organism: Human herpesvirus 1

sequence_variant_note: Resolved canonical sequence from UniProtKB:P10186 direct accession lookup plus direct mutation reconstruction and applied mutation signature D88N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant D88N


enzyme_display_name: uracil-DNA glycosylase

substrate_name: H2O; DNA

kcat_display: Not reported

km_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

sequence_source: UniProtKB:P10186 direct accession lookup for canonical context only

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

mutation_type: substitution

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant H210N

enzyme: uracil-DNA glycosylase

substrate: H2O; DNA


organism: Mesoplasma lactucae

substrate_name: DNA; H2O

mutation_signature: Unknown

km_unit: mM

sequence_source: UniProtKB:A0A291IS31 direct accession lookup

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

substrate: DNA; H2O


organism: Monkeypox virus

substrate_name: uracil-mismatched double-stranded DNA

source_db: brenda

source_license: CC BY 4.0

sequence_source: UniProtKB:Q8V4Y4 direct accession lookup

proof_lines: pH 7.5, 37°C, excision of a single uracil residue from U-A, recombinant enzyme

proof_lines: pH 7.0, 37°C, excision of a single uracil residue from U-G, recombinant enzyme

proof_lines: pH 7.5, 37°C, excision of a single uracil residue from PS-U, recombinant enzyme

substrate: uracil-mismatched double-stranded DNA

source: brenda


organism: Orthopoxvirus vaccinia

sequence_source: UniProtKB:P20536 direct accession lookup

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


organism: Thermus thermophilus

substrate_name: uracil-mismatched single-stranded DNA

sequence_source: UniProtKB:Q5SKC5 direct accession lookup

substrate: uracil-mismatched single-stranded DNA


sequence_source: UniProtKB:Q5SKC5 direct accession lookup for canonical context only

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant G42D C-terminal His6-tagged


enzyme_display_name: non-specific protein-tyrosine kinase

organism: Abelson murine leukemia virus

substrate_name: Protein tyrosine; ATP

proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant Y59W fusion protein to glutathione S-transferase

enzyme: non-specific protein-tyrosine kinase

substrate: Protein tyrosine; ATP


substrate_name: ATP; Protein tyrosine

proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant L444E fusion protein to glutathione S-transferase

substrate: ATP; Protein tyrosine


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant W525H fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant Y59L fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant I523V fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant L444K fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant F521A fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant G556V fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant S558N fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant W525F fusion protein to glutathione S-transferase


organism: Homo sapiens

substrate_name: ATP; Peptide

substrate: ATP; Peptide


verification_status: unverified

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

status: unverified


substrate_name: Unknown

ki_unit: mM

proof_lines:
30°C, Lck
30°C, Src

substrate: Unknown


organism: Mus musculus


organism: Opisthokonta

substrate_name: p-cyclin_cdc2; ATP

assay_conditions_summary: cofactor ATP

substrate: p-cyclin_cdc2; ATP


substrate_name: H2O; 4-Nitrophenyl phenyl phosphonate

sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q13822 (ENPP2_HUMAN)

substrate: H2O; 4-Nitrophenyl phenyl phosphonate


sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q9R1E6 (ENPP2_MOUSE)


sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q9CRY7 (GDPD1_MOUSE)

proof_lines: pH 7.4, temperature not specified in the publication


sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q99LY2 (GDPD3_MOUSE)


organism: Rattus norvegicus

substrate_name: 1-Acyl-sn-glycero-3-phosphocholine; H2O

sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q64610 (ENPP2_RAT)

substrate: 1-Acyl-sn-glycero-3-phosphocholine; H2O


enzyme_display_name: chitosanase

organism: Aspergillus sp. W-2

substrate_name: chitosan

sequence_source: UniProtKB REST direct accession check on 2026-06-17: A0A0B5L773 (A0A0B5L773_9EURO)

enzyme: chitosanase

substrate: chitosan


organism: Bacillus sp. TS

sequence_source: UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318N and applied mutation signature D318N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318K and applied mutation signature D318K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318R and applied mutation signature D318R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318E and applied mutation signature D318E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318A and applied mutation signature D318A to reconstruct the assayed variant sequence.


organism: Microbacterium sp.

sequence_source: UniProtKB REST direct accession check on 2026-06-17: A7KBW5 (A7KBW5_9MICO)


organism: Paenibacillus ehimensis

sequence_source: UniProtKB REST direct accession check on 2026-06-17: O24825 (O24825_9BACL)

proof_lines: 40°C, pH not specified in the publication, wild-type enzyme, calculated as micromol reducing sugar liberated from chitosan


enzyme_display_name: low-specificity L-threonine aldolase

organism: Caulobacter vibrioides

substrate_name: L-allo-Threonine

source_db: oed

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95Y and applied mutation signature D95Y to reconstruct the assayed variant sequence.

data_origin: experimental

enzyme: low-specificity L-threonine aldolase

substrate: L-allo-Threonine

source: oed


substrate_name: L-Threonine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95M and applied mutation signature D95M to reconstruct the assayed variant sequence.

substrate: L-Threonine


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95N/E96S and applied mutation signature D95N/E96S to reconstruct the assayed variant sequence.


substrate_name: L-threonine

sequence_source: UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95Y

substrate: L-threonine


sequence_source: UniProtKB REST accession Q9A3V8


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95G/E96G and applied mutation signature D95G/E96G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95G/E96G


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95L and applied mutation signature D95L to reconstruct the assayed variant sequence.


substrate_name: L-allo-threonine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95W and applied mutation signature D95W to reconstruct the assayed variant sequence.

substrate: L-allo-threonine


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95Y/E96T and applied mutation signature D95Y/E96T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95Y/E96T


organism: Escherichia coli

sequence_source: UniProtKB REST accession P75823


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P75823 and applied mutation signature K222A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-Threonine', enzyme heading 'K222A'; the enzyme heading spans three numeric columns: column 'kcat' = 43, column 'Km' = 72, column 'kcat/Km' = 0.6. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 43 min^-1; 43 / 60 = 0.7166666667 s^-1; the exported value is 0.72 s^(-1). km: printed Table 4 cell 72 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 72.0 mM. kcat/Km: printed Table 4 cell 0.6 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.6 / 60 = 0.01 s^-1 mM^-1; the exported value is 0.01 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-Threonine', enzyme column 'K222A': kcat = 43 min^-1; Km = 72 mM; printed kcat/Km = 0.6 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.

table_label: Table 4: Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine (FEBS J. 2014, 281(1):129-145)

status: corrected


column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-allo-Threonine', enzyme heading 'K222A'; the enzyme heading spans three numeric columns: column 'kcat' = 80, column 'Km' = 1.2, column 'kcat/Km' = 67. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 80 min^-1; 80 / 60 = 1.3333333333 s^-1; the exported value is 1.33 s^(-1). km: printed Table 4 cell 1.2 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 1.2 mM. kcat/Km: printed Table 4 cell 67 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 67 / 60 = 1.1166666667 s^-1 mM^-1; the exported value is 1.1083333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-allo-Threonine', enzyme column 'K222A': kcat = 80 min^-1; Km = 1.2 mM; printed kcat/Km = 67 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P75823 and applied mutation signature H83F/H126F to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-allo-Threonine', enzyme heading 'H83F/H126F'; the enzyme heading spans three numeric columns: column 'kcat' = 1.7, column 'Km' = 7.4, column 'kcat/Km' = 0.23. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.7 min^-1; 1.7 / 60 = 0.0283333333 s^-1; the exported value is 0.028 s^(-1). km: printed Table 4 cell 7.4 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 7.4 mM. kcat/Km: printed Table 4 cell 0.23 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.23 / 60 = 0.0038333333 s^-1 mM^-1; the exported value is 0.0037837837837837837 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-allo-Threonine', enzyme column 'H83F/H126F': kcat = 1.7 min^-1; Km = 7.4 mM; printed kcat/Km = 0.23 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P75823 and applied mutation signature F87A to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-Threonine', enzyme heading 'F87A'; the enzyme heading spans three numeric columns: column 'kcat' = 43, column 'Km' = 8.7, column 'kcat/Km' = 4.9. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 43 min^-1; 43 / 60 = 0.7166666667 s^-1; the exported value is 0.72 s^(-1). km: printed Table 4 cell 8.7 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 8.7 mM. kcat/Km: printed Table 4 cell 4.9 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 4.9 / 60 = 0.0816666667 s^-1 mM^-1; the exported value is 0.08275862068965517 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-Threonine', enzyme column 'F87A': kcat = 43 min^-1; Km = 8.7 mM; printed kcat/Km = 4.9 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


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

proof_lines: 40°C, pH not specified in the publication, mutant enzyme A207C/L286C, calculated as micromol reducing sugar liberated from chitosan


organism: Paenibacillus sp.

