sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T317A to reconstruct the assayed variant sequence.


enzyme_display_name: non-chaperonin molecular chaperone ATPase

organism: Saccharomyces cerevisiae

substrate_name: ATP

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Mutation signature N728A matches the mutant residue at offset +3 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

data_origin: experimental

substrate: ATP

status: unverified

source: oed


substrate_name: ATP; H2O

kcat_over_km_display: Not reported

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

assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104 N728A

substrate: ATP; H2O


enzyme_display_name: Deleted entry

organism: Bos taurus

substrate_name: Ubiquinone; NADH

mutation_signature: Unknown

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

assay_conditions_summary: cofactor NADH

enzyme: Deleted entry

substrate: Ubiquinone; NADH


organism: Clostridium thermohydrosulfuricum

substrate_name: NADH; O2; H+

kcat_display: Not reported

substrate: NADH; O2; H+


organism: Homo sapiens

substrate_name: Ferricytochrome c; NADH; H+

substrate: Ferricytochrome c; NADH; H+


organism: Lactococcus lactis subsp. lactis


organism: Rattus norvegicus

substrate_name: NADH; Ubiquinone

substrate: NADH; Ubiquinone


organism: Treponema hyodysenteriae

substrate_name: NADH; H+; Acceptor

substrate: NADH; H+; Acceptor


organism: Enterococcus faecalis

substrate_name: NADH

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: NADH; H+; O2

km_display: Not reported

ki_unit: mM

sequence_variant_note: Mutation signature E4R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: Procion Yellow H-E4R

substrate: NADH; H+; O2


substrate_name: Hexacyanoferrate(III); NADH

substrate: Hexacyanoferrate(III); NADH


substrate_name: NADH; Hexacyanoferrate(III)

substrate: NADH; Hexacyanoferrate(III)


organism: Thermus thermophilus

substrate_name: FAD; NADH

substrate: FAD; NADH


kcat_over_km_origin: calculated

assay_conditions_summary: pH 7; 293.15 K; cofactor NADH


enzyme_display_name: Transferred entry: 2.1.1.354

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

proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant residues 191-352 H347A

enzyme: Transferred entry: 2.1.1.354


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant residues 191-352 H347E


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant residues 191-352 H347F


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant residues 191-352


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant residues 191-352 C270A


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant residues 191-352 E259Q


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant residues 191-352 E259A


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant K317A


organism: Drosophila melanogaster

mutation_type: deletion

proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant delta213 (N-terminally truncated)


substrate_name: S-Adenosyl-L-methionine

substrate: S-Adenosyl-L-methionine


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant H293A


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant residues 191-352 Y334A


proof_lines: SABIO-RK modifier species: histone-lysine N-methyltransferase(Enzyme) mutant residues 191-352 Y334F


substrate_name: Histone H3-K4; S-Adenosyl-L-methionine

substrate: Histone H3-K4; S-Adenosyl-L-methionine


substrate_name: S-Adenosyl-L-methionine; Histone H3-K4

substrate: S-Adenosyl-L-methionine; Histone H3-K4


enzyme_display_name: Transferred entry: 4.98.1.1

substrate_name: Protoporphyrin; Zn2+

proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant W282L

enzyme: Transferred entry: 4.98.1.1

substrate: Protoporphyrin; Zn2+


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant Y248L


enzyme_display_name: UniProt Q820M5

organism: Nitrosomonas europaea

substrate_name: UDP-glucose

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q820M5

substrate: UDP-glucose

source: skid


substrate_name: ADP-glucose

substrate: ADP-glucose


substrate_name: CDP

substrate: CDP


substrate_name: GDP

substrate: GDP


substrate_name: ADP

substrate: ADP


substrate_name: D-fructose

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=60°C, pH=7

substrate: D-fructose


substrate_name: UDP

substrate: UDP


enzyme_display_name: sucrose synthase

organism: Solanum tuberosum

enzyme: sucrose synthase


substrate_name: D-Lyxose

substrate: D-Lyxose


substrate_name: D-Xylulose

substrate: D-Xylulose


substrate_name: L-Sorbose

substrate: L-Sorbose


substrate_name: UDP-D-galactose

substrate: UDP-D-galactose


substrate_name: UDP-D-glucose

substrate: UDP-D-glucose


enzyme_display_name: UniProt Q837U7

substrate_name: L-ornithine

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

enzyme: UniProt Q837U7

substrate: L-ornithine


enzyme_display_name: UniProt P84010

organism: Ovis aries

proof_lines:
Raw SKiD Env: Temp=37°C, pH=9
Raw SKiD Env: Temp=37°C, pH=8.2

enzyme: UniProt P84010


enzyme_display_name: UniProt P00480

substrate_name: Carbamoyl phosphate

enzyme: UniProt P00480

substrate: Carbamoyl phosphate


enzyme_display_name: ornithine carbamoyltransferase

organism: Caretta caretta

substrate_name: Carbamoyl phosphate; L-Ornithine

enzyme: ornithine carbamoyltransferase

substrate: Carbamoyl phosphate; L-Ornithine


organism: Nocardia lactamdurans

substrate_name: L-Ornithine; Carbamoyl phosphate

substrate: L-Ornithine; Carbamoyl phosphate


substrate_name: L-Ornithine

substrate: L-Ornithine


organism: Escherichia coli

substrate_name: L-Citrulline; Arsenate

substrate: L-Citrulline; Arsenate


substrate_name: Arsenate; L-Citrulline

substrate: Arsenate; L-Citrulline


substrate_name: Hydrogencarbonate; ATP; L-Ornithine; NH3


substrate_name: ATP; Hydrogencarbonate; NH3; L-Ornithine


organism: Gallus gallus

substrate_name: carbamoyl phosphate (at pH 7.5)

source_db: uniprot

proof_lines: With an increase in pH, a decrease in KM values for ornithine and an increase in the extent of inhibition by ornithine are observed.

substrate: carbamoyl phosphate (at pH 7.5)

source: uniprot


substrate_name: ornithine (at pH 7.5)

substrate: ornithine (at pH 7.5)


organism: Acer pseudoplatanus

substrate_name: Sucrose; ADP

assay_conditions_summary: cofactor ADP

substrate: Sucrose; ADP


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

proof_lines: kcat is 14000 min(-1) for L-ornithine. kcat is 13000 min(-1) for carbamoyl phosphate.

source_databases_merged: skid uniprot


organism: Moritella abyssi

substrate_name: carbamoyl phosphate (at pH 9 and at 30 degrees Celsius)

proof_lines: kcat is 15 and 766 sec(-1) at 30 degrees Celsius and pH 9 for L-ornithine and carbamoyl phosphate, respectively. kcat is 87 and 694 sec(-1) at 20 degrees Celsius and pH 9 for L-ornithine and carbamoyl phosphate, respectively. kcat is 132 an


substrate_name: L-ornithine (at pH 9 and at 5 degrees Celsius)


organism: Stenella sp.


organism: Bacillus subtilis


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


organism: Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)

substrate_name: ADP-glucose for sucrose synthesis, pH 7.0

assay_conditions_summary: pH 7; cofactor ADP

proof_lines: kcat/KM for sucrose synthesis is 70094 for ADP-gluce and 2673 for UDP-glucose.


substrate_name: UDP-glucose for sucrose synthesis, pH 7.0


organism: Anabaena sp.

substrate_name: ADP alpha-D-glucoside; D-Fructose

substrate: ADP alpha-D-glucoside; D-Fructose


organism: Daucus carota

substrate_name: Sucrose; UDP

substrate: Sucrose; UDP


organism: Hordeum vulgare

substrate_name: UDP; Sucrose

substrate: UDP; Sucrose


organism: Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)

substrate_name: ADP in sucrose breakdown

substrate: ADP in sucrose breakdown


organism: Oryza sativa

substrate_name: D-Fructose; UDPglucose

substrate: D-Fructose; UDPglucose


organism: Rattus norvegicus

substrate_name: L-Ornithine; Carbamoyl phosphate


organism: Saccharomyces cerevisiae


organism: Salmonella typhimurium


organism: Thermus thermophilus

substrate_name: Carbamoyl phosphate; L-Ornithine


organism: Acidithiobacillus caldus (strain ATCC 51756 / DSM 8584 / KU)


organism: Phaseolus aureus

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


organism: Pyrus pyrifolia


organism: Saccharum officinarum

substrate_name: D-Fructose; UDP-D-glucose

substrate: D-Fructose; UDP-D-glucose


organism: Solanum lycopersicum


organism: Solanum tuberosum

substrate_name: ADP; Sucrose

substrate: ADP; Sucrose


organism: Pseudomonas aeruginosa

sequence_variant_note: Mutation signature E105G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant E105G


organism: Pseudomonas putida

sequence: MAFNIHNRNLLSLEHHTNRELRYLLDLTRDLKAK

wild_type_sequence: MAFNIHNRNLLSLEHHTNRELRYLLDLTRDLKAK


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K263R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant K263R


