column_label: Table 4: Malonyl-CoA Decarboxylation Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1). Table 4, row F215W; column kcat (x10^-3 min^-1) = 49.3; column Km (uM) = 124; column kcat/Km (s^-1 M^-1) = 7.9. captured primary segment: Malonyl-CoA | F215W | Table 4, row F215W | kcat 49.3 x 10^-3 min^-1 | Km 124 uM | kcat/Km 7.9 s^-1 M^-1

raw_value_unit_evidence: Table 4, row F215W: kcat = 49.3 x 10^-3 min^-1 (printed cell 49.3 in the column headed kcat (x10^-3 min^-1)); Km = 124 uM; printed kcat/Km = 7.9 s^-1 M^-1.

row_label: Table 4, row F215W


enzyme_display_name: chalcone synthase

organism: Medicago sativa

substrate_name: 4-Coumaroyl-CoA; Malonyl-CoA

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 canonical sequence with row-specific F215Y substitution reconstructed during review. and applied mutation signature F215Y to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: cofactor CoA

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant F215Y

enzyme: chalcone synthase

substrate: 4-Coumaroyl-CoA; Malonyl-CoA


substrate_name: Malonyl-CoA

source_db: oed

verification_status: corrected

source_license: CC BY 4.0

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature F215S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM potassium phosphate; cofactor CoA

column_label: Table 3: CHS Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1), printed in a p-Coumaroyl-CoA section and a Malonyl-CoA section. Table 3, Malonyl-CoA section, row F215S; column kcat (x10^-3 min^-1) = 37.5; column Km (uM) = 104; column kcat/Km (s^-1 M^-1) = 6.0. captured primary segment: Malonyl-CoA | F215S | Table 3, Malonyl-CoA section, row F215S | kcat 37.5 x 10^-3 min^-1 | Km 104 uM | kcat/Km 6.0 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed Table 3, Malonyl-CoA section, row F215S kcat cell 37.5 in a column headed x10^-3 min^-1, that is 37.5 x 10^-3 min^-1 = 0.0375 min^-1; 1 min^-1 is 1/60 s^-1, so 0.0375 / 60 = 0.000625 s^(-1). Km: printed Km cell 104 uM; 1 uM is 1/1000 mM, so 104 / 1000 = 0.104 mM. kcat/Km: printed kcat/Km cell 6.0 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.0 / 1000 = 0.006 s^-1 mM^-1. Quotient disclosure for this measurement: 0.000625 / 0.104 = 0.006009615384615385 s^-1 mM^-1, alongside the printed efficiency cell 0.006 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, Malonyl-CoA section, row F215S: kcat = 37.5 x 10^-3 min^-1 (printed cell 37.5 in the column headed kcat (x10^-3 min^-1)); Km = 104 uM; printed kcat/Km = 6.0 s^-1 M^-1.

row_label: Table 3, Malonyl-CoA section, row F215S

data_origin: experimental

substrate: Malonyl-CoA

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 canonical sequence with row-specific F215S substitution reconstructed during review. and applied mutation signature F215S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant F215S CHS2, N-terminal His-tag


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature N336A to reconstruct the assayed variant sequence.

column_label: Table 3: CHS Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1), printed in a p-Coumaroyl-CoA section and a Malonyl-CoA section. Table 3, p-Coumaroyl-CoA section, row N336A; column kcat (x10^-3 min^-1) = 31.7; column Km (uM) = 5.8; column kcat/Km (s^-1 M^-1) = 91.0. captured primary segment: p-Coumaroyl-CoA | N336A | Table 3, p-Coumaroyl-CoA section, row N336A | kcat 31.7 x 10^-3 min^-1 | Km 5.8 uM | kcat/Km 91.0 s^-1 M^-1

raw_value_unit_evidence: Table 3, p-Coumaroyl-CoA section, row N336A: kcat = 31.7 x 10^-3 min^-1 (printed cell 31.7 in the column headed kcat (x10^-3 min^-1)); Km = 5.8 uM; printed kcat/Km = 91.0 s^-1 M^-1.


substrate_name: Chalcone synthase; Coenzyme A

kcat_display: Not reported

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 canonical sequence with row-specific N336Q substitution reconstructed during review. and applied mutation signature N336Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant N336Q

substrate: Chalcone synthase; Coenzyme A


sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 canonical sequence with row-specific H303T substitution reconstructed during review. and applied mutation signature H303T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant H303T


substrate_name: Malonyl-CoA; 4-Coumaroyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 canonical sequence with row-specific F215W substitution reconstructed during review. and applied mutation signature F215W to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant F215W

substrate: Malonyl-CoA; 4-Coumaroyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature H303Q to reconstruct the assayed variant sequence.

column_label: Table 3: CHS Steady-State Kinetic Parameters (Biochemistry 2000, 39(5):890-902); printed column heads kcat (x10^-3 min^-1) | Km (uM) | kcat/Km (s^-1 M^-1), printed in a p-Coumaroyl-CoA section and a Malonyl-CoA section. Table 3, p-Coumaroyl-CoA section, row H303Q; column kcat (x10^-3 min^-1) = 289; column Km (uM) = 7.6; column kcat/Km (s^-1 M^-1) = 634. captured primary segment: p-Coumaroyl-CoA | H303Q | Table 3, p-Coumaroyl-CoA section, row H303Q | kcat 289 x 10^-3 min^-1 | Km 7.6 uM | kcat/Km 634 s^-1 M^-1

raw_value_unit_evidence: Table 3, p-Coumaroyl-CoA section, row H303Q: kcat = 289 x 10^-3 min^-1 (printed cell 289 in the column headed kcat (x10^-3 min^-1)); Km = 7.6 uM; printed kcat/Km = 634 s^-1 M^-1.


enzyme_display_name: catalase

organism: Aspergillus niger

mutation_signature: Unknown

kcat_over_km_origin: calculated

sequence_source: UniProt REST uniprotkb/P55303.json, accessed 2026-06-05

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

smiles: OO

enzyme: catalase


organism: Bacillus altitudinis

verification_status: unverified

sequence_source: UniProt REST uniprotkb/W6AYH3.json, accessed 2026-06-05

status: unverified


organism: Bacillus subtilis

source_db: brenda

sequence_source: UniProt REST uniprotkb/Q9AQQ9.json, accessed 2026-06-05

source: brenda


organism: Bacteroides fragilis

sequence_source: UniProt REST uniprotkb/P45737.json, accessed 2026-06-05


organism: Bordetella pertussis

sequence_source: UniProt REST uniprotkb/P0A323.json, accessed 2026-06-05


sequence_source: UniProtKB P0A323 direct REST check on 2026-06-05


organism: Bos taurus

sequence_source: UniProtKB P00432 direct REST check on 2026-06-05


organism: Brucella abortus

sequence_source: UniProtKB P0A327 direct REST check on 2026-06-05


organism: Burkholderia pseudomallei

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


substrate_name: H+; NADH; O2

assay_conditions_summary: cofactor NADH

substrate: H+; NADH; O2


substrate_name: NADH

assay_conditions_summary: pH 8.75; 298.15 K; cofactor NADH

substrate: NADH


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB:P21179 direct REST check on 2026-06-05 plus R260A reconstruction from PMID 10091651 context and applied mutation signature R260A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: catalase(Enzyme) mutant Arg260Ala


sequence_source: UniProtKB:P21179 direct REST check on 2026-06-05


organism: Helicobacter pylori

sequence_source: UniProtKB:P77872 direct REST check on 2026-06-05


organism: Homo sapiens

sequence_source: UniProtKB:P04040 direct REST check on 2026-06-05


organism: Mycothermus thermophilus

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


organism: Neurospora crassa

ki_unit: mM

sequence_source: UniProtKB:Q9C168 reviewed FASTA direct check


organism: Oryza sativa

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0D9C4 reviewed FASTA plus direct L189W/H225T reconstruction and applied mutation signature L189W/H225T to reconstruct the assayed variant sequence.


organism: Synechocystis sp.

sequence_variant_note: Resolved canonical sequence from UniProtKB:P73911 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature N153D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: catalase(Enzyme) mutant KatG N153D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P73911 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature N153A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P73911 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature Y249F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: catalase(Enzyme) mutant Y249F


sequence_source: UniProtKB:P73911 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present


sequence_variant_note: Resolved canonical sequence from UniProtKB:P73911 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature M275I to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: catalase(Enzyme) mutant M275I


sequence_variant_note: Resolved canonical sequence from UniProtKB:P73911 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature R439A to reconstruct the assayed variant sequence.