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


organism: Streptomyces sp.

sequence_source: UniProtKB:P33665 reviewed canonical sequence checked during exact accession review

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

assay_conditions_summary: pH 5.5; 310.15 K; buffer 50 mM sodium acetate

proof_lines: wild type enzyme, at 37°C in 50 mM sodium acetate buffer (pH 5.5)


proof_lines: mutant enzyme R42E at 37°C in 50 mM sodium acetate buffer (pH 5.5)


proof_lines: mutant enzyme R42K, at 37°C in 50 mM sodium acetate buffer (pH 5.5)


proof_lines: chitosan with less than 75% deacetylation, at pH 6.0 and 45°C

proof_lines: chitosan with 75-85% deacetylation, at pH 6.0 and 45°C

proof_lines: chitosan with more than 90% deacetylation, at pH 6.0 and 45°C


substrate_name: Chitosan; H2O

proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant E22A

unit: lgwedgeoneswedgeone

substrate: Chitosan; H2O


substrate_name: H2O; Chitosan

substrate: H2O; Chitosan


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant E22D


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D40E


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant E36Q


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D37N


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant E22Q


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D37E


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D40N


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D6N


substrate_name: 30% N-acetylated chitosan

sequence_source: UniProtKB reviewed accession P33665 direct lookup; variant reconstructed from source mutation label.

sequence_variant_note: Mutation signature W28F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: 30% N-acetylated chitosan


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -10, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33665 direct lookup; variant reconstructed from source mutation label. and applied mutation signature W28F/W101F with inferred residue-numbering offset +40 to reconstruct the assayed variant sequence.


organism: Streptomyces sp. N174

sequence_source: UniProtKB reviewed accession P33665 direct lookup.

proof_lines: wild-type, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.

proof_lines: mutant E36Q, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature E36N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E36N, assayed as the amount of D-glucosamine released from chitosan


organism: Archaeoglobus fulgidus

sequence_source: UniProtKB reviewed accession O28007 direct lookup.

proof_lines:
pH 7.8, 95°C
pH 7.5, 80°C, recombinant enzyme
pH 7.5, 80°C


substrate_name: uracil-mismatched double-stranded DNA

proof_lines: pH 7.5, 80°C, cell extract (wild-type enzyme)

substrate: uracil-mismatched double-stranded DNA


organism: Bacillus subtilis

substrate_name: DNA; H2O

sequence_source: UniProtKB reviewed accession P39615 direct lookup.

substrate: DNA; H2O


organism: Chlamydia pneumoniae

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9Z7D3 direct lookup; variant reconstructed from source mutation label. and applied mutation signature H200Q to reconstruct the assayed variant sequence.


substrate_name: uracil-mismatched double-stranded DNA with A-U mismatch +

sequence_source: UniProtKB reviewed accession Q9Z7D3 direct lookup.

proof_lines: pH 8.0, 37°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9Z7D3 direct lookup; variant reconstructed from source mutation label. and applied mutation signature A205S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9Z7D3 direct lookup; variant reconstructed from source mutation label. and applied mutation signature D77N to reconstruct the assayed variant sequence.


organism: Deinococcus radiodurans

sequence_source: UniProtKB reviewed accession Q9RWH9 direct lookup.


enzyme_display_name: 4-hydroxyacetophenone monooxygenase

organism: Pseudomonas fluorescens

sequence_source: UniProtKB reviewed entry Q93TJ5 / HAPMO_PSEFL direct lookup

enzyme: 4-hydroxyacetophenone monooxygenase


substrate_name: methyl 4-tolyl sulfide

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Methyl 4-tolyl sulfide'; column 'Km (uM)' = 370 (50); column 'kcat (s^-1)' = 7.3 (0.6); column 'kcat/Km (10^3 s^-1 . M^-1)' = 20; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 370 uM; 370 / 1000 = 0.37 mM. kcat: printed Table 1 cell 7.3 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 7.3 s^(-1). kcat/Km: printed Table 1 cell 20 in the column headed 10^3 s^-1 M^-1, that is 20000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 20000 / 1000 = 20 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Methyl 4-tolyl sulfide': Km = 370 uM; kcat = 7.3 s^-1; printed kcat/Km = 20 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Methyl 4-tolyl sulfide'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

table_label: Table 1: Steady-state kinetic parameters for HAPMO (Appl. Environ. Microbiol. 2003, 69(1):419-426)

substrate: methyl 4-tolyl sulfide


substrate_name: Benzaldehyde

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Benzaldehyde'; column 'Km (uM)' = 1,600 (200); column 'kcat (s^-1)' = 2.2 (0.2); column 'kcat/Km (10^3 s^-1 . M^-1)' = 1.4; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,600 uM; 1600 / 1000 = 1.6 mM. kcat: printed Table 1 cell 2.2 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 2.2 s^(-1). kcat/Km: printed Table 1 cell 1.4 in the column headed 10^3 s^-1 M^-1, that is 1400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1400 / 1000 = 1.4 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Benzaldehyde': Km = 1,600 uM; kcat = 2.2 s^-1; printed kcat/Km = 1.4 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Benzaldehyde'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Benzaldehyde


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

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '3-Chloro-2-butanone'; column 'Km (uM)' = 23,000 (4,000); column 'kcat (s^-1)' = 7.4 (1.0); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.32; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 23,000 uM; 23000 / 1000 = 23 mM. kcat: printed Table 1 cell 7.4 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 7.4 s^(-1). kcat/Km: printed Table 1 cell 0.32 in the column headed 10^3 s^-1 M^-1, that is 320 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 320 / 1000 = 0.32 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '3-Chloro-2-butanone': Km = 23,000 uM; kcat = 7.4 s^-1; printed kcat/Km = 0.32 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '3-Chloro-2-butanone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: NADPH; O2; 4'-Hydroxyacetophenone; H+

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

substrate: NADPH; O2; 4'-Hydroxyacetophenone; H+


column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '3-Hydroxyacetophenone'; column 'Km (uM)' = 1,400 (200); column 'kcat (s^-1)' = 4.8 (0.3); column 'kcat/Km (10^3 s^-1 . M^-1)' = 3.4; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,400 uM; 1400 / 1000 = 1.4 mM. kcat: printed Table 1 cell 4.8 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 4.8 s^(-1). kcat/Km: printed Table 1 cell 3.4 in the column headed 10^3 s^-1 M^-1, that is 3400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3400 / 1000 = 3.4 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '3-Hydroxyacetophenone': Km = 1,400 uM; kcat = 4.8 s^-1; printed kcat/Km = 3.4 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '3-Hydroxyacetophenone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: Hydroxyacetone

smiles: CC(=O)CO

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Hydroxyacetone (acetol)'; column 'Km (uM)' = 29,000 (3,000); column 'kcat (s^-1)' = 4.1 (0.3); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.14; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 29,000 uM; 29000 / 1000 = 29 mM. kcat: printed Table 1 cell 4.1 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 4.1 s^(-1). kcat/Km: printed Table 1 cell 0.14 in the column headed 10^3 s^-1 M^-1, that is 140 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 140 / 1000 = 0.14 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Hydroxyacetone (acetol)': Km = 29,000 uM; kcat = 4.1 s^-1; printed kcat/Km = 0.14 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Hydroxyacetone (acetol)'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Hydroxyacetone


verification_status: verified

column_label: Table 1: Steady-state kinetic parameters for HAPMO. Substrate row '2-Acetylpyridine'; column 'K_m (uM)' = 1,200; column 'k_cat (s^-1)' = 7.8; column 'k_cat/K_m (10^3 s^-1 . M^-1)' = 6.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,200 uM; 1200 / 1000 = 1.2 mM; the exported value is 1.2 mM. kcat: printed Table 1 cell 7.8 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 7.8 s^(-1). kcat/Km: printed Table 1 cell 6.5 in the column unit 10^3 s^-1 . M^-1; 10^3 M^-1 is exactly mM^-1, so the cell is 6.5 s^-1 mM^-1 with no numeric rescaling; the exported value is 6.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row '2-Acetylpyridine': K_m = 1,200 uM; k_cat = 7.8 s^-1; k_cat/K_m = 6.5 in the printed column unit 10^3 s^-1 . M^-1.

