sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature K63R/F65L to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, Acetyl-CoA block, enzyme row KF (K63R/F65L); column Km (uM) = 19; column kcat (s^-1) = 42; column kcat/Km (s^-1 uM^-1) = 2.2. captured primary segment: Acetyl-CoA | KF variant Mpr1 (K63R/F65L) | Km 19 uM | kcat 42 s^-1 | kcat/Km 2.2 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 19 uM; 1 uM is 1/1000 mM, giving 0.019 mM; the exported value is 0.019 mM. kcat: printed cell 42 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 42.0 s^(-1); the exported value is 42.0 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 2.2 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 2200.0 s^(-1)*mM^(-1). The exported kcat_over_km 2210.5263157894738 s^(-1)*mM^(-1) is the exact full-precision quotient of the two printed cells of this same row, and the printed efficiency cell is that quotient written to the precision the column uses. The quotient of this row's own printed component cells is 42 / 0.019 = 2210.5263157894738 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Acetyl-CoA block, enzyme row KF: Km = 19 uM; kcat = 42 s^-1; printed kcat/Km = 2.2 s^-1 uM^-1.


organism: Saccharomyces cerevisiae

substrate_name: acetyl-CoA

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature F65L to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 8.5; 303.15 K; buffer 50 mM Tris-HCl; cofactor CoA

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, Acetyl-CoA block, enzyme row F65L; column Km (uM) = 10; column kcat (s^-1) = 31; column kcat/Km (s^-1 uM^-1) = 2.9. captured primary segment: Acetyl-CoA | F65L variant Mpr1 | Km 10 uM | kcat 31 s^-1 | kcat/Km 2.9 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 10 uM; 1 uM is 1/1000 mM, giving 0.01 mM; the exported value is 0.01 mM. kcat: printed cell 31 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 31.0 s^(-1); the exported value is 31.0 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 2.9 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 2900.0 s^(-1)*mM^(-1). The exported kcat_over_km is 3100.0 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 31 / 0.01 = 3100.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Acetyl-CoA block, enzyme row F65L: Km = 10 uM; kcat = 31 s^-1; printed kcat/Km = 2.9 s^-1 uM^-1.

data_origin: experimental

substrate: acetyl-CoA

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature F65L/L117V to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, Acetyl-CoA block, enzyme row FL (F65L/L117V); column Km (uM) = 13; column kcat (s^-1) = 31; column kcat/Km (s^-1 uM^-1) = 2.3. captured primary segment: Acetyl-CoA | FL variant Mpr1 (F65L/L117V) | Km 13 uM | kcat 31 s^-1 | kcat/Km 2.3 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 13 uM; 1 uM is 1/1000 mM, giving 0.013 mM; the exported value is 0.013 mM. kcat: printed cell 31 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 31.0 s^(-1); the exported value is 31.0 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 2.3 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 2300.0 s^(-1)*mM^(-1). The exported kcat_over_km is 2384.6153846153848 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 31 / 0.013 = 2384.6153846153848 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Acetyl-CoA block, enzyme row FL: Km = 13 uM; kcat = 31 s^-1; printed kcat/Km = 2.3 s^-1 uM^-1.


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature L117V to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, Acetyl-CoA block, enzyme row L117V; column Km (uM) = 7.6; column kcat (s^-1) = 38; column kcat/Km (s^-1 uM^-1) = 5.0. captured primary segment: Acetyl-CoA | L117V variant Mpr1 | Km 7.6 uM | kcat 38 s^-1 | kcat/Km 5.0 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 7.6 uM; 1 uM is 1/1000 mM, giving 0.0076 mM; the exported value is 0.0076 mM. kcat: printed cell 38 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 38.0 s^(-1); the exported value is 38.0 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 5.0 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 5000.0 s^(-1)*mM^(-1). The exported kcat_over_km is 5000.0 s^(-1)*mM^(-1), which is exactly that printed cell. The quotient of this row's own printed component cells is 38 / 0.0076 = 5000.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Acetyl-CoA block, enzyme row L117V: Km = 7.6 uM; kcat = 38 s^-1; printed kcat/Km = 5.0 s^-1 uM^-1.

status: verified


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature K63P to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, AZC block, enzyme row K63P; column Km (mM) = 1.6; column kcat (s^-1) = 19; column kcat/Km (s^-1 mM^-1) = 12. captured primary segment: AZC | K63P variant Mpr1 | Km 1.6 mM | kcat 19 s^-1 | kcat/Km 12 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table II AZC block Km cell 1.6 mM; the printed Km column of the AZC block is already in mM, so no unit conversion applies, giving 1.6 mM; the exported value is 1.6 mM. kcat: printed cell 19 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 19.0 s^(-1); the exported value is 19.0 s^(-1). kcat/Km: printed AZC efficiency cell 12 s^-1 mM^-1; the printed efficiency column of the AZC block is already in s^-1 mM^-1, so no unit conversion applies, giving 12.0 s^(-1)*mM^(-1). The exported kcat_over_km 11.875 s^(-1)*mM^(-1) is the exact full-precision quotient of the two printed cells of this same row, and the printed efficiency cell is that quotient written to the precision the column uses. The quotient of this row's own printed component cells is 19 / 1.6 = 11.875 s^-1 mM^-1.

raw_value_unit_evidence: Table II, AZC block, enzyme row K63P: Km = 1.6 mM; kcat = 19 s^-1; printed kcat/Km = 12 s^-1 mM^-1.

row_label: Table II, AZC block, enzyme row K63P


source_db: brenda

kcat_over_km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature K63P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 303.15 K; cofactor CoA

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature L117V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme LK63R/L117V, at pH 8.5 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature K63R/F65L/L117V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K63R/F65L/L117V, at pH 8.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature K63R/F65L/L117V to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, Acetyl-CoA block, enzyme row KFL (K63R/F65L/L117V); column Km (uM) = 4.9; column kcat (s^-1) = 9.1; column kcat/Km (s^-1 uM^-1) = 2.3. captured primary segment: Acetyl-CoA | KFL variant Mpr1 (K63R/F65L/L117V) | Km 4.9 uM | kcat 9.1 s^-1 | kcat/Km 2.3 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 4.9 uM; 1 uM is 1/1000 mM, giving 0.0049 mM; the exported value is 0.0049 mM. kcat: printed cell 9.1 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 9.1 s^(-1); the exported value is 9.1 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 2.3 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 2300.0 s^(-1)*mM^(-1). The exported kcat_over_km is 1857.142857142857 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 9.1 / 0.0049 = 1857.142857142857 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Acetyl-CoA block, enzyme row KFL: Km = 4.9 uM; kcat = 9.1 s^-1; printed kcat/Km = 2.3 s^-1 uM^-1.


verification_status: unverified

mutation_signature: Unknown

sequence_source: UniProtKB E9P8D2 direct REST check

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

status: unverified


enzyme_display_name: arylsulfatase (type I)

organism: Pseudoalteromonas carrageenovora

substrate_name: p-Nitrophenyl sulfate

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

proof_lines: 6.5 nM purified arylsulfatase, at 45°C and pH 7.0

proof_lines: 6.5 nM purified arylsulfatase incubated at 45°C and at pH 7.0 in the presence of 10 mM sulfate

enzyme: arylsulfatase (type I)

substrate: p-Nitrophenyl sulfate


organism: Pseudomonas aeruginosa

substrate_name: 4-nitrophenyl sulfate

proof_lines: mutant enzyme C51A, in 100 mM Tris, pH 8.0, 25°C

substrate: 4-nitrophenyl sulfate


substrate_name: 4-nitrophenyl phosphate

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

proof_lines: wild type enzyme, in 100 mM Tris, pH 8.0, 25°C

substrate: 4-nitrophenyl phosphate


proof_lines: mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25°C


substrate_name: 4-nitrocatechol sulfate

kcat_display: Not reported

proof_lines:
beta enzyme
pH 8.9, 30°C
alpha enzyme

substrate: 4-nitrocatechol sulfate


organism: Rattus norvegicus


organism: Serratia sp. SM1


organism: Sphingomonas sp.


organism: Streptomyces griseorubiginosus

proof_lines:
in absence CaCl2
in presence of 1 mM CaCl2


organism: Strongylocentrotus intermedius

substrate_name: Ascorbate 2-sulfate

substrate: Ascorbate 2-sulfate


organism: Sus scrofa

substrate_name: epinephrine 4-sulfate

proof_lines:
pH 6.9
pH 7.4
arylsulfatase B

substrate: epinephrine 4-sulfate


enzyme_display_name: chitosanase

organism: Renibacterium sp. QD1

substrate_name: chitosan

km_display: Not reported

proof_lines: fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module PfCBM32-2 from Paenibacillus fukuinensis (CsnA-CBM32-2), pH 5.6, 55°C

proof_lines: fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5), pH 5.6, 55°C

proof_lines: fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module AoCBM35 from Amycolatopsis orientalis (CsnA-CBM35), pH 5.6, 55°C

enzyme: chitosanase

substrate: chitosan


enzyme_display_name: thioredoxin-dependent peroxiredoxin

organism: Aeropyrum pernix

sequence_source: UniProtKB:Q9Y9L0 REST lookup, release 2026_02

enzyme: thioredoxin-dependent peroxiredoxin


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Y9L0 canonical sequence with C207S reconstructed during review and applied mutation signature C207S to reconstruct the assayed variant sequence.