organism: Pseudomonas syringae

sequence_source: UniProtKB reviewed primary accession P46206 direct REST lookup on 2026-06-05


organism: Psychrobacter piscatorii

sequence_source: UniProtKB unreviewed primary accession A0A0T6DN91 direct REST lookup on 2026-06-05


organism: Pyrobaculum calidifontis

sequence_source: UniProtKB unreviewed primary accession Q6LA34 direct REST lookup on 2026-06-05

proof_lines:
pH 7.0, 25°C, per subunit
pH 7.0, 25°C


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: SABIO-RK modifier species: catalase(Enzyme) mutant KatG N153A


sequence_source: UniProtKB reviewed Swiss-Prot Q0D9C4 direct lookup


sequence_source: UniProtKB unreviewed TrEMBL A3REN3 direct lookup


organism: Pigmentiphaga sp. DL-8

sequence_source: UniProtKB unreviewed TrEMBL A0A0C4Y3B2 direct lookup


organism: Proteus mirabilis

sequence_source: UniProtKB reviewed Swiss-Prot P42321 direct lookup


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed Swiss-Prot Q59635 direct lookup


sequence_source: UniProtKB reviewed Swiss-Prot P46206 direct lookup


organism: Listeria seeligeri

sequence_source: UniProtKB:P24168 direct REST check 2026-06-05


organism: Micrococcus luteus

sequence_source: UniProtKB:P29422 direct REST check 2026-06-05


sequence_source: UniProtKB:M4GGR7 plus RCSB 5XVZ direct checks 2026-06-05


sequence_variant_note: Resolved canonical sequence from UniProtKB:M4GGR7 plus RCSB 5Y17 residue-numbering check 2026-06-05 and applied mutation signature E316H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:M4GGR7 direct REST check 2026-06-05


organism: Medicago sativa

substrate_name: Benzoyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB P30074 reviewed canonical sequence plus row-specific F265V reconstruction performed during worker6 review. and applied mutation signature F265V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

substrate: Benzoyl-CoA


substrate_name: n-Valeryl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P30074 and applied mutation signature F215S to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Valeryl-CoA', F215S column group; column 'kcat (min^-1)' = 0.04; column 'Km (uM)' = 4.5; column 'kcat/Km (M^-1 s^-1)' = 151.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row Valeryl-CoA: kcat = 0.04 min^-1; Km = 4.5 uM; printed kcat/Km = 151 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'Valeryl-CoA'

table_label: Table 2. Steady-state kinetic parameters (Proc. Natl. Acad. Sci. U.S.A. 2002, 99(8): 5319-5324, journal page 5321)

substrate: n-Valeryl-CoA


substrate_name: Acetyl-CoA

verification_status: verified

sequence_source: UniProtKB P30074 reviewed canonical sequence retrieved during worker6 review.

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Acetyl-CoA; kcat column raw 0.19 min^-1; Km column raw 8.4 uM; kcat/Km column raw 376 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 0.19 min^-1 / 60 = 0.003167 s^-1, carried at the export precision as normalized_value=0.003 normalized_unit=s^-1; Km 8.4 uM / 1000 = 0.008400 mM, carried at the export precision as normalized_value=0.008 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 0.375 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 376 M^-1 s^-1 normalizes to 0.376 s^-1*mM^-1 (deviation 0.3%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, CHS column group, row Acetyl-CoA: kcat raw_value=0.19 raw_unit=min^-1; Km raw_value=8.4 raw_unit=uM; kcat/Km raw_value=376 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: CHS column group | Acetyl-CoA

substrate: Acetyl-CoA

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P30074 and applied mutation signature F265V to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Acetyl-CoA', F265V column group; column 'kcat (min^-1)' = 0.39; column 'Km (uM)' = 8.6; column 'kcat/Km (M^-1 s^-1)' = 755.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Acetyl-CoA: kcat = 0.39 min^-1; Km = 8.6 uM; printed kcat/Km = 755 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Acetyl-CoA'


substrate_name: heptanoyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Heptanoyl-CoA', F265V column group; column 'kcat (min^-1)' = 6.58; column 'Km (uM)' = 7.8; column 'kcat/Km (M^-1 s^-1)' = 14,060.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Heptanoyl-CoA: kcat = 6.58 min^-1; Km = 7.8 uM; printed kcat/Km = 14,060 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Heptanoyl-CoA'

substrate: heptanoyl-CoA


substrate_name: Octanoyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Octanoyl-CoA; kcat column raw 2.74 min^-1; Km column raw 3.8 uM; kcat/Km column raw 12,017 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 2.74 min^-1 / 60 = 0.045667 s^-1, carried at the export precision as normalized_value=0.046 normalized_unit=s^-1; Km 3.8 uM / 1000 = 0.003800 mM, carried at the export precision as normalized_value=0.004 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 11.5 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 12,017 M^-1 s^-1 normalizes to 12.017 s^-1*mM^-1 (deviation 4.3%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, CHS column group, row Octanoyl-CoA: kcat raw_value=2.74 raw_unit=min^-1; Km raw_value=3.8 raw_unit=uM; kcat/Km raw_value=12,017 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: CHS column group | Octanoyl-CoA

substrate: Octanoyl-CoA


column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Valeryl-CoA; kcat column raw 1.86 min^-1; Km column raw 4.5 uM; kcat/Km column raw 6,889 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 1.86 min^-1 / 60 = 0.031000 s^-1, carried at the export precision as normalized_value=0.031 normalized_unit=s^-1; Km 4.5 uM / 1000 = 0.004500 mM, carried at the export precision as normalized_value=0.005 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 6.2 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 6,889 M^-1 s^-1 normalizes to 6.889 s^-1*mM^-1 (deviation 10.0%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, CHS column group, row Valeryl-CoA: kcat raw_value=1.86 raw_unit=min^-1; Km raw_value=4.5 raw_unit=uM; kcat/Km raw_value=6,889 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: CHS column group | Valeryl-CoA


sequence_source: UniProtKB P30074 reviewed canonical sequence plus row-specific F265V reconstruction performed during worker6 review.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant F265V CHS2, N-terminal His-tag


proof_lines: SABIO-RK modifier species: catalase(Enzyme) mutant R439N


proof_lines: SABIO-RK modifier species: catalase(Enzyme) mutant R439A


organism: Xanthomonas campestris

sequence_source: UniProtKB:Q8L2Z7 exact accession lookup, retrieved 2026-06-05


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30074 canonical sequence plus row-specific N336D substitution reconstructed during review on 2026-06-05 and applied mutation signature N336D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant N336D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30074 canonical sequence plus row-specific C164A substitution reconstructed during review on 2026-06-05 and applied mutation signature C164A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant C164A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30074 canonical sequence plus row-specific N336A substitution reconstructed during review on 2026-06-05 and applied mutation signature N336A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: naringenin-chalcone synthase(Enzyme) mutant N336A


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Heptanoyl-CoA', F215S column group; column 'kcat (min^-1)' = 0.05; column 'Km (uM)' = 5.4; column 'kcat/Km (M^-1 s^-1)' = 154.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row Heptanoyl-CoA: kcat = 0.05 min^-1; Km = 5.4 uM; printed kcat/Km = 154 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'Heptanoyl-CoA'


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Benzoyl-CoA', F215S column group; column 'kcat (min^-1)' = 0.04; column 'Km (uM)' = 3.8; column 'kcat/Km (M^-1 s^-1)' = 175.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row Benzoyl-CoA: kcat = 0.04 min^-1; Km = 3.8 uM; printed kcat/Km = 175 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'Benzoyl-CoA'


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'm-Coumaroyl-CoA', F265V column group; column 'kcat (min^-1)' = 1.67; column 'Km (uM)' = 5.5; column 'kcat/Km (M^-1 s^-1)' = 5,060.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row m-Coumaroyl-CoA: kcat = 1.67 min^-1; Km = 5.5 uM; printed kcat/Km = 5,060 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'm-Coumaroyl-CoA'


substrate_name: Phenylacetyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Phenylacetyl-CoA', F215S column group; column 'kcat (min^-1)' = 0.04; column 'Km (uM)' = 4.5; column 'kcat/Km (M^-1 s^-1)' = 145.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row Phenylacetyl-CoA: kcat = 0.04 min^-1; Km = 4.5 uM; printed kcat/Km = 145 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'Phenylacetyl-CoA'

substrate: Phenylacetyl-CoA


sequence_source: UniProt P30074 direct REST lookup.