status: verified


column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'rac-Bicyclo[3.2.0]hept-2-en-6-one'; column 'Km (uM)' = 3,300 (300); column 'kcat (s^-1)' = 6.7 (0.3); column 'kcat/Km (10^3 s^-1 . M^-1)' = 2.0; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 3,300 uM; 3300 / 1000 = 3.3 mM. kcat: printed Table 1 cell 6.7 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 6.7 s^(-1). kcat/Km: printed Table 1 cell 2.0 in the column headed 10^3 s^-1 M^-1, that is 2000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2000 / 1000 = 2 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'rac-Bicyclo[3.2.0]hept-2-en-6-one': Km = 3,300 uM; kcat = 6.7 s^-1; printed kcat/Km = 2.0 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'rac-Bicyclo[3.2.0]hept-2-en-6-one'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: butyrophenone

column_label: Table 1: Steady-state kinetic parameters for HAPMO. Substrate row 'Butyrophenone'; column 'K_m (uM)' = 2,000; column 'k_cat (s^-1)' = 1.2; column 'k_cat/K_m (10^3 s^-1 . M^-1)' = 0.60.

normalized_value_unit_evidence: Km: printed Table 1 cell 2,000 uM; 2000 / 1000 = 2.0 mM; the exported value is 2.0 mM. kcat: printed Table 1 cell 1.2 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 1.2 s^(-1). kcat/Km: printed Table 1 cell 0.60 in the column unit 10^3 s^-1 . M^-1; 10^3 M^-1 is exactly mM^-1, so the cell is 0.6 s^-1 mM^-1 with no numeric rescaling; the exported value is 0.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row 'Butyrophenone': K_m = 2,000 uM; k_cat = 1.2 s^-1; k_cat/K_m = 0.60 in the printed column unit 10^3 s^-1 . M^-1.

row_label: Table 1, substrate row 'Butyrophenone'

substrate: butyrophenone


substrate_name: Acetylcyclohexane

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Acetylcyclohexane'; column 'Km (uM)' = 4,800 (900); column 'kcat (s^-1)' = 3.9 (0.3); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.81; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 4,800 uM; 4800 / 1000 = 4.8 mM. kcat: printed Table 1 cell 3.9 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 3.9 s^(-1). kcat/Km: printed Table 1 cell 0.81 in the column headed 10^3 s^-1 M^-1, that is 810 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 810 / 1000 = 0.81 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Acetylcyclohexane': Km = 4,800 uM; kcat = 3.9 s^-1; printed kcat/Km = 0.81 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Acetylcyclohexane'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Acetylcyclohexane


sequence_source: UniProtKB Q93TJ5 direct REST/FASTA lookup


substrate_name: 2-Pyrrole carboxaldehyde

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '2-Pyrrole carboxaldehyde'; column 'Km (uM)' = 410 (30); column 'kcat (s^-1)' = 8.6 (0.2); column 'kcat/Km (10^3 s^-1 . M^-1)' = 21; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 410 uM; 410 / 1000 = 0.41 mM. kcat: printed Table 1 cell 8.6 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 8.6 s^(-1). kcat/Km: printed Table 1 cell 21 in the column headed 10^3 s^-1 M^-1, that is 21000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '2-Pyrrole carboxaldehyde': Km = 410 uM; kcat = 8.6 s^-1; printed kcat/Km = 21 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '2-Pyrrole carboxaldehyde'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: 2-Pyrrole carboxaldehyde


substrate_name: methylphenyl sulfide

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Methylphenyl sulfide'; column 'Km (uM)' = 1,400 (400); column 'kcat (s^-1)' = 4.7 (0.6); column 'kcat/Km (10^3 s^-1 . M^-1)' = 3.4; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,400 uM; 1400 / 1000 = 1.4 mM. kcat: printed Table 1 cell 4.7 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 4.7 s^(-1). kcat/Km: printed Table 1 cell 3.4 in the column headed 10^3 s^-1 M^-1, that is 3400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3400 / 1000 = 3.4 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Methylphenyl sulfide': Km = 1,400 uM; kcat = 4.7 s^-1; printed kcat/Km = 3.4 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Methylphenyl sulfide'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: methylphenyl sulfide


column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '2-Acetylpyrrole'; column 'Km (uM)' = 330 (20); column 'kcat (s^-1)' = 9.4 (0.14); column 'kcat/Km (10^3 s^-1 . M^-1)' = 28; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 330 uM; 330 / 1000 = 0.33 mM. kcat: printed Table 1 cell 9.4 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 9.4 s^(-1). kcat/Km: printed Table 1 cell 28 in the column headed 10^3 s^-1 M^-1, that is 28000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 28000 / 1000 = 28 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '2-Acetylpyrrole': Km = 330 uM; kcat = 9.4 s^-1; printed kcat/Km = 28 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '2-Acetylpyrrole'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


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

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '2,4-Pentanedione'; column 'Km (uM)' = 4,900 (900); column 'kcat (s^-1)' = 2.1 (0.5); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.43; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 4,900 uM; 4900 / 1000 = 4.9 mM. kcat: printed Table 1 cell 2.1 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 2.1 s^(-1). kcat/Km: printed Table 1 cell 0.43 in the column headed 10^3 s^-1 M^-1, that is 430 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 430 / 1000 = 0.43 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '2,4-Pentanedione': Km = 4,900 uM; kcat = 2.1 s^-1; printed kcat/Km = 0.43 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '2,4-Pentanedione'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: cyclohexane carboxaldehyde

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Cyclohexane carboxaldehyde'; column 'Km (uM)' = 3,000 (500); column 'kcat (s^-1)' = 5.0 (0.4); column 'kcat/Km (10^3 s^-1 . M^-1)' = 1.7; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 3,000 uM; 3000 / 1000 = 3 mM. kcat: printed Table 1 cell 5.0 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 5 s^(-1). kcat/Km: printed Table 1 cell 1.7 in the column headed 10^3 s^-1 M^-1, that is 1700 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1700 / 1000 = 1.7 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Cyclohexane carboxaldehyde': Km = 3,000 uM; kcat = 5.0 s^-1; printed kcat/Km = 1.7 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Cyclohexane carboxaldehyde'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: cyclohexane carboxaldehyde


column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '4-Acetylpyridine'; column 'Km (uM)' = 1,900 (100); column 'kcat (s^-1)' = 0.5 (0.2); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.3; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,900 uM; 1900 / 1000 = 1.9 mM. kcat: printed Table 1 cell 0.5 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.5 s^(-1). kcat/Km: printed Table 1 cell 0.3 in the column headed 10^3 s^-1 M^-1, that is 300 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 300 / 1000 = 0.3 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '4-Acetylpyridine': Km = 1,900 uM; kcat = 0.5 s^-1; printed kcat/Km = 0.3 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '4-Acetylpyridine'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: Isobutyrophenone

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Isobutyrophenone'; column 'Km (uM)' = 540 (40); column 'kcat (s^-1)' = 2.5 (0.1); column 'kcat/Km (10^3 s^-1 . M^-1)' = 4.6; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 540 uM; 540 / 1000 = 0.54 mM. kcat: printed Table 1 cell 2.5 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 2.5 s^(-1). kcat/Km: printed Table 1 cell 4.6 in the column headed 10^3 s^-1 M^-1, that is 4600 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4600 / 1000 = 4.6 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Isobutyrophenone': Km = 540 uM; kcat = 2.5 s^-1; printed kcat/Km = 4.6 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Isobutyrophenone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Isobutyrophenone


substrate_name: Acetophenone

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Acetophenone'; column 'Km (uM)' = 2,300 (900); column 'kcat (s^-1)' = 13.2 (1.7); column 'kcat/Km (10^3 s^-1 . M^-1)' = 5.7; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 2,300 uM; 2300 / 1000 = 2.3 mM. kcat: printed Table 1 cell 13.2 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 13.2 s^(-1). kcat/Km: printed Table 1 cell 5.7 in the column headed 10^3 s^-1 M^-1, that is 5700 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5700 / 1000 = 5.7 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Acetophenone': Km = 2,300 uM; kcat = 13.2 s^-1; printed kcat/Km = 5.7 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Acetophenone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Acetophenone


substrate_name: Propiophenone

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Propiophenone'; column 'Km (uM)' = 530 (100); column 'kcat (s^-1)' = 11.0 (0.2); column 'kcat/Km (10^3 s^-1 . M^-1)' = 21; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 530 uM; 530 / 1000 = 0.53 mM. kcat: printed Table 1 cell 11.0 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 11 s^(-1). kcat/Km: printed Table 1 cell 21 in the column headed 10^3 s^-1 M^-1, that is 21000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Propiophenone': Km = 530 uM; kcat = 11.0 s^-1; printed kcat/Km = 21 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Propiophenone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Propiophenone


substrate_name: 4'-Hydroxyacetophenone; H+; NADH

sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TJ5 direct REST/FASTA lookup and applied mutation signature K439F to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NADP+

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant K439F

substrate: 4'-Hydroxyacetophenone; H+; NADH


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: NADH


sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TJ5 direct REST/FASTA lookup and applied mutation signature R339A to reconstruct the assayed variant sequence.