organism: Fasciola hepatica

sequence_source: UniProtKB:P91883 REST lookup, release 2026_02


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8

proof_lines: wild type enzyme, in 25 mM Tris-HCl (pH 8)


organism: Salmonella enterica subsp. enterica serovar Typhimurium

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


organism: Seriola lalandi

substrate_name: t-butyl hydroperoxide

sequence_source: UniProtKB:B9USM4 REST lookup, release 2026_02

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication, Prx197

proof_lines: pH 7.0, temperature not specified in the publication, Prx231

substrate: t-butyl hydroperoxide


organism: Synechocystis sp. PCC 6803

substrate_name: thioredoxin Q

sequence_source: UniProtKB:P72719 REST lookup, release 2026_02

proof_lines: pH 7.0, temperature not specified in the publication

substrate: thioredoxin Q


substrate_name: thioredoxin A

sequence_source: UniProtKB:Q55624 REST lookup, release 2026_02

substrate: thioredoxin A


sequence_source: UniProtKB:P72697 REST lookup, release 2026_02


organism: Thunnus maccoyii

substrate_name: thioredoxin

sequence_source: UniProtKB:A9QKS0 REST lookup, release 2026_02

substrate: thioredoxin


organism: Saccharomyces cerevisiae

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, AZC block, enzyme row L117V; column Km (mM) = 1.4; column kcat (s^-1) = 48; column kcat/Km (s^-1 mM^-1) = 33. captured primary segment: AZC | L117V variant Mpr1 | Km 1.4 mM | kcat 48 s^-1 | kcat/Km 33 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table II AZC block Km cell 1.4 mM; the printed Km column of the AZC block is already in mM, so no unit conversion applies, giving 1.4 mM; the exported value is 1.4 mM. kcat: printed cell 48 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 48.0 s^(-1); the exported value is 48.0 s^(-1). kcat/Km: printed AZC efficiency cell 33 s^-1 mM^-1; the printed efficiency column of the AZC block is already in s^-1 mM^-1, so no unit conversion applies, giving 33.0 s^(-1)*mM^(-1). The exported kcat_over_km is 34.285714285714285 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 48 / 1.4 = 34.285714285714285 s^-1 mM^-1.

raw_value_unit_evidence: Table II, AZC block, enzyme row L117V: Km = 1.4 mM; kcat = 48 s^-1; printed kcat/Km = 33 s^-1 mM^-1.

row_label: Table II, AZC block, enzyme row L117V


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature F65L/L117V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F65L/L117V, at pH 8.5 and 30°C


column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, AZC block, enzyme row KFL (K63R/F65L/L117V); column Km (mM) = 1.2; column kcat (s^-1) = 11; column kcat/Km (s^-1 mM^-1) = 9.5. captured primary segment: AZC | KFL variant Mpr1 (K63R/F65L/L117V) | Km 1.2 mM | kcat 11 s^-1 | kcat/Km 9.5 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table II AZC block Km cell 1.2 mM; the printed Km column of the AZC block is already in mM, so no unit conversion applies, giving 1.2 mM; the exported value is 1.2 mM. kcat: printed cell 11 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 11.0 s^(-1); the exported value is 11.0 s^(-1). kcat/Km: printed AZC efficiency cell 9.5 s^-1 mM^-1; the printed efficiency column of the AZC block is already in s^-1 mM^-1, so no unit conversion applies, giving 9.5 s^(-1)*mM^(-1). The exported kcat_over_km is 9.166666666666668 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 11 / 1.2 = 9.166666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table II, AZC block, enzyme row KFL: Km = 1.2 mM; kcat = 11 s^-1; printed kcat/Km = 9.5 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature K63R to reconstruct the assayed variant sequence.


column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, AZC block, enzyme row KF (K63R/F65L); column Km (mM) = 2.2; column kcat (s^-1) = 51; column kcat/Km (s^-1 mM^-1) = 23. captured primary segment: AZC | KF variant Mpr1 (K63R/F65L) | Km 2.2 mM | kcat 51 s^-1 | kcat/Km 23 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table II AZC block Km cell 2.2 mM; the printed Km column of the AZC block is already in mM, so no unit conversion applies, giving 2.2 mM; the exported value is 2.2 mM. kcat: printed cell 51 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 51.0 s^(-1); the exported value is 51.0 s^(-1). kcat/Km: printed AZC efficiency cell 23 s^-1 mM^-1; the printed efficiency column of the AZC block is already in s^-1 mM^-1, so no unit conversion applies, giving 23.0 s^(-1)*mM^(-1). The exported kcat_over_km 23.18181818181818 s^(-1)*mM^(-1) is the exact full-precision quotient of the two printed cells of this same row, and the printed efficiency cell is that quotient written to the precision the column uses. The quotient of this row's own printed component cells is 51 / 2.2 = 23.181818181818183 s^-1 mM^-1.

raw_value_unit_evidence: Table II, AZC block, enzyme row KF: Km = 2.2 mM; kcat = 51 s^-1; printed kcat/Km = 23 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature F65G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature K63R/L117V to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, Acetyl-CoA block, enzyme row KL (K63R/L117V); column Km (uM) = 11; column kcat (s^-1) = 38; column kcat/Km (s^-1 uM^-1) = 3.7. captured primary segment: Acetyl-CoA | KL variant Mpr1 (K63R/L117V) | Km 11 uM | kcat 38 s^-1 | kcat/Km 3.7 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 11 uM; 1 uM is 1/1000 mM, giving 0.011 mM; the exported value is 0.011 mM. kcat: printed cell 38 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 38.0 s^(-1); the exported value is 38.0 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 3.7 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 3700.0 s^(-1)*mM^(-1). The exported kcat_over_km is 3454.545454545455 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 38 / 0.011 = 3454.5454545454545 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Acetyl-CoA block, enzyme row KL: Km = 11 uM; kcat = 38 s^-1; printed kcat/Km = 3.7 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature F65G to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, AZC block, enzyme row F65G; column Km (mM) = 3.3; column kcat (s^-1) = 16; column kcat/Km (s^-1 mM^-1) = 4.7. captured primary segment: AZC | F65G variant Mpr1 | Km 3.3 mM | kcat 16 s^-1 | kcat/Km 4.7 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table II AZC block Km cell 3.3 mM; the printed Km column of the AZC block is already in mM, so no unit conversion applies, giving 3.3 mM; the exported value is 3.3 mM. kcat: printed cell 16 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 16.0 s^(-1); the exported value is 16.0 s^(-1). kcat/Km: printed AZC efficiency cell 4.7 s^-1 mM^-1; the printed efficiency column of the AZC block is already in s^-1 mM^-1, so no unit conversion applies, giving 4.7 s^(-1)*mM^(-1). The exported kcat_over_km is 4.848484848484849 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 16 / 3.3 = 4.848484848484849 s^-1 mM^-1.

raw_value_unit_evidence: Table II, AZC block, enzyme row F65G: Km = 3.3 mM; kcat = 16 s^-1; printed kcat/Km = 4.7 s^-1 mM^-1.

row_label: Table II, AZC block, enzyme row F65G


sequence_source: UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature F65L to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 10 uM; 1 uM is 1/1000 mM, giving 0.01 mM; the exported value is 0.01 mM. kcat: printed cell 31 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 31.0 s^(-1); the exported value is 31.0 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 2.9 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 2900.0 s^(-1)*mM^(-1). The live export row carries no kcat_over_km field, so this record exports none. The quotient of this row's own printed component cells is 31 / 0.01 = 3100.0 s^-1 mM^-1.

row_label: Table II, Acetyl-CoA block, enzyme row F65L

table_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature K63R to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, AZC block, enzyme row K63R; column Km (mM) = 1.2; column kcat (s^-1) = 31; column kcat/Km (s^-1 mM^-1) = 25. captured primary segment: AZC | K63R variant Mpr1 | Km 1.2 mM | kcat 31 s^-1 | kcat/Km 25 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table II AZC block Km cell 1.2 mM; the printed Km column of the AZC block is already in mM, so no unit conversion applies, giving 1.2 mM; the exported value is 1.2 mM. kcat: printed cell 31 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 31.0 s^(-1); the exported value is 31.0 s^(-1). kcat/Km: printed AZC efficiency cell 25 s^-1 mM^-1; the printed efficiency column of the AZC block is already in s^-1 mM^-1, so no unit conversion applies, giving 25.0 s^(-1)*mM^(-1). The exported kcat_over_km is 25.833333333333336 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 31 / 1.2 = 25.833333333333332 s^-1 mM^-1.

raw_value_unit_evidence: Table II, AZC block, enzyme row K63R: Km = 1.2 mM; kcat = 31 s^-1; printed kcat/Km = 25 s^-1 mM^-1.

row_label: Table II, AZC block, enzyme row K63R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E9P8D2 and applied mutation signature F65L/L117V to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, AZC block, enzyme row FL (F65L/L117V); column Km (mM) = 1.8; column kcat (s^-1) = 38; column kcat/Km (s^-1 mM^-1) = 21. captured primary segment: AZC | FL variant Mpr1 (F65L/L117V) | Km 1.8 mM | kcat 38 s^-1 | kcat/Km 21 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table II AZC block Km cell 1.8 mM; the printed Km column of the AZC block is already in mM, so no unit conversion applies, giving 1.8 mM; the exported value is 1.8 mM. kcat: printed cell 38 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 38.0 s^(-1); the exported value is 38.0 s^(-1). kcat/Km: printed AZC efficiency cell 21 s^-1 mM^-1; the printed efficiency column of the AZC block is already in s^-1 mM^-1, so no unit conversion applies, giving 21.0 s^(-1)*mM^(-1). The exported kcat_over_km 21.11111111111111 s^(-1)*mM^(-1) is the exact full-precision quotient of the two printed cells of this same row, and the printed efficiency cell is that quotient written to the precision the column uses. The quotient of this row's own printed component cells is 38 / 1.8 = 21.11111111111111 s^-1 mM^-1.