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K265R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant K265R


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature D182N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant D182N


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature E123S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant E123S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K263A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant K263A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K260R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant K260R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N184Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant N184Q


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q294P to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant Q294P


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C191M/C194N/F197V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant C191M-C194N-F197V


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K265A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant K265A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K268R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant K268R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E256A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant E256A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E256Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant E256Q


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K260A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant K260A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E123A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant E123A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N185Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant N185Q


organism: Escherichia coli

substrate_name: L-ornithine

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

proof_lines: kcat is 14000 min(-1) for L-ornithine. kcat is 13000 min(-1) for carbamoyl phosphate.

substrate: L-ornithine


organism: Arabidopsis thaliana

substrate_name: Unknown

substrate: Unknown


organism: Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)

proof_lines: kcat/KM for sucrose synthesis is 70094 for ADP-gluce and 2673 for UDP-glucose.


organism: Vigna radiata

substrate_name: UDPglucose; D-Fructose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S11D with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sucrose synthase(Enzyme) mutant S11D

substrate: UDPglucose; D-Fructose


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +6, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: sucrose synthase(Enzyme) mutant S11E


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T68G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant T68G

substrate: L-Ornithine; Carbamoyl phosphate


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature C289S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant C289S


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature L290S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant L290S


sequence_variant_note: Mutation signature L290Q matches the mutant residue at offset +4 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant L290Q

substrate: Carbamoyl phosphate; L-Ornithine


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

sequence_source: multiple


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R57G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant R57G


organism: Homo sapiens

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

proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant


organism: Moritella abyssi


proof_lines: SABIO-RK modifier species: ornithine carbamoyltransferase(Enzyme) mutant arcB3670


organism: Enterococcus faecalis

substrate_name: Phosphate

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

substrate: Phosphate


substrate_name: Carbamoyl phosphate

smiles: NC(=O)OP(=O)(O)O

substrate: Carbamoyl phosphate


substrate_name: D-fructose (synthetic reaction) at pH 9.4


substrate_name: UDP-glucose (synthetic reaction) at pH 9.4


substrate_name: sucrose (degradative reaction) at pH 6

assay_conditions_summary: pH 6

substrate: sucrose (degradative reaction) at pH 6


substrate_name: UDP (degradative reaction) at pH 6

substrate: UDP (degradative reaction) at pH 6


substrate_name: D-fructose (synthetic reaction)

substrate: D-fructose (synthetic reaction)


substrate_name: UDP-glucose (synthetic reaction)

substrate: UDP-glucose (synthetic reaction)


substrate_name: sucrose (degradative reaction)

substrate: sucrose (degradative reaction)


substrate_name: UDP (degradative reaction)

substrate: UDP (degradative reaction)


substrate: D-fructose (synthetic reaction) at pH 9.4


substrate: UDP-glucose (synthetic reaction) at pH 9.4


sequence_variant_note: Mutation signature C273A matches the mutant residue at offset +4 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature D140N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of OTC and its variants with respect to carbamoyl phosphate), variant row 'D140N'; column 'Layer' = 2nd; column 'KM (mM)' = 1.4; column 'kcat (s-1)' = 360; column 'kcat/KM (x10^4 M-1 s-1)' = 29.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.4 mM; already in mM, no conversion; the exported value is 1.4 mM. kcat: printed Table 2 cell 360 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 360.0 s^(-1). kcat/Km: printed Table 2 cell 29 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 29 x 10^4 / 1000 = 290.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, variant row 'D140N': KM = 1.4 mM; kcat = 360 s-1; printed kcat/KM = 29 x 10^4 M^-1 s^-1.

row_label: Table 2, variant row 'D140N'

table_label: Table 2: Steady-state kinetic parameters of OTC and its variants with respect to carbamoyl phosphate.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature D231A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of OTC and its variants with respect to carbamoyl phosphate), variant row 'D231A'; column 'Layer' = 1st; column 'KM (mM)' = 0.15; column 'kcat (s-1)' = 0.48; column 'kcat/KM (x10^4 M-1 s-1)' = 0.34.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.15 mM; already in mM, no conversion; the exported value is 0.15 mM. kcat: printed Table 2 cell 0.48 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.48 s^(-1). kcat/Km: printed Table 2 cell 0.34 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.34 x 10^4 / 1000 = 3.4000000000000004 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, variant row 'D231A': KM = 0.15 mM; kcat = 0.48 s-1; printed kcat/KM = 0.34 x 10^4 M^-1 s^-1.

row_label: Table 2, variant row 'D231A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature E299D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of OTC and its variants with respect to carbamoyl phosphate), variant row 'E299D'; column 'Layer' = 3rd; column 'KM (mM)' = 0.22; column 'kcat (s-1)' = 120; column 'kcat/KM (x10^4 M-1 s-1)' = 62.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.22 mM; already in mM, no conversion; the exported value is 0.22 mM. kcat: printed Table 2 cell 120 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 120.0 s^(-1). kcat/Km: printed Table 2 cell 62 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 62 x 10^4 / 1000 = 620.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, variant row 'E299D': KM = 0.22 mM; kcat = 120 s-1; printed kcat/KM = 62 x 10^4 M^-1 s^-1.

row_label: Table 2, variant row 'E299D'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E299Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature H272L 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H272N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature Q104L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of OTC and its variants with respect to carbamoyl phosphate), variant row 'Q104L (-)'; column 'Layer' = 3rd; column 'KM (mM)' = 0.40; column 'kcat (s-1)' = 88; column 'kcat/KM (x10^4 M-1 s-1)' = 26.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.40 mM; already in mM, no conversion; the exported value is 0.4 mM. kcat: printed Table 2 cell 88 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 88.0 s^(-1). kcat/Km: printed Table 2 cell 26 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 26 x 10^4 / 1000 = 260.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, variant row 'Q104L (-)': KM = 0.40 mM; kcat = 88 s-1; printed kcat/KM = 26 x 10^4 M^-1 s^-1.

row_label: Table 2, variant row 'Q104L (-)'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R57A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S61A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Pseudomonas savastanoi pv. phaseolicola

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


substrate_name: carbamoyl phosphate

substrate: carbamoyl phosphate


organism: Escherichia coli (strain K12)


organism: Bos taurus


substrate_name: L-Ornithine

substrate: L-Ornithine


substrate_name: Sucrose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S11D to reconstruct the assayed variant sequence.

substrate: Sucrose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S11E to reconstruct the assayed variant sequence.


column_label: PLOS ONE DOI 10.1371/journal.pone.0228487 Table 2; Wild-type row; columns KM (mM), kcat (s^-1), and kcat/KM (x10^4 M^-1 s^-1).

row_label: Wild-type

table_label: Table 2. Steady-state kinetic parameters of OTC and its variants with respect to carbamoyl phosphate


sequence_variant_note: Mutation signature Y160F matches the mutant residue at offset -6 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature Y160S matches the mutant residue at offset +12 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature Y229F matches the mutant residue at offset -1 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature Y229S matches the mutant residue at offset +7 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature C273A matches the mutant residue at offset +4 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature D140N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of OTC and its variants with respect to ornithine), variant row 'D140N'; column 'Layer' = 2nd; column 'KM (mM)' = 17; column 'kcat (s-1)' = 460; column 'kcat/KM (x10^4 M-1 s-1)' = 3.0.

normalized_value_unit_evidence: Km: printed Table 3 cell 17 mM; already in mM, no conversion; the exported value is 17.0 mM. kcat: printed Table 3 cell 460 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 460.0 s^(-1). kcat/Km: printed Table 3 cell 3.0 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.0 x 10^4 / 1000 = 30.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row 'D140N': KM = 17 mM; kcat = 460 s-1; printed kcat/KM = 3.0 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'D140N'

table_label: Table 3: Steady-state kinetic parameters of OTC and its variants with respect to ornithine.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature D231A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of OTC and its variants with respect to ornithine), variant row 'D231A'; column 'Layer' = 1st; column 'KM (mM)' = 0.59; column 'kcat (s-1)' = 0.70; column 'kcat/KM (x10^4 M-1 s-1)' = 0.14.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.59 mM; already in mM, no conversion; the exported value is 0.59 mM. kcat: printed Table 3 cell 0.70 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.7 s^(-1). kcat/Km: printed Table 3 cell 0.14 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.14 x 10^4 / 1000 = 1.4000000000000001 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row 'D231A': KM = 0.59 mM; kcat = 0.70 s-1; printed kcat/KM = 0.14 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'D231A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature E299D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of OTC and its variants with respect to ornithine), variant row 'E299D'; column 'Layer' = 3rd; column 'KM (mM)' = 0.90; column 'kcat (s-1)' = 170; column 'kcat/KM (x10^4 M-1 s-1)' = 20.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.90 mM; already in mM, no conversion; the exported value is 0.9 mM. kcat: printed Table 3 cell 170 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 170.0 s^(-1). kcat/Km: printed Table 3 cell 20 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 20 x 10^4 / 1000 = 200.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row 'E299D': KM = 0.90 mM; kcat = 170 s-1; printed kcat/KM = 20 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'E299D'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature E299Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of OTC and its variants with respect to ornithine), variant row 'E299Q'; column 'Layer' = 3rd; column 'KM (mM)' = 0.33; column 'kcat (s-1)' = 5.1; column 'kcat/KM (x10^4 M-1 s-1)' = 1.6.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.33 mM; already in mM, no conversion; the exported value is 0.33 mM. kcat: printed Table 3 cell 5.1 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 5.1 s^(-1). kcat/Km: printed Table 3 cell 1.6 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^4 / 1000 = 16.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row 'E299Q': KM = 0.33 mM; kcat = 5.1 s-1; printed kcat/KM = 1.6 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'E299Q'


