-1*min^-1

row_label: GPP

substrate: geranyl diphosphate


substrate_name: geranylgeranyl diphosphate

column_label: Table 2; substrate column GGPP; row Kcat (min^-1) raw value 1.8; row Km (uM) raw value 40; row Kcat/Km raw value 4.3 x 10^5 with unit M^-1*min^-1 from Kcat/Km using Km in M

normalized_value_unit_evidence: kcat normalized_value=0.03 normalized_unit=s^-1; Km normalized_value=0.04 normalized_unit=mM; kcat/Km normalized_value=7.166666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.8 raw_unit=min^-1; Km raw_value=40 raw_unit=uM; kcat/Km raw_value=4.3 x 10^5 raw_unit=M^-1*min^-1

row_label: GGPP

substrate: geranylgeranyl diphosphate


substrate_name: neryl diphosphate

smiles: CC(C)=CCC/C(C)=C\COP(=O)(O)OP(=O)(O)O

column_label: Official PMC HTML Table 2 row NPP columns Km=29 uM, Kcat=3.1 min^-1, Kcat/Km=1.1 x 10^5.

row_label: NPP

table_label: Table 2. Kinetic parameters for Rv2361c.

substrate: neryl diphosphate


substrate_name: D-Fructose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V605L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: D-Fructose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W74L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: L-Glutamine

sequence_variant_note: Mutation signature A602L matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: L-Glutamine


organism: Arabidopsis thaliana

smiles: NCCCC(=O)O

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate GABA (4-aminobutanoate) / fixed substrate pyruvate, column kcat s^-1, raw cell 10.6, normalized 10.6 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate GABA (4-aminobutanoate) / fixed substrate pyruvate, column Km mM, raw cell 0.34+/-0.02, normalized 0.34 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate GABA (4-aminobutanoate) / fixed substrate pyruvate, column kcat/Km s^-1 mM^-1, raw cell 31, normalized 31 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.6 normalized_unit=s^-1; Km normalized_value=0.34 normalized_unit=mM; kcat/Km normalized_value=31 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.6 raw_unit=s^-1 raw_cell=10.6; Km raw_value=0.34+/-0.02 raw_unit=mM raw_cell=0.34+/-0.02; kcat/Km raw_value=31 raw_unit=s^-1*mM^-1 raw_cell=31


column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (4-oxobutanoate; succinate semialdehyde) / fixed substrate alanine, column kcat s^-1, raw cell 10.8, normalized 10.8 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (4-oxobutanoate; succinate semialdehyde) / fixed substrate alanine, column Km mM, raw cell 0.014+/-0.002, normalized 0.014 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (4-oxobutanoate; succinate semialdehyde) / fixed substrate alanine, column kcat/Km s^-1 mM^-1, raw cell 770, normalized 770 s^-1*mM^-1

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

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


substrate_name: glyoxylate

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate glyoxylate / fixed substrate GABA, column kcat s^-1, raw cell 9.7, normalized 9.7 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate glyoxylate / fixed substrate GABA, column Km mM, raw cell 0.11+/-0.01, normalized 0.11 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate glyoxylate / fixed substrate GABA, column kcat/Km s^-1 mM^-1, raw cell 88, normalized 88 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=9.7 normalized_unit=s^-1; Km normalized_value=0.11 normalized_unit=mM; kcat/Km normalized_value=88 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=9.7 raw_unit=s^-1 raw_cell=9.7; Km raw_value=0.11+/-0.01 raw_unit=mM raw_cell=0.11+/-0.01; kcat/Km raw_value=88 raw_unit=s^-1*mM^-1 raw_cell=88

substrate: glyoxylate


substrate_name: L-alanine

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate alanine / fixed substrate SSA, column kcat s^-1, raw cell 15.4, normalized 15.4 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate alanine / fixed substrate SSA, column Km mM, raw cell 2.4+/-0.3, normalized 2.4 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate alanine / fixed substrate SSA, column kcat/Km s^-1 mM^-1, raw cell 6.4, normalized 6.4 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=15.4 normalized_unit=s^-1; Km normalized_value=2.4 normalized_unit=mM; kcat/Km normalized_value=6.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=15.4 raw_unit=s^-1 raw_cell=15.4; Km raw_value=2.4+/-0.3 raw_unit=mM raw_cell=2.4+/-0.3; kcat/Km raw_value=6.4 raw_unit=s^-1*mM^-1 raw_cell=6.4

substrate: L-alanine


substrate_name: pyruvate

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat s^-1, raw cell 10.6, normalized 10.6 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column Km mM, raw cell 0.14+/-0.01, normalized 0.14 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat/Km s^-1 mM^-1, raw cell 76, normalized 76 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.6 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM; kcat/Km normalized_value=76 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.6 raw_unit=s^-1 raw_cell=10.6; Km raw_value=0.14+/-0.01 raw_unit=mM raw_cell=0.14+/-0.01; kcat/Km raw_value=76 raw_unit=s^-1*mM^-1 raw_cell=76

substrate: pyruvate


enzyme_display_name: Serine 3-dehydrogenase

organism: Agrobacterium tumefaciens

substrate_name: L-serine

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

enzyme: Serine 3-dehydrogenase

substrate: L-serine


substrate_name: L-glycerate

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

column_label: Kinetic prose; ordered analytes D-serine, L-glycerate, D-glycerate; ordered Km values 44, 54, 56 mM; L-glycerate maps to 54 mM.

normalized_value_unit_evidence: L-glycerate Km = 54 mM.

raw_value_unit_evidence: Primary Kinetic prose: Km for D-serine, L-glycerate, and D-glycerate were 44, 54, and 56 mM, respectively.

row_label: D-serine, L-glycerate, and D-glycerate Km sentence; L-glycerate

table_label: Kinetic prose, journal page 155

substrate: L-glycerate


substrate_name: D-glycerate

column_label: Kinetic prose; ordered analytes D-serine, L-glycerate, D-glycerate; ordered Km values 44, 54, 56 mM; D-glycerate maps to 56 mM.

normalized_value_unit_evidence: D-glycerate Km = 56 mM.

row_label: D-serine, L-glycerate, and D-glycerate Km sentence; D-glycerate

substrate: D-glycerate


substrate_name: NADP(+)

assay_conditions_summary: cofactor NADP+

substrate: NADP(+)


organism: Leptosphaeria maculans

substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-Tyr (at pH 7.5 and 37 degrees Celsius)


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

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


substrate_name: L-tryptophan (at pH 7.5 and 37 degrees Celsius)


enzyme_display_name: 4-hydroxybenzoate geranyltransferase 1

organism: Lithospermum erythrorhizon

column_label: Results prose gives LePGT-1 and LePGT-2 Km values of 10.3 and 53.8 uM for 4HB, respectively; current accession Q8W405 is LePGT-1.

raw_value_unit_evidence: LePGT-1 Km for 4HB = 10.3 uM.

row_label: Recombinant LePGT-1 (Q8W405)

table_label: Results prose, PDF page 3 / JBC page 6243

enzyme: 4-hydroxybenzoate geranyltransferase 1


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

column_label: Results prose gives LePGT-1 and LePGT-2 Km values of 5.1 and 45.9 uM for GPP, respectively; current accession Q8W405 is LePGT-1.

raw_value_unit_evidence: LePGT-1 Km for GPP = 5.1 uM.


enzyme_display_name: 4-hydroxybenzoate geranyltransferase 2

column_label: Results prose gives LePGT-1 and LePGT-2 Km values of 10.3 and 53.8 uM for 4HB, respectively; current accession Q8W404 is LePGT-2.

raw_value_unit_evidence: LePGT-2 Km for 4HB = 53.8 uM.

row_label: Recombinant LePGT-2 (Q8W404)

enzyme: 4-hydroxybenzoate geranyltransferase 2


column_label: Results prose gives LePGT-1 and LePGT-2 Km values of 5.1 and 45.9 uM for GPP, respectively; current accession Q8W404 is LePGT-2.

raw_value_unit_evidence: LePGT-2 Km for GPP = 45.9 uM.


enzyme_display_name: carbazole 1,9a-dioxygenase

organism: Janthinobacterium sp. J3

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I262V to reconstruct the assayed variant sequence.

enzyme: carbazole 1,9a-dioxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q282N to reconstruct the assayed variant sequence.