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 kinetic parameters; CHS column group; row 4-Methylcinnamoyl-CoA; kcat column raw 1.57 min^-1; Km column raw 3.4 uM; kcat/Km column raw 7,696 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 1.57 min^-1 / 60 = 0.026167 s^-1, carried at the export precision as normalized_value=0.026 normalized_unit=s^-1; Km 3.4 uM / 1000 = 0.003400 mM, carried at the export precision as normalized_value=0.003 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 8.666666666666666 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 7,696 M^-1 s^-1 normalizes to 7.696 s^-1*mM^-1 (deviation 12.6%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, CHS column group, row 4-Methylcinnamoyl-CoA: kcat raw_value=1.57 raw_unit=min^-1; Km raw_value=3.4 raw_unit=uM; kcat/Km raw_value=7,696 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: CHS column group | 4-Methylcinnamoyl-CoA


substrate_name: Cinnamoyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Cinnamoyl-CoA', F265V column group; column 'kcat (min^-1)' = 1.67; column 'Km (uM)' = 17.1; column 'kcat/Km (M^-1 s^-1)' = 1,628.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Cinnamoyl-CoA: kcat = 1.67 min^-1; Km = 17.1 uM; printed kcat/Km = 1,628 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Cinnamoyl-CoA'

substrate: Cinnamoyl-CoA


column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Phenylacetyl-CoA; kcat column raw 2.17 min^-1; Km column raw 5.1 uM; kcat/Km column raw 7,092 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 2.17 min^-1 / 60 = 0.036167 s^-1, carried at the export precision as normalized_value=0.036 normalized_unit=s^-1; Km 5.1 uM / 1000 = 0.005100 mM, carried at the export precision as normalized_value=0.005 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 7.199999999999999 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 7,092 M^-1 s^-1 normalizes to 7.092 s^-1*mM^-1 (deviation 1.5%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, CHS column group, row Phenylacetyl-CoA: kcat raw_value=2.17 raw_unit=min^-1; Km raw_value=5.1 raw_unit=uM; kcat/Km raw_value=7,092 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: CHS column group | Phenylacetyl-CoA


substrate_name: butanoyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Butyryl-CoA', F265V column group; column 'kcat (min^-1)' = 0.56; column 'Km (uM)' = 5.2; column 'kcat/Km (M^-1 s^-1)' = 1,794.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Butyryl-CoA: kcat = 0.56 min^-1; Km = 5.2 uM; printed kcat/Km = 1,794 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Butyryl-CoA'

substrate: butanoyl-CoA


column_label: Table 2 (Steady-state kinetic parameters), substrate row '4-Methylcinnamoyl-CoA', F265V column group; column 'kcat (min^-1)' = 0.82; column 'Km (uM)' = 7.4; column 'kcat/Km (M^-1 s^-1)' = 1,846.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row 4-Methylcinnamoyl-CoA: kcat = 0.82 min^-1; Km = 7.4 uM; printed kcat/Km = 1,846 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row '4-Methylcinnamoyl-CoA'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature F215S to reconstruct the assayed variant sequence.

column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Octanoyl-CoA; F215S column group; kcat cell = 0.04 min^-1; Km cell = 4.8 uM; kcat/Km cell = 150 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.04 min^-1; the printed turnover column is per MINUTE, so 0.04 / 60 = 0.0006666666666666666 s^-1; the exported value is 0.04 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 4.8 uM; 1 uM = 1/1000 mM, so 4.8 / 1000 = 0.0048 mM; the exported value is 4.8 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 150 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 150 / 1000 = 0.15 s^-1 mM^-1; the exported value is 150.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row Octanoyl-CoA: kcat = 0.04 min^-1; Km = 4.8 uM; kcat/Km = 150 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P30074 and applied mutation signature F265V to reconstruct the assayed variant sequence.


substrate_name: Hexanoyl-CoA

column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Hexanoyl-CoA; CHS column group; kcat cell = 2.52 min^-1; Km cell = 4.1 uM; kcat/Km cell = 10,243 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.52 min^-1; the printed turnover column is per MINUTE, so 2.52 / 60 = 0.042 s^-1; the exported value is 2.52 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 4.1 uM; 1 uM = 1/1000 mM, so 4.1 / 1000 = 0.0041 mM; the exported value is 4.1 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 10,243 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 10,243 / 1000 = 10.243 s^-1 mM^-1; the exported value is 10243.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, CHS column group, substrate row Hexanoyl-CoA: kcat = 2.52 min^-1; Km = 4.1 uM; kcat/Km = 10,243 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.

substrate: Hexanoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30074 and applied mutation signature F265V to reconstruct the assayed variant sequence.

column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Hexanoyl-CoA; F265V column group; kcat cell = 3.56 min^-1; Km cell = 5.0 uM; kcat/Km cell = 11,866 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.56 min^-1; the printed turnover column is per MINUTE, so 3.56 / 60 = 0.059333333333333335 s^-1; the exported value is 3.56 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 5.0 uM; 1 uM = 1/1000 mM, so 5.0 / 1000 = 0.005 mM; the exported value is 5.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 11,866 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 11,866 / 1000 = 11.866 s^-1 mM^-1; the exported value is 11866.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Hexanoyl-CoA: kcat = 3.56 min^-1; Km = 5.0 uM; kcat/Km = 11,866 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.


column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Phenylacetyl-CoA; F265V column group; kcat cell = 4.37 min^-1; Km cell = 5.7 uM; kcat/Km cell = 12,778 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.37 min^-1; the printed turnover column is per MINUTE, so 4.37 / 60 = 0.07283333333333333 s^-1; the exported value is 4.37 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 5.7 uM; 1 uM = 1/1000 mM, so 5.7 / 1000 = 0.0057 mM; the exported value is 5.7 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 12,778 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 12,778 / 1000 = 12.778 s^-1 mM^-1; the exported value is 12778.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Phenylacetyl-CoA: kcat = 4.37 min^-1; Km = 5.7 uM; kcat/Km = 12,778 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.


substrate_name: Feruloyl-CoA

column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Feruloyl-CoA; CHS column group; kcat cell = 1.04 min^-1; Km cell = 5.2 uM; kcat/Km cell = 3,333 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.04 min^-1; the printed turnover column is per MINUTE, so 1.04 / 60 = 0.017333333333333333 s^-1; the exported value is 1.04 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 5.2 uM; 1 uM = 1/1000 mM, so 5.2 / 1000 = 0.0052 mM; the exported value is 5.2 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 3,333 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 3,333 / 1000 = 3.333 s^-1 mM^-1; the exported value is 3333.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, CHS column group, substrate row Feruloyl-CoA: kcat = 1.04 min^-1; Km = 5.2 uM; kcat/Km = 3,333 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.

substrate: Feruloyl-CoA


column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Feruloyl-CoA; F265V column group; kcat cell = 2.43 min^-1; Km cell = 9.0 uM; kcat/Km cell = 4,500 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.43 min^-1; the printed turnover column is per MINUTE, so 2.43 / 60 = 0.0405 s^-1; the exported value is 2.43 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 9.0 uM; 1 uM = 1/1000 mM, so 9.0 / 1000 = 0.009 mM; the exported value is 9.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 4,500 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 4,500 / 1000 = 4.5 s^-1 mM^-1; the exported value is 4500.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Feruloyl-CoA: kcat = 2.43 min^-1; Km = 9.0 uM; kcat/Km = 4,500 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.


column_label: Table 2. Steady-state kinetic parameters, journal page 5321 (PDF page 4). Substrate row Octanoyl-CoA; F265V column group; kcat cell = 9.82 min^-1; Km cell = 5.6 uM; kcat/Km cell = 29,226 M^-1 s^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 9.82 min^-1; the printed turnover column is per MINUTE, so 9.82 / 60 = 0.16366666666666668 s^-1; the exported value is 9.82 s^-1, which is the printed per-minute cell carrying the canonical per-second label without conversion. Km: printed Table 2 cell 5.6 uM; 1 uM = 1/1000 mM, so 5.6 / 1000 = 0.0056 mM; the exported value is 5.6 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat/Km: printed Table 2 cell 29,226 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 29,226 / 1000 = 29.226 s^-1 mM^-1; the exported value is 29226.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Octanoyl-CoA: kcat = 9.82 min^-1; Km = 5.6 uM; kcat/Km = 29,226 M^-1 s^-1. Values for kcat, Km, and kcat/Km are min-1, uM, M-1*s-1, respectively.


organism: Sorbus aucuparia

sequence_source: UniProtKB Q27Z06 direct REST lookup; EMBL DQ286037 protein ABB89213.1; reference PMID 17109150


assay_conditions_summary: pH 7; 308.15 K; cofactor CoA


sequence_source: UniProtKB:P30074 REST lookup on 2026-06-05

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row o-Coumaroyl-CoA; kcat column raw 2.32 min^-1; Km column raw 3.8 uM; kcat/Km column raw 10,175 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 2.32 min^-1 / 60 = 0.038667 s^-1, carried at the export precision as normalized_value=0.039 normalized_unit=s^-1; Km 3.8 uM / 1000 = 0.003800 mM, carried at the export precision as normalized_value=0.004 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 9.75 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 10,175 M^-1 s^-1 normalizes to 10.175 s^-1*mM^-1 (deviation 4.2%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, CHS column group, row o-Coumaroyl-CoA: kcat raw_value=2.32 raw_unit=min^-1; Km raw_value=3.8 raw_unit=uM; kcat/Km raw_value=10,175 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: CHS column group | o-Coumaroyl-CoA


column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Cinnamoyl-CoA; kcat column raw 4.76 min^-1; Km column raw 5.0 uM; kcat/Km column raw 15,866 M^-1 s^-1. kcat and Km come from the same single row and the same single column group, so the exported tuple does not span two rows or two enzymes.