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


substrate: L-ornithine


organism: Hordeum vulgare

verification_status: verified

column_label: The abstract reports Km values for Suc and UDP were 30 mM and 5 microM, respectively.

raw_value_unit_evidence: Km raw_value=30 mM raw_unit=mM

row_label: Prose segment: Sucrose Km

table_label: PubMed PMID 12223688 abstract

status: verified


substrate_name: UDP

raw_value_unit_evidence: Km raw_value=5 microM raw_unit=microM

row_label: Prose segment: UDP Km

substrate: UDP


substrate_name: ADP

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

assay_conditions_summary: pH 7; 310.15 K; cofactor ADP

substrate: ADP


substrate_name: ADP (degradative reaction) at pH 7

substrate: ADP (degradative reaction) at pH 7


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)


substrate_name: L-ornithine


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R57G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)

column_label: Abstract reports Michaelis-Menten kinetics with both carbamylphosphate and ornithine as substrates with Km values of 0.4 and 8 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.4 mM raw_unit=mM

row_label: Halobacterium catabolic ornithine transcarbamylase / carbamylphosphate

table_label: PubMed XML abstract PMID 7868583


raw_value_unit_evidence: Km raw_value=8 mM raw_unit=mM

row_label: Halobacterium catabolic ornithine transcarbamylase / ornithine


substrate_name: Carbamoyl phosphate; L-Ornithine

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

substrate: Carbamoyl phosphate; L-Ornithine


organism: Nitrosomonas europaea

substrate_name: sucrose

assay_conditions_summary: pH 7; 333.15 K; cofactor ADP

substrate: sucrose


organism: Solanum tuberosum

substrate_name: D-Fructose

substrate: D-Fructose


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


organism: Pseudomonas syringae phaseolicola

substrate_name: L-Ornithine; Carbamoyl phosphate

substrate: L-Ornithine; Carbamoyl phosphate


organism: Trichomonas vaginalis

substrate_name: L-Citrulline; Phosphate

substrate: L-Citrulline; Phosphate


organism: Streptomyces clavuligerus


organism: Oryza sativa

substrate_name: Sucrose; ADP

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

substrate: Sucrose; ADP


organism: Saccharum officinarum

substrate_name: UDP; Sucrose

substrate: UDP; Sucrose


organism: Spinacia oleracea

substrate_name: ADP; Sucrose

substrate: ADP; Sucrose


organism: Escherichia coli

sequence_variant_note: Mutation signature H272L matches the mutant residue at offset +0 and the reference residue at offset +7; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H272N with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

column_label: PLOS ONE DOI 10.1371/journal.pone.0228487 Table 3; H272N row; columns KM (mM), kcat (s^-1), and kcat/KM (x10^4 M^-1 s^-1).

table_label: Table 3. Steady-state kinetic parameters of OTC and its variants with respect to ornithine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q104L with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

column_label: PLOS ONE DOI 10.1371/journal.pone.0228487 Table 3; Q104L (-) row; columns KM (mM), kcat (s^-1), and kcat/KM (x10^4 M^-1 s^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R57A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: PLOS ONE DOI 10.1371/journal.pone.0228487 Table 3; R57A (+) row; columns KM (mM), kcat (s^-1), and kcat/KM (x10^4 M^-1 s^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature S61A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of OTC and its variants with respect to ornithine), variant row 'S61A (-)'; column 'Layer' = 2nd; column 'KM (mM)' = 0.53; column 'kcat (s-1)' = 240; column 'kcat/KM (x10^4 M-1 s-1)' = 46.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.53 mM; already in mM, no conversion; the exported value is 0.53 mM. kcat: printed Table 3 cell 240 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 240.0 s^(-1). kcat/Km: printed Table 3 cell 46 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 46 x 10^4 / 1000 = 460.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row 'S61A (-)': KM = 0.53 mM; kcat = 240 s-1; printed kcat/KM = 46 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'S61A (-)'


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

column_label: PLOS ONE DOI 10.1371/journal.pone.0228487 Table 3; Wild-type row; columns KM (mM), kcat (s^-1), and kcat/KM (x10^4 M^-1 s^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature Y160F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of OTC and its variants with respect to ornithine), variant row 'Y160F'; column 'Layer' = 2nd; column 'KM (mM)' = 1.0; column 'kcat (s-1)' = 110; column 'kcat/KM (x10^4 M-1 s-1)' = 10.

normalized_value_unit_evidence: Km: printed Table 3 cell 1.0 mM; already in mM, no conversion; the exported value is 1.0 mM. kcat: printed Table 3 cell 110 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 110.0 s^(-1). kcat/Km: printed Table 3 cell 10 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 10 x 10^4 / 1000 = 100.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row 'Y160F': KM = 1.0 mM; kcat = 110 s-1; printed kcat/KM = 10 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'Y160F'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature Y160S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of OTC and its variants with respect to ornithine), variant row 'Y160S'; column 'Layer' = 2nd; column 'KM (mM)' = 7.3; column 'kcat (s-1)' = 410; column 'kcat/KM (x10^4 M-1 s-1)' = 6.1.

normalized_value_unit_evidence: Km: printed Table 3 cell 7.3 mM; already in mM, no conversion; the exported value is 7.3 mM. kcat: printed Table 3 cell 410 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 410.0 s^(-1). kcat/Km: printed Table 3 cell 6.1 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.1 x 10^4 / 1000 = 61.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row 'Y160S': KM = 7.3 mM; kcat = 410 s-1; printed kcat/KM = 6.1 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'Y160S'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature Y229F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of OTC and its variants with respect to ornithine), variant row 'Y229F'; column 'Layer' = 2nd; column 'KM (mM)' = 0.45; column 'kcat (s-1)' = 130; column 'kcat/KM (x10^4 M-1 s-1)' = 31.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.45 mM; already in mM, no conversion; the exported value is 0.45 mM. kcat: printed Table 3 cell 130 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 130.0 s^(-1). kcat/Km: printed Table 3 cell 31 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 31 x 10^4 / 1000 = 310.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row 'Y229F': KM = 0.45 mM; kcat = 130 s-1; printed kcat/KM = 31 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'Y229F'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04391 and applied mutation signature Y229S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of OTC and its variants with respect to ornithine), variant row 'Y229S'; column 'Layer' = 2nd; column 'KM (mM)' = 0.61; column 'kcat (s-1)' = 350; column 'kcat/KM (x10^4 M-1 s-1)' = 59.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.61 mM; already in mM, no conversion; the exported value is 0.61 mM. kcat: printed Table 3 cell 350 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 350.0 s^(-1). kcat/Km: printed Table 3 cell 59 x 10^4 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 59 x 10^4 / 1000 = 590.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row 'Y229S': KM = 0.61 mM; kcat = 350 s-1; printed kcat/KM = 59 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'Y229S'


organism: Saccharum hybrid

substrate_name: D-Fructose; UDP-D-glucose

substrate: D-Fructose; UDP-D-glucose


organism: Mycobacterium smegmatis


organism: Pisum sativum

substrate_name: Fe2+; Protoporphyrin

substrate: Fe2+; Protoporphyrin


organism: Rattus norvegicus


organism: Bos taurus

substrate_name: Mesoporphyrin IX; Fe2+

substrate: Mesoporphyrin IX; Fe2+


organism: Gallus gallus

substrate_name: Protoporphyrin; Fe2+

substrate: Protoporphyrin; Fe2+


organism: Homo sapiens


organism: Saccharomyces cerevisiae

substrate_name: Protoporphyrin; Zn2+

substrate: Protoporphyrin; Zn2+


substrate_name: Zn2+; Protoporphyrin

proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant Sm12

proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant Sm41

substrate: Zn2+; Protoporphyrin


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant D246V/Y248F


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant Y95L


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant D246A/Y248L


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant E314A


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant Q273E


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant D246A


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant H235L


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant F308A


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant W282L


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant Q111E


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant Y248L


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant R87A


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant L62F (hem15-7 allele)