raw_value_unit_evidence: Table II, AZC block, enzyme row FL: Km = 1.8 mM; kcat = 38 s^-1; printed kcat/Km = 21 s^-1 mM^-1.


column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, Acetyl-CoA block, enzyme row K63R; column Km (uM) = 8.0; column kcat (s^-1) = 27; column kcat/Km (s^-1 uM^-1) = 3.3. captured primary segment: Acetyl-CoA | K63R variant Mpr1 | Km 8.0 uM | kcat 27 s^-1 | kcat/Km 3.3 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table II Acetyl-CoA block Km cell 8.0 uM; 1 uM is 1/1000 mM, giving 0.008 mM; the exported value is 0.008 mM. kcat: printed cell 27 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 27.0 s^(-1); the exported value is 27.0 s^(-1). kcat/Km: printed Acetyl-CoA efficiency cell 3.3 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, giving 3300.0 s^(-1)*mM^(-1). The exported kcat_over_km is 3375.0 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 27 / 0.008 = 3375.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Acetyl-CoA block, enzyme row K63R: Km = 8.0 uM; kcat = 27 s^-1; printed kcat/Km = 3.3 s^-1 uM^-1.


column_label: Table II: Kinetic constants and thermal stability of the wild-type and variant Mpr1 proteins (Biotechnology and Bioengineering 2009, volume 103, number 2, pages 341-352); printed column heads Enzyme, then the AZC block km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1), then the Acetyl-CoA block Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1), then Half-life at 50 C (min). Table II, AZC block, enzyme row F65L; column Km (mM) = 0.70; column kcat (s^-1) = 31; column kcat/Km (s^-1 mM^-1) = 46. captured primary segment: AZC | F65L variant Mpr1 | Km 0.70 mM | kcat 31 s^-1 | kcat/Km 46 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table II AZC block Km cell 0.70 mM; the printed Km column of the AZC block is already in mM, so no unit conversion applies, giving 0.7 mM; the exported value is 0.7 mM. kcat: printed cell 31 s^-1; the printed turnover column is already per second, so no unit conversion applies, giving 31.0 s^(-1); the exported value is 31.0 s^(-1). kcat/Km: printed AZC efficiency cell 46 s^-1 mM^-1; the printed efficiency column of the AZC block is already in s^-1 mM^-1, so no unit conversion applies, giving 46.0 s^(-1)*mM^(-1). The exported kcat_over_km is 44.28571428571429 s^(-1)*mM^(-1), which is that quotient of the row's own kcat and Km; this record writes the article's printed efficiency cell in its place. The quotient of this row's own printed component cells is 31 / 0.7 = 44.285714285714285 s^-1 mM^-1.

raw_value_unit_evidence: Table II, AZC block, enzyme row F65L: Km = 0.70 mM; kcat = 31 s^-1; printed kcat/Km = 46 s^-1 mM^-1.

row_label: Table II, AZC block, enzyme row F65L


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature K63R/F65L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K63R/F65L, at pH 8.5 and 30°C


organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

source_db: uniprot

smiles: OO

source: uniprot


enzyme_display_name: uracil-DNA glycosylase

organism: Gadus morhua

substrate_name: uracil-containing calf thymus DNA

proof_lines:
mutant enzyme G183D, at pH 7.5 and 15°C
mutant enzyme G183D, at pH 7.5 and 22°C
mutant enzyme G183D, at pH 7.5 and 37°C

enzyme: uracil-DNA glycosylase

substrate: uracil-containing calf thymus DNA


organism: Homo sapiens

substrate_name: uracil-mismatched double-stranded DNA with U-G mismatch

proof_lines:
pH 7.5, 30°C, recombinant hUNG2
pH 7.5


organism: Orthopoxvirus vaccinia

substrate_name: uracil-mismatched single-stranded DNA

substrate: uracil-mismatched single-stranded DNA


organism: Xenopus laevis


enzyme_display_name: acylaminoacyl-peptidase

organism: Cucumis sativus

substrate_name: N-acetyl-Ala-p-nitroanilide

enzyme: acylaminoacyl-peptidase

substrate: N-acetyl-Ala-p-nitroanilide


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


organism: Oryctolagus cuniculus

substrate_name: N-acetyl-Ala-Ala-Arg-Gly

substrate: N-acetyl-Ala-Ala-Arg-Gly


organism: Pyrococcus horikoshii

proof_lines:
pH 5.4, 85°C
pH 5.4, 85°C, heat-activated enzyme


organism: Rattus norvegicus

substrate_name: formylmethionine-Leu

substrate: formylmethionine-Leu


organism: Saccharolobus solfataricus

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Streptomyces morookaense

substrate_name: Phe-beta-naphthylamide

substrate: Phe-beta-naphthylamide


organism: Sus scrofa


organism: Cereibacter sphaeroides

proof_lines: PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25°C

proof_lines: PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25°C


proof_lines:
pH 7.0, 37°C
Escherichia coli thioredoxin, at 25°C
Km below 0.0007 mM, at 25°C and pH 7.4


organism: Lathyrus oleraceus


organism: Leishmania infantum

substrate_name: tryparedoxin 2

substrate: tryparedoxin 2


organism: Mycobacterium tuberculosis variant bovis


organism: Plasmodium falciparum


organism: Toxoplasma gondii


organism: Saccharomyces cerevisiae

substrate_name: L-azetidine-2-carboxylic acid

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

substrate: L-azetidine-2-carboxylic acid


organism: Gadus morhua

proof_lines: mutant enzyme G183D/R302K, at pH 7.5 and 15°C

proof_lines: mutant enzyme G183D/R302K, at pH 7.5 and 22°C

proof_lines: mutant enzyme G183D/R302K, at pH 7.5 and 37°C


substrate_name: N-acetyl-Met-Ala

proof_lines:
wild-type enzyme
recombinant wild-type enzyme

substrate: N-acetyl-Met-Ala


organism: synthetic construct


organism: Trematomus bernacchii

proof_lines:
50°C, pH 8
15°C, pH 8


enzyme_display_name: aqualysin 1

organism: Thermus aquaticus

enzyme: aqualysin 1


proof_lines:
pH 7.5, 40°C, wild-type
40°C pH 7.5, wild-type
wild type enzyme, 40°C, pH 7.5


proof_lines:
pH 7.4, 40°C
pH 7.5, 40°C
pH 7.5, 40°C, presence of DMSO


enzyme_display_name: histone deacetylase

organism: Homo sapiens

substrate_name: Fluor de Lys HDAC8 substrate

proof_lines: presence of activator N-(phenylcarbamothioyl)benzamide, pH not specified in the publication, temperature not specified in the publication

enzyme: histone deacetylase

substrate: Fluor de Lys HDAC8 substrate


organism: Mus musculus

substrate_name: H2O; Acetylhistone

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

proof_lines: SABIO-RK modifier species: histone deacetylase(Enzyme) mutant

substrate: H2O; Acetylhistone


enzyme_display_name: cytidine deaminase

organism: Arabidopsis thaliana

substrate_name: deoxycytidine

proof_lines:
recombinant At-CDA1
recombinant AT-CDA
recombinant

enzyme: cytidine deaminase

substrate: deoxycytidine


organism: Brassica oleracea

substrate_name: cytosine beta-D-arabinofuranoside

substrate: cytosine beta-D-arabinofuranoside


organism: Canis lupus familiaris


organism: Crithidia fasciculata


organism: Escherichia coli

proof_lines: at pH 7.5 with H2O and pH 8.4 with H2O or D2O


substrate_name: cytidine

substrate: cytidine


sequence_source: UniProtKB reviewed accession E9P8D2 / MPR1_YEASX direct REST and FASTA lookup


proof_lines: tetramer of recombinant subunit CDA2, 37°C


substrate_name: cytosine arabinoside

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

substrate: cytosine arabinoside


proof_lines:
normal and leukemic spleen enzyme
leukemic spleen enzyme


organism: Nocardioides sp.

substrate_name: CMP

substrate: CMP


organism: Trypanosoma cruzi


enzyme_display_name: aliphatic nitrilase

organism: Cupriavidus necator

enzyme: aliphatic nitrilase


organism: Pannonibacter carbonis


organism: Pseudomonas sp.

substrate_name: potassium cyanide

substrate: potassium cyanide


organism: Pyrococcus abyssi

substrate_name: Malononitrile

proof_lines: in 20 mM potassium phosphate, pH 7.4, with 1 mM dithiothreitol, at 80°C

substrate: Malononitrile


organism: Rhodococcus rhodochrous

substrate_name: adiponitrile

substrate: adiponitrile


substrate_name: glutaronitrile

substrate: glutaronitrile


substrate_name: Crotonitrile

substrate: Crotonitrile


enzyme_display_name: low-specificity L-threonine aldolase

organism: Aeromonas veronii

substrate_name: D-threonine

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: low-specificity L-threonine aldolase

substrate: D-threonine


substrate_name: L-threonine

substrate: L-threonine


substrate_name: L-allo-threonine

sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature H83N to reconstruct the assayed variant sequence.

substrate: L-allo-threonine


sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature H83F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature H83F/H126F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature K222A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature F87A to reconstruct the assayed variant sequence.


organism: Streptomyces coelicolor

substrate_name: L-Thr

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

assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl

proof_lines: mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)

substrate: L-Thr


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

proof_lines: recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)


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

proof_lines: kcat is 4.5 sec(-1) for H(2)O(2). kcat is 2.75 sec(-1) for thioredoxin.


organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

proof_lines: kcat is 12.53 sec(-1) with H(2)O(2) as substrate and 12.96 sec(-1) with tert-butyl hydroperoxide as substrate.


organism: Chlamydomonas reinhardtii

proof_lines: kcat is 7.4 sec(-1) for the reduction of hydrogen peroxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) (PubMed:19690965). kcat is 7.4 sec(-1) for the reduction of tert-butyl hydroperoxide (with cytosolic thioredoxin) (at


organism: Escherichia coli (strain K12)

proof_lines: kcat is 76.0 sec(-1) with H(2)O(2) as substrate and 70.1 sec(-1) with cumene hydroperoxide as substrate.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: tert-butyl hydroperoxide (using thioredoxin TrxB as electron donor)

proof_lines: kcat is 0.70 sec(-1) with tert-butyl hydroperoxide as substrate and TrxB as reductant and 11.1 sec(-1) with tert-butyl hydroperoxide as substrate and TrxC as reductant.