substrate_name: H+; 4'-Hydroxyacetophenone; NADH

sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TJ5 direct REST/FASTA lookup and applied mutation signature K439A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant K439A

substrate: H+; 4'-Hydroxyacetophenone; NADH


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific K439P variant reconstructed during review and applied mutation signature K439P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: NADH; 4'-Hydroxyacetophenone; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific R339A variant reconstructed during review and applied mutation signature R339A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant R339A

substrate: NADH; 4'-Hydroxyacetophenone; H+


sequence_source: UniProtKB:Q93TJ5 FASTA/JSON direct accession check


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific K439A variant reconstructed during review and applied mutation signature K439A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q93TJ5 canonical sequence; row-specific K439P variant reconstructed during review


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific K439F variant reconstructed during review and applied mutation signature K439F to reconstruct the assayed variant sequence.


substrate_name: 4'-Hydroxyacetophenone; NADH; H+

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant K439P

substrate: 4'-Hydroxyacetophenone; NADH; H+


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific K439N variant reconstructed during review and applied mutation signature K439N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q93TJ5 canonical sequence; row-specific K439A variant reconstructed during review


sequence_source: UniProtKB:Q93TJ5 canonical sequence; row-specific K439N variant reconstructed during review

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant K439N


substrate_name: H+; 4'-Hydroxyacetophenone; O2; NADPH

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific R440A variant reconstructed during review and applied mutation signature R440A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NADPH

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant R440A

substrate: H+; 4'-Hydroxyacetophenone; O2; NADPH


sequence_source: UniProtKB:Q93TJ5 canonical sequence; row-specific K439F variant reconstructed during review


organism: Pseudomonas putida

sequence_source: UniProtKB:B7T912 FASTA/JSON direct accession check

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

assay_conditions_summary: pH 8; 303.15 K; buffer air-saturated; cofactor NADPH

column_label: TABLE 2. Kinetic parameters of HAPMO from P. putida JD1 (footnote a: All values were measured in Tris-HCl buffer (pH 8.0, 50 mM) at 30°C using a fixed NADPH concentration of 312 μM.) Block 'Aromatic compounds'; substrate row '2-Phenylpropionaldehyde'; column 'Km (uM)' = 21,241; column 'kcat (s^-1)' = 8.7; column 'kcat/Km (10^3 s^-1 M^-1)' = 0.4.

normalized_value_unit_evidence: Km: printed Table 2 cell 21,241 uM; 21241 / 1000 = 21.241 mM; the exported value is 21.24 mM. kcat: printed Table 2 cell 8.7 s^-1; already in s^-1, no conversion; the exported value is 8.7 s^(-1). kcat/Km: printed Table 2 cell 0.4 in the column headed 10^3 s^-1 M^-1; 1 unit of 10^3 M^-1 s^-1 is 1 mM^-1 s^-1, so the printed cell is 0.4 s^(-1)*mM^(-1); the exported value is 0.4096045197740113 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, block 'Aromatic compounds', substrate row '2-Phenylpropionaldehyde': Km = 21,241 uM; kcat = 8.7 s^-1; printed kcat/Km = 0.4 (column unit 10^3 s^-1 M^-1).


column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row '4-Aminoacetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 5.6; column 'kcat (s-1)' = 8.2; column 'kcat/Km (10^3 s-1 . M-1)' = 1,450; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 5.6 uM for the substrate row '4-Aminoacetophenone'; 5.6 / 1000 = 0.0056 mM; the exported value is 0.0056 mM. kcat: printed Table 2 cell 8.2 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 8.2 s^(-1). kcat/Km: printed Table 2 cell 1,450 in the column head unit 10^3 s^-1 M^-1, i.e. 1,450 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1,450 x 10^3 x 0.001 = 1450.0 s^-1 mM^-1; the exported value is 1464.2857142857142 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row '4-Aminoacetophenone': Km = 5.6 uM; kcat = 8.2 s^-1; printed kcat/Km = 1,450 in the column head unit 10^3 s^-1 M^-1.

table_label: Table 2: Kinetic parameters of HAPMO from P. putida JD1 (Applied and Environmental Microbiology 2009, 75(10):3106-3114)


column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row '3-Aminoacetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 287; column 'kcat (s-1)' = 1.0; column 'kcat/Km (10^3 s-1 . M-1)' = 3.3; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 287 uM for the substrate row '3-Aminoacetophenone'; 287 / 1000 = 0.287 mM; the exported value is 0.287 mM. kcat: printed Table 2 cell 1.0 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 1.0 s^(-1). kcat/Km: printed Table 2 cell 3.3 in the column head unit 10^3 s^-1 M^-1, i.e. 3.3 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.3 x 10^3 x 0.001 = 3.3 s^-1 mM^-1; the exported value is 3.4843205574912894 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row '3-Aminoacetophenone': Km = 287 uM; kcat = 1.0 s^-1; printed kcat/Km = 3.3 in the column head unit 10^3 s^-1 M^-1.


substrate_name: methyl-4-tolyl sulfide

sequence_source: UniProtKB REST FASTA accession B7T912

column_label: TABLE 2. Kinetic parameters of HAPMO from P. putida JD1 (footnote a: All values were measured in Tris-HCl buffer (pH 8.0, 50 mM) at 30°C using a fixed NADPH concentration of 312 μM.) Block 'Aromatic compounds'; substrate row 'Methyl-4-tolyl sulfide'; column 'Km (uM)' = 18,848; column 'kcat (s^-1)' = 20; column 'kcat/Km (10^3 s^-1 M^-1)' = 1.1.

normalized_value_unit_evidence: Km: printed Table 2 cell 18,848 uM; 18848 / 1000 = 18.848 mM; the exported value is 18.85 mM. kcat: printed Table 2 cell 20 s^-1; already in s^-1, no conversion; the exported value is 20.0 s^(-1). kcat/Km: printed Table 2 cell 1.1 in the column headed 10^3 s^-1 M^-1; 1 unit of 10^3 M^-1 s^-1 is 1 mM^-1 s^-1, so the printed cell is 1.1 s^(-1)*mM^(-1); the exported value is 1.0610079575596816 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, block 'Aromatic compounds', substrate row 'Methyl-4-tolyl sulfide': Km = 18,848 uM; kcat = 20 s^-1; printed kcat/Km = 1.1 (column unit 10^3 s^-1 M^-1).

substrate: methyl-4-tolyl sulfide


substrate_name: trifluoroacetophenone

substrate: trifluoroacetophenone


enzyme_display_name: dopamine beta-monooxygenase

organism: Bos taurus

sequence_source: UniProtKB REST FASTA accession P15101

enzyme: dopamine beta-monooxygenase


organism: Gallus gallus

substrate_name: Dopamine; O2; L-Ascorbate

sequence_source: UniProtKB REST FASTA accession Q9I9A1

substrate: Dopamine; O2; L-Ascorbate


enzyme_display_name: histone deacetylase

organism: Homo sapiens

substrate_name: Fluor de Lys

sequence_source: UniProtKB REST FASTA accession Q9UBN7

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q9UBN7 and applied mutation signature H216A to reconstruct the assayed variant sequence.

enzyme: histone deacetylase

substrate: Fluor de Lys


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q9UBN7 and applied mutation signature H611A to reconstruct the assayed variant sequence.


substrate_name: RHK(acetyl)K(acetyl)-fluorophore

sequence_source: UniProtKB REST FASTA accession Q9BY41

proof_lines:
presence of Zn(II), 25°C. pH 8.0
pH 8, 30Â°C
presence of Co(II), 25°C. pH 8.0

substrate: RHK(acetyl)K(acetyl)-fluorophore


substrate_name: Fluor de Lys HDAC substrate

sequence_source: UniProtKB REST FASTA accession Q8WUI4

substrate: Fluor de Lys HDAC substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q8WUI4 and applied mutation signature H843F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q8WUI4 and applied mutation signature H843A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q8WUI4 and applied mutation signature H843Y to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST FASTA accession Q13547


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q13547 and applied mutation signature F150A to reconstruct the assayed variant sequence.


substrate_name: Fluor de Lys HDAC8 substrate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q9BY41 and applied mutation signature D101L to reconstruct the assayed variant sequence.

substrate: Fluor de Lys HDAC8 substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98); reconstructed D101A variant after residue check and applied mutation signature D101A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98); reconstructed D101E variant after residue check and applied mutation signature D101E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98)

proof_lines:
Zn2+-wild type
Co2+-wild type


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98); reconstructed D101N variant after residue check and applied mutation signature D101N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98); reconstructed H143A variant after residue check and applied mutation signature H143A to reconstruct the assayed variant sequence.