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant L205P (hem15-8 allele)


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant P221L (hem15-9 allele)


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant G47S (hem15-6 allele)


proof_lines: SABIO-RK modifier species: ferrochelatase(Enzyme) mutant S102F (hem15-2 allele)


organism: Xenopus laevis


enzyme_display_name: gibberellin-44 dioxygenase

substrate_name: O2; 2-Oxoglutarate; (Pro-Pro-Gly)10

enzyme: gibberellin-44 dioxygenase

substrate: O2; 2-Oxoglutarate; (Pro-Pro-Gly)10


enzyme_display_name: aspartate kinase

substrate_name: ATP; L-Aspartate

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant isoenzyme AKIII E119D

enzyme: aspartate kinase

substrate: ATP; L-Aspartate


substrate_name: L-Aspartate; ATP

substrate: L-Aspartate; ATP


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant isoenzyme AKIII R198K


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant isoenzyme AKIII K8R


substrate_name: L-Malate

substrate: L-Malate


substrate_name: L-Malate; ATP

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E119C His-tagged

substrate: L-Malate; ATP


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E119G His-tagged


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E119A His-tagged


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E119N His-tagged


substrate_name: ATP; L-Malate

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E119P His-tagged

substrate: ATP; L-Malate


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E119S His-tagged


substrate_name: L-Aspartate

substrate: L-Aspartate


organism: Arabidopsis thaliana


substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP


organism: Daucus carota


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant isoenzyme AKIII D202E


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E119V His-tagged


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant V115A E119S His6-tag


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E119S E434V His6-tag


sequence_variant_note: Resolved canonical sequence from uniprotkb:P08660;refseq:NP_418448.1;rcsb:2J0W and applied mutation signature E119G to reconstruct the assayed variant sequence.

column_label: Supplementary Table 3 row E119G under (L)-Malate columns lists kcat 1.4 +/- 0.1, Km 10.9 +/- 0.4, kcat/Km 0.14 +/- 0.01

normalized_value_unit_evidence: {'kcat': {'unit': 's^-1', 'value': 1.4}, 'kcat_over_km': {'note': 'expected central-value ratio from kcat/Km; paper table reports rounded metric value 0.14 +/- 0.01', 'unit': 's^-1 mM^-1', 'value': 0.12844036697247704}, 'km': {'unit': 'mM', 'value': 10.9}}

table_label: Supplementary Table 3


sequence_variant_note: Resolved canonical sequence from uniprotkb:P08660;refseq:NP_418448.1;rcsb:2J0W and applied mutation signature V115A/E119S/E434V to reconstruct the assayed variant sequence.

column_label: Supplementary Table 3 row V115A:E119S:E434V under (L)-Aspartate columns lists kcat 1.14 +/- 0.2, Km 119.5 +/- 29.8, kcat/Km 0.010 +/- 0.003

normalized_value_unit_evidence: {'kcat': {'unit': 's^-1', 'value': 1.14}, 'kcat_over_km': {'note': 'expected central-value ratio from kcat/Km; paper table reports rounded metric value 0.010 +/- 0.003', 'unit': 's^-1 mM^-1', 'value': 0.009539748953974895}, 'km': {'unit': 'mM', 'value': 119.5}}


column_label: Supplementary Table 3 row WT under (L)-Aspartate columns lists kcat 13.2 +/- 0.4, Km 7.9 +/- 0.24, kcat/Km 1.678 +/- 0.07

normalized_value_unit_evidence: {'kcat': {'unit': 's^-1', 'value': 13.2}, 'kcat_over_km': {'note': 'expected central-value ratio from kcat/Km; paper table reports rounded metric value 1.678 +/- 0.07', 'unit': 's^-1 mM^-1', 'value': 1.670886075949367}, 'km': {'unit': 'mM', 'value': 7.9}}

row_label: WT


sequence_variant_note: Resolved canonical sequence from uniprotkb:P08660;refseq:NP_418448.1;rcsb:2J0W and applied mutation signature E119Q to reconstruct the assayed variant sequence.

column_label: Supplementary Table 3 row E119Q under (L)-Malate columns lists kcat 0.03 +/- 0.004, Km 38.5 +/- 0.7, kcat/Km 0.001 +/- 0.00

normalized_value_unit_evidence: {'kcat': {'unit': 's^-1', 'value': 0.03}, 'kcat_over_km': {'note': 'expected central-value ratio from kcat/Km; paper table reports rounded metric value 0.001 +/- 0.00', 'unit': 's^-1 mM^-1', 'value': 0.0007792207792207792}, 'km': {'unit': 'mM', 'value': 38.5}}


sequence_variant_note: Resolved canonical sequence from uniprotkb:P08660;refseq:NP_418448.1;rcsb:2J0W and applied mutation signature E119A to reconstruct the assayed variant sequence.

column_label: Supplementary Table 3 row E119A under (L)-Malate columns lists kcat 2.5 +/- 0.1, Km 10.5 +/- 1.0, kcat/Km 0.24 +/- 0.03

normalized_value_unit_evidence: {'kcat': {'unit': 's^-1', 'value': 2.5}, 'kcat_over_km': {'note': 'expected central-value ratio from kcat/Km; paper table reports rounded metric value 0.24 +/- 0.03', 'unit': 's^-1 mM^-1', 'value': 0.23809523809523808}, 'km': {'unit': 'mM', 'value': 10.5}}


sequence_variant_note: Resolved canonical sequence from uniprotkb:P08660;refseq:NP_418448.1;rcsb:2J0W and applied mutation signature E119T to reconstruct the assayed variant sequence.

column_label: Supplementary Table 3 row E119T under (L)-Malate columns lists kcat 0.4 +/- 0.1, Km 12.3 +/- 0.4, kcat/Km 0.03 +/- 0.01


sequence_variant_note: Resolved canonical sequence from uniprotkb:P08660;refseq:NP_418448.1;rcsb:2J0W and applied mutation signature E119P to reconstruct the assayed variant sequence.

column_label: Supplementary Table 3 row E119P under (L)-Malate columns lists kcat 0.6 +/- 0.1, Km 18.5 +/- 9.1, kcat/Km 0.04 +/- 0.02

normalized_value_unit_evidence: {'kcat': {'unit': 's^-1', 'value': 0.6}, 'kcat_over_km': {'note': 'expected central-value ratio from kcat/Km; paper table reports rounded metric value 0.04 +/- 0.02', 'unit': 's^-1 mM^-1', 'value': 0.032432432432432434}, 'km': {'unit': 'mM', 'value': 18.5}}


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q443A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant Q443A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q524A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant Q524A


column_label: J. Biol. Chem. 280(50):41178-41183 (2005); journal page 41179 (PDF page 2) RESULTS prose for the catalytic constant and journal page 41180 (PDF page 3) TABLE ONE for the Km: AK I pair: catalytic constant 5 +/- 0.5 s^-1 (RESULTS prose) with TABLE ONE row AK I | ATP | Asp (50 mM) | Km minus Ala 6.5 +/- 1 mM: kcat (catalytic constant v/[E]0) = 5 +/- 0.5 s^-1; Km = 6.5 +/- 1 mM.

normalized_value_unit_evidence: Printed catalytic constant 5 +/- 0.5 s^-1 is already in the catalog unit s^(-1); no conversion needed; catalog kcat = 5.0. Printed Km 6.5 +/- 1 mM is already in the catalog unit mM; catalog km = 6.5. The paper prints no kcat/Km value for this measurement. The catalog kcat_over_km 0.7692307692307693 s^(-1)*mM^(-1) is the exact full-precision quotient of this same printed pair, 5.0 / 6.5 = 0.7692307692307693.

raw_value_unit_evidence: AK I pair: catalytic constant 5 +/- 0.5 s^-1 (RESULTS prose) with TABLE ONE row AK I | ATP | Asp (50 mM) | Km minus Ala 6.5 +/- 1 mM: printed kcat (catalytic constant v/[E]0) 5 +/- 0.5 s^-1; printed Km 6.5 +/- 1 mM; no printed kcat/Km.

table_label: TABLE ONE  Km of AK I and AK II for ATP and Asp in the absence and presence of a saturating concentration of Ala


organism: Thermus thermophilus

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

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant D154N


assay_conditions_summary: pH 7.5; 333.15 K; cofactor ATP


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


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant F136A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant K18Q


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant K18R


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant H292A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant S23A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant K18A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant V115A E119C His6-tag


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant V115A E119S E434V His6-tag