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: H(2)O(2) (in the presence of 5 mM DTT)

proof_lines: kcat is 67 min(-1) with H(2)O(2) as substrate (PubMed:11231293). kcat is 56 min(-1) with t-butylhydroperoxide as substrate (PubMed:11231293). kcat is 41 min(-1) with cumene hydroperoxide as substrate (PubMed:11231293).

substrate: H(2)O(2) (in the presence of 5 mM DTT)


substrate_name: H(2)O(2) (in the presence of TRX1)

proof_lines: kcat is 7.5 sec(-1) with H(2)O(2) as substrate (in the presence of TRX1) (PubMed:16879648). kcat is 15.0 sec(-1) with H(2)O(2) as substrate (in the presence of TRX2) (PubMed:16879648). kcat is 8.3 sec(-1) with ert-butylhydroperoxide as subs

substrate: H(2)O(2) (in the presence of TRX1)


organism: Saccharomyces cerevisiae

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 17.9 sec(-1) with azetidine-2-carboxylate as substrate and 121 sec(-1) with (S)-1-pyrroline-5-carboxylate as substrate.


enzyme_display_name: ornithine decarboxylase

organism: Aquifex aeolicus

substrate_name: L-Ornithine

sequence_source: UniProt O66940 canonical sequence from direct accession lookup

enzyme: ornithine decarboxylase

substrate: L-Ornithine


organism: Atropa belladonna

substrate_name: L-ornithine

sequence_source: UniProt A0A060IEJ3 canonical sequence from direct accession lookup

substrate: L-ornithine


organism: Bartonella henselae

sequence_source: UniProt A0A0R4J8C9 canonical sequence from direct accession lookup


organism: Caldisericum exile

substrate_name: L-arginine

substrate: L-arginine


organism: Clostridium botulinum


organism: Erythroxylum coca

sequence_source: UniProt G4XUJ8 canonical sequence from direct accession lookup


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature I163A reconstructed and applied mutation signature I163A to reconstruct the assayed variant sequence.

proof_lines: mutant I163A, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature I163V reconstructed and applied mutation signature I163V to reconstruct the assayed variant sequence.

proof_lines: mutant I163V, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature E165V reconstructed and applied mutation signature E165V to reconstruct the assayed variant sequence.

proof_lines: mutant E165V, pH 7.0, temperature not specified in the publication


sequence_source: UniProt P21169 canonical sequence from direct accession lookup

proof_lines: wild-type, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature I163T/E165T reconstructed and applied mutation signature I163T/E165T to reconstruct the assayed variant sequence.

proof_lines: mutant I163T/E165T, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature E165S reconstructed and applied mutation signature E165S to reconstruct the assayed variant sequence.

proof_lines: mutant E165S, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature E165G reconstructed and applied mutation signature E165G to reconstruct the assayed variant sequence.

proof_lines: mutant E165G, pH 7.0, temperature not specified in the publication


organism: Nicotiana glutinosa

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup for Q9FPK5 and applied mutation signature K95A to reconstruct the assayed variant sequence.


substrate_name: L-Lysine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9FPK5 and applied mutation signature C338A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; 310.15 K; buffer 40 mM potassium phosphate

column_label: Table 2(B) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'C338A'; column 'Km (uM)' = 1114; column 'Vmax (nmol/min per mg)' = 0.150; column 'kcat (s^-1)' = 0.204; column 'kcat/Km (M^-1 s^-1)' = 183.21; column 'Optimal pH' = 7.6.

normalized_value_unit_evidence: Km: printed Table 2(B) cell 1114 uM; 1114 / 1000 = 1.114 mM. kcat: printed Table 2(B) cell 0.204 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(B) cell 183.21 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 183.21 / 1000 = 0.18321 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(B), enzyme row 'C338A', L-Lysine as the varied substrate: Km = 1114 uM; kcat = 0.204 s^-1; printed kcat/Km = 183.21 M^-1 s^-1.

substrate: L-Lysine


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup for Q9FPK5 and applied mutation signature C377A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB direct accession lookup for Q9FPK5

assay_conditions_summary: pH 8; 310.15 K; buffer 40 mM Tris/HCl

column_label: Table 2(A) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'WT'; column 'Km (uM)' = 562; column 'Vmax (nmol/min per mg)' = 12.54; column 'kcat (s^-1)' = 77.78; column 'kcat/Km (M^-1 s^-1)' = 1.5 x 10^5; column 'Optimal pH' = 8.0.

normalized_value_unit_evidence: Km: printed Table 2(A) cell 562 uM; 562 / 1000 = 0.562 mM. kcat: printed Table 2(A) cell 77.78 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(A) cell 1.5 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 150000 / 1000 = 150.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(A), enzyme row 'WT', L-Ornithine as the varied substrate: Km = 562 uM; kcat = 77.78 s^-1; printed kcat/Km = 1.5 x 10^5 M^-1 s^-1.

row_label: Table 2(A), enzyme row 'WT' (wild type), L-Ornithine as the varied substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup for Q9FPK5 and applied mutation signature C338A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant C338A


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


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant C377A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9FPK5 and applied mutation signature C96A to reconstruct the assayed variant sequence.

column_label: Table 2(A) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'C96A'; column 'Km (uM)' = 812; column 'Vmax (nmol/min per mg)' = 11.22; column 'kcat (s^-1)' = 32.73; column 'kcat/Km (M^-1 s^-1)' = 4.1 x 10^4; column 'Optimal pH' = 8.6.

normalized_value_unit_evidence: Km: printed Table 2(A) cell 812 uM; 812 / 1000 = 0.812 mM. kcat: printed Table 2(A) cell 32.73 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(A) cell 4.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 41000 / 1000 = 41.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(A), enzyme row 'C96A', L-Ornithine as the varied substrate: Km = 812 uM; kcat = 32.73 s^-1; printed kcat/Km = 4.1 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup for Q9FPK5 and applied mutation signature C115A to reconstruct the assayed variant sequence.


organism: Nitrosomonas europaea

sequence_source: UniProtKB direct accession lookup for Q82VZ0


organism: Oenococcus oeni

sequence_source: UniProtKB direct accession lookup for Q5ZH57

column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'O. oeni' and 'Reaction pH' = '5.5'; within the 'Ornithine' substrate block the column 'kcat (min^-1)' = 416, the column 'Km (mM)' = 0.7 and the column 'kcat/Km (M^-1 min^-1)' = 5.5 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 416 min^-1; one min^-1 is 1/60 s^-1, so 416 / 60 = 6.933333333333334 s^(-1). Km: printed Table 1 cell 0.7 mM; no unit conversion applies, so the canonical value is 0.7 mM. kcat/Km: printed Table 1 cell 5.5 x 10^5 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 550000 / 60000 = 9.166666666666668 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, 'Ornithine' substrate block: printed kcat cell 416 min^-1; printed Km cell 0.7 mM; printed kcat/Km cell 5.5 x 10^5 M^-1 min^-1.

row_label: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, Ornithine substrate block


column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'O. oeni' and 'Reaction pH' = '5.5'; within the 'DABA' substrate block the column 'kcat (min^-1)' = 2.7, the column 'Km (mM)' = 4.9 and the column 'kcat/Km (M^-1 min^-1)' = 0.5 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.7 min^-1; one min^-1 is 1/60 s^-1, so 2.7 / 60 = 0.045000000000000005 s^(-1). Km: printed Table 1 cell 4.9 mM; no unit conversion applies, so the canonical value is 4.9 mM. kcat/Km: printed Table 1 cell 0.5 x 10^3 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 500 / 60000 = 0.008333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, 'DABA' substrate block: printed kcat cell 2.7 min^-1; printed Km cell 4.9 mM; printed kcat/Km cell 0.5 x 10^3 M^-1 min^-1.

row_label: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, DABA substrate block


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature E165A and applied mutation signature E165A to reconstruct the assayed variant sequence.

proof_lines: mutant E165A, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature I163S and applied mutation signature I163S to reconstruct the assayed variant sequence.

proof_lines: mutant I163S, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature I163T and applied mutation signature I163T to reconstruct the assayed variant sequence.

proof_lines: mutant I163T, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature I163V/E165V and applied mutation signature I163V/E165V to reconstruct the assayed variant sequence.

proof_lines: mutant I163V/E165V, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature E165T and applied mutation signature E165T to reconstruct the assayed variant sequence.