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


enzyme_display_name: 4-aminobutyrate aminotransferase PuuE

organism: Escherichia coli (strain K12)

substrate_name: SSA (at pH 7.8 and at 30 degrees Celsius)

enzyme: 4-aminobutyrate aminotransferase PuuE


substrate_name: GABA (at pH 7.8 and at 30 degrees Celsius)

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


substrate_name: KG (at pH 7.8 and at 30 degrees Celsius)

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


substrate_name: L-glutamate (at pH 7.8 and at 30 degrees Celsius)

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


substrate_name: D-aspartate

substrate: D-aspartate


substrate_name: D-alanine

substrate: D-alanine


substrate_name: D-glutamate

substrate: D-glutamate


enzyme_display_name: glyoxylate reductase

organism: Thermococcus litoralis

substrate_name: NADH

assay_conditions_summary: pH 6.5; cofactor NADH

column_label: Wiley full-text Abstract prose reports Km values for glyoxylate, hydroxypyruvate, and NADH in that order as 0.73, 1.3, and 0.067 mM; NADH maps to the third value.

raw_value_unit_evidence: NADH Km 0.067 mM

row_label: NADH

table_label: Wiley full-text Abstract prose

source_databases_merged: brenda uniprot

enzyme: glyoxylate reductase

substrate: NADH


substrate_name: glyoxylate

column_label: Wiley full-text Abstract prose reports Km values for glyoxylate, hydroxypyruvate, and NADH in that order as 0.73, 1.3, and 0.067 mM; glyoxylate maps to the first value.

raw_value_unit_evidence: glyoxylate Km 0.73 mM

row_label: glyoxylate


substrate_name: hydroxypyruvate

column_label: Wiley full-text Abstract prose reports Km values for glyoxylate, hydroxypyruvate, and NADH in that order as 0.73, 1.3, and 0.067 mM; hydroxypyruvate maps to the second value.

raw_value_unit_evidence: hydroxypyruvate Km 1.3 mM

row_label: hydroxypyruvate

substrate: hydroxypyruvate


enzyme_display_name: Fatty acid oxidation complex subunit alpha

substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: acetoacetyl-CoA

enzyme: Fatty acid oxidation complex subunit alpha

substrate: acetoacetyl-CoA


assay_conditions_summary: cofactor NADH


enzyme_display_name: Polyamine aminopropyltransferase

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

substrate_name: S-adenosylmethioninamine (at 78 degrees Celsius and at pH 7.5)

enzyme: Polyamine aminopropyltransferase


substrate_name: 1,3-diaminopropane (at 78 degrees Celsius and at pH 7.5)

smiles: C(CN)CN

column_label: Abstract lists 1,3-diaminopropane (Km = 1675 microM) among recognized amine acceptor substrates.

raw_value_unit_evidence: Km raw_value=1675 microM raw_unit=microM

row_label: Propylamine transferase / 1,3-diaminopropane amine acceptor

table_label: PubMed XML abstract PMID 3096734


substrate_name: putrescine (at 78 degrees Celsius and at pH 7.5)

smiles: C(CCN)CN

column_label: Abstract lists putrescine (Km = 3850 microM) among recognized amine acceptor substrates.

raw_value_unit_evidence: Km raw_value=3850 microM raw_unit=microM

row_label: Propylamine transferase / putrescine amine acceptor


enzyme_display_name: (2Z,6Z)-farnesyl diphosphate synthase

organism: Solanum habrochaites

substrate_name: dimethylallyl diphosphate

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

proof_lines: very short-chain polyisoprenoid products

enzyme: (2Z,6Z)-farnesyl diphosphate synthase

substrate: dimethylallyl diphosphate


substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


substrate_name: neryl diphosphate

substrate: neryl diphosphate


organism: Cereibacter sphaeroides

substrate_name: geranyl diphosphate

column_label: Table 2, GPP column, kcat/KM/KM rows: 4 min^-1; 18.5 +/- 3.5 microM; 0.21 min^-1 microM^-1.

raw_value_unit_evidence: Table 2 GPP: kcat = 4 min^-1; KM = 18.5 +/- 3.5 microM; printed kcat/KM = 0.21 min^-1 microM^-1.

table_label: Table 2: Calculated kinetic parameters of Rsdds

substrate: geranyl diphosphate


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

column_label: Springer abstract/prose sentence for FPP kinetic parameters; metric labels Vmax, KM, kcat, and kcat/KM are explicit.

raw_value_unit_evidence: Springer abstract reports Vmax 264.6 pmol/min, KM 13.1 uM, kcat 8.8 1/min, and kcat/KM 0.67 for FPP.

row_label: omega,E,E-farnesyl diphosphate (FPP), most appropriate substrate

table_label: Springer abstract/prose preview

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


column_label: Table 2, IPP column, kcat/KM/KM rows: 8.6 min^-1; 13.8 +/- 4.6 microM; 0.62 min^-1 microM^-1.

raw_value_unit_evidence: Table 2 IPP: kcat = 8.6 min^-1; KM = 13.8 +/- 4.6 microM; printed kcat/KM = 0.62 min^-1 microM^-1.


organism: Trypanosoma cruzi


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


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


enzyme_display_name: salicylate 1-monooxygenase

organism: Sphingomonas sp.

substrate_name: salicylate

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

assay_conditions_summary: pH 7

enzyme: salicylate 1-monooxygenase

substrate: salicylate


substrate_name: anthranilate

substrate: anthranilate


enzyme_display_name: Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1

proof_lines: AIM1 beta-oxidation Arabidopsis


enzyme_display_name: Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2

proof_lines: beta-oxidation Arabidopsis AIM1


enzyme_display_name: D-alanine aminotransferase

organism: Bacillus sp. (strain YM-1)

substrate_name: alpha-ketoglutarate

enzyme: D-alanine aminotransferase

substrate: alpha-ketoglutarate


substrate_name: alpha-ketobutyrate

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

substrate: alpha-ketobutyrate


substrate_name: alpha-ketovalerate

substrate: alpha-ketovalerate


enzyme_display_name: Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

organism: Homo sapiens

column_label: Table 2, Acetoacetyl-CoA block, Km row, Normal column reports 11.9 uM; normalized value is 0.0119 mM.

raw_value_unit_evidence: Km raw_value=11.9 raw_unit=uM

row_label: Normal column; Acetoacetyl-CoA block; Km row

table_label: Table 2. Kinetic properties of expressed M/SCHAD proteins


substrate_name: NADH

column_label: Table 2, NADH block, Km row, Normal column reports 24.2 uM; normalized value is 0.0242 mM.

raw_value_unit_evidence: Km raw_value=24.2 raw_unit=uM

row_label: Normal column; NADH block; Km row

enzyme: Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial


organism: Streptomyces anulatus

substrate_name: 5,10-dihydrophenazine 1-carboxylate

substrate: 5,10-dihydrophenazine 1-carboxylate


organism: Sus scrofa

column_label: Table 1, row 3-Hydroxydecanoyl-CoA, column Apparent Km (uM): 2.9. Row carries footnote b, From Ref. (19); shared footnote a states pH 8 forward-direction measurements with L-3-hydroxyacyl-CoA as variable substrate, several fixed NAD+ concentrations, CoASH, and 3-ketoacyl-CoA thiolase.

raw_value_unit_evidence: Apparent Km 2.9 uM.

row_label: 3-Hydroxydecanoyl-CoA (footnote b: From Ref. (19))


column_label: Table 1, row 3-Hydroxyhexadecanoyl-CoA, column Apparent Km (uM): 3.0. Shared footnote a states pH 8 forward-direction measurements with L-3-hydroxyacyl-CoA as variable substrate, several fixed NAD+ concentrations, CoASH, and 3-ketoacyl-CoA thiolase.

raw_value_unit_evidence: Apparent Km 3.0 uM.


enzyme_display_name: 4-O-dimethylallyl-L-tyrosine synthase

substrate_name: benzyl diphosphate

substrate: benzyl diphosphate


substrate_name: 2-pentenyl diphosphate

smiles: CC/C=C/COP(=O)(O)OP(=O)(O)O

substrate: 2-pentenyl diphosphate


organism: Plasmodium falciparum


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


organism: Vigna radiata var. radiata

substrate_name: L-glutamine

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

column_label: The abstract reports Km values of 3.8 mM for D-fructose 6-phosphate and 0.5 mM for L-glutamine.

raw_value_unit_evidence: Km raw_value=0.5 mM raw_unit=mM

row_label: Prose segment: L-glutamine Km

table_label: PubMed PMID 16658095 abstract

substrate: L-glutamine


substrate_name: D-fructose 6-phosphate

raw_value_unit_evidence: Km raw_value=3.8 mM raw_unit=mM

row_label: Prose segment: D-fructose 6-phosphate Km

substrate: D-fructose 6-phosphate


organism: Arabidopsis thaliana


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

substrate_name: N-acetylornithine (at pH 9.5 and 25 degrees Celsius)

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


substrate_name: ornithine (at pH 9.5 and 25 degrees Celsius)

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


organism: Pseudomonas sp.

assay_conditions_summary: pH 8


organism: Ovis aries


enzyme_display_name: 4-aminobutyrate aminotransferase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: 4-aminobutyrate aminotransferase


organism: Rattus norvegicus


substrate_name: beta-alanine

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

substrate: beta-alanine


enzyme_display_name: D-amino-acid transaminase

organism: Bacillus sp.

substrate_name: D-Alanine

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +13, so it is treated as a source-provided variant sequence.