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant V115A:E119S:E434V His-tagged


organism: Pseudomonas stutzeri


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E254A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant S12A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant V39A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant A23L


sequence_source: UniProtKB P10869 canonical sequence

sequence_variant_note: Resolved canonical sequence from UniProtKB P10869 canonical sequence and applied mutation signature H292A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row H292A / L-Asp; columns L-Asp Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=6.81 +/- 0.953 mM; kcat=2.49 +/- 0.13 s^-1; kcat/Km=366 M^-1 s^-1; normalized evidence Km=6.81 mM; kcat=2.49 s^-1; kcat/Km=0.365639 s^-1 mM^-1; paper explicitly prints 366 M^-1 s^-1 (= 0.366 s^-1 mM^-1) and the exported value is consistent with the same rounded Km/kcat row.

row_label: H292A / L-Asp


sequence_variant_note: Resolved canonical sequence from UniProtKB P10869 canonical sequence and applied mutation signature T22A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant T22A


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

column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row AKSc / L-Asp; columns L-Asp Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=4.59 +/- 0.514 mM; kcat=46.6 +/- 1.54 s^-1; kcat/Km=10200 M^-1 s^-1; normalized evidence Km=4.59 mM; kcat=46.6 s^-1; kcat/Km=10.1525 s^-1 mM^-1; paper explicitly prints 10200 M^-1 s^-1 (= 10.2 s^-1 mM^-1) and the exported value is consistent with the same rounded Km/kcat row.

row_label: AKSc / L-Asp


sequence_variant_note: Resolved canonical sequence from UniProtKB P10869 canonical sequence and applied mutation signature S23A to reconstruct the assayed variant sequence.

column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row S23A / ATP; columns ATP Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=1.05 +/- 0.11 mM; kcat=19.1 +/- 0.56 s^-1; kcat/Km=18200 M^-1 s^-1; normalized evidence Km=1.05 mM; kcat=19.1 s^-1; kcat/Km=18.1905 s^-1 mM^-1; paper explicitly prints 18200 M^-1 s^-1 (= 18.2 s^-1 mM^-1) and the exported value is consistent with the same rounded Km/kcat row.

row_label: S23A / ATP


column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row T22A / L-Asp; columns L-Asp Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=7.08 +/- 0.779 mM; kcat=45 +/- 1.76 s^-1; kcat/Km=6350 M^-1 s^-1; normalized evidence Km=7.08 mM; kcat=45 s^-1; kcat/Km=6.35593 s^-1 mM^-1; paper explicitly prints 6350 M^-1 s^-1 (= 6.35 s^-1 mM^-1) and the exported value is consistent with the same rounded Km/kcat row.

row_label: T22A / L-Asp


sequence_variant_note: Resolved canonical sequence from UniProtKB P10869 canonical sequence and applied mutation signature H497A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant H497A


sequence_variant_note: Resolved canonical sequence from UniProtKB P10869 canonical sequence and applied mutation signature E279A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E279A


column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row H497A / ATP; columns ATP Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=1.26 +/- 0.11 mM; kcat=7.33 +/- 0.17 s^-1; kcat/Km=5820 M^-1 s^-1; normalized evidence Km=1.26 mM; kcat=7.33 s^-1; kcat/Km=5.81746 s^-1 mM^-1; paper explicitly prints 5820 M^-1 s^-1 (= 5.82 s^-1 mM^-1) and the exported value is consistent with the same rounded Km/kcat row.

row_label: H497A / ATP


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant Y8A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant P183A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant T238A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant D182A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant A157L


sequence_source: UniProtKB P61489 canonical sequence

sequence_variant_note: Resolved canonical sequence from UniProtKB P61489 canonical sequence and applied mutation signature T47A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant T47A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature A157L to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'A157L'; column 'kcat (min-1)' = 280±10; column 'Km for ATP (mM)' = 0.45±0.05; column 'Km for Asp (mM)' = 0.19±0.04; column 'Remaining activity in the presence of 10 uM Thr (%)' = 43; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 280 min-1; min^-1 to s^-1 is a division by 60, so 280 / 60 = 4.666666666666667 s^(-1). Km: printed Table 3 cell 0.45 mM in the 'Km for ATP (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 0.45 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 10.37037037037037 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.666666666666667 / 0.45 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'A157L': kcat = 280 min-1; Km for ATP (mM) = 0.45 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'A157L'

table_label: Table 3: Kinetic parameters for aspartate kinase mutants (J. Biosci. Bioeng. 1999, 87(6):739-745)


sequence_variant_note: Resolved canonical sequence from UniProtKB P61489 canonical sequence and applied mutation signature A42S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant A42S


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature P183A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'P183A'; column 'kcat (min-1)' = 260±40; column 'Km for Asp (mM)' = 1.20±0.31; column 'Km for ATP (mM)' = 1.90±0.45; column 'Remaining activity in the presence of 10 uM Thr (%)' = 72; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 260 min-1; min^-1 to s^-1 is a division by 60, so 260 / 60 = 4.333333333333333 s^(-1). Km: printed Table 3 cell 1.20 mM in the 'Km for Asp (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 1.2 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 3.611111111111111 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.333333333333333 / 1.2 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'P183A': kcat = 260 min-1; Km for Asp (mM) = 1.20 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'P183A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature S153A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'S153A'; column 'kcat (min-1)' = 740±50; column 'Km for ATP (mM)' = 0.44±0.07; column 'Km for Asp (mM)' = 0.47±0.09; column 'Remaining activity in the presence of 10 uM Thr (%)' = 60; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 740 min-1; min^-1 to s^-1 is a division by 60, so 740 / 60 = 12.333333333333334 s^(-1). Km: printed Table 3 cell 0.44 mM in the 'Km for ATP (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 0.44 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 28.03030303030303 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 12.333333333333334 / 0.44 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'S153A': kcat = 740 min-1; Km for ATP (mM) = 0.44 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'S153A'


sequence_variant_note: Resolved canonical sequence from UniProtKB P61489 canonical sequence and applied mutation signature D154A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant D154A


assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table 3. Kinetic parameters for aspartate kinase mutants; row Wild; kcat column 1500 min^-1 normalized to 25 s^-1; Km for ATP column 0.5 mM; Km for Asp column 0.27 mM; exported substrate context uses L-Aspartate; ATP and selected Km-for-ATP cell 0.5 mM.

normalized_value_unit_evidence: kcat 25 s^-1 from 1500 min^-1 / 60; Km for ATP 0.5 mM

raw_value_unit_evidence: Table 3 row Wild: kcat 1500 min^-1; Km for ATP 0.5 mM; Km for Asp 0.27 mM.

row_label: Wild-type aspartate kinase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature T238A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'T238A'; column 'kcat (min-1)' = 440±20; column 'Km for ATP (mM)' = 0.56±0.08; column 'Km for Asp (mM)' = 0.39±0.06; column 'Remaining activity in the presence of 10 uM Thr (%)' = 58; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 440 min-1; min^-1 to s^-1 is a division by 60, so 440 / 60 = 7.333333333333333 s^(-1). Km: printed Table 3 cell 0.56 mM in the 'Km for ATP (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 0.56 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 13.095238095238093 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 7.333333333333333 / 0.56 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'T238A': kcat = 440 min-1; Km for ATP (mM) = 0.56 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'T238A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature F136A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'F136A'; column 'kcat (min-1)' = 1000±200; column 'Km for ATP (mM)' = 0.57±0.26; column 'Km for Asp (mM)' = 5.29±1.18; column 'Remaining activity in the presence of 10 uM Thr (%)' = 67; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1000 min-1; min^-1 to s^-1 is a division by 60, so 1000 / 60 = 16.666666666666668 s^(-1). Km: printed Table 3 cell 0.57 mM in the 'Km for ATP (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 0.57 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 29.23976608187135 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 16.666666666666668 / 0.57 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'F136A': kcat = 1000 min-1; Km for ATP (mM) = 0.57 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'F136A'


sequence_variant_note: Resolved canonical sequence from UniProtKB P61489 canonical sequence and applied mutation signature R150A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant R150A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature A189L to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'A189L'; column 'kcat (min-1)' = 360±20; column 'Km for ATP (mM)' = 0.98±0.13; column 'Km for Asp (mM)' = 0.45±0.08; column 'Remaining activity in the presence of 10 uM Thr (%)' = 83; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 360 min-1; min^-1 to s^-1 is a division by 60, so 360 / 60 = 6.0 s^(-1). Km: printed Table 3 cell 0.98 mM in the 'Km for ATP (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 0.98 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 6.122448979591836 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 6.0 / 0.98 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'A189L': kcat = 360 min-1; Km for ATP (mM) = 0.98 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'A189L'