proof_lines: mutant E165T, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature I163G and applied mutation signature I163G to reconstruct the assayed variant sequence.

proof_lines: mutant I163G, pH 7.0, temperature not specified in the publication


organism: Giardia lamblia

sequence_source: UniProtKB:A8BFD3 REST lookup

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


organism: Homo sapiens

sequence_source: UniProtKB:P11926 REST lookup


organism: Hyoscyamus niger

sequence_source: UniProtKB:A0A4D6ZW66 REST lookup

proof_lines: pH 8.0, temperature not specified in the publication


organism: Lacticaseibacillus casei

sequence_source: UniProtKB:Q038E5 REST lookup


column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'L. casei' and 'Reaction pH' = '7.5'; within the 'DABA' substrate block the column 'kcat (min^-1)' = 3, the column 'Km (mM)' = 3.9 and the column 'kcat/Km (M^-1 min^-1)' = 0.7 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3 min^-1; one min^-1 is 1/60 s^-1, so 3 / 60 = 0.05 s^(-1). Km: printed Table 1 cell 3.9 mM; no unit conversion applies, so the canonical value is 3.9 mM. kcat/Km: printed Table 1 cell 0.7 x 10^3 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 700 / 60000 = 0.011666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'L. casei' at Reaction pH 7.5, 'DABA' substrate block: printed kcat cell 3 min^-1; printed Km cell 3.9 mM; printed kcat/Km cell 0.7 x 10^3 M^-1 min^-1.

row_label: Table 1, Microorganism row 'L. casei' at Reaction pH 7.5, DABA substrate block


organism: Lactobacillus gasseri

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


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


organism: Lactobacillus sp.

sequence_source: UniProtKB:P43099 REST lookup


organism: Lactobacillus sp. 30a

substrate_name: L-lysine

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P43099|reviewed_swiss_prot|direct_rest_lookup_run_20260616-233539 and applied mutation signature E698D/A713L to reconstruct the assayed variant sequence.

substrate: L-lysine


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P43099|reviewed_swiss_prot|direct_rest_lookup_run_20260616-233539 and applied mutation signature E698D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P43099|reviewed_swiss_prot|direct_rest_lookup_run_20260616-233539 and applied mutation signature A713L to reconstruct the assayed variant sequence.


organism: Leishmania donovani


substrate_name: L-Arginine

substrate: L-Arginine


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P27116|reviewed_swiss_prot|direct_rest_lookup_run_20260616-233539 and applied mutation signature K69A/C360A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant K69A:C360A heterodimer N-terminal His6-tagged


organism: Levilactobacillus brevis

column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'L. brevis' and 'Reaction pH' = '5.5'; within the 'Ornithine' substrate block the column 'kcat (min^-1)' = 290, the column 'Km (mM)' = 1.0 and the column 'kcat/Km (M^-1 min^-1)' = 2.8 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 290 min^-1; one min^-1 is 1/60 s^-1, so 290 / 60 = 4.833333333333333 s^(-1). Km: printed Table 1 cell 1.0 mM; no unit conversion applies, so the canonical value is 1.0 mM. kcat/Km: printed Table 1 cell 2.8 x 10^5 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 280000 / 60000 = 4.666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'L. brevis' at Reaction pH 5.5, 'Ornithine' substrate block: printed kcat cell 290 min^-1; printed Km cell 1.0 mM; printed kcat/Km cell 2.8 x 10^5 M^-1 min^-1.

row_label: Table 1, Microorganism row 'L. brevis' at Reaction pH 5.5, Ornithine substrate block


column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'L. brevis' and 'Reaction pH' = '5.5'; within the 'L-Lysine' substrate block the column 'kcat (min^-1)' = 34, the column 'Km (mM)' = 7.2 and the column 'kcat/Km (M^-1 min^-1)' = 4.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 34 min^-1; one min^-1 is 1/60 s^-1, so 34 / 60 = 0.5666666666666667 s^(-1). Km: printed Table 1 cell 7.2 mM; no unit conversion applies, so the canonical value is 7.2 mM. kcat/Km: printed Table 1 cell 4.6 x 10^3 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 4600 / 60000 = 0.07666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'L. brevis' at Reaction pH 5.5, 'L-Lysine' substrate block: printed kcat cell 34 min^-1; printed Km cell 7.2 mM; printed kcat/Km cell 4.6 x 10^3 M^-1 min^-1.

row_label: Table 1, Microorganism row 'L. brevis' at Reaction pH 5.5, L-Lysine substrate block


organism: Ligilactobacillus saerimneri 30a


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

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

proof_lines:
pH 5.5, 37°C
Raw SKiD Env: Temp=37°C, pH=5.5

source_databases_merged: brenda skid


organism: Methanosarcina mazei


organism: Mus musculus


sequence_source: Reconstructed from UniProtKB:P00860

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P00860 and applied mutation signature K69A/C360A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant mouse-K69A:trypanosoma-C360A heterodimer N-terminal His6-tagged


organism: Neurospora crassa


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9FPK5 and applied mutation signature C96A to reconstruct the assayed variant sequence.

column_label: Table 2(B) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'C96A'; column 'Km (uM)' = 1094; column 'Vmax (nmol/min per mg)' = 0.133; column 'kcat (s^-1)' = 0.207; column 'kcat/Km (M^-1 s^-1)' = 188.83; column 'Optimal pH' = 6.8.

normalized_value_unit_evidence: Km: printed Table 2(B) cell 1094 uM; 1094 / 1000 = 1.094 mM. kcat: printed Table 2(B) cell 0.207 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(B) cell 188.83 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 188.83 / 1000 = 0.18883 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(B), enzyme row 'C96A', L-Lysine as the varied substrate: Km = 1094 uM; kcat = 0.207 s^-1; printed kcat/Km = 188.83 M^-1 s^-1.


sequence_source: Reconstructed from UniProtKB:Q9FPK5

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q9FPK5 and applied mutation signature C96A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant C96A


column_label: Table 2(B) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'WT'; column 'Km (uM)' = 1592; column 'Vmax (nmol/min per mg)' = 0.152; column 'kcat (s^-1)' = 0.236; column 'kcat/Km (M^-1 s^-1)' = 148.00; column 'Optimal pH' = 6.8.

normalized_value_unit_evidence: Km: printed Table 2(B) cell 1592 uM; 1592 / 1000 = 1.592 mM. kcat: printed Table 2(B) cell 0.236 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(B) cell 148.00 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 148 / 1000 = 0.148 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(B), enzyme row 'WT', L-Lysine as the varied substrate: Km = 1592 uM; kcat = 0.236 s^-1; printed kcat/Km = 148.00 M^-1 s^-1.

row_label: Table 2(B), enzyme row 'WT' (wild type), L-Lysine as the varied substrate


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q9FPK5 and applied mutation signature K95A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant K95A


enzyme_display_name: 4-hydroxybenzoate 3-monooxygenase

organism: Cupriavidus pinatubonensis

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

enzyme: 4-hydroxybenzoate 3-monooxygenase

substrate: NADPH


proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHCn2, via UV/VIS-NAD(P)H consumption determination, with NADPH

proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHCn2, via product determination per HPLC, with NADPH


organism: Pseudomonas aeruginosa

sequence_variant_note: Resolved canonical sequence from UniProtKB:P20586 canonical FASTA with L199V and Y385F substitutions applied after residue check and applied mutation signature L199V/Y385F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P20586 canonical FASTA direct lookup


proof_lines: pH 8.0, 30°C, wild-type enzyme, with NADPH


sequence_source: UniProtKB:P20586 canonical FASTA with L199V and Y385F substitutions applied after residue check


sequence_source: UniProtKB:P20586 canonical FASTA used only as context; row-specific DA015/DA016 variant was not reconstructable from the selected batch

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines:
pH 8.0, 30°C, mutant DA015, with NADPH
pH 8.0, 30°C, mutant DA016, with NADPH


source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=30°C, pH=7.5

source: skid


enzyme_display_name: dextransucrase

organism: Lactobacillus hilgardii

substrate_name: Sucrose; Dextran

sequence_source: UniProtKB:E1UYR9 FASTA direct lookup

enzyme: dextransucrase

substrate: Sucrose; Dextran


organism: Leuconostoc citreum

sequence_source: UniProtKB:D5FS20 FASTA direct lookup

proof_lines: recombinant enzyme, pH 5.0, 30°C, in presence of Ca2+


organism: Leuconostoc lactis

substrate_name: sucrose

substrate: sucrose


organism: Leuconostoc mesenteroides


organism: Oenococcus oeni

sequence_source: UniProtKB direct accession lookup: Q5ZH57

column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'O. oeni' and 'Reaction pH' = '5.5'; within the 'L-Lysine' substrate block the column 'kcat (min^-1)' = 5.6, the column 'Km (mM)' = 5.0 and the column 'kcat/Km (M^-1 min^-1)' = 1.1 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.6 min^-1; one min^-1 is 1/60 s^-1, so 5.6 / 60 = 0.09333333333333332 s^(-1). Km: printed Table 1 cell 5.0 mM; no unit conversion applies, so the canonical value is 5.0 mM. kcat/Km: printed Table 1 cell 1.1 x 10^3 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 1100 / 60000 = 0.018333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, 'L-Lysine' substrate block: printed kcat cell 5.6 min^-1; printed Km cell 5.0 mM; printed kcat/Km cell 1.1 x 10^3 M^-1 min^-1.