normalized_value_unit_evidence: kcat 4.76 min^-1 / 60 = 0.079333 s^-1, carried at the export precision as normalized_value=0.079 normalized_unit=s^-1; Km 5.0 uM / 1000 = 0.005000 mM, carried at the export precision as normalized_value=0.005 normalized_unit=mM; kcat/Km normalized as the quotient of those two normalized cells = 15.8 s^-1*mM^-1, while the independently printed Table 2 kcat/Km cell 15,866 M^-1 s^-1 normalizes to 15.866 s^-1*mM^-1 (deviation 0.4%, inside the 15% cutoff this package uses).

raw_value_unit_evidence: Table 2, CHS column group, row Cinnamoyl-CoA: kcat raw_value=4.76 raw_unit=min^-1; Km raw_value=5.0 raw_unit=uM; kcat/Km raw_value=15,866 raw_unit=M^-1 s^-1. The Table 2 footnote states the three column units are min^-1, uM and M^-1*s^-1 respectively.

row_label: CHS column group | Cinnamoyl-CoA


substrate_name: phenylpropionyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row 3-Phenylpropionyl-CoA; literal cells kcat 4.95 min^-1, Km 4.9 uM, kcat/Km 16,836 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 4.95 min^-1 normalizes to 0.0825 s^-1 and is stored at current precision as 0.083; printed Km 4.9 uM normalizes to 0.004900000000000001 mM and is stored as 0.005; current stored quotient is 16.6 s^-1*mM^-1; the independently printed ratio normalizes to 16.836 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row 3-Phenylpropionyl-CoA: kcat 4.95 min^-1; Km 4.9 uM; kcat/Km 16,836 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | 3-Phenylpropionyl-CoA

substrate: phenylpropionyl-CoA


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Valeryl-CoA', F265V column group; column 'kcat (min^-1)' = 1.33; column 'Km (uM)' = 6.1; column 'kcat/Km (M^-1 s^-1)' = 3,634.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Valeryl-CoA: kcat = 1.33 min^-1; Km = 6.1 uM; printed kcat/Km = 3,634 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Valeryl-CoA'


organism: Panicum virgatum

sequence_source: UniProtKB:A0A8T0PQ54 REST lookup on 2026-06-05

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

proof_lines: in the presence of chalcone isomerase and chalcone isomerase-like protein, pH and temperature not specified in the publication

proof_lines: in the presence of chalcone isomerase, pH and temperature not specified in the publication

proof_lines: in the presence of chalcone isomerase-like protein, pH and temperature not specified in the publication


organism: Physcomitrium patens

substrate_name: p-Coumaroyl-CoA; malonyl-CoA

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

sequence_source: UniProtKB:Q2VAZ3 REST lookup on 2026-06-05

assay_conditions_summary: pH 7.2; 310.15 K; cofactor CoA

proof_lines:
37°C, pH 7.2
Raw SKiD Env: Temp=37°C, pH=7.2

source_databases_merged: brenda skid

substrate: p-Coumaroyl-CoA; malonyl-CoA


organism: Polygonum cuspidatum

substrate_name: malonyl-CoA; 4-coumaroyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:H9DV62 canonical sequence with R105Q reconstructed on 2026-06-05 and applied mutation signature R105Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication

substrate: malonyl-CoA; 4-coumaroyl-CoA


substrate_name: 4-coumaroyl-CoA; malonyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:H9DV62 canonical sequence with Q82P reconstructed on 2026-06-05 and applied mutation signature Q82P to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication

substrate: 4-coumaroyl-CoA; malonyl-CoA


sequence_source: UniProtKB:H9DV62 direct REST lookup on 2026-06-05

proof_lines: wild type enzyme, at pH 8.0, temperature not specified in the publication


substrate_name: malonyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:H9DV62 direct REST lookup on 2026-06-05 plus row mutation Q82P/C198F and applied mutation signature Q82P/C198F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication

substrate: malonyl-CoA


organism: Rheum australe

substrate_name: octanoyl-CoA

sequence_source: UniProtKB:A0A096X8J8 direct REST lookup on 2026-06-05

proof_lines: isoform CHS1, pH and temperature not specified in the publication

substrate: octanoyl-CoA


sequence_source: UniProtKB:A0A0A0P7Q3 direct REST lookup on 2026-06-05

proof_lines: isoform CHS2, pH and temperature not specified in the publication


organism: Rubus idaeus

sequence_source: UniProtKB:Q9AU11 direct REST lookup on 2026-06-05

assay_conditions_summary: pH 9.5; 308.15 K; cofactor CoA


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

assay_conditions_summary: pH 7.5; 313.15 K; cofactor CoA


sequence_source: UniProtKB:Q8L5L2 direct REST lookup on 2026-06-05


organism: Brassica oleracea

proof_lines:
isoenzyme with optimum at pH 4.5
isoenzyme with optimum at pH 6.5
isoenzyme with optimum at pH 10.0


organism: Cytobacillus firmus

proof_lines:
isoenzyme II
isoenzyme I


organism: Escherichia coli

proof_lines: presence of 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 5.0

proof_lines: presence of 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 5.5


enzyme_display_name: bacterial leucyl aminopeptidase

organism: Vibrio proteolyticus

sequence_source: UniProtKB Q01693 canonical FASTA checked directly by UniProt REST.

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tricine

proof_lines: wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C

enzyme: bacterial leucyl aminopeptidase


substrate_name: H2O; L-Leucinyl-p-nitroanilide

sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; E151D reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 257 E with D. and applied mutation signature E151D with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bacterial leucyl aminopeptidase(Enzyme) mutant E151D-AAP

substrate: H2O; L-Leucinyl-p-nitroanilide


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

sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; E151H reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 257 E with H. and applied mutation signature E151H with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bacterial leucyl aminopeptidase(Enzyme) mutant E151H-AAP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; M180A reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 286 M with A. and applied mutation signature M180A with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M180A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; S228A reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 334 S with A. and applied mutation signature S228A with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S228A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; D118N reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 224 D with N. and applied mutation signature D118N with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D118N, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q01693 canonical sequence; D99M reconstructed by applying residue-numbering offset +106, replacing Q01693 residue 205 D with M. and applied mutation signature D99M with inferred residue-numbering offset +106 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer 10 mM Tricine

proof_lines: apparent value, mutant enzyme D99M, in 10 mM Tricine buffer, pH 8.0, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F265V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F215S to reconstruct the assayed variant sequence.


substrate_name: N-Methylanthraniloyl-CoA

substrate: N-Methylanthraniloyl-CoA


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


substrate_name: Benzoyl-CoA

substrate: Benzoyl-CoA


organism: Spinacia oleracea

proof_lines:
isozyme AII
isozyme AI


organism: Unknown

substrate_name: L-leucine 4-nitroanilide

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

substrate: L-leucine 4-nitroanilide


organism: Humulus lupulus

source_db: uniprot

source: uniprot


organism: Hypericum androsaemum


organism: Bacillus subtilis (strain 168)

substrate_name: Arg-pNA

substrate: Arg-pNA


organism: Bacillus subtilis

substrate_name: hydrogen peroxide

substrate: hydrogen peroxide


organism: Lentzea aerocolonigenes

proof_lines: kcat is 64000 min(-1) for 2-imino-3-(indol-3-yl)propanoate (at pH 7.5).


organism: Oryza sativa subsp. japonica

proof_lines: kcat is 6.6 min(-1) with H(2)O(2) as substrate (at pH 7.5).


proof_lines: kcat is 20 min(-1) with H(2)O(2) as substrate (at pH 7.5).


substrate_name: H(2)O(2) (at pH 7.4 and 30 degrees Celsius)

proof_lines: kcat is 0.5 min(-1) with H(2)O(2) as substrate (at pH 7.5) (PubMed:21979082). kcat is 28 sec(-1) with H(2)O(2) as substrate (at pH 7.4 and 30 degrees Celsius) (PubMed:26900141).


proof_lines: kcat is 0.21x10(-3) sec(-1) with 4-coumaroyl-CoA as substrate (PubMed:29760092). kcat is 0.24x10(-3) sec(-1) with malonyl-CoA as substrate (PubMed:29760092). kcat is 1.2x10(-3) sec(-1) with 4-coumaroyl-CoA as substrate (in the presence of C


substrate_name: L-Arginyl-p-nitroanilide; H2O

sequence_source: UniProtKB P25152 direct accession lookup; reviewed Bacillus subtilis strain 168 BSAP/aminopeptidase sequence checked 2026-06-05

substrate: L-Arginyl-p-nitroanilide; H2O


sequence_source: UniProtKB O32106 direct accession lookup; reviewed Bacillus subtilis strain 168 aminopeptidase sequence checked 2026-06-05