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

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant S153A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant G135A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant G149A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant I171A


organism: Bacillus subtilis (strain 168)

substrate_name: ATP (at 25 degrees Celsius)

substrate: ATP (at 25 degrees Celsius)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: aspartate (at 30 degrees Celsius)

proof_lines: kcat is 46.6 sec(-1) for aspartate (PubMed:14623312). kcat is 49.3 sec(-1) for ATP (PubMed:14623312). kcat is 228 sec(-1) for aspartate and ATP (PubMed:15358146).

substrate: aspartate (at 30 degrees Celsius)


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


organism: Streptococcus mutans


substrate_name: aspartate

substrate: aspartate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature G73A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'G73A'; column 'kcat (min-1)' = 1900±100; column 'Km for ATP (mM)' = 1.28±0.17; column 'Km for Asp (mM)' = 0.61±0.07; column 'Remaining activity in the presence of 10 uM Thr (%)' = 55; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1900 min-1; min^-1 to s^-1 is a division by 60, so 1900 / 60 = 31.666666666666668 s^(-1). Km: printed Table 3 cell 1.28 mM in the 'Km for ATP (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 1.28 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 24.739583333333332 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 31.666666666666668 / 1.28 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'G73A': kcat = 1900 min-1; Km for ATP (mM) = 1.28 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'G73A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature D154N to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'D154N'; column 'kcat (min-1)' = 130±7; column 'Km for Asp (mM)' = 0.47±0.07; column 'Km for ATP (mM)' = 0.63±0.14; column 'Remaining activity in the presence of 10 uM Thr (%)' = 51; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 130 min-1; min^-1 to s^-1 is a division by 60, so 130 / 60 = 2.1666666666666665 s^(-1). Km: printed Table 3 cell 0.47 mM in the 'Km for Asp (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 0.47 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 4.609929078014185 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.1666666666666665 / 0.47 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'D154N': kcat = 130 min-1; Km for Asp (mM) = 0.47 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'D154N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature G10A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'G10A'; column 'kcat (min-1)' = 170±20; column 'Km for Asp (mM)' = 1.34±0.28; column 'Km for ATP (mM)' = 3.57±0.87; column 'Remaining activity in the presence of 10 uM Thr (%)' = 67; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 170 min-1; min^-1 to s^-1 is a division by 60, so 170 / 60 = 2.8333333333333335 s^(-1). Km: printed Table 3 cell 1.34 mM in the 'Km for Asp (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 1.34 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 2.1144278606965172 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.8333333333333335 / 1.34 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'G10A': kcat = 170 min-1; Km for Asp (mM) = 1.34 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'G10A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature V39A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'V39A'; column 'kcat (min-1)' = 1920±70; column 'Km for ATP (mM)' = 0.89±0.11; column 'Km for Asp (mM)' = 0.33±0.04; column 'Remaining activity in the presence of 10 uM Thr (%)' = 46; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1920 min-1; min^-1 to s^-1 is a division by 60, so 1920 / 60 = 32.0 s^(-1). Km: printed Table 3 cell 0.89 mM in the 'Km for ATP (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 0.89 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 35.95505617977528 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 32.0 / 0.89 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'V39A': kcat = 1920 min-1; Km for ATP (mM) = 0.89 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'V39A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61489 and applied mutation signature T47A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'T47A'; column 'kcat (min-1)' = 400±60; column 'Km for Asp (mM)' = 19.5±4.1; column 'Km for ATP (mM)' = 2.10±0.65; column 'Remaining activity in the presence of 10 uM Thr (%)' = 42; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 400 min-1; min^-1 to s^-1 is a division by 60, so 400 / 60 = 6.666666666666667 s^(-1). Km: printed Table 3 cell 19.5 mM in the 'Km for Asp (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 19.5 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.3418803418803419 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 6.666666666666667 / 19.5 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'T47A': kcat = 400 min-1; Km for Asp (mM) = 19.5 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row 'T47A'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G152A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant G152A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E202A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant E202A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G73A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant G73A


substrate_name: aspartate for the aspartokinase activity (in the presence of 40 mM ATP)

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


substrate_name: aspartate for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl(2), 200 uM NADPH and 20 mM ATP)

assay_conditions_summary: cofactor NADPH


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


organism: Stutzerimonas stutzeri (strain A1501)


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant L148A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant S41A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant D174A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant G177A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant G10A


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant A189L


proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant H292Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P10869 canonical sequence and applied mutation signature T295V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant T295V


column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row AKSc / ATP; columns ATP Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=0.74 +/- 0.05 mM; kcat=49.3 +/- 1.39 s^-1; kcat/Km=66600 M^-1 s^-1; normalized evidence: paper row has Km=0.74 mM, kcat=49.3 s^-1, explicit kcat/Km=66.6 s^-1 mM^-1; exported values do not match the required metric identity.

normalized_value_unit_evidence: Paper row has Km=0.74 mM, kcat=49.3 s^-1, explicit kcat/Km=66.6 s^-1 mM^-1; exported values do not match the required metric identity.

row_label: AKSc / ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB P10869 canonical sequence and applied mutation signature H292A to reconstruct the assayed variant sequence.

column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row H292A / ATP; columns ATP Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=3.36 +/- 0.41 mM; kcat=0.41 +/- 0.2 s^-1; kcat/Km=121 M^-1 s^-1; normalized evidence Km=3.36 mM; kcat=0.41 s^-1; kcat/Km=0.122024 s^-1 mM^-1; paper explicitly prints 121 M^-1 s^-1 (= 0.121 s^-1 mM^-1) and the exported value is consistent with the same rounded Km/kcat row.

row_label: H292A / ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB P10869 canonical sequence and applied mutation signature R419A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aspartate kinase(Enzyme) mutant R419A


sequence_variant_note: Resolved canonical sequence from UniProtKB P10869 canonical sequence and applied mutation signature E279A to reconstruct the assayed variant sequence.

column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row E279A / ATP; columns ATP Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=1.15 +/- 0.23 mM; kcat=1.13 +/- 0.08 s^-1; kcat/Km=983 M^-1 s^-1; normalized evidence Km=1.15 mM; kcat=1.13 s^-1; kcat/Km=0.982609 s^-1 mM^-1; paper explicitly prints 983 M^-1 s^-1 (= 0.983 s^-1 mM^-1) and the exported value is consistent with the same rounded Km/kcat row.

row_label: E279A / ATP


column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row E279A / L-Asp; columns L-Asp Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=2.33 +/- 0.327 mM; kcat=0.98 +/- 0.03 s^-1; kcat/Km=421 M^-1 s^-1; normalized evidence Km=2.33 mM; kcat=0.98 s^-1; kcat/Km=0.420601 s^-1 mM^-1; paper explicitly prints 421 M^-1 s^-1 (= 0.421 s^-1 mM^-1) and the exported value is consistent with the same rounded Km/kcat row.

row_label: E279A / L-Asp


column_label: Table 2. Steady state kinetics for AKSc and engineered variants; row T295V / L-Asp; columns L-Asp Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); raw cells Km=3.19 +/- 0.394 mM; kcat=18 +/- 0.54 s^-1; kcat/Km=5640 M^-1 s^-1; normalized evidence Km=3.19 mM; kcat=18 s^-1; kcat/Km=5.64263 s^-1 mM^-1; paper explicitly prints 5640 M^-1 s^-1 (= 5.64 s^-1 mM^-1) and the exported value is consistent with the same rounded Km/kcat row.

row_label: T295V / L-Asp


substrate_name: Ferricytochrome c; NADH; H+

substrate: Ferricytochrome c; NADH; H+


organism: Enterococcus faecalis

substrate_name: NADH; H+; O2

sequence_variant_note: Mutation signature E4R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: Procion Yellow H-E4R

substrate: NADH; H+; O2


substrate_name: NADH

substrate: NADH


enzyme_display_name: RNA helicase

sequence_source: UniProtKB Q03532 canonical sequenceVersion 1, reconstructed with T230A after direct residue validation on 2026-05-22

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

assay_conditions_summary: pH 6.5; 303.15 K; cofactor ATP

enzyme: RNA helicase


sequence_source: UniProtKB P06634 canonical sequenceVersion 2, reconstructed with F405L after direct residue validation on 2026-05-22

sequence_variant_note: Mutation signature F405L matches the mutant residue at offset +0 and the reference residue at offset +13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


enzyme_display_name: ATP-dependent RNA helicase HAS1

sequence_source: UniProtKB Q03532 FASTA fetched by exact accession lookup; variant substitutions directly applied after residue-position checks.

column_label: Table 1 | row Has1p | columns KM (uM), kcat (min^-1), Relative kcat/KM.

raw_value_unit_evidence: Table 1 row Has1p: KM (ATP)=440 +/- 90 uM; kcat=5.4 +/- 0.9 min^-1; Relative kcat/KM=1.