row_label: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, L-Lysine substrate block


organism: Panagrellus redivivus

sequence_source: UniProtKB direct accession lookup: P49725


organism: Paramecium bursaria chlorella virus 1

sequence_source: UniProtKB direct accession lookup: Q84527


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup: Q84527 and applied mutation signature E296D to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant His-tagged E296D


sequence_source: UniProtKB direct accession lookup: Q9HVQ3


organism: Rattus norvegicus

sequence_source: UniProtKB direct accession lookup: P09057


organism: Selenomonas ruminantium

sequence_source: UniProtKB direct accession lookup: O50657


organism: Thermotoga maritima

sequence_source: UniProtKB direct accession lookup: Q9X2I6


organism: Trypanosoma brucei

sequence_source: UniProtKB direct accession lookup: P07805


proof_lines: pH 5.2, 25°C, recombinant mutant H463R/T464V/S512T


proof_lines: pH 5.2, 25°C, recombinant mutant H463R/T464D/S512T


proof_lines: pH 5.2, 25°C, recombinant mutant D460A/H463S/T464L


proof_lines: pH 5.2, 25°C, recombinant mutant D460M/H463Y/T464M/S512C


sequence_source: UniProtKB Q2I2N5 direct lookup

proof_lines: recombinant wild-type enzyme dexYG, pH 5.4, 25°C


proof_lines: recombinant enzyme variant D-F, pH 5.4, 25°C


mutation_type: deletion

proof_lines: recombinant enzyme mutant DELTAN190LmDexA, pH 5.6, 30°C


substrate_name: Dextran

sequence: DSTNY

wild_type_sequence: DSTNY

sequence_source: UniProtKB direct accession lookup P85089 (https://rest.uniprot.org/uniprotkb/P85089.json)

proof_lines: pH 5.5, 45°C, isozyme DS-II, low dextran substrate concentration

proof_lines: pH 5.5, 45°C, isozyme DS-II, high dextran substrate concentration

substrate: Dextran


sequence: DSTNTV

wild_type_sequence: DSTNTV

sequence_source: UniProtKB direct accession lookup P85080 (https://rest.uniprot.org/uniprotkb/P85080.json)

proof_lines: pH 5.5, 45°C, isozyme DS-III, low dextran substrate concentration

proof_lines: pH 5.5, 45°C, isozyme DS-III, high dextran substrate concentration


sequence_source: UniProtKB direct accession lookup B2MUU6 (https://rest.uniprot.org/uniprotkb/B2MUU6.json)

proof_lines: pH 5.5, 45°C, isozyme DS-I, low dextran substrate concentration

proof_lines: pH 5.5, 45°C, isozyme DS-I, high dextran substrate concentration


organism: Streptococcus mutans


substrate_name: Dextran; Sucrose

substrate: Dextran; Sucrose


organism: Weissella cibaria

sequence_source: UniProtKB direct accession lookup B9UNL6 (https://rest.uniprot.org/uniprotkb/B9UNL6.json)


organism: Weissella confusa


sequence_source: UniProtKB direct accession lookup X4QKX0 (https://rest.uniprot.org/uniprotkb/X4QKX0.json)

proof_lines:
pH 5.4, 35°C, recombinant enzyme
pH 5.0, 35°C


enzyme_display_name: phospholipase A2

organism: Clonorchis sinensis

substrate_name: phosphatidylcholine

sequence_source: UniProtKB direct accession lookup C6YBD6 (https://rest.uniprot.org/uniprotkb/C6YBD6.json)

assay_conditions_summary: pH 8.5; 313.15 K; buffer 100 mM Tris-HCl

proof_lines: recombinant group III sPLA2, in 100 mM Tris-HCl buffer, pH 8.5, at 40°C, 50 mM sodium bis(2-ethylhexyl) sulfosuccinate and 0.05mM phenolsulfonphthalein in isooctane

enzyme: phospholipase A2

substrate: phosphatidylcholine


organism: Crotalus durissus terrificus

substrate_name: 1-Palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid; H2O


substrate: 1-Palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid; H2O


sequence_source: UniProtKB direct accession lookup P0CG56 (https://rest.uniprot.org/uniprotkb/P0CG56.json)


substrate_name: H2O; 1-Palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid

sequence_source: UniProtKB direct accession lookup P24027 (https://rest.uniprot.org/uniprotkb/P24027.json)


sequence_source: UniProtKB:P07805 reconstructed variant

sequence_variant_note: Mutation signature D361A matches the mutant residue at offset -2 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07805 reconstructed variant and applied mutation signature D88A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07805 reconstructed variant and applied mutation signature D361E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant D88A N-terminal His6-tagged


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:
Ki above 0.1 mM, at pH 7.5 and 37°C
at pH 7.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.5

source_databases_merged: sabio_rk brenda skid


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant K69A:C360A heterodimer N-terminal His6-tagged


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant trypanosoma-K69A:mouse-C360A heterodimer N-terminal His6-tagged


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


organism: Trypanosoma brucei brucei

sequence_variant_note: Resolved canonical sequence from UniProtKB:P07805 reconstructed variant and applied mutation signature F397A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant F397A


organism: Vibrio vulnificus


organism: Xenopus laevis

proof_lines: 37°C, pH not specified in the publication


organism: Acanthophis antarcticus

substrate_name: Unknown

sequence: NLLQFGFMIRCANKRRRPVWPYEESGC

wild_type_sequence: NLLQFGFMIRCANKRRRPVWPYEESGC

substrate: Unknown


organism: Agkistrodon piscivorus leucostoma

substrate_name: 4-nitro-3-(octanoyloxy) benzoic acid (NOBA)


organism: Anuroctonus phaiodactylus


organism: Arabidopsis thaliana


organism: Beauveria bassiana (strain ARSEF 2860)

substrate_name: phosphatidyl-choline

substrate: phosphatidyl-choline


organism: Bitis arietans

sequence: SLIEFGKMITEETNRPVFPYEATIVVCDCGNGNGS

wild_type_sequence: SLIEFGKMITEETNRPVFPYEATIVVCDCGNGNGS


organism: Bos taurus

assay_conditions_summary: pH 4


organism: Bothrocophias hyoprora

substrate: 4-nitro-3-(octanoyloxy) benzoic acid (NOBA)


organism: Bothrops bilineatus smaragdinus


sequence_source: UniProtKB direct accession lookup: P62022


sequence_source: UniProtKB direct accession lookup: P08878 and P62022

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

substrate: H2O; 1-Palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid


organism: Crotalus lutosus

substrate_name: 4-nitro-3-octanoyloxy benzoic acid

sequence_source: UniProtKB direct accession lookup: C0HK05

substrate: 4-nitro-3-octanoyloxy benzoic acid


organism: Crotalus viridis lutosus


organism: Daboia russelii russelii

substrate_name: soya lecithin

sequence_source: UniProtKB direct accession lookup: P59071

proof_lines: at pH 8.9, temperature not specified in the publication

substrate: soya lecithin


organism: Echis carinatus

substrate_name: Phosphatidylcholine; H2O

sequence_source: UniProtKB direct accession lookup: Q7T3S7

substrate: Phosphatidylcholine; H2O


organism: Homo sapiens

sequence_source: UniProtKB direct accession lookup: Q13093

proof_lines: pH 7.4, 37°C, recombinant His-tagged Lp-PLA2


sequence_source: UniProtKB direct accession lookup: P14555


organism: Mus musculus

sequence_source: UniProtKB direct accession lookup: P47713


organism: Oryctolagus cuniculus

sequence_source: UniProtKB direct accession lookup: P14422

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


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB direct accession lookup: Q12405


organism: Sus scrofa

sequence_source: UniProtKB direct accession lookup: P00592

proof_lines: mutant A12T/H15D/M20L/E71N, pH 8.0, 24°C


proof_lines:
pH 8.5, 37°C
Raw SKiD Env: Temp=24°C, pH=8


enzyme_display_name: myeloblastin

sequence_source: UniProtKB direct accession lookup: P24158

proof_lines: 52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0

proof_lines: pH and temperature not specified in the publication

enzyme: myeloblastin


sequence_source: UniProtKB direct accession lookup: Q61096


enzyme_display_name: acetylspermidine deacetylase

organism: Danio rerio

sequence_source: UniProtKB reviewed F1QCV2 canonical protein sequence, checked directly on 2026-06-17.

enzyme: acetylspermidine deacetylase


sequence_variant_note: Resolved canonical sequence from F1QCV2 canonical sequence with row-specific N93A substitution reconstructed after direct residue check on 2026-06-17. and applied mutation signature N93A to reconstruct the assayed variant sequence.

smiles: CC(=O)NCCCCNCCCN


sequence_variant_note: Resolved canonical sequence from F1QCV2 canonical sequence with row-specific E274L substitution reconstructed after direct residue check on 2026-06-17. and applied mutation signature E274L to reconstruct the assayed variant sequence.


substrate_name: Acetylcadaverine

smiles: CC(=O)NCCCCCN

substrate: Acetylcadaverine


substrate_name: N-butylacetamide

smiles: CCCCN=C(C)O

substrate: N-butylacetamide


sequence_source: F1QCV2 canonical sequence with row-specific N93A substitution reconstructed after direct residue check on 2026-06-17.


sequence_variant_note: Resolved canonical sequence from F1QCV2 canonical sequence with row-specific D94A substitution reconstructed after direct residue check on 2026-06-17. and applied mutation signature D94A to reconstruct the assayed variant sequence.


sequence_source: F1QCV2 canonical sequence with row-specific E274L substitution reconstructed after direct residue check on 2026-06-17.