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


organism: Geobacillus stearothermophilus

sequence_variant_note: Resolved canonical sequence from UniProtKB P24828 direct accession lookup plus H227L substitution reconstructed against the canonical sequence on 2026-06-05 and applied mutation signature H227L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P24828 direct accession lookup plus H191L substitution reconstructed against the canonical sequence on 2026-06-05 and applied mutation signature H191L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P24828 direct accession lookup; reviewed Geobacillus stearothermophilus aminopeptidase 2 sequence checked 2026-06-05


sequence_source: UniProtKB Q01693 direct accession lookup checked 2026-06-05; canonical sequence retained as context only because E151Q could not be safely reconstructed from full-sequence numbering

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: SABIO-RK modifier species: bacterial leucyl aminopeptidase(Enzyme) mutant E151Q


substrate_name: Met-Leu-p-nitroanilide

sequence_source: UniProtKB Q01693 direct accession lookup; reviewed Vibrio proteolyticus bacterial leucyl aminopeptidase sequence checked 2026-06-05

substrate: Met-Leu-p-nitroanilide


substrate_name: H2O; Met-Leu-p-nitroanilide

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

proof_lines: pH 8.0, 37°C, recombinant His6-tagged enzyme, with preincubation (72 h of incubation at 37°C)

proof_lines: pH 8.0, 37°C, recombinant His6-tagged enzyme, without preincubation

source_databases_merged: sabio_rk brenda skid

substrate: H2O; Met-Leu-p-nitroanilide


enzyme_display_name: nitronate monooxygenase

organism: Neurospora crassa

sequence_source: UniProtKB reviewed accession Q01284 FASTA, retrieved 2026-06-05

enzyme: nitronate monooxygenase


smiles: O=O


smiles: CCCCCC[N+](=O)[O-]


substrate_name: O2; 2-Nitropropane

proof_lines: pH and temperature not specified in the publication

substrate: O2; 2-Nitropropane


substrate_name: nitroethane

substrate: nitroethane


organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)


organism: Aspergillus niger

substrate_name: 2-Nitropropane; O2

substrate: 2-Nitropropane; O2


organism: Cyberlindnera mrakii

sequence_source: UniProtKB direct accession check: Q12723 reviewed Swiss-Prot entry 2NPD_CYBMR

proof_lines:
anionic form of the substrate
neutral form of the substrate


organism: Metarhizium brunneum

sequence_source: UniProtKB direct accession check: A0A6C0WWH2 unreviewed TrEMBL entry A0A6C0WWH2_9HYPO


substrate_name: ethyl nitronate

sequence_source: UniProtKB direct accession check: Q01284 reviewed Swiss-Prot entry 2NPD_NEUCR

substrate: ethyl nitronate


organism: Anopheles gambiae


proof_lines:
pH 7.0, 25°C, immobilized enzyme
pH 7.0, 25°C, free enzyme


organism: Bacillus anthracis

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


organism: Bacillus pumilus


organism: Bacillus sp. (in: firmicutes)

assay_conditions_summary: pH 8.5; 277.15 K; buffer conditions

proof_lines: in 50 mM potassium phosphate buffer (pH 7.0), at 4°C

proof_lines: in 50 mM potassium phosphate buffer (pH 7.0), at 25°C


organism: Beta vulgaris subsp. cicla


organism: Bos taurus

assay_conditions_summary: pH 7; 298.15 K; buffer pH 7

proof_lines: free catalase, in 50 mM phosphate buffer pH 7.0, at 25°C


organism: Brassica oleracea var. gongylodes

proof_lines:
first isoform, 25°C, pH 4.5
second isoform, 25°C, pH 6.5
third isoform, 25°C, pH 10.0


sequence_source: UniProtKB reviewed entry Q01284, retrieved 2026-06-05


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed entry Q9HWH9, retrieved 2026-06-05


substrate_name: ethylnitronate

substrate: ethylnitronate


organism: Williopsis mrakii

sequence_source: UniProtKB reviewed entry Q12723, retrieved 2026-06-05


enzyme_display_name: catechol oxidase

organism: Portulaca grandiflora

substrate_name: L-Dopa

proof_lines:
isoenzyme Ia
isoenzyme Ib
isoenzyme II

enzyme: catechol oxidase

substrate: L-Dopa


organism: Prunus persica

substrate_name: catechol

proof_lines:
isoenzyme C
isoenzyme D
isoenzyme A

substrate: catechol


organism: Ipomoea batatas

sequence_source: UniProtKB direct accession lookup Q9ZP19 via rest.uniprot.org/uniprotkb/Q9ZP19.json on 2026-06-05


substrate_name: caffeic acid

sequence_source: UniProtKB direct accession lookup B5M680 via rest.uniprot.org/uniprotkb/B5M680.json on 2026-06-05

substrate: caffeic acid


substrate_name: chlorogenic acid

sequence_source: UniProtKB direct accession lookup Q5ENY2 via rest.uniprot.org/uniprotkb/Q5ENY2.json on 2026-06-05

substrate: chlorogenic acid


organism: Mangifera indica

sequence_source: UniProtKB direct accession lookup D2XZ13 via rest.uniprot.org/uniprotkb/D2XZ13.json on 2026-06-05

proof_lines:
pH 6.2, 25°C, sodium phosphate buffer
pH 5.8, 25°C, sodium phosphate buffer
pH 5.8, 25°C


organism: Solanum lycopersicum

substrate_name: dopamine

sequence_source: UniProtKB direct accession lookup A0A3P3ZKL1 via rest.uniprot.org/uniprotkb/A0A3P3ZKL1.json on 2026-06-05

substrate: dopamine


organism: Unknown


organism: Mycothermus thermophilus

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_M4GGR7_and_PMID_30289408_I314F and applied mutation signature I314F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 333.15 K; buffer 100 mM sodium phosphate


organism: Pouteria sapota

substrate_name: pyrogallol

proof_lines: isozyme PPO 1, in 0.2 M sodium phosphate buffer pH 7.0, 25°C

substrate: pyrogallol


organism: Agaricus bisporus

proof_lines:
pH 7.0
pH 4.5, dependent on the assay method
pH 6.0


organism: Alternaria alternata

substrate_name: D-catechin

substrate: D-catechin


organism: Amphioctopus fangsiao

assay_conditions_summary: pH 7.1; 301.15 K; buffer 20 mM Tris-HCl

proof_lines: in 20 mM Tris-HCl buffer at pH 7.1 and 28°C


organism: Anethum foeniculum

proof_lines: at pH 6.0 and 30°C, with catechol as substrate


organism: Aphonopelma californicum (nom. dub.)

proof_lines: at substrate concentrations above 4 mM, substrate inhibition is observed and the data are fitted to a simple model for substrate inhibition. KM, kcat and KI are obtained for the inhibitory binding site


organism: Asimina triloba

proof_lines: Km of pawpaw fruit PPO is comparable with the Km of PPO from other fruits


organism: Prunus armeniaca

proof_lines: kcat is 700 sec(-1) with 4-methylcatechol as substrate. kcat is 1400 sec(-1) with chlorogenic acid as substrate. kcat is 210 sec(-1) with catechol as substrate. kcat is 590 sec(-1) with pyrogallol as substrate.


organism: Cydonia oblonga


organism: Cynara cardunculus var. scolymus


organism: Erimacrus isenbeckii

proof_lines: at 22°C, pH not specified in the publication


organism: Eriobotrya japonica

substrate_name: tert-butyl-catechol

proof_lines: pH 4.5, 25°C, soluble, active enzyme form

proof_lines: pH 4.5, 25°C, particulate, latent enzyme form

substrate: tert-butyl-catechol


organism: Ferula sp.

substrate_name: (+)-catechin

proof_lines:
pH 6.5, 30°C, stem enzyme
pH 6.0, 20°C, stem enzyme
pH 7.0, 12°C, stem enzyme

substrate: (+)-catechin


organism: Fragaria x ananassa


organism: Beta vulgaris

proof_lines: pH 6.0, 25°C, soluble enzyme in presence of SDS

proof_lines: pH 6.0, 25°C, membrane enzyme in presence of SDS


organism: Bos taurus


organism: Citrus unshiu


organism: Clonorchis sinensis


organism: Coffea arabica

proof_lines:
leaf enzyme
endosperm enzyme


organism: Cucumis melo

substrate_name: 3,4-dihydroxyphenylacetic acid

proof_lines: for Cucumis melo L. inodorus cv. Amarillo

proof_lines: for Cucumis melo L. cantalupensis cv. Charentais

substrate: 3,4-dihydroxyphenylacetic acid


organism: Lycopus europaeus


organism: Malus domestica

proof_lines:
isoform mPPO, at pH 6.8 and 25°C
isoform sPPO, at pH 6.8 and 25°C


organism: Musa acuminata


organism: Musa x paradisiaca


organism: Mycelia sterilia


organism: Neurospora crassa


organism: Nicotiana tabacum


organism: Ocimum basilicum


organism: Panulirus argus


organism: Physalis peruviana


organism: Pycnoporus coccineus

substrate_name: O2; Catechol

substrate: O2; Catechol


organism: Raphanus sativus


organism: Vigna unguiculata


organism: Zea mays


organism: Capra capra


organism: Cereibacter sphaeroides


organism: Escherichia coli


organism: Sarcophaga bullata


organism: Scyllarides latus


organism: Streptomyces cyaneofuscatus


organism: Streptomyces glaucescens

substrate_name: 3,4-Dihydroxyphenyl acetic acid

substrate: 3,4-Dihydroxyphenyl acetic acid


organism: Urtica dioica


organism: Kloeckera sp.