table_label: Table 1

enzyme: ATP-dependent RNA helicase HAS1


assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06634 and applied mutation signature Q169A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer of 50 mM potassium acetate; cofactor ATP

column_label: Table I (Kinetic parameters for RNA-dependent ATPase activity), enzyme row 'Q169A'; column 'Km (mM)' = 33; column 'Vmax (%wt)' = 29; column 'kcat (min^-1)' = 61; column 'kcat/Km (M^-1 min^-1)' = 1900; column 'Ki (mM)' = ND.

normalized_value_unit_evidence: Km: printed Table I cell 33 under the head Km (mM); mM is already the canonical unit, so no unit conversion applies and the value is 33.0 mM, which is what the catalog carries. kcat: printed Table I cell 61 under the head kcat (min^-1); 1 min^-1 is 1/60 s^(-1), so 61 / 60 = 1.0166666666666666 s^(-1). The catalog carries 1.017 s^(-1), that same conversion written to three decimal places; this pass carries the full-precision conversion of the printed cell. kcat/Km: printed Table I cell 1900 under the head kcat/Km (M^-1 min^-1); 1 M^-1 min^-1 is 0.001 mM^-1 combined with 1/60 s^(-1), that is 1/60000 s^(-1)*mM^(-1), so 1900 / 60000 = 0.03166666666666667 s^(-1)*mM^(-1). The catalog carries 0.030818181818181814 s^(-1)*mM^(-1), the arithmetic quotient 1.017 / 33.0 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy adopted 2026-09-03 carries the printed primary cell on kcat_over_km.

raw_value_unit_evidence: PMID: 15201868; Table I, enzyme row 'Q169A': Km = 33 in a column headed Km (mM); kcat = 61 in a column headed kcat (min^-1); printed kcat/Km = 1900 in a column headed kcat/Km (M^-1 min^-1).

row_label: Table I, enzyme row 'Q169A'

table_label: Table I: Kinetic parameters for RNA-dependent ATPase activity (The EMBO Journal 2004, 23(13):2478-2487). Printed column heads: Km (mM); Vmax (%wt); kcat (min^-1); kcat/Km (M^-1 min^-1); Ki (mM).


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


sequence_variant_note: Mutation signature T166S matches the mutant residue at offset +0 and the reference residue at offset -3; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06634 and applied mutation signature F162A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters for RNA-dependent ATPase activity), enzyme row 'F162A'; column 'Km (mM)' = 3.5; column 'Vmax (%wt)' = 9.3; column 'kcat (min^-1)' = 20; column 'kcat/Km (M^-1 min^-1)' = 5600; column 'Ki (mM)' = ND.

normalized_value_unit_evidence: Km: printed Table I cell 3.5 under the head Km (mM); mM is already the canonical unit, so no unit conversion applies and the value is 3.5 mM, which is what the catalog carries. kcat: printed Table I cell 20 under the head kcat (min^-1); 1 min^-1 is 1/60 s^(-1), so 20 / 60 = 0.3333333333333333 s^(-1). The catalog carries 0.333 s^(-1), that same conversion written to three decimal places; this pass carries the full-precision conversion of the printed cell. kcat/Km: printed Table I cell 5600 under the head kcat/Km (M^-1 min^-1); 1 M^-1 min^-1 is 0.001 mM^-1 combined with 1/60 s^(-1), that is 1/60000 s^(-1)*mM^(-1), so 5600 / 60000 = 0.09333333333333334 s^(-1)*mM^(-1). The catalog carries 0.09514285714285715 s^(-1)*mM^(-1), the arithmetic quotient 0.333 / 3.5 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy adopted 2026-09-03 carries the printed primary cell on kcat_over_km.

raw_value_unit_evidence: PMID: 15201868; Table I, enzyme row 'F162A': Km = 3.5 in a column headed Km (mM); kcat = 20 in a column headed kcat (min^-1); printed kcat/Km = 5600 in a column headed kcat/Km (M^-1 min^-1).

row_label: Table I, enzyme row 'F162A'


sequence_source: UniProt REST P06634 canonical sequence; row-specific sequence reconstructed from selected mutation_signature after residue checks

sequence_variant_note: Mutation signature F405Y matches the mutant residue at offset +0 and the reference residue at offset +13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P06634 canonical sequence; reconstructed variant after validating I348T against the canonical residues.

sequence_variant_note: Mutation signature I348T matches the mutant residue at offset +0 and the reference residue at offset +12; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P06634 canonical sequence; reconstructed variant after validating F405L, P174S against the canonical residues.


sequence_source: UniProtKB P06634 canonical sequence; reconstructed variant after validating A457D against the canonical residues.


substrate_name: RNA

sequence_source: UniProtKB P20448 canonical sequence from direct accession lookup.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: RNA


sequence_source: UniProtKB P45818 canonical sequence from direct accession lookup.

assay_conditions_summary: pH 6.5; 298.15 K; cofactor ATP


sequence_source: UniProtKB C7GTW8 canonical sequence from direct accession lookup.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06634 and applied mutation signature F162L to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters for RNA-dependent ATPase activity), enzyme row 'F162L'; column 'Km (mM)' = 0.78; column 'Vmax (%wt)' = 55; column 'kcat (min^-1)' = 120; column 'kcat/Km (M^-1 min^-1)' = 150 000; column 'Ki (mM)' = 3.0.

normalized_value_unit_evidence: Km: printed Table I cell 0.78 under the head Km (mM); mM is already the canonical unit, so no unit conversion applies and the value is 0.78 mM, which is what the catalog carries. kcat: printed Table I cell 120 under the head kcat (min^-1); 1 min^-1 is 1/60 s^(-1), so 120 / 60 = 2.0 s^(-1). The catalog carries 2.0 s^(-1), the same value. kcat/Km: printed Table I cell 150 000 under the head kcat/Km (M^-1 min^-1); 1 M^-1 min^-1 is 0.001 mM^-1 combined with 1/60 s^(-1), that is 1/60000 s^(-1)*mM^(-1), so 150000 / 60000 = 2.5 s^(-1)*mM^(-1). The catalog carries 2.564102564102564 s^(-1)*mM^(-1), the arithmetic quotient 2.0 / 0.78 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy adopted 2026-09-03 carries the printed primary cell on kcat_over_km.

raw_value_unit_evidence: PMID: 15201868; Table I, enzyme row 'F162L': Km = 0.78 in a column headed Km (mM); kcat = 120 in a column headed kcat (min^-1); printed kcat/Km = 150 000 in a column headed kcat/Km (M^-1 min^-1).

row_label: Table I, enzyme row 'F162L'


sequence_source: UniProt REST FASTA P06634 fetched 2026-05-22; canonical T166 confirmed and T166A applied in review.

sequence_variant_note: Mutation signature T166A matches the mutant residue at offset +0 and the reference residue at offset -3; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06634 and applied mutation signature Q169E to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters for RNA-dependent ATPase activity), enzyme row 'Q169E'; column 'Km (mM)' = 1.1; column 'Vmax (%wt)' = 1.2; column 'kcat (min^-1)' = 2.6; column 'kcat/Km (M^-1 min^-1)' = 2300; column 'Ki (mM)' = ND.

normalized_value_unit_evidence: Km: printed Table I cell 1.1 under the head Km (mM); mM is already the canonical unit, so no unit conversion applies and the value is 1.1 mM, which is what the catalog carries. kcat: printed Table I cell 2.6 under the head kcat (min^-1); 1 min^-1 is 1/60 s^(-1), so 2.6 / 60 = 0.043333333333333335 s^(-1). The catalog carries 0.043 s^(-1), that same conversion written to three decimal places; this pass carries the full-precision conversion of the printed cell. kcat/Km: printed Table I cell 2300 under the head kcat/Km (M^-1 min^-1); 1 M^-1 min^-1 is 0.001 mM^-1 combined with 1/60 s^(-1), that is 1/60000 s^(-1)*mM^(-1), so 2300 / 60000 = 0.03833333333333334 s^(-1)*mM^(-1). The catalog carries 0.039090909090909086 s^(-1)*mM^(-1), the arithmetic quotient 0.043 / 1.1 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy adopted 2026-09-03 carries the printed primary cell on kcat_over_km.

raw_value_unit_evidence: PMID: 15201868; Table I, enzyme row 'Q169E': Km = 1.1 in a column headed Km (mM); kcat = 2.6 in a column headed kcat (min^-1); printed kcat/Km = 2300 in a column headed kcat/Km (M^-1 min^-1).

row_label: Table I, enzyme row 'Q169E'


sequence_source: UniProt REST FASTA Q03532 fetched 2026-05-22; canonical H375 confirmed and H375E applied in review.