enzyme: D-amino-acid transaminase

substrate: D-Alanine


enzyme_display_name: 2,4-dinitrotoluene dioxygenase

organism: Burkholderia sp.

proof_lines:
2,4-DNT degradation
2,4-dinitrotoluene dioxygenase
Burkholderia

enzyme: 2,4-dinitrotoluene dioxygenase


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase

organism: Euglena gracilis

substrate_name: acetoacetyl-CoA

assay_conditions_summary: pH 6.5; cofactor CoA

enzyme: 3-hydroxyacyl-CoA dehydrogenase

substrate: acetoacetyl-CoA


organism: Leptosphaeria maculans

substrate_name: L-tryptophan

enzyme: 4-O-dimethylallyl-L-tyrosine synthase

substrate: L-tryptophan


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

substrate_name: spermidine (at 78 degrees Celsius and at pH 7.5)

smiles: C(CCNCCCN)CN


substrate_name: 3-ethylpent-2-en-1-yl diphosphate

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

substrate: 3-ethylpent-2-en-1-yl diphosphate


enzyme_display_name: norspermine synthase

organism: Thermus thermophilus

proof_lines: Crystal Structures and Enzymatic Properties of a Triamine/Agmatine Aminopropyltransferase from Thermus thermophilus

enzyme: norspermine synthase


enzyme_display_name: Ophiobolin F synthase oblA

organism: Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)

substrate_name: geranylgeranyl diphosphate

enzyme: Ophiobolin F synthase oblA


enzyme_display_name: Decaprenyl diphosphate synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: IPP (at pH 7.9 and 37 degrees Celsius)

column_label: PubMed abstract metric sentence gives Km for isopentenyl diphosphate as 89 microM, normalized to 0.089 mM

normalized_value_unit_evidence: PubMed abstract Km normalized_value=0.089 normalized_unit=mM

raw_value_unit_evidence: PubMed abstract: The Km value for isopentenyl diphosphate is 89 microM

row_label: Rv2361c isopentenyl diphosphate Km sentence

table_label: PubMed abstract

enzyme: Decaprenyl diphosphate synthase

substrate: IPP (at pH 7.9 and 37 degrees Celsius)


organism: Neurospora crassa


enzyme_display_name: Alanine--glyoxylate aminotransferase 2, mitochondrial

column_label: The paper's Km Values paragraph reports beta-alanine, 1.4 mM, among amino-donor Km values at pH 7.3.

raw_value_unit_evidence: Km raw_value=1.4 raw_unit=mM

row_label: beta-alanine as amino donor

table_label: Properties section. Km Values paragraph following Table III substrate-specificity context


enzyme_display_name: glutamine--pyruvate transaminase

organism: Mus musculus

enzyme: glutamine--pyruvate transaminase


enzyme_display_name: 4,4'-diapophytoene synthase

organism: Staphylococcus aureus

substrate_name: trans,trans-Farnesyl diphosphate

column_label: PMID 16269684 Table 2, DAP from FPP row, Vmax column 3.2 uM/h and FPP Km column 1.2 uM.

raw_value_unit_evidence: Table 2 reports DAP from FPP Vmax = 3.2 uM/h and FPP Km = 1.2 uM.

row_label: DAP from FPP

table_label: Table 2

enzyme: 4,4'-diapophytoene synthase

substrate: trans,trans-Farnesyl diphosphate


enzyme_display_name: UniProt Q988B8

organism: Mesorhizobium loti

substrate_name: L-glutamate

enzyme: UniProt Q988B8

substrate: L-glutamate


substrate_name: pyridoxamine 5'-phosphate

substrate: pyridoxamine 5'-phosphate


enzyme_display_name: pyridoxamine--pyruvate transaminase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M2T/Y35H/V70K to reconstruct the assayed variant sequence.

enzyme: pyridoxamine--pyruvate transaminase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M2T/Y35H/V70K/E212G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V70K with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V70R/F247C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y35H/V70K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y35H/V70R/F247C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M2T/V70K to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M2T/V70K/E212G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V70K/E212G with inferred residue-numbering offset +24 to reconstruct the assayed variant sequence.


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


substrate_name: L-Alanine

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

substrate: L-Alanine


organism: Escherichia coli (strain K12)

substrate_name: N-acetylornithine

substrate: N-acetylornithine


organism: Vitis vinifera

substrate_name: 2-keto-L-gulonate (in presence of NADPH)


substrate_name: hydroxypyruvate (in presence of NADPH)

substrate: hydroxypyruvate (in presence of NADPH)


substrate_name: glyoxylate (in presence of NADPH)

substrate: glyoxylate (in presence of NADPH)


substrate_name: pyruvate (in presence of NADPH)

substrate: pyruvate (in presence of NADPH)


enzyme_display_name: tryptophan-phenylpyruvate transaminase

organism: Pseudomonas sp.

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

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

enzyme: tryptophan-phenylpyruvate transaminase


smiles: CCCCC(=O)C(=O)[O-]


substrate_name: Indolepyruvate

substrate: Indolepyruvate


substrate_name: L-leucine

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

substrate: L-leucine


substrate_name: L-isoleucine

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

substrate: L-isoleucine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-tryptophan


substrate_name: L-norleucine

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

substrate: L-norleucine


substrate_name: L-valine

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

substrate: L-valine


substrate_name: L-norvaline

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

substrate: L-norvaline


substrate_name: pyruvate

substrate: pyruvate


substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-alanine

substrate: L-alanine


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Drosophila melanogaster

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

assay_conditions_summary: pH 6.4; cofactor CoA

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


substrate_name: (3S)-3-hydroxybutanoyl-CoA (beta-hydroxybutyryl-CoA) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: 17beta-hydroxy-5alpha-androstan-3-one (5-alpha-dihydrotestosterone) (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

assay_conditions_summary: pH 6.4; cofactor NADH


substrate_name: 17-beta-estradiol (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: 5alpha-pregnan-20beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: 3beta,7beta-dihydroxy-5beta-cholan-24-oate (also known as isoursodeoxycholate or 7beta-hydroxyisolithocholate) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

proof_lines:
Drosophila 17beta-HSD10
isoursodeoxycholate
bile-acid substrate class


substrate_name: NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADH

proof_lines:
Drosophila 17beta-HSD10
hydroxyacyl-CoA dehydrogenase
acetoacetyl-CoA


substrate_name: NAD (in the presence of aldosterone, at pH 9.3 and 25 degrees Celsius)

proof_lines:
Drosophila 17beta-HSD10
C21 steroids
aldosterone


enzyme_display_name: pyridoxamine-pyruvate transaminase

enzyme: pyridoxamine-pyruvate transaminase


substrate_name: pyridoxal

substrate: pyridoxal


substrate_name: pyridoxamine

proof_lines: with 3-hydroxy-4-aminomethylpyridine, pH 8.9, 25°C

substrate: pyridoxamine


proof_lines: with omega-methylpyridoxal, pH 8.9, 25°C


enzyme_display_name: UniProt P9WQ77

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WQ77


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

substrate_name: (2-aminoethyl)phosphonate (at 25 degrees Celsius, pH 8.5)

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


substrate_name: pyruvate (at 25 degrees Celsius, pH 8.5)


substrate_name: 2-phosphonoacetaldehyde (at 25 degrees Celsius, pH 8.5)


substrate_name: L-alanine (at 25 degrees Celsius, pH 8.5)


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)


substrate_name: pyruvate


enzyme_display_name: UniProt Q72LL6

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

enzyme: UniProt Q72LL6


enzyme_display_name: branched-chain-amino-acid transaminase

organism: Enterobacter sp.

substrate_name: trimethylpyruvate

enzyme: branched-chain-amino-acid transaminase

substrate: trimethylpyruvate


substrate_name: 3-methyl-2-oxovaleric acid

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

substrate: 3-methyl-2-oxovaleric acid


substrate_name: 3-methyl-2-oxobutyric acid

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

substrate: 3-methyl-2-oxobutyric acid


substrate_name: 4-methyl-2-oxovaleric acid

substrate: 4-methyl-2-oxovaleric acid


organism: [Brevibacterium] flavum


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: prephenate

substrate: prephenate


substrate_name: L-glutamate

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

substrate: L-glutamate


enzyme_display_name: UniProt D0LR31

organism: Haliangium ochraceum

substrate_name: L-norvaline

enzyme: UniProt D0LR31


substrate_name: L-isoleucine

substrate: L-isoleucine


substrate_name: L-leucine

substrate: L-leucine


substrate_name: L-valine


enzyme_display_name: UniProt D1CCW1

organism: Thermobaculum terrenum

enzyme: UniProt D1CCW1


enzyme_display_name: UniProt O15382

organism: Homo sapiens

enzyme: UniProt O15382


enzyme_display_name: UniProt P0AB80

organism: Escherichia coli

enzyme: UniProt P0AB80


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


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


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


enzyme_display_name: UniProt O86428

organism: Pseudomonas aeruginosa

enzyme: UniProt O86428


enzyme_display_name: UniProt P9WQ75

enzyme: UniProt P9WQ75


organism: Nicotiana tabacum

substrate_name: pyridoxamine


organism: Oryctolagus cuniculus

substrate_name: Oxaloacetate; Pyridoxamine

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

substrate: Oxaloacetate; Pyridoxamine


enzyme_display_name: pyridoxamine-oxaloacetate transaminase

substrate_name: oxaloacetate

enzyme: pyridoxamine-oxaloacetate transaminase

substrate: oxaloacetate


proof_lines: with omega-methylpyridoxamine, pH 8.9, 25°C


enzyme_display_name: UniProt P21549

substrate_name: L-cysteine

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

enzyme: UniProt P21549

substrate: L-cysteine


enzyme_display_name: alanine--glyoxylate transaminase

substrate_name: glyoxylate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I56N to reconstruct the assayed variant sequence.