proof_lines:
catalase activity
peroxidase activity


organism: Komagataella pastoris


organism: Mycobacterium sp.

substrate_name: o-Dianisidine

proof_lines:
peroxidase activity, pH 4.5, 30°C
catalase activity, pH 7.0, 30°C

substrate: o-Dianisidine


organism: Neurospora crassa


organism: Lablab purpureus


organism: Lactarius salmonicolor


organism: Lilium brownii var. viridulum

substrate_name: gallic acid

proof_lines:
at pH 4.0 and 25°C
at pH 7.0 and 25°C

substrate: gallic acid


organism: Lilium davidii var. unicolor


organism: Lilium lancifolium


organism: Lonicera japonica


organism: Oceanobacillus oncorhynchi

assay_conditions_summary: pH 9; 303.15 K; buffer 20 mM Tris-HCl

proof_lines: in 20 mM Tris-HCl buffer (pH 9.0), at 30°C


organism: Pseudomonas aeruginosa


organism: Pseudomonas syringae


organism: Pteris ensiformis

assay_conditions_summary: pH 7; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.0)


organism: Rhodospirillum rubrum


organism: Saccharomyces cerevisiae


organism: Serratia marcescens


organism: Talaromyces piceae

proof_lines: catalase from Penicillium piceum strain F-648 at the minimum degree of association (0.3 nM)


organism: Thermoascus aurantiacus


organism: Thermus brockianus


organism: Escherichia coli


organism: Gluconobacter oxydans

proof_lines: pH and temperature not specified in the publication


organism: Haloarcula marismortui


organism: Halobacterium salinarum

proof_lines:
peroxidase activity
catalase activity


organism: Helicobacter pylori


organism: Cyberlindnera mrakii

sequence_source: UniProtKB reviewed Q12723 FASTA fetched by direct EC+organism lookup.

proof_lines:
anionic
anionic form of substrate
neutral form of substrate


organism: Cyberlindnera saturnus

substrate_name: propionate 3-nitronate

proof_lines:
at pH 7.5 and 30°C
pH 8, 30°C
pH 5.5, 30°C

substrate: propionate 3-nitronate


organism: Fusarium oxysporum

substrate_name: nitroethane

assay_conditions_summary: pH 7; 303.15 K; cofactor FAD

substrate: nitroethane


organism: Metarhizium brunneum


organism: Neurospora crassa

substrate_name: ethylnitronate

sequence_source: UniProtKB reviewed Q01284 FASTA fetched by direct EC+organism lookup.

proof_lines: 30°C, pH 8, wild-type enzyme, ethylnitronate as a substrate

substrate: ethylnitronate


sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB reviewed Q01284 after direct residue check. and applied mutation signature H196N to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH 8, mutant enzyme H196N, ethylnitronate as a substrate


organism: Hordeum vulgare

substrate_name: feruloyl-CoA

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

assay_conditions_summary: cofactor CoA

substrate: feruloyl-CoA


organism: Humulus lupulus

substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


organism: Hypericum androsaemum

substrate_name: benzoyl-CoA

substrate: benzoyl-CoA


proof_lines: pH 7.0, 35°C, mutant enzyme L263M/F265Y/S338G


organism: Juglans sp.

substrate_name: malonyl-CoA

substrate: malonyl-CoA


organism: Oryza sativa Japonica Group

assay_conditions_summary: pH 7.2; 303.15 K; cofactor CoA

proof_lines:
isoform CHS8, at pH 7.2 and 30°C
isoform CHS24, at pH 7.2 and 30°C


organism: Petroselinum crispum

substrate_name: hexanoyl-CoA

sequence_source: UniProtKB P16107 FASTA retrieved by direct EC+organism lookup

substrate: hexanoyl-CoA


organism: Phaseolus vulgaris


organism: Scutellaria baicalensis

substrate_name: Malonyl-CoA; Cinnamoyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: Malonyl-CoA; Cinnamoyl-CoA


organism: Secale cereale

substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


organism: Sinapis alba


organism: Styphnolobium japonicum

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


organism: Tulipa hybrid cultivar


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Trichoderma viride

enzyme: glucan 1,3-beta-glucosidase


organism: Verruciconidia persicina

substrate_name: Laminarin

proof_lines: enzyme I, based on molecular mass for laminarin of 5300

proof_lines: enzyme II, based on molecular mass for laminarin of 5300

proof_lines: enzyme IIII, based on molecular mass for laminarin of 5300

substrate: Laminarin


enzyme_display_name: licheninase

organism: Acetivibrio thermocellus

assay_conditions_summary: pH 7; 310.15 K; buffer pH 7

proof_lines: pH 7.0, 37°C, 50 mM sodium phosphate buffer

enzyme: licheninase


organism: Aspergillus niger

substrate_name: lichenan

substrate: lichenan


organism: Bacillus amyloliquefaciens

substrate_name: AZO blue beta-glucan

proof_lines: recombinant wild-type enzyme, pH 6.5, 40°C

substrate: AZO blue beta-glucan


proof_lines: recombinant optimally-modified enzyme, pH 6.5, 40°C


organism: Bacillus sp. (in: firmicutes)


proof_lines:
wild type
wild type, mg/ml


enzyme_display_name: phosphate acetyltransferase

organism: Methanosarcina thermophila

substrate_name: CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature S309A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 296.15 K; cofactor CoA

enzyme: phosphate acetyltransferase

substrate: CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature D316E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature S309C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature R310K to reconstruct the assayed variant sequence.


substrate_name: Acetyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature C312A to reconstruct the assayed variant sequence.

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

substrate: Acetyl phosphate


substrate_name: Acetyl phosphate; Coenzyme A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature C159A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C159A

substrate: Acetyl phosphate; Coenzyme A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature C277A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 direct FASTA plus selected mutation_signature reconstruction and applied mutation signature R287Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R287Q


organism: Azotobacter vinelandii

substrate_name: acetyl-CoA

sequence_source: UniProtKB C1DQG8 direct REST lookup on 2026-06-05.

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

assay_conditions_summary: pH 7.2; 308.15 K; cofactor CoA

proof_lines: pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB

substrate: acetyl-CoA


sequence_source: UniProtKB C1DER7 direct REST lookup on 2026-06-05.


organism: Escherichia coli

substrate_name: Coenzyme A; Acetyl phosphate

sequence_source: UniProtKB P0A9M8 direct REST lookup on 2026-06-05.

substrate: Coenzyme A; Acetyl phosphate


sequence_source: UniProtKB P0A9M8 canonical sequence checked on 2026-06-05; row-specific construct sequence unresolved.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant Pta-F1 (last 326 amino acids), N-terminal His-tag

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant Pta-F2 (last 352 amino acids), N-terminal His-tag

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant Pta-F3 (last 470 amino acids), N-terminal His-tag


proof_lines: wild-type, pH 8.0, 30°C, Hill-constatn 1.7

proof_lines: wild-type, pH 8.0, 30°C, S0.5-value, Hill constant 1.3


sequence_source: UniProtKB P38503 direct REST lookup on 2026-06-05.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific R310A substitution reconstructed on 2026-06-05. and applied mutation signature R310A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific S309T substitution reconstructed on 2026-06-05. and applied mutation signature S309T to reconstruct the assayed variant sequence.


enzyme_display_name: Phosphate acetyltransferase

substrate_name: Coenzyme A

sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature R310Q to reconstruct the assayed variant sequence.

enzyme: Phosphate acetyltransferase

substrate: Coenzyme A


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature C325A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C325A


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature C312A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature R133Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R133Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature R28Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R28Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature C159S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical FASTA fetched directly 2026-06-05; variant rows reconstructed by applying validated substitution coordinates. and applied mutation signature C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature R87Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R87Q


sequence_source: UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature R28Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature R310Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant R310Q


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P38503 canonical sequence with row-specific mutation reconstruction and applied mutation signature C312A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C312A


organism: Escherichia coli (strain K12)