substrate_name: Poly(dA)

substrate: Poly(dA)


organism: Bamboo mosaic virus

sequence_variant_note: Resolved canonical sequence from accession_anchored:O37174 and applied mutation signature Q826A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 293.15 K; cofactor ATP

column_label: Table 2, enzyme row 'Q826A'; ATPase column group: column 'Km (uM)' = 8.7 ± 2.3, column 'kcat (s^-1)' = 0.73 ± 0.07; RNA 5'-triphosphatase column group: column 'Km (uM)' = 120 ± 34, column 'kcat (min^-1)' = 1.0 ± 0.4; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 ATPase cell 0.73 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.73 s^(-1). Km: printed Table 2 ATPase cell 8.7 uM; 8.7 / 1000 = 0.0087 mM. kcat/Km: Table 2 carries no kcat/Km column, so the paper value 83.9080459770115 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.73 / 0.0087 of this row's own two printed ATPase cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row Q826A, ATPase column group: Km = 8.7 ± 2.3 uM; kcat = 0.73 ± 0.07 s^-1; Table 2 carries no kcat/Km column.

row_label: Table 2, enzyme row 'Q826A', ATPase column group

table_label: Table 2: Effects of selected mutations on ATPase and RNA 5'-triphosphatase activities (Virology 2007, 367:41-50)


sequence_variant_note: Resolved canonical sequence from accession_anchored:O37174 and applied mutation signature D858A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'D858A'; ATPase column group: column 'Km (uM)' = 73 ± 26, column 'kcat (s^-1)' = 6.2 ± 0.7; RNA 5'-triphosphatase column group: column 'Km (uM)' = 220 ± 50, column 'kcat (min^-1)' = 1.2 ± 0.4; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 ATPase cell 6.2 s^-1; already in s^-1, no unit conversion applies; the paper value is 6.2 s^(-1). Km: printed Table 2 ATPase cell 73 uM; 73 / 1000 = 0.073 mM. kcat/Km: Table 2 carries no kcat/Km column, so the paper value 84.93150684931507 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 6.2 / 0.073 of this row's own two printed ATPase cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row D858A, ATPase column group: Km = 73 ± 26 uM; kcat = 6.2 ± 0.7 s^-1; Table 2 carries no kcat/Km column.

row_label: Table 2, enzyme row 'D858A', ATPase column group


sequence_variant_note: Resolved canonical sequence from accession_anchored:O37174 and applied mutation signature L543A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'L543A'; ATPase column group: column 'Km (uM)' = 150 ± 45, column 'kcat (s^-1)' = 4.6 ± 0.6; RNA 5'-triphosphatase column group: column 'Km (uM)' = 82 ± 23, column 'kcat (min^-1)' = 1.2 ± 0.2; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 ATPase cell 4.6 s^-1; already in s^-1, no unit conversion applies; the paper value is 4.6 s^(-1). Km: printed Table 2 ATPase cell 150 uM; 150 / 1000 = 0.15 mM. kcat/Km: Table 2 carries no kcat/Km column, so the paper value 30.666666666666664 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.6 / 0.15 of this row's own two printed ATPase cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row L543A, ATPase column group: Km = 150 ± 45 uM; kcat = 4.6 ± 0.6 s^-1; Table 2 carries no kcat/Km column.

row_label: Table 2, enzyme row 'L543A', ATPase column group


substrate_name: H2O; ATP

sequence_source: UniProtKB:Q13838 direct FASTA lookup on 2026-05-22

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

assay_conditions_summary: cofactor ATP

substrate: H2O; ATP


substrate_name: dATP

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

substrate: dATP


organism: Caenorhabditis elegans

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


organism: Classical swine fever virus (strain Alfort/Tuebingen)

substrate_name: Sub-UpU

substrate: Sub-UpU


organism: Deformed wing virus

substrate_name: a 15 AA peptide

substrate: a 15 AA peptide


organism: Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969)

substrate_name: N-acetyl-Gly-Arg-Arg-AMC

substrate: N-acetyl-Gly-Arg-Arg-AMC


organism: Hepatitis GB virus B

substrate_name: ATP for NS3 NTPase

substrate: ATP for NS3 NTPase


organism: Homo sapiens

substrate_name: ATP


organism: Tick-borne encephalitis virus European subtype (strain Neudoerfl)


organism: Semliki forest virus

substrate_name: nsP2 RNA triphosphatase activity (at pH 8.0)

assay_conditions_summary: pH 8; cofactor ATP


organism: Venezuelan equine encephalitis virus (strain 3880)

substrate_name: a 12 residues substrate for nsp2 protease activity


organism: Dengue virus type 2 (strain Thailand/NGS-C/1944)

substrate_name: triphosphorylated RNA

proof_lines: Vmax with 0.65 nmol/s/ug enzyme for RTPase activity with triphosphorylated RNA as substrate.

substrate: triphosphorylated RNA


substrate_name: ATP (in the absence of nucleic acid)

proof_lines: kcat is 14 min(-1) for ATP hydrolysis in the absence of nucleic acid (PubMed:17357160). kcat is 36 min(-1) for ATP hydrolysis in the presence of ssDNA oligonucleoside dA200 (PubMed:17357160). kcat is 1.6 min(-1) for ATP hydrolysis in the ab

substrate: ATP (in the absence of nucleic acid)


proof_lines: kcat is 1.9 min(-1) for ATP hydrolysis in the absence of nucleic acid (PubMed:21589879). kcat is 3.8 min(-1) for ATP hydrolysis in the presence of RNA oligo(rU)20 (PubMed:21589879). kcat is 2.1 min(-1) for ATP hydrolysis in the presence of


organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

proof_lines: The kinetic parameters are studied for the 3C-like proteinase domain.

substrate: peptide TSAVLQSGFRK-NH(2)


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

substrate: ATP


organism: Kokobera virus


organism: Reovirus type 3 (strain Dearing)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Venezuelan equine encephalitis virus (strain Trinidad donkey)

substrate: a 12 residues substrate for nsp2 protease activity


organism: Saccharomyces cerevisiae

substrate_name: ATP; H2O

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

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged K92A

substrate: ATP; H2O


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged S228A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged T230A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant I348T


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant A457D


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405Y


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


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

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L + P174S


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L + D479N


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L + I348T


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L + A457D


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant T166S


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F162L


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant T166A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged R376A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged K389A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged K92A-K389A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged H375E


organism: Bamboo mosaic virus

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant NTPase L543A (aa 514-892)

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant RNA 5'-triphosphatase L543A (aa 514-892)


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant NTPase Q826A (aa 514-892)

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant RNA 5'-triphosphatase Q826A (aa 514-892)


unit: Mswedgeone


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant NTPase D858A (aa 514-892)

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant RNA 5'-triphosphatase D858A (aa 514-892)


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant Q169E


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant Q169A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F162A


organism: Xenopus laevis

substrate_name: H2O; dATP

substrate: H2O; dATP


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104delta38 (C-terminal)


mutation_signature: Δ4

proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104delta4 (C-terminal)


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Y662K


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Y662W


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant K620T


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant E285Q


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant K218T


enzyme: non-chaperonin molecular chaperone ATPase


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant E687Q


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104delta22 (C-terminal)


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104 T317A


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104 Y819W


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104 R826M


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant E645K


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Y662A


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Y662F


organism: Escherichia coli


sequence_variant_note: Mutation signature K220T matches the mutant residue at offset +0 and the reference residue at offset -13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant ClpAT K220T


organism: Pseudomonas aeruginosa


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104 N728A


organism: Bacillus subtilis


organism: Enterococcus hirae


organism: Gallus gallus


organism: Salmo salar


organism: Methanocaldococcus jannaschii

mutation_signature: Δ1

proof_lines: SABIO-RK modifier species: adenosinetriphosphatase(Enzyme) mutant delta1-73


organism: Mycoplasma hominis


proof_lines: SABIO-RK modifier species: adenosinetriphosphatase(Enzyme) mutant His-tagged OppA deltaCS2

proof_lines: SABIO-RK modifier species: adenosinetriphosphatase(Enzyme) mutant His-tagged OppA deltaCS3


organism: Rattus norvegicus


organism: Clostridium thermocellum

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


proof_lines: SABIO-RK modifier species: adenosinetriphosphatase(Enzyme) mutant K8A His10-tagged


organism: Helicobacter pylori

assay_conditions_summary: pH 6; 303.15 K; cofactor ATP


substrate_name: GTP

substrate: GTP


enzyme_display_name: alanine--oxo-acid transaminase

organism: Trypanosoma cruzi

substrate_name: L-Tyrosine; Pyruvate

proof_lines: SABIO-RK modifier species: alanine---oxo-acid transaminase(Enzyme) mutant N17S

enzyme: alanine--oxo-acid transaminase

substrate: L-Tyrosine; Pyruvate


substrate_name: L-Alanine

substrate: L-Alanine


substrate_name: pyruvate

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

substrate: pyruvate


substrate_name: L-Tyrosine

substrate: L-Tyrosine


proof_lines: SABIO-RK modifier species: alanine---oxo-acid transaminase(Enzyme) mutant R20A


organism: Homo sapiens

substrate_name: dIMP; H2O

substrate: dIMP; H2O