mutation_signature: recombinant deletion mutant DELTAnuA2

proof_lines: pH 8.0, 22°C, recombinant deletion mutant DELTAnuA2


substrate_name: acetylputrescine

smiles: CC(O)=NCCCCN

substrate: acetylputrescine


sequence_source: F1QCV2 canonical sequence with row-specific D94A substitution reconstructed after direct residue check on 2026-06-17.


enzyme_display_name: amidophosphoribosyltransferase

substrate_name: 5-Phospho-alpha-D-ribose 1-diphosphate; H2O; L-Glutamine

sequence_source: UniProtKB:Q9T0J5 direct lookup

enzyme: amidophosphoribosyltransferase


substrate_name: 5-Phospho-alpha-D-ribose 1-diphosphate; L-Glutamine; H2O

sequence_source: UniProtKB:Q9STG9 direct lookup

proof_lines: at pH 7.8, temperature not specified in the publication

proof_lines: cell extracts of recombinant AtGPRAT2 expressing Escherichia coli


organism: Escherichia coli

substrate_name: L-Glutamine; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature L415A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant L415A

substrate: L-Glutamine; H2O


sequence_source: UniProtKB:P0AG16 canonical sequence only

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant Y74L

substrate: 5-Phospho-alpha-D-ribose 1-diphosphate; H2O; L-Glutamine


substrate_name: L-Glutamine; H2O; 5-Phospho-alpha-D-ribose 1-diphosphate

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant R73L


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature R73H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant R73H


substrate_name: H2O; 5-Phospho-alpha-D-ribose 1-diphosphate; L-Glutamine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature G102A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant G102A


substrate_name: H2O; L-Glutamine; 5-Phospho-alpha-D-ribose 1-diphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature N101G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant N101G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature Y74S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant Y74S

substrate: H2O; 5-Phospho-alpha-D-ribose 1-diphosphate; L-Glutamine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature N101D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant N101D

substrate: 5-Phospho-alpha-D-ribose 1-diphosphate; L-Glutamine; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature R73L/Y74L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant R73L/Y74L

substrate: H2O; L-Glutamine; 5-Phospho-alpha-D-ribose 1-diphosphate


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: amidophosphoribosyltransferase(Enzyme) mutant Y74F


substrate_name: L-Glutamine; 5-Phospho-alpha-D-ribose 1-diphosphate; H2O

sequence_source: UniProtKB:P0AG16 direct lookup


proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant D127A

substrate: L-Glutamine; 5-Phospho-alpha-D-ribose 1-diphosphate; H2O


proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant Ala insert


organism: Glycine max

sequence_source: UniProtKB:P52418 direct lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:F1QCV2 and applied mutation signature N93A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F1QCV2 and applied mutation signature D94A to reconstruct the assayed variant sequence.


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

proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:F1QCV2 and applied mutation signature E274L to reconstruct the assayed variant sequence.


smiles: CC(O)=NCCCCCCCCN


enzyme_display_name: uridine phosphorylase

organism: Phytophthora capsici

substrate_name: uridine

sequence_source: UniProtKB:A0A6G6VYG7 direct REST sequence

proof_lines: pH and temperature not specified in the publication

enzyme: uridine phosphorylase

substrate: uridine


organism: Plasmodium falciparum

substrate_name: Inosine

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

substrate: Inosine


organism: Schistosoma mansoni

substrate_name: thymidine

substrate: thymidine


organism: Shewanella oneidensis

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer, pH 7.5, 25°C


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


substrate_name: phosphate

sequence_source: UniProtKB:Q8E9X9 direct REST sequence

substrate: phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8E9X9 direct REST sequence with row-specific mutation reconstruction and applied mutation signature R176K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8E9X9 direct REST sequence with row-specific mutation reconstruction and applied mutation signature R176A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8E9X9 direct REST sequence with row-specific mutation reconstruction and applied mutation signature R89K to reconstruct the assayed variant sequence.


enzyme_display_name: acetylglutamate kinase

organism: Arabidopsis thaliana

substrate_name: ATP; N-Acetyl-L-glutamate

sequence_source: UniProtKB:Q9SCL7 direct REST sequence

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5

proof_lines: in the absence of protein PII, in 50 mM imidazole, pH 7.5

proof_lines: in the presence of protein PII, in 50 mM imidazole, pH 7.5

enzyme: acetylglutamate kinase

substrate: ATP; N-Acetyl-L-glutamate


substrate_name: N-Acetyl-L-glutamate; ATP

assay_conditions_summary: cofactor ATP

substrate: N-Acetyl-L-glutamate; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6C8 direct REST sequence with row-specific mutation reconstruction and applied mutation signature R66K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: SABIO-RK modifier species: acetylglutamate kinase(Enzyme) mutant R66K


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

sequence_source: UniProtKB:P0A6C8 direct REST sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6C8 direct REST sequence with row-specific mutation reconstruction and applied mutation signature K8R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetylglutamate kinase(Enzyme) mutant K8R


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6C8 direct REST sequence with row-specific mutation reconstruction and applied mutation signature N158Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetylglutamate kinase(Enzyme) mutant N158Q


organism: Unknown

substrate_name: N-acetyl-L-glutamate

substrate: N-acetyl-L-glutamate


enzyme_display_name: glucan 1,6-alpha-glucosidase

organism: Lactobacillus acidophilus

substrate_name: isomaltotetraose

sequence_source: UniProtKB Q5FMB7 direct REST lookup on 2026-06-17

assay_conditions_summary: pH 6; 310.15 K; buffer 60 mM MES-NaOH

column_label: TABLE 4: Kinetic parameters of LaGH13_31 at 37°C and pH 6.0 (J Bacteriol 2012, 194(16):4249-4259); substrate row 'IG4'; column 'kcat (s-1)' = 501; column 'Km (mM)' = 16.1; column 'kcat/Km (s-1 mM-1)' = 31; column 'Relative kcat/Km' holds the same row's efficiency normalized to panose, which is a ratio of the table's own cells and not a kinetic constant.

normalized_value_unit_evidence: kcat: printed Table 4 cell 501 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 501.0 s^(-1). Km: printed Table 4 cell 16.1 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 16.1 mM. kcat/Km: printed Table 4 cell 31 s-1 mM-1; that unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 31.0 s^(-1)*mM^(-1). The exported efficiency 31.118012422360245 s^(-1)*mM^(-1) is the full-precision quotient 501.0 / 16.1 of the two printed component cells, and the printed efficiency cell is that same quotient rendered at the integer precision Table 4 uses for this column.

raw_value_unit_evidence: Table 4, substrate row 'IG4': kcat = 501 s-1 under the column head kcat (s-1); Km = 16.1 mM under the column head Km (mM); printed kcat/Km = 31 under the column head kcat/Km (s-1 mM-1).

row_label: Table 4, substrate row 'IG4'

enzyme: glucan 1,6-alpha-glucosidase

substrate: isomaltotetraose


substrate_name: Dextran

substrate: Dextran


substrate_name: isomaltotriose

column_label: TABLE 4: Kinetic parameters of LaGH13_31 at 37°C and pH 6.0 (J Bacteriol 2012, 194(16):4249-4259); substrate row 'IG3'; column 'kcat (s-1)' = 475; column 'Km (mM)' = 14.1; column 'kcat/Km (s-1 mM-1)' = 34; column 'Relative kcat/Km' holds the same row's efficiency normalized to panose, which is a ratio of the table's own cells and not a kinetic constant.

normalized_value_unit_evidence: kcat: printed Table 4 cell 475 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 475.0 s^(-1). Km: printed Table 4 cell 14.1 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 14.1 mM. kcat/Km: printed Table 4 cell 34 s-1 mM-1; that unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 34.0 s^(-1)*mM^(-1). The exported efficiency 33.687943262411345 s^(-1)*mM^(-1) is the full-precision quotient 475.0 / 14.1 of the two printed component cells, and the printed efficiency cell is that same quotient rendered at the integer precision Table 4 uses for this column.

raw_value_unit_evidence: Table 4, substrate row 'IG3': kcat = 475 s-1 under the column head kcat (s-1); Km = 14.1 mM under the column head Km (mM); printed kcat/Km = 34 under the column head kcat/Km (s-1 mM-1).

row_label: Table 4, substrate row 'IG3'

substrate: isomaltotriose


substrate_name: isomaltose

column_label: TABLE 4: Kinetic parameters of LaGH13_31 at 37°C and pH 6.0 (J Bacteriol 2012, 194(16):4249-4259); substrate row 'IG2'; column 'kcat (s-1)' = 517; column 'Km (mM)' = 22.5; column 'kcat/Km (s-1 mM-1)' = 23; column 'Relative kcat/Km' holds the same row's efficiency normalized to panose, which is a ratio of the table's own cells and not a kinetic constant.

normalized_value_unit_evidence: kcat: printed Table 4 cell 517 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 517.0 s^(-1). Km: printed Table 4 cell 22.5 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 22.5 mM. kcat/Km: printed Table 4 cell 23 s-1 mM-1; that unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 23.0 s^(-1)*mM^(-1). The exported efficiency 22.977777777777778 s^(-1)*mM^(-1) is the full-precision quotient 517.0 / 22.5 of the two printed component cells, and the printed efficiency cell is that same quotient rendered at the integer precision Table 4 uses for this column.

raw_value_unit_evidence: Table 4, substrate row 'IG2': kcat = 517 s-1 under the column head kcat (s-1); Km = 22.5 mM under the column head Km (mM); printed kcat/Km = 23 under the column head kcat/Km (s-1 mM-1).