smiles: O=CC(=O)O

enzyme: alanine--glyoxylate transaminase

substrate: glyoxylate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P11R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P11R/I56N to reconstruct the assayed variant sequence.


substrate_name: L-alanine


organism: Sus scrofa

substrate_name: Pyridoxamine; Oxaloacetate

substrate: Pyridoxamine; Oxaloacetate


organism: Rattus norvegicus

proof_lines: somewhat higher at very high levels of pyridoxamine, 14 mM


organism: Mesorhizobium loti

substrate_name: pyridoxamine 5'-phosphate

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

assay_conditions_summary: pH 9

substrate: pyridoxamine 5'-phosphate


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


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


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: UniProt P23721

enzyme: UniProt P23721


substrate_name: L-homoserine

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

substrate: L-homoserine


enzyme_display_name: UniProt Q59196

organism: Niallia circulans

proof_lines:
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=-----, pH=9

enzyme: UniProt Q59196


enzyme_display_name: UniProt Q60I38

organism: Entamoeba histolytica

enzyme: UniProt Q60I38


substrate_name: O-phospho-L-serine

proof_lines:
Raw SKiD Env: Temp=-----, pH=8.5
Raw SKiD Env: Temp=25°C, pH=8.5

substrate: O-phospho-L-serine


enzyme_display_name: UniProt A0A0A7I435

organism: Bifidobacterium catenulatum subsp. kashiwanohense

enzyme: UniProt A0A0A7I435


substrate_name: taurine

substrate: taurine


enzyme_display_name: UniProt A0A1D8PMC5

organism: Candida albicans

enzyme: UniProt A0A1D8PMC5


substrate_name: L-tryptophan

substrate: L-tryptophan


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


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: alpha-aminoadipate

substrate: alpha-aminoadipate


enzyme_display_name: pyridoxamine-pyruvate transaminase

substrate_name: L-glutamate

enzyme: pyridoxamine-pyruvate transaminase

substrate: L-glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V70K with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y35H/V70K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M2T/Y35H/V70K/E212G to reconstruct the assayed variant sequence.

proof_lines: M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M2T/Y35H/V70K to reconstruct the assayed variant sequence.

proof_lines: M2T/Y35H/V70K mutant protein, pH 9.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M2T/V70K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V70R/F247C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V70K/E212G with inferred residue-numbering offset +24 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M2T/V70K/E212G to reconstruct the assayed variant sequence.

proof_lines: M2T/V70K/E212G mutant protein, pH 9.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y35H/V70R/F247C to reconstruct the assayed variant sequence.

proof_lines: Y35H/V70R/F247C mutant protein, pH 9.0, 30°C


enzyme_display_name: UniProt B0F481

organism: Arabidopsis thaliana

substrate_name: S-adenosyl-L-methionine

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

enzyme: UniProt B0F481

substrate: S-adenosyl-L-methionine


enzyme_display_name: UniProt P12995

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

enzyme: UniProt P12995


enzyme_display_name: UniProt P9WQ81

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WQ81


enzyme_display_name: glycine-oxaloacetate transaminase

organism: Paracoccus denitrificans

proof_lines: pH 7.1, 25°C, with substrate L-aspartate

proof_lines: kcat is 58 sec(-1) for the transamination of glyoxylate using L-aspartate. kcat is 0.76 sec(-1) for the transamination of glycine using oxaloacetate. kcat is 8.8 sec(-1) for the transamination of glyoxylate using L-serine. kcat is 5.0 sec(-

enzyme: glycine-oxaloacetate transaminase


substrate_name: L-aspartate

substrate: L-aspartate


organism: Paracoccus denitrificans (strain Pd 1222)

substrate_name: glycine

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

substrate: glycine


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: L-serine

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

substrate: L-serine


substrate_name: pyridoxamine

normalized_value_unit_evidence: kcat normalized_value=28 normalized_unit=s^-1; Km normalized_value=0.044 normalized_unit=mM; kcat/Km ratio normalized_value=636.3636363636364 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 PM cells: kcat raw_value=28 +/- 0.5 raw_unit=s^-1; Km raw_value=0.044 +/- 0.004 raw_unit=mM; kcat/Km raw_value=640000 raw_unit=s^-1 M^-1.

row_label: PM

table_label: Table 1. Kinetic parameters of PPAT.

source_databases_merged: brenda skid uniprot

substrate: pyridoxamine


column_label: Official PMC Table 1 row (S)-2-Aminobutyrate: (S)-2-Aminobutyrate | Km 20 +/- 0.9 mM | kcat 9.0 +/- 0.2 s^-1 | kcat/Km 450 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=9 normalized_unit=s^-1; Km normalized_value=20 normalized_unit=mM; kcat/Km ratio normalized_value=0.45 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 (S)-2-Aminobutyrate cells: kcat raw_value=9.0 +/- 0.2 raw_unit=s^-1; Km raw_value=20 +/- 0.9 raw_unit=mM; kcat/Km raw_value=450 raw_unit=s^-1 M^-1.


column_label: Official PMC Table 1 row 2-Oxobutyrate: 2-Oxobutyrate | Km 7.1 +/- 0.1 mM | kcat 24 +/- 0.2 s^-1 | kcat/Km 3400 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=24 normalized_unit=s^-1; Km normalized_value=7.1 normalized_unit=mM; kcat/Km ratio normalized_value=3.3802816901408455 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 2-Oxobutyrate cells: kcat raw_value=24 +/- 0.2 raw_unit=s^-1; Km raw_value=7.1 +/- 0.1 raw_unit=mM; kcat/Km raw_value=3400 raw_unit=s^-1 M^-1.


column_label: Official PMC Table 1 row Pyruvate: Pyruvate | Km 0.34 +/- 0.02 mM | kcat 29 +/- 0.6 s^-1 | kcat/Km 85000 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=29 normalized_unit=s^-1; Km normalized_value=0.34 normalized_unit=mM; kcat/Km ratio normalized_value=85.29411764705881 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Pyruvate cells: kcat raw_value=29 +/- 0.6 raw_unit=s^-1; Km raw_value=0.34 +/- 0.02 raw_unit=mM; kcat/Km raw_value=85000 raw_unit=s^-1 M^-1.

row_label: Pyruvate


substrate_name: pyridoxal

normalized_value_unit_evidence: kcat normalized_value=41 normalized_unit=s^-1; Km normalized_value=0.059 normalized_unit=mM; kcat/Km ratio normalized_value=694.9152542372882 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 PL cells: kcat raw_value=41 +/- 0.8 raw_unit=s^-1; Km raw_value=0.059 +/- 0.005 raw_unit=mM; kcat/Km raw_value=690000 raw_unit=s^-1 M^-1.

row_label: PL

substrate: pyridoxal


substrate_name: L-alanine

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

column_label: Official PMC Table 1 row L-Alanine: L-Alanine | Km 11 +/- 0.6 mM | kcat 41 +/- 0.7 s^-1 | kcat/Km 3700 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=41 normalized_unit=s^-1; Km normalized_value=11 normalized_unit=mM; kcat/Km ratio normalized_value=3.727272727272727 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 L-Alanine cells: kcat raw_value=41 +/- 0.7 raw_unit=s^-1; Km raw_value=11 +/- 0.6 raw_unit=mM; kcat/Km raw_value=3700 raw_unit=s^-1 M^-1.