substrate_name: GK(Ac)F

sequence_source: UniProtKB reviewed Q9UBN7 (HDAC6_HUMAN, Protein deacetylase HDAC6, Homo sapiens, UniProt EC 3.5.1.-)

substrate: GK(Ac)F


substrate_name: GGK(Ac)FF

proof_lines:
pH 7.4, 37°C, recombinant enzyme
catalytic domain II, pH 7.2, 23°C

substrate: GGK(Ac)FF


substrate_name: RYSSRRK(Ac)ARPYML

substrate: RYSSRRK(Ac)ARPYML


substrate_name: RGGK(Ac)FFR

substrate: RGGK(Ac)FFR


substrate_name: TYSRGGK(Ac)FFRRFP

substrate: TYSRGGK(Ac)FFRRFP


substrate_name: SQSEEEK(Ac)FFRRFP

substrate: SQSEEEK(Ac)FFRRFP


substrate_name: SRGGK(Ac)FFRR

substrate: SRGGK(Ac)FFRR


substrate_name: YSRGGK(Ac)FFRRF

substrate: YSRGGK(Ac)FFRRF


substrate_name: TYSRGGK(Ac)KSEESE

substrate: TYSRGGK(Ac)KSEESE


organism: Mus musculus

substrate_name: H2O; Acetylhistone

sequence_source: UniProtKB reviewed O09106 (HDAC1_MOUSE, Histone deacetylase 1, Mus musculus, EC 3.5.1.98)

substrate: H2O; Acetylhistone


enzyme_display_name: cytidine deaminase

organism: Mycobacterium tuberculosis

substrate_name: cytidine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WPH3 and applied mutation signature E47D to reconstruct the assayed variant sequence.

enzyme: cytidine deaminase

substrate: cytidine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WPH3 and applied mutation signature E47Q to reconstruct the assayed variant sequence.


organism: Trypanosoma brucei brucei

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


organism: Caulobacter vibrioides

substrate_name: L-threonine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95C to reconstruct the assayed variant sequence.

substrate: L-threonine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95M to reconstruct the assayed variant sequence.


substrate_name: L-Threonine

substrate: L-Threonine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95N/E96S to reconstruct the assayed variant sequence.


substrate_name: L-allo-Threonine

substrate: L-allo-Threonine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95W 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.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95G/E96G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95L to reconstruct the assayed variant sequence.


organism: Plasmodium falciparum

sequence_source: UniProtKB Q7K6A1 direct REST lookup


organism: Schistosoma mansoni

sequence_source: UniProtKB A5H660 direct REST lookup

proof_lines: presence of 5 microM inhibitor 5-[(7-bromo-2-phenyl-2,3-dihydro-4H-thieno[3,2-b]indol-4-yl)methyl]-N-hydroxythiophene-2-carboxamide, pH 8, 30°C

proof_lines: presence of 5 microM inhibitor 5-((2-(3-chlorophenyl)-1-methylspiro[indoline-3,4-piperidin]-1-yl)methyl)-N-hydroxythiophene-2-carboxamide, pH 8, 30°C


organism: Zea mays

substrate_name: Acetylhistone; H2O; Acetylhistone; H2O; Histone; Acetate; H2O; Acetylhistone

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


substrate_name: cytidine; deoxycytidine

sequence_source: UniProtKB P19079 direct REST lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB P19079 direct REST lookup and applied mutation signature R56A to reconstruct the assayed variant sequence.

proof_lines:
pH 7.6, 25°C, mutant enzyme R56A
pH 7.8, 25°C, mutant enzyme R56A

substrate: cytidine; deoxycytidine


substrate_name: deoxycytidine; cytidine

proof_lines:
pH 7.8, 25°C, wild-type enzyme
pH 7.6, 25°C, wild-type enzyme

substrate: deoxycytidine; cytidine


sequence_variant_note: Resolved canonical sequence from UniProtKB P19079 direct REST lookup and applied mutation signature R56Q to reconstruct the assayed variant sequence.

proof_lines:
pH 7.8, 25°C, mutant enzyme R56Q
pH 7.6, 25°C, mutant enzyme R56Q


source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.8
Raw SKiD Env: Temp=25°C, pH=7.6

source: skid


substrate_name: H2O; Cytidine; H2O; Cytidine; NH3; Uridine; H2O; 2'-Deoxycytidine; 2'-Deoxycytidine; 2'-Deoxyuridine; Cytarabine; H2O; Cytarabine; Arabinofuranosyluracil

sequence_source: UniProtKB P32320 direct REST lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB P32320 direct REST lookup and applied mutation signature R68G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cytidine deaminase(Enzyme) mutant R68G


substrate_name: H2O; Cytidine; H2O; Cytidine; NH3; Uridine; H2O; 2'-Deoxycytidine; 2'-Deoxycytidine; 2'-Deoxyuridine; Cytarabine; H2O; Cytarabine; Arabinofuranosyluracil; 2'-Deoxycytidine; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB P32320 direct REST lookup and applied mutation signature R68Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cytidine deaminase(Enzyme) mutant R68Q


substrate_name: Cytidine; H2O; Cytidine; H2O; Uridine; NH3; H2O; 2'-Deoxycytidine; 2'-Deoxycytidine; 2'-Deoxyuridine; Cytarabine; H2O; Cytarabine; Arabinofuranosyluracil; 2'-Deoxycytidine; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB P32320 direct REST lookup and applied mutation signature Y60G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cytidine deaminase(Enzyme) mutant Y60G


substrate_name: H2O; Cytidine; H2O; Cytidine; NH3; Uridine; 2'-Deoxycytidine; H2O; 2'-Deoxycytidine; 2'-Deoxyuridine; H2O; Cytarabine; Cytarabine; Arabinofuranosyluracil; H2O; 2'-Deoxycytidine

proof_lines: substrate 4-amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]-5-methylthieno[3,4-d]pyrimidin-2(1H)-one, pH 7.4, 24°C


substrate_name: 2'-deoxycytidine; cytidine

source_db: brenda,skid

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

sequence_source: UniProtKB P9WPH3 direct REST lookup

proof_lines:
in 50 mM Tris-HCl buffer pH 7.5 at 25°C
Raw SKiD Env: Temp=25°C, pH=7.5

source_databases_merged: brenda skid

substrate: 2'-deoxycytidine; cytidine

source: brenda,skid


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WPH3 direct REST lookup and applied mutation signature E47Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WPH3 direct REST lookup and applied mutation signature E47D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9A3V8 canonical sequence with reviewed mutation reconstruction and applied mutation signature D95Y to reconstruct the assayed variant sequence.


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P75823 and applied mutation signature F87D to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-Threonine', enzyme heading 'F87D'; the enzyme heading spans three numeric columns: column 'kcat' = 19.8, column 'Km' = 24.9, column 'kcat/Km' = 0.79. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 19.8 min^-1; 19.8 / 60 = 0.33 s^-1; the exported value is 0.33 s^(-1). km: printed Table 4 cell 24.9 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 24.9 mM. kcat/Km: printed Table 4 cell 0.79 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.79 / 60 = 0.0131666667 s^-1 mM^-1; the exported value is 0.013253012048192772 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-Threonine', enzyme column 'F87D': kcat = 19.8 min^-1; Km = 24.9 mM; printed kcat/Km = 0.79 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P75823 and applied mutation signature H83F/H126F to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-Threonine', enzyme heading 'H83F/H126F'; the enzyme heading spans three numeric columns: column 'kcat' = 0.44, column 'Km' = 21, column 'kcat/Km' = 0.02. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.44 min^-1; 0.44 / 60 = 0.0073333333 s^-1; the exported value is 0.0073 s^(-1). km: printed Table 4 cell 21 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 21.0 mM. kcat/Km: printed Table 4 cell 0.02 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.02 / 60 = 0.0003333333 s^-1 mM^-1; the exported value is 0.0003476190476190476 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-Threonine', enzyme column 'H83F/H126F': kcat = 0.44 min^-1; Km = 21 mM; printed kcat/Km = 0.02 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-allo-Threonine', enzyme heading 'F87D'; the enzyme heading spans three numeric columns: column 'kcat' = 117, column 'Km' = 0.41, column 'kcat/Km' = 285. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 117 min^-1; 117 / 60 = 1.95 s^-1; the exported value is 1.95 s^(-1). km: printed Table 4 cell 0.41 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.41 mM. kcat/Km: printed Table 4 cell 285 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 285 / 60 = 4.75 s^-1 mM^-1; the exported value is 4.7560975609756095 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-allo-Threonine', enzyme column 'F87D': kcat = 117 min^-1; Km = 0.41 mM; printed kcat/Km = 285 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