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


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature R133Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature R310Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature C159A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature C159A/C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row SABIO-RK PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature C159A/C277A/C312A/C325A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C159A, C277A, C312A, C325A


sequence_source: UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 FASTA/JSON direct check; source row OED PMID 9401029; variant reconstructed from canonical sequence and applied mutation signature R287Q to reconstruct the assayed variant sequence.


organism: Neurospora crassa

substrate_name: 3-nitropropionic acid

sequence_source: UniProtKB reviewed accession Q01284 (2NPD_NEUCR), direct EC 1.13.12.16 plus organism Neurospora crassa lookup

assay_conditions_summary: pH 7.4; 303.15 K; cofactor FMN

proof_lines:
at pH 7.4 and 30°C
at pH 9.0 and 30°C
anionic form of substrate

substrate: 3-nitropropionic acid


organism: Antirrhinum majus

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: in the absence of chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C

proof_lines: in the presence of 0.001 mM chalcone isomerase-like protein CHIL, at pH 7.5 and 30°C


organism: Avena sativa

substrate_name: Malonyl-CoA; 4-Coumaroyl-CoA

substrate: Malonyl-CoA; 4-Coumaroyl-CoA


organism: Daucus carota


organism: Fagopyrum esculentum


organism: Glycine max

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Porphyromonas gingivalis

sequence_source: UniProtKB:B2RK03 direct lookup

assay_conditions_summary: pH 9; 310.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific R287Q reconstruction and applied mutation signature R287Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific C277A reconstruction and applied mutation signature C277A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C277A


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 canonical sequence with row-specific R133Q reconstruction and applied mutation signature R133Q to reconstruct the assayed variant sequence.


organism: Moorella thermoacetica

substrate_name: acetyl phosphate

substrate: acetyl phosphate


assay_conditions_summary: pH 7.6; 328.15 K; cofactor CoA


substrate_name: propionyl-CoA

substrate: propionyl-CoA


organism: Neomoorella thermoacetica

sequence_source: UniProtKB Q2RK58 canonical sequence


sequence_source: UniProtKB Q2RJ94 canonical sequence


sequence_source: UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence.


substrate_name: Coenzyme A; Acetyl phosphate / Acetyl phosphate; Coenzyme A

sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature C159S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C159S


substrate_name: Acetyl phosphate; Coenzyme A / Coenzyme A; Acetyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature C277A/C312A/C325A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphate acetyltransferase(Enzyme) mutant C277A, C312A, C325A


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature R28Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature C277A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature R87Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 FASTA direct lookup; variant rows reconstructed from that canonical sequence. and applied mutation signature C159A to reconstruct the assayed variant sequence.


enzyme_display_name: UMP kinase

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D93A/D159N to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP

proof_lines: D93A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP

enzyme: UMP kinase


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature N72A/D93A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: pH 7.4, 30°C, mutants N72A and N72A/D93A

proof_lines: pH 7.4, 30°C, mutant N72A/D93A, in absence of GTP

substrate: ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature N140A/D159N to reconstruct the assayed variant sequence.

proof_lines: N140A/D159N mutant protein, 0.3 mM UMP, 0.5 mM GTP, 0.5 mM UTP


substrate_name: ATP; UMP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D201N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) mutant D201N

substrate: ATP; UMP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D174N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor ATP

proof_lines:
mutant D174N, at pH 6
mutant D174N, at pH 8


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D146N to reconstruct the assayed variant sequence.

proof_lines:
mutant D146N, at pH 6
mutant D146N, at pH 8


substrate_name: UMP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature R62H to reconstruct the assayed variant sequence.

proof_lines:
mutant R62H, at pH 8
mutant R62H, at pH 6

substrate: UMP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7E9 canonical sequence plus validated mutation reconstruction and applied mutation signature D168N to reconstruct the assayed variant sequence.

proof_lines:
mutant D168N, at pH 8
mutant D168N, at pH 6


sequence_source: UniProtKB direct accession lookup P0A7E9 on 2026-06-05

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

assay_conditions_summary: pH 6; 303.15 K; cofactor ATP

proof_lines:
wild-type
wild-type, at pH 6
wild-type, at pH 6.0


substrate_name: UMP; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based N140A reconstruction on 2026-06-05 and applied mutation signature N140A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) wildtype N140A His-tagged

substrate: UMP; ATP


sequence_source: UniProtKB direct accession lookup A7ZWB7 on 2026-06-05

proof_lines: in presence of 1.0 mM UMP and 0.5 mM GTP

proof_lines: in presence of 2.0 mM ATP and 0.5 mM GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based D159N reconstruction on 2026-06-05 and applied mutation signature D159N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) wildtype D159N His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based N72A/D93A/D159N reconstruction on 2026-06-05 and applied mutation signature N72A/D93A/D159N to reconstruct the assayed variant sequence.

proof_lines: N72A/D93A/D159N mutant protein, 0.3 mM UMP

proof_lines: N72A/D93A/D159N mutant protein, 2 mM ATP

proof_lines: N72A/D93A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based N72A/D159N reconstruction on 2026-06-05 and applied mutation signature N72A/D159N to reconstruct the assayed variant sequence.

proof_lines: N72A/D159N mutant protein, 1 mM UMP, 0.5 mM GTP

proof_lines: N72A/D159N mutant protein, 2 mM ATP, 0.5 mM GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based N72A reconstruction on 2026-06-05 and applied mutation signature N72A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P0A7E9 plus local one-based D93A reconstruction on 2026-06-05 and applied mutation signature D93A to reconstruct the assayed variant sequence.


organism: Haemophilus influenzae

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

sequence_source: UniProtKB P43890 canonical FASTA retrieved by direct exact accession lookup


organism: Helicobacter pylori

source_db: brenda;skid

sequence_source: UniProtKB P56106 canonical FASTA retrieved by direct exact accession lookup

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

proof_lines: in the presence of 2 mM Mg2+, at pH 7.4 and 30°C

proof_lines: in the presence of 2 mM Mn2+, at pH 7.4 and 30°C

source: brenda;skid


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 canonical FASTA; P139A reconstructed from the returned canonical sequence and applied mutation signature P139A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P9WHK5 canonical FASTA retrieved by direct exact accession lookup

proof_lines: Ki above 1 mM, wild type enzyme, at pH 7.4 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 canonical FASTA; F81W/S96A reconstructed from the returned canonical sequence and applied mutation signature F81W/S96A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F81W/S96A, at pH 7.4 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 canonical FASTA; D113A reconstructed from the returned canonical sequence and applied mutation signature D113A to reconstruct the assayed variant sequence.


organism: Staphylococcus aureus

sequence_source: UniProtKB Q2FZ22 REST lookup, reviewed Swiss-Prot entry PYRH_STAA8.


sequence_source: UniProtKB B8XPY6 REST lookup, live TrEMBL entry flagged as fragment.

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

proof_lines: crude cytosolic extract, in 50 mM Tris-HCl pH 7.4, at 30°C

proof_lines: purified enzyme, in 50 mM Tris-HCl pH 7.4, at 30°C


organism: Streptococcus pneumoniae

sequence_source: UniProtKB Q97R83 REST lookup, reviewed Swiss-Prot entry PYRH_STRPN.

proof_lines:
in the presence of MnCl2
in the presence of MgCl2


organism: Ureaplasma parvum

sequence_source: UniProtKB Q9PPX6 REST lookup, reviewed Swiss-Prot entry PYRH_UREPA.

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines:
pH 6.8
recombinant UpUMPK
competitive inhibitor towards UMP


enzyme_display_name: pepsin A

organism: Lateolabrax japonicus

substrate_name: hemoglobin

sequence_source: UniProtKB E2IKQ9 REST lookup, live TrEMBL pepsin A entry.

enzyme: pepsin A

substrate: hemoglobin


assay_conditions_summary: pH 3; 310.15 K; buffer sodium acetate

proof_lines: isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C


organism: Micropterus salmoides

substrate_name: KPAEFFRL

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

substrate: KPAEFFRL


sequence_source: UniProtKB A0A125SQG8 REST lookup, live TrEMBL pepsin A entry.

proof_lines:
pepsin A1, at pH 4.0 and 20°C
pepsin A1, at pH 4.0 and 37°C
pepsin A1, at pH 4.0 and 45°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed P139H substitution and applied mutation signature P139H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed P139W substitution and applied mutation signature P139W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed R82H substitution and applied mutation signature R82H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed R150A substitution and applied mutation signature R150A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WHK5 direct check plus reconstructed F81W substitution and applied mutation signature F81W to reconstruct the assayed variant sequence.