row_label: L-Alanine

substrate: L-alanine


enzyme_display_name: UniProt P42588

substrate_name: 2-oxoglutaric acid

enzyme: UniProt P42588

substrate: 2-oxoglutaric acid


enzyme_display_name: UniProt A8IW39

organism: Chlamydomonas reinhardtii

substrate_name: tetrahydrodipicolinate

enzyme: UniProt A8IW39

substrate: tetrahydrodipicolinate


substrate_name: LL-diaminopimelate

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

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

substrate: LL-diaminopimelate


enzyme_display_name: glutamine-phenylpyruvate transaminase

organism: Thermus thermophilus

substrate_name: pyruvate

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

enzyme: glutamine-phenylpyruvate transaminase

substrate: pyruvate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: Indolepyruvate

substrate: Indolepyruvate


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-asparagine

substrate: L-asparagine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: L-kynurenine

substrate: L-kynurenine


substrate_name: L-glutamine

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

substrate: L-glutamine


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-aspartate

substrate: L-aspartate


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: L-serine

substrate: L-serine


substrate_name: L-threonine

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

substrate: L-threonine


substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: L-leucine

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

substrate: L-leucine


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


enzyme_display_name: kynurenine-glyoxylate transaminase

organism: Macaca fuscata

substrate_name: glyoxylate

enzyme: kynurenine-glyoxylate transaminase

substrate: glyoxylate


enzyme_display_name: 4-aminobutyrate--pyruvate transaminase

organism: Malus domestica

smiles: NCCCC(=O)O

enzyme: 4-aminobutyrate--pyruvate transaminase


substrate_name: pyruvate

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

substrate: pyruvate


enzyme_display_name: 4-aminobutyrate-pyruvate transaminase

enzyme: 4-aminobutyrate-pyruvate transaminase


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

proof_lines:
cosubstrate pyruvate, pH 9.0, 25°C
cosubstrate glyoxylate, pH 9.0, 25°C


proof_lines:
cosubstrate L-alanine, 37°C
L-kynurenine, pH 8.0, 37°C


proof_lines:
cosubstrate L-serine, 37°C
cosubstrate L-histidine, 37°C
cosubstrate L-phenylalanine, 37°C


substrate_name: alanine

substrate: alanine


substrate_name: phenylalanine

substrate: phenylalanine


substrate_name: histidine

substrate: histidine


substrate_name: serine

substrate: serine


enzyme_display_name: UniProt F2XBU9

organism: Vibrio fluvialis

enzyme: UniProt F2XBU9


substrate_name: benzylamine

substrate: benzylamine


smiles: CCCCCN


smiles: C(CCC(=O)[O-])CC=O


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


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


enzyme_display_name: N6-acetyl-beta-lysine transaminase

organism: Pseudomonas sp.

enzyme: N6-acetyl-beta-lysine transaminase


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


organism: Nicotiana tabacum

proof_lines: pH 8.2, temperature not specified in the publication


enzyme_display_name: 2-aminohexanoate transaminase

organism: Candida guilliermondii var. membranaefaciens

substrate_name: L-norleucine

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

proof_lines: pH 7.8, 35°C, in the presence of 2-oxoglutarate

enzyme: 2-aminohexanoate transaminase

substrate: L-norleucine


proof_lines: pH 7.8, 35°C, in the presence of L-norleucine or L-leucine


organism: Rattus norvegicus

substrate_name: L-kynurenine

substrate: L-kynurenine


enzyme_display_name: L-arginine:2-oxoglutarate transaminase

organism: Pimelobacter simplex

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

enzyme: L-arginine:2-oxoglutarate transaminase


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


substrate_name: spermidine

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

smiles: C(CCNCCCN)CN

proof_lines: mutant enzyme R797Q, in the presence of 100 mM bicarbonate, at pH 8.6 and 25°C

proof_lines: mutant enzyme R797Q, in the absence of bicarbonate, at pH 8.6 and 25°C

substrate: spermidine


proof_lines: wild type enzyme, in the presence of 100 mM bicarbonate, at pH 8.6 and 25°C

proof_lines: wild type enzyme, in the absence of bicarbonate, at pH 8.6 and 25°C


enzyme_display_name: Kynurenine aminotransferase

organism: Aedes aegypti

substrate_name: cysteine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Cysteine, column Km (mM), cell 1.3 ± 0.6 mM

raw_value_unit_evidence: Table 1 row Cysteine, Km (mM) = 1.3 ± 0.6 mM

row_label: Cysteine

table_label: Table 1. Kinetic parameters of AeKAT towards different amino acids

enzyme: Kynurenine aminotransferase


substrate_name: tyrosine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Tyrosine, column Km (mM), cell 0.9 ± 0.2 mM

raw_value_unit_evidence: Table 1 row Tyrosine, Km (mM) = 0.9 ± 0.2 mM

row_label: Tyrosine


substrate_name: glutamine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Glutamine, column Km (mM), cell 3.8 ± 0.8 mM

raw_value_unit_evidence: Table 1 row Glutamine, Km (mM) = 3.8 ± 0.8 mM

row_label: Glutamine


substrate_name: methionine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Methionine, column Km (mM), cell 1.4 ± 0.4 mM

raw_value_unit_evidence: Table 1 row Methionine, Km (mM) = 1.4 ± 0.4 mM

row_label: Methionine


substrate_name: histidine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Histidine, column Km (mM), cell 1.5 ± 0.3 mM

raw_value_unit_evidence: Table 1 row Histidine, Km (mM) = 1.5 ± 0.3 mM

row_label: Histidine


substrate_name: phenylalanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Phenylalanine, column Km (mM), cell 3.5 ± 0.3 mM

raw_value_unit_evidence: Table 1 row Phenylalanine, Km (mM) = 3.5 ± 0.3 mM

row_label: Phenylalanine


substrate_name: kynurenine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Kynurenine, column Km (mM), cell 4.3 ± 0.5 mM

raw_value_unit_evidence: Table 1 row Kynurenine, Km (mM) = 4.3 ± 0.5 mM

row_label: Kynurenine


substrate_name: asparagine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Asparagine, column Km (mM), cell 6.1 ± 0.8 mM

raw_value_unit_evidence: Table 1 row Asparagine, Km (mM) = 6.1 ± 0.8 mM

row_label: Asparagine


substrate_name: tryptophan (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Tryptophan, column Km (mM), cell 12.9 ± 4.2 mM

raw_value_unit_evidence: Table 1 row Tryptophan, Km (mM) = 12.9 ± 4.2 mM

row_label: Tryptophan


substrate_name: leucine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Leucine, column Km (mM), cell 34.5 ± 7.5 mM

raw_value_unit_evidence: Table 1 row Leucine, Km (mM) = 34.5 ± 7.5 mM

row_label: Leucine


substrate_name: serine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Serine, column Km (mM), cell 32.7 ± 7.9 mM

raw_value_unit_evidence: Table 1 row Serine, Km (mM) = 32.7 ± 7.9 mM

row_label: Serine


substrate_name: alanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Alanine, column Km (mM), cell 246 ± 164 mM

raw_value_unit_evidence: Table 1 row Alanine, Km (mM) = 246 ± 164 mM

row_label: Alanine


substrate_name: amino-butyrate (at 45 degrees Celsius, at pH 8.5 and with pyruvate as cosubstrate)

smiles: CCCC(=O)ON

column_label: Table 1, row Amino-butyrate, column Km (mM), cell 92.7 ± 15.9 mM

raw_value_unit_evidence: Table 1 row Amino-butyrate, Km (mM) = 92.7 ± 15.9 mM

row_label: Amino-butyrate


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

proof_lines: forward reaction with glyoxylate, pH 9.0, 30°C

proof_lines: forward reaction with pyruvate, pH 9.0, 30°C


substrate_name: glyoxylate

proof_lines: forward reaction with 4-aminobutanoate, pH 9.0, 30°C

proof_lines: reverse reaction with L-alanine, pH 9.0, 30°C


substrate_name: pyruvate

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat s^-1, raw cell 10.6, normalized 10.6 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column Km mM, raw cell 0.14+/-0.01, normalized 0.14 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat/Km s^-1 mM^-1, raw cell 76, normalized 76 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.6 raw_unit=s^-1 raw_cell=10.6; Km raw_value=0.14+/-0.01 raw_unit=mM raw_cell=0.14+/-0.01; kcat/Km raw_value=76 raw_unit=s^-1*mM^-1 raw_cell=76


substrate_name: succinate semialdehyde

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

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

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

substrate: succinate semialdehyde


substrate_name: L-alanine

proof_lines: reverse reaction with glyoxylate, pH 9.0, 30°C

proof_lines: reverse reaction with succinate semialdehyde, pH 9.0, 30°C


organism: Psychrobacter cryohalolentis

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

proof_lines: pH 8.0, 35°C, with (S)-(-)-1-phenylethylamine


proof_lines:
pH 8.0, 35°C, with 2,3-butanedione
pH 8.0, 35°C, with isobutyraldehyde


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


enzyme_display_name: UniProt Q9A9H3

organism: Caulobacter vibrioides

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

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

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

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

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

enzyme: UniProt Q9A9H3


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

normalized_value_unit_evidence: Km 0.016 mM; kcat 0.015 s^-1; kcat/Km 940 M^-1 s^-1 = 0.94 s^-1*mM^-1, consistent with expected 0.9375 by rounding/uncertainty.