row_label: Table 4, substrate row 'IG2'

substrate: isomaltose


proof_lines: purified recombinant enzyme, pH 6.0, 37°C


column_label: TABLE 4: Kinetic parameters of LaGH13_31 at 37°C and pH 6.0 (J Bacteriol 2012, 194(16):4249-4259); substrate row 'PNPG'; column 'kcat (s-1)' = 597; column 'Km (mM)' = 2.38; column 'kcat/Km (s-1 mM-1)' = 251; column 'Relative kcat/Km' holds the same row's efficiency normalized to panose, which is a ratio of the table's own cells and not a kinetic constant.

normalized_value_unit_evidence: kcat: printed Table 4 cell 597 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 597.0 s^(-1). Km: printed Table 4 cell 2.38 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 2.38 mM. kcat/Km: printed Table 4 cell 251 s-1 mM-1; that unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 251.0 s^(-1)*mM^(-1). The exported efficiency 250.8403361344538 s^(-1)*mM^(-1) is the full-precision quotient 597.0 / 2.38 of the two printed component cells, and the printed efficiency cell is that same quotient rendered at the integer precision Table 4 uses for this column.

raw_value_unit_evidence: Table 4, substrate row 'PNPG': kcat = 597 s-1 under the column head kcat (s-1); Km = 2.38 mM under the column head Km (mM); printed kcat/Km = 251 under the column head kcat/Km (s-1 mM-1).

row_label: Table 4, substrate row 'PNPG'


substrate_name: panose

column_label: TABLE 4: Kinetic parameters of LaGH13_31 at 37°C and pH 6.0 (J Bacteriol 2012, 194(16):4249-4259); substrate row 'Panose'; column 'kcat (s-1)' = 612; column 'Km (mM)' = 3.9; column 'kcat/Km (s-1 mM-1)' = 157; column 'Relative kcat/Km' holds the same row's efficiency normalized to panose, which is a ratio of the table's own cells and not a kinetic constant.

normalized_value_unit_evidence: kcat: printed Table 4 cell 612 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 612.0 s^(-1). Km: printed Table 4 cell 3.9 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 3.9 mM. kcat/Km: printed Table 4 cell 157 s-1 mM-1; that unit is already the canonical efficiency unit, so no unit conversion applies and the printed cell is 157.0 s^(-1)*mM^(-1). The exported efficiency 156.92307692307693 s^(-1)*mM^(-1) is the full-precision quotient 612.0 / 3.9 of the two printed component cells, and the printed efficiency cell is that same quotient rendered at the integer precision Table 4 uses for this column.

raw_value_unit_evidence: Table 4, substrate row 'Panose': kcat = 612 s-1 under the column head kcat (s-1); Km = 3.9 mM under the column head Km (mM); printed kcat/Km = 157 under the column head kcat/Km (s-1 mM-1).

row_label: Table 4, substrate row 'Panose'

substrate: panose


organism: Streptococcus mutans


substrate_name: isomaltohexaose

sequence_variant_note: Resolved canonical sequence from UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238A substitution and applied mutation signature W238A to reconstruct the assayed variant sequence.

substrate: isomaltohexaose


substrate_name: isomaltoheptaose

sequence_source: UniProtKB Q99040 direct REST lookup on 2026-06-17

assay_conditions_summary: pH 6; 310.15 K; buffer pH 6

column_label: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column group 'Wild type', substrate row 'IG7' (isomaltoheptaose (IG7)); column 'kcat (s-1)' = 449; column 'Km (mM)' = 12.0; column 'kcat/Km (s-1 mM-1)' = 37.4; column 'Relative(a)' = 72.3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 449 s^-1; the turnover column is already per second, so no unit conversion applies and the paper value is 449.0 s^(-1). Km: printed Table 3 cell 12.0 mM; the column is already millimolar, so the paper value is 12.0 mM. kcat/Km: printed Table 3 cell 37.4 s^-1 mM^-1; the column is already in s^-1 mM^-1, so the paper value is 37.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column 'Wild type', substrate row 'IG7': kcat = 449 s^-1; Km = 12.0 mM; printed kcat/Km = 37.4 s^-1 mM^-1.

table_label: Table 3: Kinetic parameters of wild type and mutated SMDGs (Biochimica et Biophysica Acta 1764 (2006) 688-698)

substrate: isomaltoheptaose


substrate_name: Panose

column_label: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column group 'Wild type', substrate row 'Panose' (panose); column 'kcat (s-1)' = 538; column 'Km (mM)' = 1.03; column 'kcat/Km (s-1 mM-1)' = 522; column 'Relative(a)' = 1010.

normalized_value_unit_evidence: kcat: printed Table 3 cell 538 s^-1; the turnover column is already per second, so no unit conversion applies and the paper value is 538.0 s^(-1). Km: printed Table 3 cell 1.03 mM; the column is already millimolar, so the paper value is 1.03 mM. kcat/Km: printed Table 3 cell 522 s^-1 mM^-1; the column is already in s^-1 mM^-1, so the paper value is 522.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column 'Wild type', substrate row 'Panose': kcat = 538 s^-1; Km = 1.03 mM; printed kcat/Km = 522 s^-1 mM^-1.

substrate: Panose


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238P substitution and applied mutation signature W238P to reconstruct the assayed variant sequence.


substrate_name: p-Nitrophenyl-alpha-D-glucoside

sequence_variant_note: Resolved canonical sequence from UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238N substitution and applied mutation signature W238N to reconstruct the assayed variant sequence.

substrate: p-Nitrophenyl-alpha-D-glucoside


sequence_source: UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238A substitution


sequence_source: UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238N substitution


substrate_name: Isomaltose; H2O

proof_lines: SABIO-RK modifier species: glucan 1,6-alpha-glucosidase(Enzyme) mutant W238N

unit: lgwedgeoneswedgeone

substrate: Isomaltose; H2O


substrate_name: acetylputrescine

sequence_source: UniProtKB reviewed accession Q969S8 fetched by direct REST lookup during review

substrate: acetylputrescine


substrate_name: Nalpha,Nepsilon-diacetyl-L-lysinamide

substrate: Nalpha,Nepsilon-diacetyl-L-lysinamide


smiles: CC(O)=NCCCNCCCCNCCCN


substrate_name: Acetylcadaverine

substrate: Acetylcadaverine


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


organism: Trypanosoma brucei

substrate_name: L-Ornithine

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant His-tagged D332E

substrate: L-Ornithine


substrate_name: L-ornithine

substrate: L-ornithine


sequence_source: UniProtKB reviewed accession P07805 fetched by direct REST lookup during review

proof_lines:
wild type enzyme, at pH 7.5 and 37°C
wild-type, pH 8.0, 37°C


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant E94A N-terminal His6-tagged


enzyme_display_name: Amidophosphoribosyltransferase

organism: Homo sapiens

substrate_name: Unknown

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) Q06203 direct REST lookup on 2026-06-17

enzyme: Amidophosphoribosyltransferase

substrate: Unknown


organism: Rattus norvegicus

substrate_name: L-Glutamine; H2O; 5-Phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) P35433 direct REST lookup on 2026-06-17


enzyme_display_name: Uridine phosphorylase

organism: Aeropyrum pernix

substrate_name: uridine

sequence_source: UniProtKB UniProtKB unreviewed (TrEMBL) Q9YA34 direct REST lookup on 2026-06-17

enzyme: Uridine phosphorylase

substrate: uridine


sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) P12758 direct REST lookup on 2026-06-17


enzyme_display_name: Uridine phosphorylase 1

substrate_name: Phosphate; Uridine

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) Q16831 direct REST lookup on 2026-06-17

proof_lines:
in 100 mMn Tris buffer pH 7.4, at 37°C
pH 7.4, 37°C, versus uridine
pH 7.4, 37°C, versus phosphate

enzyme: Uridine phosphorylase 1

substrate: Phosphate; Uridine


enzyme_display_name: Uridine phosphorylase 2

substrate_name: Uridine; Phosphate

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) O95045 direct REST lookup on 2026-06-17

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

enzyme: Uridine phosphorylase 2

substrate: Uridine; Phosphate


organism: Mus musculus

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) Q8CGR7 direct REST lookup on 2026-06-17


sequence_source: UniProtKB UniProtKB unreviewed (TrEMBL) A0A410UCT3 direct REST lookup on 2026-06-17


enzyme_display_name: Acetylglutamate kinase

substrate_name: N-acetyl-L-glutamate

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) P0A6C8 direct REST lookup on 2026-06-17

enzyme: Acetylglutamate kinase

substrate: N-acetyl-L-glutamate


substrate_name: ATP; N-Acetyl-L-glutamate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0A6C8 canonical sequence fetched by direct REST lookup on 2026-06-17; row-specific variant reconstructed from selected mutation_signature D162E. and applied mutation signature D162E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetylglutamate kinase(Enzyme) mutant D162E

substrate: ATP; N-Acetyl-L-glutamate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C, mutant G11A, Vmax: 9.7
pH 7.5, 37°C, mutant G11A, Vmax: 11.1


substrate_name: ATP

proof_lines:
pH 7.5, 37°C, wild-type, Vmax: 72.6
pH 7.5, 37°C, wild-type, Vmax: 80

substrate: ATP


enzyme_display_name: Protein ARG5,6, mitochondrial

organism: Saccharomyces cerevisiae

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) Q01217 direct REST lookup on 2026-06-17

assay_conditions_summary: 310.15 K; cofactor ATP

enzyme: Protein ARG5,6, mitochondrial