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB P9WHK5 direct check

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

source: skid


organism: Neisseria meningitidis

sequence_source: UniProtKB P65932 direct check

proof_lines: in presence of 0.05 mM UMP and 0.5 mM GTP

proof_lines: in presence of 1.0 mM UMP and 0.5 mM GTP


organism: Saccharolobus solfataricus

sequence_source: UniProtKB Q97ZE2 direct check

assay_conditions_summary: 333.15 K; cofactor ATP

proof_lines: radioactive assay, at 60°C, the more commonly used photometric assay using auxiliary enzymes is incompatible with high temperature

proof_lines: radioactive assay, 500 microM ATP and 100 microM UMP, at 60°C, the more commonly used photometric assay using auxiliary enzymes is incompatible with high temperature


sequence_source: UniProtKB A0A125SQG9 direct accession lookup

proof_lines:
pepsin A2, at pH 4.0 and 20°C
pepsin A2, at pH 4.0 and 30°C
pepsin A2, at pH 4.0 and 10°C


organism: Shewanella amazonensis

substrate_name: Mca-KKPAEFFALK-Dnp

sequence_source: UniProtKB A1S3N8 direct accession lookup

substrate: Mca-KKPAEFFALK-Dnp


organism: Shewanella denitrificans

sequence_source: UniProtKB Q12R32 direct accession lookup


organism: Sus scrofa

substrate_name: H2O; Casein

sequence_source: UniProtKB P00791 direct accession lookup

substrate: H2O; Casein


organism: Trematomus bernacchii

sequence_source: UniProtKB Q6HA04 direct accession lookup


sequence_source: UniProtKB Q6HA05 direct accession lookup


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O31749 direct REST lookup on 2026-06-05; variant reconstructed from selected SABIO-RK N137A note and applied mutation signature N137A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) mutant N137A His-tagged


sequence_source: UniProtKB reviewed O31749 direct REST lookup on 2026-06-05

proof_lines:
in the presence of GTP
in the absence of GTP
in presence of 2.0 mM ATP without GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O31749 direct REST lookup on 2026-06-05; variant reconstructed from selected SABIO-RK T135A note and applied mutation signature T135A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) mutant T135A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O31749 direct REST lookup on 2026-06-05; variant reconstructed from selected SABIO-RK T135A/N137A note and applied mutation signature T135A/N137A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UMP kinase(Enzyme) mutant T135A/N137A His-tagged


organism: Escherichia coli

sequence_source: UniProtKB reviewed P0A7E9 direct REST lookup on 2026-06-05

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=6


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0A7E9 direct REST lookup on 2026-06-05; variant reconstructed from selected BRENDA T138A/N140A note and applied mutation signature T138A/N140A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0A7E9 direct REST lookup on 2026-06-05; variant reconstructed from selected BRENDA T138A note and applied mutation signature T138A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0A7E9 direct REST lookup on 2026-06-05; variant reconstructed from selected BRENDA D77N note and applied mutation signature D77N to reconstruct the assayed variant sequence.

proof_lines:
mutant D77N, at pH 6
mutant D77N, at pH 8


organism: Bacillus subtilis (strain 168)

sequence_source: UniProtKB reviewed accession O31749 (PYRH_BACSU), direct lookup


enzyme_display_name: holo-[acyl-carrier-protein] synthase

substrate_name: Apo-[acyl-carrier protein]; Coenzyme A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 direct accession lookup; row-specific reconstruction from R14K/K44D and applied mutation signature R14K/K44D to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor CoA

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS R14K, K44D

enzyme: holo-[acyl-carrier-protein] synthase

substrate: Apo-[acyl-carrier protein]; Coenzyme A


substrate_name: Coenzyme A; Apo-[acyl-carrier protein]

sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 direct accession lookup; row-specific reconstruction from R14A and applied mutation signature R14A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS R14A

substrate: Coenzyme A; Apo-[acyl-carrier protein]


substrate_name: apo-[acyl-carrier protein]

sequence_source: UniProtKB:P39135 direct accession lookup for enzyme context only

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant F44M ACP substrate from Leishmania major

substrate: apo-[acyl-carrier protein]


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, Escherichia coli mutant M44F ACP substrate


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/F44M ACP substrate from Leishmania major


sequence_source: UniProtKB:P39135 direct accession lookup

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, Escherichia coli ACP substrate

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, ACP substrate from Mycobacterium tuberculosis

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, ACP substrate from Plasmodium falciparum


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/F44M/Q48E ACP substrate from Leishmania major


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/Q48E ACP substrate from Leishmania major


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 canonical sequence with selected source mutation R14K applied after residue check and applied mutation signature R14K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS R14K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 canonical sequence with selected source mutation K44A applied after residue check and applied mutation signature K44A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS K44A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96618 canonical sequence with selected source mutation K44D applied after residue check and applied mutation signature K44D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant AcpS K44D


sequence_source: UniProtKB:P96618 direct accession lookup


sequence_source: UniProtKB:P39135 canonical lookup only; row-specific N35D variant sequence unresolved

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D ACP substrate from Leishmania major


proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme, wild-type ACP substrate from Leishmania major


substrate_name: butyryl-CoA

sequence_source: UniProtKB:P24224 direct accession lookup

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

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

substrate: butyryl-CoA


organism: Homo sapiens

substrate_name: Acetyl-CoA; Apo-[acyl-carrier protein]

sequence_source: UniProtKB:Q9NRN7 direct accession lookup

substrate: Acetyl-CoA; Apo-[acyl-carrier protein]


substrate_name: acetyl-CoA / Mg2+

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical sequence with reconstructed Q112E/E181Q variant and applied mutation signature Q112E/E181Q to reconstruct the assayed variant sequence.

proof_lines:
double mutant Q112E, E181Q
+/-0.001 mM, double mutant Q112E, E181Q
+/-51 mM, double mutant Q112E, E181Q

substrate: acetyl-CoA / Mg2+


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical sequence with reconstructed E181A variant and applied mutation signature E181A to reconstruct the assayed variant sequence.


substrate_name: Acetyl-CoA; Apo-[acyl-carrier protein] plus Mg2+/acetyl-CoA source notes

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical sequence with reconstructed H111A variant and applied mutation signature H111A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site H111A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical sequence with reconstructed R47A variant and applied mutation signature R47A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site R47A

substrate: Acetyl-CoA; Apo-[acyl-carrier protein] plus Mg2+/acetyl-CoA source notes


substrate_name: Acetyl-CoA; Apo-[acyl-carrier protein] / Apo-[acyl-carrier protein]; Acetyl-CoA plus Mg2+/acetyl-CoA source notes

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical sequence with reconstructed R86A variant and applied mutation signature R86A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site R86A


sequence_source: UniProtKB Q9NRN7 canonical sequence with reconstructed E181A variant

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site E181A

substrate: Acetyl-CoA; Apo-[acyl-carrier protein] / Apo-[acyl-carrier protein]; Acetyl-CoA plus Mg2+/acetyl-CoA source notes


substrate_name: Apo-[acyl-carrier protein]; Acetyl-CoA / Acetyl-CoA; Apo-[acyl-carrier protein] plus Mg2+/acetyl-CoA source notes

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9NRN7 canonical sequence with reconstructed D129A variant and applied mutation signature D129A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: holo-[acyl-carrier-protein] synthase(Enzyme) mutant active-site D129A


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB P50113 canonical sequence

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


substrate_name: Coenzyme A

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

assay_conditions_summary: pH 5.5; 310.15 K; cofactor CoA

substrate: Coenzyme A


organism: Streptomyces griseus

substrate_name: apo-[fredericamycin H acyl-carrier protein]

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


organism: Streptomyces verticillus

substrate_name: apo-[peptidyl carrier protein]

proof_lines:
pH 8.0, 37°C, substrate BlmI
pH 8.0, 37°C, substrate TcmM
pH 8.0, 37°C

substrate: apo-[peptidyl carrier protein]


organism: Vibrio harveyi

substrate_name: apo-acyl-carrier protein

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

proof_lines: pH 7.8, 37°C, mutant acyl carrier protein I54L

substrate: apo-acyl-carrier protein


proof_lines: pH 7.8, 37°C, Escherichia coli acyl carrier protein


proof_lines: pH 7.8, 37°C, mutant acyl carrier protein Y71A


proof_lines: pH 7.8, 37°C, mutant acyl carrier protein V12G


substrate_name: apo-ACP

proof_lines: pH 7.8, 37°C, mutant acyl carrier protein F50A

substrate: apo-ACP


substrate_name: GDSLSWLLRCLN

assay_conditions_summary: pH 8.8; 310.15 K; cofactor CoA

proof_lines:
pH 8.8, 37°C, isoenzyme Sfp
pH 8.8, 37°C, isoenzyme Sfp, apo-hPCP
pH 6.0, 37°C

substrate: GDSLSWLLRCLN


organism: Unknown


proof_lines: pH 7.8, 37°C, mutant acyl carrier protein A59G


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: CoA

substrate: CoA


organism: Escherichia coli (strain K12)

substrate_name: acetyl phosphate

proof_lines: kcat is 415.5 sec(-1) for acetyl-CoA formation, kcat is 119.8 sec(-1) for acetyl phosphate formation.

substrate: acetyl phosphate