raw_value_unit_evidence: Unnatural substrate row: Km sugar 0.016 +/- 0.003 mM; Km glutamate 0.13 +/- 0.02 mM; Ki sugar N/A; kcat 0.015 +/- 0.001 s^-1; kcat/Km sugar (9.4 +/- 1.8) x 10^2 M^-1 s^-1.

row_label: GDP-4-keto-3,6-dideoxymannose reaction


enzyme_display_name: GDP-perosamine synthase

organism: Vibrio cholerae serotype O1

column_label: Abstract reports His-tag RfbE has a Km of 0.06 mM for GDP-4-keto-6-deoxy-D-mannose.

raw_value_unit_evidence: Km raw_value=0.06 mM raw_unit=mM

row_label: Vibrio cholerae RfbE / GDP-4-keto-6-deoxy-D-mannose

table_label: PubMed XML abstract PMID 11479276

enzyme: GDP-perosamine synthase


substrate_name: L-glutamate

substrate: L-glutamate


enzyme_display_name: UDP-N-acetylbacillosamine transaminase

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

enzyme: UDP-N-acetylbacillosamine transaminase


organism: Escherichia coli O157:H7

proof_lines: kcat is 18.98 sec(-1) for GDP-4-keto-6-deoxy-D-mannose. kcat is 10.41 sec(-1) for L-glutamate.


column_label: PMID 17888872, Table 1, row Km (mM), column Sodium-L-glutamate: 2.0 mM. Sodium-L-glutamate is the assayed form of the expected L-glutamate amino donor.

raw_value_unit_evidence: Table 1: Km (mM), Sodium-L-glutamate column, raw value 2.0 mM.

row_label: Km (mM)

table_label: Table 1. Kinetics parameters of GDP-perosamine synthetase


enzyme_display_name: 3-hydroxykynurenine transaminase

substrate_name: 3-hydroxykynurenine (at 50 degrees Celsius and pH 7.0)

proof_lines: kcat is 2424 min(-1) for 3-hydroxykynurenine (at 50 degrees Celsius and pH 7) (PubMed:11880382). kcat is 1640 min(-1) for L-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate) (PubMed:11880382). kcat is 1200 min(-1) f

enzyme: 3-hydroxykynurenine transaminase


substrate_name: L-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)


substrate_name: L-kynurenine (at 50 degrees Celsius and pH 7.0)


organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)

substrate_name: L-glutamate (with GDP-4-keto-6-deoxy-D-mannose as cosubstrate)

proof_lines: kcat is 2.7 sec(-1) for GDP-4-keto-6-deoxy-D-mannose. kcat is 0.015 sec(-1) for GDP-4-keto-3,6-dideoxymannose.


organism: Helicobacter pylori (strain ATCC 700392 / 26695)

proof_lines: kcat is 43 min(-1) with (2E,6E)-farnesyl UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate.


substrate_name: glyoxylate (at 50 degrees Celsius, pH 7.0 and with alanine as cosubstrate)


enzyme_display_name: UniProt P19367

organism: Homo sapiens

substrate_name: D-glucose

enzyme: UniProt P19367

substrate: D-glucose


enzyme_display_name: UniProt P04806

organism: Saccharomyces cerevisiae

enzyme: UniProt P04806


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: UniProt P33284

organism: Kluyveromyces lactis

enzyme: UniProt P33284


substrate_name: ATP

substrate: ATP


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


enzyme_display_name: UniProt P17709

enzyme: UniProt P17709


organism: Zea mays

substrate_name: fructose

substrate: fructose


substrate_name: UTP

substrate: UTP


organism: Anopheles gambiae

proof_lines: kcat is 988.5 min(-1) for D,L-3-hydroxykynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate) (PubMed:16262702). kcat is 1077.2 min(-1) for D,L-kynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate)


substrate_name: glyoxylate (at 50 degrees Celsius, pH 7 and with D,L-3-hydroxykynurenine as cosubstrate)


enzyme_display_name: kynurenine---glyoxylate transaminase

substrate_name: Glyoxylate; 3-Hydroxy-L-kynurenine

enzyme: kynurenine---glyoxylate transaminase

substrate: Glyoxylate; 3-Hydroxy-L-kynurenine


enzyme_display_name: Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial

organism: Arabidopsis thaliana

substrate_name: Unknown

proof_lines: kcat is 0.072 min(-1) for 7,8-diamino-pelargonic acid aminotransferase + dethiobiotin synthetase activities, and 1.85 min(-1) for 7,8-diamino-pelargonic acid aminotransferase activity only (at pH 7.5 and 30 degrees Celsius).

substrate: Unknown


substrate_name: L,D-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)


substrate_name: D,L-3-hydroxykynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate)


enzyme_display_name: Kynurenine--oxoglutarate transaminase 1

enzyme: Kynurenine--oxoglutarate transaminase 1


enzyme_display_name: 4-aminobutyrate---pyruvate transaminase

substrate_name: 4-Aminobutanoate; Pyruvate

proof_lines: forward reaction with 4-aminobutanoate and pyruvate, pH 9.0, 30°C

source_databases_merged: sabio_rk brenda uniprot

enzyme: 4-aminobutyrate---pyruvate transaminase

substrate: 4-Aminobutanoate; Pyruvate


enzyme_display_name: L-tryptophan-pyruvate aminotransferase

ki_unit: mM

proof_lines: inhibition of TAA1, competitive versus L-Tryp, pH not specificied in the publication, 55°C

enzyme: L-tryptophan-pyruvate aminotransferase


enzyme_display_name: hexokinase

organism: Aeropyrum pernix

assay_conditions_summary: pH 6.2; 363.15 K; cofactor ATP

enzyme: hexokinase


substrate_name: D-glucosamine

substrate: D-glucosamine


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


organism: Brugia malayi

substrate_name: D-Glucose; ATP

substrate: D-Glucose; ATP


organism: Mus musculus

assay_conditions_summary: cofactor ATP


organism: Rattus norvegicus


substrate_name: alpha-D-Glucose 6-phosphate; ADP

assay_conditions_summary: cofactor ADP

substrate: alpha-D-Glucose 6-phosphate; ADP


substrate_name: alpha-D-Glucose; ATP

substrate: alpha-D-Glucose; ATP


substrate_name: ATP; alpha-D-Glucose

substrate: ATP; alpha-D-Glucose


organism: Bubalus bubalis


assay_conditions_summary: pH 8.1; 303.15 K; cofactor ATP

proof_lines:
MgATP2-, at 30°C, pH 8.1
at 30°C, pH 8.1


proof_lines:
at 30°C, pH 8.1
versus MgATP2-, at 30°C, pH 8.1
versus glucose, at 30°C, pH 8.1


organism: Mammalia

proof_lines:
type III isozyme
type I isozyme
type II isozyme


proof_lines:
type I isozyme
type II isozyme
type III isozyme


proof_lines:
type I and type II isozymes
type III isozyme


enzyme_display_name: ketohexokinase

organism: Haloarcula vallismortis

assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

enzyme: ketohexokinase


enzyme_display_name: fructokinase

organism: Solanum tuberosum

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
FK 2, pH 8
FK 1, pH 8
isoenzyme FK-I, 25°C, pH 8.5

enzyme: fructokinase


proof_lines:
isoenzyme FK-I, 25°C, pH 8.5
FK 1, pH 8
FK 2, pH 8


substrate_name: GTP

proof_lines:
isoenzyme FK-I, 25°C, pH 8.5
isoenzyme FK-III, 25°C, pH 8.5
isoenzyme FK-II, 25°C, pH 8.5

substrate: GTP


substrate_name: CTP

substrate: CTP


proof_lines:
isoenzyme FK-III, 25°C, pH 8.5
isoenzyme FK-I, 25°C, pH 8.5
isoenzyme FK-II, 25°C, pH 8.5


substrate_name: D-Hexose; ATP

substrate: D-Hexose; ATP


organism: Trypanosoma cruzi


enzyme_display_name: glucokinase

substrate_name: Glucose; ATP

enzyme: glucokinase

substrate: Glucose; ATP


organism: Shewanella woodyi

substrate_name: D-glucose

substrate: D-glucose


organism: Catharanthus roseus

substrate_name: ATP

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: with D-fructose as cosubstrate, pH 7.4, 30°C


substrate_name: D-fructose

substrate: D-fructose


substrate_name: UTP


substrate: ATP


organism: Brassica rapa subsp. oleifera

proof_lines:
isozyme HKII
isozyme HKI


organism: Littorina littorea

proof_lines: enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C

proof_lines: enzyme from hepatopancreas, pH 7.5, 22°C


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


organism: Lithobates sylvaticus

proof_lines:
control, pH 8.2, 5°C, no glucose
control, pH 8.2, 25°C
control, pH 8.2, 25°C, no glucose


assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP

proof_lines:
control, pH 8.2, 25°C, 250 mM glucose
control, pH 8.2, 25°C
control, pH 8.2, 25°C, no glucose