sequence_source: UniProt REST P75823 canonical sequence


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P75823 and applied mutation signature F87A to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-allo-Threonine', enzyme heading 'F87A'; the enzyme heading spans three numeric columns: column 'kcat' = 160, column 'Km' = 0.31, column 'kcat/Km' = 516. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 160 min^-1; 160 / 60 = 2.6666666667 s^-1; the exported value is 2.7 s^(-1). km: printed Table 4 cell 0.31 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.31 mM. kcat/Km: printed Table 4 cell 516 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 516 / 60 = 8.6 s^-1 mM^-1; the exported value is 8.70967741935484 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-allo-Threonine', enzyme column 'F87A': kcat = 160 min^-1; Km = 0.31 mM; printed kcat/Km = 516 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


proof_lines:
pH 7.2, 30°C, recombinant enzyme
pH 7.0, 37°C


substrate_name: DL-threo-phenylserine

proof_lines:
pH 8.0, 30°C
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=30°C, pH=8

substrate: DL-threo-phenylserine


organism: Glycine max

substrate_name: L-phenylserine

proof_lines: pH 7.5, temperature not specified in the publication, enzyme SHMT8 from Glycine max cv. Essex

substrate: L-phenylserine


substrate_name: Unknown

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProt REST A0A166JNM8 canonical sequence with reviewed mutation reconstruction and applied mutation signature Y312E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST A0A166JNM8 canonical sequence with reviewed mutation reconstruction and applied mutation signature A9L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST A0A166JNM8 canonical sequence with reviewed mutation reconstruction and applied mutation signature H133Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST A0A166JNM8 canonical sequence with reviewed mutation reconstruction and applied mutation signature Y13Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST A0A166JNM8 canonical sequence with reviewed mutation reconstruction and applied mutation signature Y13R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST A0A166JNM8 canonical sequence with reviewed mutation reconstruction and applied mutation signature Y312R to reconstruct the assayed variant sequence.


substrate_name: benzaldehyde

sequence_source: UniProtKB:B7T912 direct REST/FASTA lookup

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

proof_lines: 312 microM NADPH, 50 mM Tris-HCl, pH 8.0, 30°C

substrate: benzaldehyde


column_label: TABLE 2. Kinetic parameters of HAPMO from P. putida JD1 (footnote a: All values were measured in Tris-HCl buffer (pH 8.0, 50 mM) at 30°C using a fixed NADPH concentration of 312 μM.) Block 'Aromatic compounds'; substrate row 'Benzaldehyde'; column 'Km (uM)' = 275; column 'kcat (s^-1)' = 2.2; column 'kcat/Km (10^3 s^-1 M^-1)' = 8.1.

normalized_value_unit_evidence: Km: printed Table 2 cell 275 uM; 275 / 1000 = 0.275 mM; the exported value is 0.257 mM. kcat: printed Table 2 cell 2.2 s^-1; already in s^-1, no conversion; the exported value is 2.2 s^(-1). kcat/Km: printed Table 2 cell 8.1 in the column headed 10^3 s^-1 M^-1; 1 unit of 10^3 M^-1 s^-1 is 1 mM^-1 s^-1, so the printed cell is 8.1 s^(-1)*mM^(-1); the exported value is 8.560311284046692 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, block 'Aromatic compounds', substrate row 'Benzaldehyde': Km = 275 uM; kcat = 2.2 s^-1; printed kcat/Km = 8.1 (column unit 10^3 s^-1 M^-1).


smiles: CCCCCCCCC(C)=O


column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row '3-Methoxyacetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 88.5; column 'kcat (s-1)' = 0.4; column 'kcat/Km (10^3 s-1 . M-1)' = 4.3; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 88.5 uM for the substrate row '3-Methoxyacetophenone'; 88.5 / 1000 = 0.0885 mM; the exported value is 0.0885 mM. kcat: printed Table 2 cell 0.4 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 0.4 s^(-1). kcat/Km: printed Table 2 cell 4.3 in the column head unit 10^3 s^-1 M^-1, i.e. 4.3 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.3 x 10^3 x 0.001 = 4.3 s^-1 mM^-1; the exported value is 4.519774011299435 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row '3-Methoxyacetophenone': Km = 88.5 uM; kcat = 0.4 s^-1; printed kcat/Km = 4.3 in the column head unit 10^3 s^-1 M^-1.


column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row '4-Methoxyacetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 199; column 'kcat (s-1)' = 1.2; column 'kcat/Km (10^3 s-1 . M-1)' = 5.9; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 199 uM for the substrate row '4-Methoxyacetophenone'; 199 / 1000 = 0.199 mM; the exported value is 0.199 mM. kcat: printed Table 2 cell 1.2 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 1.2 s^(-1). kcat/Km: printed Table 2 cell 5.9 in the column head unit 10^3 s^-1 M^-1, i.e. 5.9 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.9 x 10^3 x 0.001 = 5.9 s^-1 mM^-1; the exported value is 6.030150753768844 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row '4-Methoxyacetophenone': Km = 199 uM; kcat = 1.2 s^-1; printed kcat/Km = 5.9 in the column head unit 10^3 s^-1 M^-1.


substrate_name: acetophenone

column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row 'Acetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 393; column 'kcat (s-1)' = 16.3; column 'kcat/Km (10^3 s-1 . M-1)' = 41.6; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 393 uM for the substrate row 'Acetophenone'; 393 / 1000 = 0.393 mM; the exported value is 0.393 mM. kcat: printed Table 2 cell 16.3 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 16.3 s^(-1). kcat/Km: printed Table 2 cell 41.6 in the column head unit 10^3 s^-1 M^-1, i.e. 41.6 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 41.6 x 10^3 x 0.001 = 41.6 s^-1 mM^-1; the exported value is 41.475826972010175 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row 'Acetophenone': Km = 393 uM; kcat = 16.3 s^-1; printed kcat/Km = 41.6 in the column head unit 10^3 s^-1 M^-1.

row_label: Table 2, substrate row 'Acetophenone'

substrate: acetophenone


substrate_name: propiophenone

column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row 'Propiophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 89.4; column 'kcat (s-1)' = 2.6; column 'kcat/Km (10^3 s-1 . M-1)' = 28.5; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 89.4 uM for the substrate row 'Propiophenone'; 89.4 / 1000 = 0.0894 mM; the exported value is 0.0894 mM. kcat: printed Table 2 cell 2.6 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 2.6 s^(-1). kcat/Km: printed Table 2 cell 28.5 in the column head unit 10^3 s^-1 M^-1, i.e. 28.5 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 28.5 x 10^3 x 0.001 = 28.5 s^-1 mM^-1; the exported value is 29.082774049217004 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row 'Propiophenone': Km = 89.4 uM; kcat = 2.6 s^-1; printed kcat/Km = 28.5 in the column head unit 10^3 s^-1 M^-1.

row_label: Table 2, substrate row 'Propiophenone'

substrate: propiophenone


column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row '3'-Hydroxyacetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 246; column 'kcat (s-1)' = 8.1; column 'kcat/Km (10^3 s-1 . M-1)' = 32.7; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 246 uM for the substrate row '3'-Hydroxyacetophenone'; 246 / 1000 = 0.246 mM; the exported value is 0.246 mM. kcat: printed Table 2 cell 8.1 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 8.1 s^(-1). kcat/Km: printed Table 2 cell 32.7 in the column head unit 10^3 s^-1 M^-1, i.e. 32.7 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 32.7 x 10^3 x 0.001 = 32.7 s^-1 mM^-1; the exported value is 32.92682926829268 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row '3'-Hydroxyacetophenone': Km = 246 uM; kcat = 8.1 s^-1; printed kcat/Km = 32.7 in the column head unit 10^3 s^-1 M^-1.


substrate_name: butyrophenone

column_label: TABLE 2. Kinetic parameters of HAPMO from P. putida JD1 (footnote a: All values were measured in Tris-HCl buffer (pH 8.0, 50 mM) at 30°C using a fixed NADPH concentration of 312 μM.) Block 'Aromatic compounds'; substrate row 'Butyrophenone'; column 'Km (uM)' = 30,746; column 'kcat (s^-1)' = 4.9; column 'kcat/Km (10^3 s^-1 M^-1)' = 0.2.

normalized_value_unit_evidence: Km: printed Table 2 cell 30,746 uM; 30746 / 1000 = 30.746 mM; the exported value is 30.75 mM. kcat: printed Table 2 cell 4.9 s^-1; already in s^-1, no conversion; the exported value is 4.9 s^(-1). kcat/Km: printed Table 2 cell 0.2 in the column headed 10^3 s^-1 M^-1; 1 unit of 10^3 M^-1 s^-1 is 1 mM^-1 s^-1, so the printed cell is 0.2 s^(-1)*mM^(-1); the exported value is 0.15934959349593497 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, block 'Aromatic compounds', substrate row 'Butyrophenone': Km = 30,746 uM; kcat = 4.9 s^-1; printed kcat/Km = 0.2 (column unit 10^3 s^-1 M^-1).