organism: Ogataea angusta


assay_conditions_summary: pH 7.5; cofactor ATP


substrate_name: Unknown


organism: Lysinibacillus sphaericus


organism: Thermus thermophilus


organism: Paracoccus versutus


organism: Nicotiana tabacum

proof_lines: pH 8.4, 30°C, recombinant isozyme hexokinase 2


organism: Dictyostelium discoideum


assay_conditions_summary: pH 7; 293.15 K; cofactor ATP


organism: Asterias amurensis


organism: Thermococcus litoralis

assay_conditions_summary: pH 7.5; 353.15 K; cofactor ATP


organism: Saccharomyces cerevisiae


organism: Streptomyces violaceoruber


organism: Pisum sativum


organism: Acer pseudoplatanus


organism: Rattus norvegicus

substrate_name: 2-Deoxy-D-glucose; Phosphate

substrate: 2-Deoxy-D-glucose; Phosphate


organism: Yarrowia lipolytica


organism: Urocitellus undulatus

proof_lines: enzyme from active animals, S0.5 value, Hill coefficient 1.16, pH 7.8, 2°C

proof_lines: enzyme from active animals, S0.5 value, Hill coefficient 1.7, pH 7.8, 25°C

proof_lines: enzyme from hibernating animals, S0.5 value, Hill coefficient 1.6, pH 7.8, 25°C


organism: Zea mays

substrate_name: ATP; D-Glucose

substrate: ATP; D-Glucose


organism: Bufo marinus

substrate_name: ATP; Glucose

substrate: ATP; Glucose


substrate_name: ATP; D-Fructose

substrate: ATP; D-Fructose


organism: Camellia japonica


organism: Shewanella woodyi


organism: Lilium longiflorum


organism: Saccharum officinarum

substrate_name: D-Glucose; ATP


organism: Persea americana

substrate_name: fructose

substrate: fructose


organism: Sus scrofa


organism: Gleditsia triacanthos


substrate_name: D-Fructose; ATP

substrate: D-Fructose; ATP


organism: Entamoeba histolytica


assay_conditions_summary: pH 8


assay_conditions_summary: pH 8; cofactor ATP


enzyme_display_name: UniProt P35557

organism: Homo sapiens

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.1

enzyme: UniProt P35557


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=°C, pH=7.6
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=30°C, pH=7.4


substrate_name: 2-deoxyglucose (at 30 degrees Celsius and pH 7.5)

proof_lines: kcat is 66.4 sec(-1) with glucose as substrate (at 30 degrees Celsius and pH 7.5) (PubMed:7742312). kcat is 56.4 sec(-1) with mannose as substrate (at 30 degrees Celsius and pH 7.5) (PubMed:7742312). kcat is 56.4 sec(-1) with 2-deoxyglucose


substrate_name: fructose (at 30 degrees Celsius and pH 7.5)


substrate_name: glucosamine (at 30 degrees Celsius and pH 9)

assay_conditions_summary: pH 9


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ATP

proof_lines:
pH 7.5, 50°C, ATP as phosphoryl donor
pH 7.5, 50°C
Raw SKiD Env: Temp=50°C, pH=7.5

source_databases_merged: brenda skid


proof_lines: pH 7.5, 50°C, D-glucose as phosphoryl acceptor


substrate_name: D-glucosamine

substrate: D-glucosamine


substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


substrate_name: CTP


substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V452L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.1; cofactor ATP

column_label: Table 1; row label: V452L; column label: kcat (sec^-1); raw value: 122.0; raw unit: sec^-1; normalized value: 122.0; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 122.0; normalized unit: s^-1

table_label: Table 1


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68V to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68V; column label: ATP Km (mM); raw value: 0.31; raw unit: mM; normalized value: 0.31; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.31; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V455M to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V455M; column label: ATP Km (mM); raw value: 0.38; raw unit: mM; normalized value: 0.38; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.38; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68K to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68K; column label: ATP Km (mM); raw value: 0.39; raw unit: mM; normalized value: 0.39; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.39; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197E to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197E; column label: ATP Km (mM); raw value: 0.4; raw unit: mM; normalized value: 0.4; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.4; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V91L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V91L; column label: ATP Km (mM); raw value: 0.48; raw unit: mM; normalized value: 0.48; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.48; normalized unit: mM


column_label: Table 1; row label: V452L; column label: ATP Km (mM); raw value: 0.53; raw unit: mM; normalized value: 0.53; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.53; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G72R to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G72R; column label: ATP Km (mM); raw value: 0.72; raw unit: mM; normalized value: 0.72; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.72; normalized unit: mM

raw_value_unit_evidence: raw value: 0.72 +−0.19; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature C252Y to reconstruct the assayed variant sequence.

column_label: Table 1; row label: C252Y; column label: ATP Km (mM); raw value: 0.75; raw unit: mM; normalized value: 0.75; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.75; normalized unit: mM

raw_value_unit_evidence: raw value: 0.75; raw unit: mM


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

assay_conditions_summary: cofactor ATP

proof_lines: mutant enzyme Y61S, glutathione S-transferase glucokinase B fusion protein


proof_lines: mutant enzyme E265K, glutathione S-transferase glucokinase B fusion protein


proof_lines: mutant enzyme K420E, glutathione S-transferase glucokinase B fusion protein


proof_lines: mutant enzyme A379V, glutathione S-transferase glucokinase B fusion protein


organism: Mus musculus

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

assay_conditions_summary: pH 7.4; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K414E with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V389L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V389L; column label: ATP Km (mM); raw value: 0.76; raw unit: mM; normalized value: 0.76; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.76; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature A379T to reconstruct the assayed variant sequence.

column_label: Table 1; row label: A379T; column label: ATP Km (mM); raw value: 0.87; raw unit: mM; normalized value: 0.87; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.87; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature C213R to reconstruct the assayed variant sequence.

column_label: Table 1; row label: C213R; column label: ATP Km (mM); raw value: 0.89; raw unit: mM; normalized value: 0.89; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.89; normalized unit: mM

raw_value_unit_evidence: raw value: 0.89; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197L; column label: ATP Km (mM); raw value: 1.31; raw unit: mM; normalized value: 1.31; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.31; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197I to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197I; column label: ATP Km (mM); raw value: 1.39; raw unit: mM; normalized value: 1.39; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.39; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y214A/V452A to reconstruct the assayed variant sequence.

column_label: Table 1; row label: Y214A/V452A; column label: ATP Km (mM); raw value: 1.42; raw unit: mM; normalized value: 1.42; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.42; normalized unit: mM

raw_value_unit_evidence: raw value: 1.42±0.29; raw unit: mM


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

column_label: Table 1; row label: K414E; column label: ATP Km (mM); raw value: 1.53; raw unit: mM; normalized value: 1.53; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.53; normalized unit: mM

raw_value_unit_evidence: raw value: 1.53; raw unit: mM


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M197I/A379T with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I/A379T


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S336L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S336L; column label: ATP Km (mM); raw value: 12.6; raw unit: mM; normalized value: 12.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 12.6; normalized unit: mM


column_label: Table 1; row label: S336L; column label: kcat (sec^-1); raw value: 2.46; raw unit: sec^-1; normalized value: 2.46; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 2.46; normalized unit: s^-1


column_label: Table 1; row label: M197E; column label: kcat (sec^-1); raw value: 17.7; raw unit: sec^-1; normalized value: 17.7; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 17.7; normalized unit: s^-1


column_label: Table 1; row label: K414E; column label: kcat (sec^-1); raw value: 19.9; raw unit: sec^-1; normalized value: 19.9; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 19.9; normalized unit: s^-1

raw_value_unit_evidence: raw value: 19.9; raw unit: sec^-1


column_label: Table 1; row label: Y214A/V452A; column label: kcat (sec^-1); raw value: 23.1; raw unit: sec^-1; normalized value: 23.1; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 23.1; normalized unit: s^-1

raw_value_unit_evidence: raw value: 23.1±2.38; raw unit: sec^-1


column_label: Table 1; row label: C252Y; column label: kcat (sec^-1); raw value: 29.3; raw unit: sec^-1; normalized value: 29.3; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 29.3; normalized unit: s^-1

raw_value_unit_evidence: raw value: 29.3; raw unit: sec^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68K to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68K; column label: kcat (sec^-1); raw value: 43.2; raw unit: sec^-1; normalized value: 43.2; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 43.2; normalized unit: s^-1


column_label: Table 1; row label: C213R; column label: kcat (sec^-1); raw value: 50.0; raw unit: sec^-1; normalized value: 50.0; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 50.0; normalized unit: s^-1

raw_value_unit_evidence: raw value: 50.0; raw unit: sec^-1


column_label: Table 1; row label: M197I; column label: kcat (sec^-1); raw value: 58.1; raw unit: sec^-1; normalized value: 58.1; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 58.1; normalized unit: s^-1


column_label: Table 1; row label: V91L; column label: kcat (sec^-1); raw value: 60.6; raw unit: sec^-1; normalized value: 60.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 60.6; normalized unit: s^-1


column_label: Table 1; row label: A379T; column label: kcat (sec^-1); raw value: 61.2; raw unit: sec^-1; normalized value: 61.2; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 61.2; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V455M to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V455M; column label: kcat (sec^-1); raw value: 61.8; raw unit: sec^-1; normalized value: 61.8; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 61.8; normalized unit: s^-1


column_label: Table 1; row label: M197L; column label: kcat (sec^-1); raw value: 62.6; raw unit: sec^-1; normalized value: 62.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 62.6; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68V to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68V; column label: kcat (sec^-1); raw value: 62.7; raw unit: sec^-1; normalized value: 62.7; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 62.7; normalized unit: s^-1


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

column_label: Table 1; row label: A456V; column label: kcat (sec^-1); raw value: 65.6; raw unit: sec^-1; normalized value: 65.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 65.6; normalized unit: s^-1


column_label: Table 1; row label: V389L; column label: kcat (sec^-1); raw value: 67.1; raw unit: sec^-1; normalized value: 67.1; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 67.1; normalized unit: s^-1


substrate_name: beta-D-glucose

proof_lines: co-substrate: ATP, mutant W99R/W167F 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: co-substrate: ATP, mutant W99R/W167F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/W167F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

substrate: beta-D-glucose


proof_lines: co-substrate: ATP, mutant W99R/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/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: co-substrate: ATP, mutant W99R/W257F, pH and temperature not specified in the publication


proof_lines: mutant W99R/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: mutant W99R/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: mutant W99R/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 W99R/W167F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: mutant W99R/W167F 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 W99R/W167F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication


organism: Cryptosporidium parvum

substrate_name: D-fructose

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

proof_lines: pH 7.5, temperature not specified in the publication


substrate_name: D-mannose

substrate: D-mannose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T228M to reconstruct the assayed variant sequence.

proof_lines: mutant T228M, 37°C, pH not specified in the puclication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L146R to reconstruct the assayed variant sequence.

assay_conditions_summary: 310.15 K; cofactor ATP

proof_lines: mutant L146R, 37°C, pH not specified in the puclication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N166R/S151A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S151C/N166R to reconstruct the assayed variant sequence.


enzyme_display_name: Glucokinase

organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

column_label: Table 3 row 2-Deoxyglucose lists Apparent K_m 330 uM.

raw_value_unit_evidence: K_m raw_value=330 raw_unit=uM

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

enzyme: Glucokinase


substrate_name: glucosamine

column_label: Table 3 row Glucosamine lists Apparent K_m 60 uM.

raw_value_unit_evidence: K_m raw_value=60 raw_unit=uM

row_label: Glucosamine

substrate: glucosamine


column_label: Table 3 row Fructose lists Apparent K_m 150 uM.

raw_value_unit_evidence: K_m raw_value=150 raw_unit=uM

row_label: Fructose


enzyme_display_name: O-ureido-L-serine synthase

organism: Streptomyces lavendulae

substrate_name: Hydroxyurea

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

smiles: C(=O)(N)NO

enzyme: O-ureido-L-serine synthase

substrate: Hydroxyurea


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


organism: Eimeria tenella

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N216K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D217H to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: glucose

proof_lines: Measured in yeast lacking glucose and hexose kinase activity.

substrate: glucose


enzyme_display_name: Fructokinase

organism: Escherichia coli (strain K12)

substrate_name: D-fructose (at 25 degrees Celsius and pH 7.6)

column_label: Table 2 row YajF with D-fructose column, Km,sugar value.

normalized_value_unit_evidence: Km 1.3 mM

raw_value_unit_evidence: Km,sugar 1.3 x 10^-3 M

row_label: YajF / D-fructose

table_label: Table 2, kinetic parameters for carbohydrate phosphorylation

enzyme: Fructokinase


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

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: Catalytic efficiency with D-fructose as substrate is 55-fold higher than that with D-glucose.

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


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

column_label: Table 2 row YajF with D-glucose column, Km,sugar value.

normalized_value_unit_evidence: Km 59 mM

raw_value_unit_evidence: Km,sugar 5.9 x 10^-2 M

row_label: YajF / D-glucose


organism: Kluyveromyces lactis

proof_lines: pH and temperature not specified in the publication

substrate: D-glucose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S64R/E67D/S69T to reconstruct the assayed variant sequence.

proof_lines: mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25°C


enzyme_display_name: Polyphosphate glucokinase

organism: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)

substrate_name: GTP (at pH 8.6)

assay_conditions_summary: pH 8.6; cofactor ATP

proof_lines: kcat is 199 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 7.5. kcat is 208 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 8.6. kcat is 108 sec(-1) with ATP as substrate at pH 7.5. kcat is 116 sec(-1) with ATP

enzyme: Polyphosphate glucokinase

substrate: GTP (at pH 8.6)


substrate_name: dATP (at pH 8.6)

substrate: dATP (at pH 8.6)


substrate_name: UTP (at pH 8.6)

substrate: UTP (at pH 8.6)


substrate_name: CTP (at pH 8.6)

substrate: CTP (at pH 8.6)


organism: Solanum tuberosum


substrate_name: fructose


substrate_name: D-glucose (at pH 7.5, in the polyphosphate-dependent glucokinase reaction)


substrate_name: ATP (at pH 7.5)

substrate: ATP (at pH 7.5)


organism: Schwanniomyces occidentalis

substrate_name: D-glucose

column_label: Official Springer PDF, abstract text extraction lines 23-24 and Results prose text extraction lines 231-233: metric label KM value; enzyme purified Schwanniomyces occidentalis hexokinase; substrate glucose; raw value 0.98 mM.

normalized_value_unit_evidence: 0.98 mM glucose is already in the exported unit and matches Km 0.98 mM.

raw_value_unit_evidence: The official Springer PDF states that purified Schwanniomyces occidentalis hexokinase had a KM value of 0.98 mM for glucose.

row_label: Purified Schwanniomyces occidentalis hexokinase, glucose substrate

table_label: Abstract and Results prose: purified Schwanniomyces occidentalis hexokinase kinetic parameters


column_label: Official Springer PDF, abstract text extraction lines 23-24 and Results prose text extraction lines 231-233: metric label KM value; enzyme purified Schwanniomyces occidentalis hexokinase; substrate fructose; raw value 9.3 mM.

normalized_value_unit_evidence: 9.3 mM fructose is already in the exported unit and matches Km 9.3 mM.

raw_value_unit_evidence: The official Springer PDF states that purified Schwanniomyces occidentalis hexokinase had a KM value of 9.3 mM for fructose.

row_label: Purified Schwanniomyces occidentalis hexokinase, fructose substrate

substrate: D-fructose


organism: Leishmania braziliensis

substrate_name: ATP

substrate: ATP


enzyme_display_name: Ketohexokinase

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

substrate_name: ATP (at pH 7.5 and 42 degrees Celsius)

proof_lines: kcat is 47 sec(-1) for the phosphorylation of fructose.

enzyme: Ketohexokinase

substrate: ATP (at pH 7.5 and 42 degrees Celsius)


substrate_name: fructose (at pH 7.5 and 42 degrees Celsius)


substrate_name: O-acetyl-L-serine

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

substrate: O-acetyl-L-serine


organism: Solanum lycopersicum

substrate_name: D-fructose


organism: Pyrobaculum calidifontis

assay_conditions_summary: pH 8.5; cofactor ATP

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

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

row_label: Pcal_1032 / D-glucose

table_label: Kinetic parameters section and Table 1


column_label: Kinetic parameters section, ATP experiment, printed Km; Table 1, P. calidifontis row, Km towards ATP column.

raw_value_unit_evidence: Kinetic parameters prose: ATP Km 900 +/- 10 uM. Table 1 P. calidifontis row: ATP Km 0.9 mM.

row_label: Pcal_1032 / ATP


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G72R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G72R, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G72R

proof_lines: mutant enzyme G72R, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol


organism: Thermotoga maritima

proof_lines:
pH 8.0, 85°C, recombinant enzyme
recombinant enyme, pH 7.3, 80°C


organism: Trypanosoma cruzi

proof_lines: His-tagged recombinant protein, pH 7.2, 22°C


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

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant A456V


organism: Aeropyrum pernix

proof_lines: kcat is 23 sec(-1) with glucose as substrate. kcat is 30 sec(-1) with 2-deoxyglucose as substrate. kcat is 18 sec(-1) with glucosamine as substrate. kcat is 10 sec(-1) with fructose as substrate. kcat is 13 sec(-1) with mannose as substrate


organism: Ascaris suum

substrate_name: Glucose; ATP

substrate: Glucose; ATP


organism: Aspergillus niger


organism: Bacteroides fragilis

substrate_name: D-Glucose; ATP

substrate: D-Glucose; ATP


organism: Bos taurus