substrate: butyrophenone


column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row '4-Methylacetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 241; column 'kcat (s-1)' = 4.4; column 'kcat/Km (10^3 s-1 . M-1)' = 18.5; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 241 uM for the substrate row '4-Methylacetophenone'; 241 / 1000 = 0.241 mM; the exported value is 0.241 mM. kcat: printed Table 2 cell 4.4 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 4.4 s^(-1). kcat/Km: printed Table 2 cell 18.5 in the column head unit 10^3 s^-1 M^-1, i.e. 18.5 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 18.5 x 10^3 x 0.001 = 18.5 s^-1 mM^-1; the exported value is 18.257261410788384 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row '4-Methylacetophenone': Km = 241 uM; kcat = 4.4 s^-1; printed kcat/Km = 18.5 in the column head unit 10^3 s^-1 M^-1.


column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row '4-Nitroacetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 313; column 'kcat (s-1)' = 2.6; column 'kcat/Km (10^3 s-1 . M-1)' = 8.4; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 313 uM for the substrate row '4-Nitroacetophenone'; 313 / 1000 = 0.313 mM; the exported value is 0.313 mM. kcat: printed Table 2 cell 2.6 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 2.6 s^(-1). kcat/Km: printed Table 2 cell 8.4 in the column head unit 10^3 s^-1 M^-1, i.e. 8.4 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.4 x 10^3 x 0.001 = 8.4 s^-1 mM^-1; the exported value is 8.30670926517572 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row '4-Nitroacetophenone': Km = 313 uM; kcat = 2.6 s^-1; printed kcat/Km = 8.4 in the column head unit 10^3 s^-1 M^-1.


organism: Acetivibrio thermocellus

substrate_name: sedoheptulose 7-phosphate

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

assay_conditions_summary: pH 7; 328.15 K; cofactor ATP

substrate: sedoheptulose 7-phosphate


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


organism: Amycolatopsis methanolica

substrate_name: Fructose 6-phosphate; Diphosphate

substrate: Fructose 6-phosphate; Diphosphate


organism: Borrelia burgdorferi


substrate_name: diphosphate

substrate: diphosphate


organism: Dictyoglomus thermophilum

substrate_name: D-Fructose 6-phosphate; Diphosphate

substrate: D-Fructose 6-phosphate; Diphosphate


organism: Entamoeba histolytica


substrate_name: Diphosphate; D-Fructose 6-phosphate

substrate: Diphosphate; D-Fructose 6-phosphate


substrate_name: Phosphate; D-Fructose 1,6-bisphosphate

substrate: Phosphate; D-Fructose 1,6-bisphosphate


substrate_name: Diphosphate; Fructose 6-phosphate

substrate: Diphosphate; Fructose 6-phosphate


substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: recombinant His-tagged enzyme, pH 7.0, 25°C

substrate: D-fructose 6-phosphate


organism: Methylobacterium nodulans


organism: Naegleria fowleri


organism: Porphyromonas gingivalis


organism: Propionibacterium freudenreichii subsp. shermanii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K148M to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: cytidine

substrate: cytidine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29495 and applied mutation signature R90A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: diphosphate---fructose-6-phosphate 1-phosphotransferase(Enzyme) mutant R90A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29495 and applied mutation signature R310A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29495 and applied mutation signature R326A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphate---fructose-6-phosphate 1-phosphotransferase(Enzyme) mutant R326A


proof_lines: SABIO-RK modifier species: diphosphate---fructose-6-phosphate 1-phosphotransferase(Enzyme) mutant R310A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29495 and applied mutation signature R186A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphate---fructose-6-phosphate 1-phosphotransferase(Enzyme) mutant R186A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29495 and applied mutation signature R78A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29495 and applied mutation signature K315A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29495 and applied mutation signature K148M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphate---fructose-6-phosphate 1-phosphotransferase(Enzyme) mutant K148M


proof_lines: SABIO-RK modifier species: diphosphate---fructose-6-phosphate 1-phosphotransferase(Enzyme) mutant K315A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29495 and applied mutation signature K315R to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: diphosphate---fructose-6-phosphate 1-phosphotransferase(Enzyme) mutant K315R


proof_lines: SABIO-RK modifier species: diphosphate---fructose-6-phosphate 1-phosphotransferase(Enzyme) mutant R78A


sequence_source: UniProtKB P29495 direct FASTA/accession lookup


organism: Pseudoclostridium thermosuccinogenes

protein_accession_database: NCBI Protein

sequence_source: NCBI Protein PNT94038.1 direct FASTA/accession lookup

assay_conditions_summary: pH 7; 328.15 K; cofactor NADH

column_label: Table label: Table 1. Kinetics of the PFKs tested. Row: CDQ83_11320 C.ts PPi-PFK | F6P (cofactor column: PPi). Columns read: K m (mM) cell 0.070, k cat (s^-1) cell 182, k cat / K m (s^-1 M^-1) cell 2.6 x 10^6. metric: kcat; raw value: 182; raw unit: s^-1; normalized value: 182.0 s^(-1); metric: Km; raw value: 0.070; raw unit: mM; normalized value: 0.07 mM; metric: kcat/Km; raw value: 2.6 x 10^6; raw unit: s^-1 M^-1; normalized value: 2600.0 s^-1 mM^-1; assay condition: 6-phosphofructokinase coupled assay carried out at 55 °C in 50 mM MOPS (pH 7.0 at room temperature) with 5 mM MgCl2, 1 mM pyrophosphate, 0.15 mM NADH, 4 units/ml rabbit aldolase, and 2 units/ml rabbit glycerol-3-phosphate dehydrogenase. Export row conditions: pH 7; 328.15 K.

normalized_value_unit_evidence: Table 1 row CDQ83_11320 C.ts PPi-PFK / F6P: kcat 182 s^-1 = 182.0 s^(-1); Km 0.070 mM = 0.07 mM (already in mM); kcat/Km 2.6 x 10^6 s^-1 M^-1 = 2600.0 s^-1 mM^-1 (1 s^-1 M^-1 = 0.001 s^-1 mM^-1). In the flattened HTML asset the multiplication sign renders as ×, superscript exponents and minus signs are flattened, and subscripts are separated, so the printed cell `2.6 × 10 6` is the paper's 2.6 x 10^6 s^-1 M^-1, the unit header `m m` is the paper's small-caps mM, `s − 1` is s^-1, `s − 1 m − 1` is s^-1 M^-1, and `PP i -PFK` is the paper's PPi-PFK.

raw_value_unit_evidence: Table 1. Kinetics of the PFKs tested | metric header row of Table 1: K m k cat n k cat / K m ; unit header row: m m s − 1 s − 1 m − 1 (K m in mM, k cat in s^-1, k cat / K m in s^-1 M^-1) | row: CDQ83_11320 C.ts PP i -PFK PP i F6P 0.070 182 NA a 2.6 × 10 6 | cells read: K m = 0.070 mM; k cat = 182 s^-1; n = NA (Hill equation not applicable to this row, table footnote a); k cat / K m = 2.6 x 10^6 s^-1 M^-1

row_label: CDQ83_11320 C.ts PPi-PFK | F6P

table_label: Table 1. Kinetics of the PFKs tested


column_label: Table 1; row CDQ83_11320 C.ts PPi-PFK; cofactor PPi; substrate S7P; Km cell 0.11 mM; kcat cell 49 s^-1; kcat/Km cell 0.46 x 10^6 s^-1 M^-1; assay at 55 C and pH 7.0.

raw_value_unit_evidence: Table 1 CDQ83_11320 C.ts PPi-PFK S7P cells: Km 0.11 mM; kcat 49 s^-1; kcat/Km 0.46 x 10^6 s^-1 M^-1.

row_label: CDQ83_11320 C.ts PPi-PFK | sedoheptulose 7-phosphate


organism: Solanum tuberosum


organism: Spirochaeta thermophila

sequence_source: UniProtKB Q9EZ02 direct FASTA/accession lookup


organism: Thermoproteus tenax

sequence_source: UniProtKB G4RK16 direct FASTA/accession lookup


organism: Triticum aestivum


organism: Xanthomonas campestris pv. campestris

sequence_source: UniProtKB B0RP51 direct FASTA/accession lookup


organism: Pseudomonas putida

sequence_variant_note: Resolved canonical sequence from UniProtKB A0A166JNM8 canonical sequence with row-specific Y13K substitution reconstructed after coordinate check and applied mutation signature Y13K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A166JNM8 canonical sequence with row-specific H133W substitution reconstructed after coordinate check and applied mutation signature H133W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A166JNM8 canonical sequence with row-specific Y13C substitution reconstructed after coordinate check and applied mutation signature Y13C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A166JNM8 canonical sequence with row-specific E147D substitution reconstructed after coordinate check and applied mutation signature E147D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A166JNM8 canonical sequence with row-specific A9V substitution reconstructed after coordinate check and applied mutation signature A9V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A166JNM8 canonical sequence with row-specific H133N substitution reconstructed after coordinate check and applied mutation signature H133N to reconstruct the assayed variant sequence.


organism: Homo sapiens

substrate_name: tyramine

source_db: uniprot

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

substrate: tyramine

source: uniprot


organism: Amycolatopsis methanolica

substrate_name: phosphate

substrate: phosphate


organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)


organism: Dictyoglomus thermophilum


organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)


organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6)


organism: Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)


organism: Methylomonas methanica


organism: Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z)


organism: Naegleria fowleri


organism: Porphyromonas gingivalis


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A166JNM8 and applied mutation signature Y312K to reconstruct the assayed variant sequence.


organism: Pseudomonas sp.


organism: Saccharomyces cerevisiae

substrate_name: L-Threonine

substrate: L-Threonine


substrate_name: L-allo-Threonine

substrate: L-allo-Threonine


organism: Thermoplasma acidophilum

substrate_name: L-threonine

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

substrate: L-threonine


organism: Dictyostelium discoideum

sequence_source: UniProtKB Q54RP0 direct REST lookup


substrate_name: UDP-galactose

sequence_variant_note: Resolved canonical sequence from UniProtKB P16442 direct REST lookup; P234S reconstructed by single-residue substitution and applied mutation signature P234S to reconstruct the assayed variant sequence.

substrate: UDP-galactose


sequence_source: UniProtKB P16442 direct REST lookup

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


proof_lines:
37°C, pH 7.0, wild-type enzyme S185N
37°C, pH 7.0, wild-type enzyme S185C
wild-type enzyme


substrate_name: UDP-N-acetylgalactosamine

sequence_variant_note: Resolved canonical sequence from UniProtKB P16442 direct REST lookup; M214T reconstructed by single-residue substitution and applied mutation signature M214T to reconstruct the assayed variant sequence.

substrate: UDP-N-acetylgalactosamine


sequence_variant_note: Resolved canonical sequence from UniProtKB P16442 direct REST lookup; M214V reconstructed by single-residue substitution and applied mutation signature M214V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P16442 direct REST lookup; M214R reconstructed by single-residue substitution and applied mutation signature M214R to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB P16442 direct REST lookup; E303A reconstructed by single-residue substitution and applied mutation signature E303A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P16442 direct REST lookup; E303C reconstructed by single-residue substitution and applied mutation signature E303C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P16442 direct REST lookup; E303D reconstructed by single-residue substitution and applied mutation signature E303D to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

substrate_name: alpha-D-glucosamine 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB accession P14192 direct lookup; canonical sequence mutated according to selected source signature C380A and applied mutation signature C380A to reconstruct the assayed variant sequence.

substrate: alpha-D-glucosamine 1-phosphate


substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB accession P14192 direct lookup; canonical sequence mutated according to selected source signature C380A/C405S and applied mutation signature C380A/C405S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 355.15 K; cofactor CoA

substrate: acetyl-CoA


organism: Escherichia coli

substrate_name: D-Glucosamine 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB accession P0ACC7 direct lookup; canonical sequence mutated according to selected source signature R18A and applied mutation signature R18A to reconstruct the assayed variant sequence.

substrate: D-Glucosamine 1-phosphate


substrate_name: Acetyl-CoA; D-Glucosamine 1-phosphate

sequence_source: UniProtKB accession P0ACC7 direct lookup; source construct is tagged/truncated and exact full variant sequence remains unresolved

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

mutation_type: truncation

assay_conditions_summary: cofactor CoA

proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant truncated His6-tagged

substrate: Acetyl-CoA; D-Glucosamine 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB accession P0ACC7 direct lookup; canonical sequence mutated according to selected source signature K25A and applied mutation signature K25A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB accession P0ACC7 direct lookup; canonical sequence mutated according to selected source signature G14A and applied mutation signature G14A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB accession P0ACC7 direct lookup; selected source notes a His6-tagged variant

proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant K25A His6-tagged


substrate_name: D-Glucosamine 1-phosphate; Acetyl-CoA

sequence_source: UniProtKB accession P0ACC7 direct FASTA lookup; selected SABIO group has no captured mutation signature

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

substrate: D-Glucosamine 1-phosphate; Acetyl-CoA


proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant R18A His6-tagged


proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant G14A His6-tagged


sequence_source: UniProtKB accession P0ACC7 direct lookup; selected SABIO records merge several tagged deletion constructs

proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant GlmU-del78 N-terminal His6-tag

proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant GlmU-del130 N-terminal His6-tag

proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant GlmU-del227 N-terminal His6-tag


substrate_name: Acetyl-CoA

sequence_source: UniProtKB accession P0ACC7 direct FASTA lookup

assay_conditions_summary: pH 8.2; 310.15 K; cofactor CoA

substrate: Acetyl-CoA


proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant GlmU C307A N-terminal His6-tagged


proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant GlmU C385A N-terminal His6-tagged


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0ACC7 and applied mutation signature C307A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.2; 310.15 K; buffer 20 mM potassium phosphate; cofactor CoA

column_label: Table 1 (page 4800), decoded plain-numeral transcription, row 'His6-GlmU C307A': column 'Km (mM) Acetyl-CoA' = 0.09; column 'kcat (s^-1) Acetyltransferase' = 1. Table 1 prints no kcat/Km column for any row.

normalized_value_unit_evidence: Km: printed cell 0.09 in the column 'Km (mM) Acetyl-CoA', so the printed unit is mM and no unit conversion applies; the exported km is 0.09 mM. kcat: printed cell 1 in the column 'kcat (s^-1) Acetyltransferase', so the printed unit is s^-1 and no unit conversion applies; the exported kcat is 1.0 s^(-1). kcat/Km: Table 1 prints no kcat/Km column, so the exported kcat_over_km is the same-measurement quotient of this row's own two printed cells, 1 / 0.09 = 11.11111111111111 s^(-1)*mM^(-1), which is the exported value.

raw_value_unit_evidence: Table 1 (decoded plain-numeral transcription), row 'His6-GlmU C307A': column 'Km (mM) Acetyl-CoA' = 0.09; column 'kcat (s^-1) Acetyltransferase' = 1. Table 1 prints no kcat/Km column.

row_label: Table 1, row 'His6-GlmU C307A', catalog substrate Acetyl-CoA

table_label: TABLE 1. Kinetic parameters of wild-type and mutant GlmU enzymes


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0ACC7 and applied mutation signature C296A to reconstruct the assayed variant sequence.

column_label: Table 1 (page 4800), decoded plain-numeral transcription, row 'His6-GlmU C296A': column 'Km (mM) GlcN-1-P' = 0.07; column 'kcat (s^-1) Acetyltransferase' = 1,350. Table 1 prints no kcat/Km column for any row.

normalized_value_unit_evidence: Km: printed cell 0.07 in the column 'Km (mM) GlcN-1-P', so the printed unit is mM and no unit conversion applies; the exported km is 0.07 mM. kcat: printed cell 1,350 in the column 'kcat (s^-1) Acetyltransferase', so the printed unit is s^-1 and no unit conversion applies; the exported kcat is 1350.0 s^(-1). kcat/Km: Table 1 prints no kcat/Km column, so the exported kcat_over_km is the same-measurement quotient of this row's own two printed cells, 1,350 / 0.07 = 19285.714285714283 s^(-1)*mM^(-1), which is the exported value.

raw_value_unit_evidence: Table 1 (decoded plain-numeral transcription), row 'His6-GlmU C296A': column 'Km (mM) GlcN-1-P' = 0.07; column 'kcat (s^-1) Acetyltransferase' = 1,350. Table 1 prints no kcat/Km column.

row_label: Table 1, row 'His6-GlmU C296A', catalog substrate GlcN-1-P


sequence_variant_note: Resolved canonical sequence from UniProtKB P14192 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature C380A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: mutant enzyme C380A, at pH 8.0 and 37Â°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P14192 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature C405S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C405S, at pH 8.0 and 37Â°C


sequence_source: UniProtKB P14192 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present


sequence_variant_note: Resolved canonical sequence from UniProtKB P14192 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature V385C/C405S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P14192 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature C405A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C405A, at pH 8.0 and 37Â°C


proof_lines: mutant enzyme V385C/C405S, at pH 8.0 and 37Â°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P14192 direct REST lookup; variant sequence reconstructed from canonical sequence when mutation_signature is present and applied mutation signature C380A/C405S to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme C380A/C405S, at pH 8.0 and 37Â°C


organism: Unknown

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