sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95W to reconstruct the assayed variant sequence.


enzyme_display_name: low-specificity L-threonine aldolase

organism: Caulobacter vibrioides

substrate_name: L-threonine

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

enzyme: low-specificity L-threonine aldolase

substrate: L-threonine

source: brenda


substrate_name: L-allo-Threonine

source_db: oed

verification_status: unverified

mutation_type: substitution

data_origin: experimental

substrate: L-allo-Threonine

status: unverified

source: oed


substrate_name: L-Threonine

kcat_over_km_origin: calculated

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

substrate: L-Threonine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95N/E96S 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.


enzyme_display_name: histone deacetylase

organism: Plasmodium falciparum

verification_status: corrected

sequence_source: UniProtKB Q7K6A1 direct REST lookup

enzyme: histone deacetylase

status: corrected


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

kcat_display: Not reported

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

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


enzyme_display_name: cytidine deaminase

organism: Bacillus subtilis

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

enzyme: cytidine deaminase

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


organism: Homo sapiens

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

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

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


organism: Mycobacterium tuberculosis

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


substrate_name: cytidine

substrate: cytidine


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.

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 '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.

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)


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

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Pseudomonas putida

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.


enzyme_display_name: 4-hydroxyacetophenone monooxygenase

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.

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

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

enzyme: 4-hydroxyacetophenone monooxygenase

substrate: benzaldehyde


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 '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.

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 '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

assay_conditions_summary: cofactor ATP

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

verification_status: verified

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

status: verified


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.


enzyme_display_name: dopamine beta-monooxygenase

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.

enzyme: dopamine beta-monooxygenase

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 UniProtKB accession P0ACC7 direct lookup; canonical sequence mutated according to selected source signature C307A and applied mutation signature C307A 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 C296A and applied mutation signature C296A 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 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.


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

proof_lines: kcat is 69.7 sec(-1) for GalN-1-P acetyltransferase activity. kcat is 123.2 sec(-1) for GlcN-1-P acetyltransferase activity.


substrate_name: UDP-Gal

proof_lines: The catalytic efficiency with the presumed natural substrate Fuc-alpha-1,2-Gal-beta-1,3-GlcNAc-alpha-1-Skp1 is 21-fold and 21000-fold higher than that of the synthetic substrates Fuc-alpha-1,2-Gal-beta-1-pNP and Fuc-alpha-1-Bn, respectively

substrate: UDP-Gal


organism: Homo sapiens

substrate_name: type I H-antigen (A transferase)

proof_lines: kcat is 1.3 sec(-1) for type I H-antigen (A transferase) (PubMed:16326711). kcat is 0.5 sec(-1) for type I H-antigen (B transferase) (PubMed:16326711). kcat is 1.8 sec(-1) for type II H-antigen (A transferase) (PubMed:16326711). kcat is 1.2

substrate: type I H-antigen (A transferase)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 4.8 and 3.5 sec(-1) with cytidine and 2-deoxycytidine as substrate, respectively.


organism: Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)

substrate_name: L-serine (at pH 7.5 and 70 degrees Celsius)

proof_lines: kcat is 18.7 sec(-1) for the L-serine hydroxymethyltransferase reaction, 2.3 sec(-1) for the L-threonine cleavage, and 18.0 sec(-1) for the L-allo-threonine cleavage, at 70 degrees Celsius. In the THF-independent aldolase reaction, the rate


organism: Mycobacterium tuberculosis

sequence_source: UniProt direct accession lookup: A5U161 / GLMU_MYCTA


sequence_source: UniProt direct accession lookup: P9WMN2 / GLMU_MYCTO


organism: Sulfurisphaera tokodaii

sequence_source: UniProt direct accession lookup: Q975F9 / S1PNA_SULTO

assay_conditions_summary: pH 7.5; 353.15 K; cofactor CoA


substrate_name: alpha-D-galactosamine 1-phosphate

mutation_signature: deletion mutant D011 of ST0452 protein

mutation_type: deletion

proof_lines: pH 7.5, 80°C, deletion mutant D011 of ST0452 protein

substrate: alpha-D-galactosamine 1-phosphate


mutation_signature: deletion mutant D005 of ST0452 protein

proof_lines: pH 7.5, 80°C, deletion mutant D005 of ST0452 protein


sequence_source: Reconstructed from UniProt Q975F9 canonical sequence using selected note: DC011 deletion of the C-terminal 11 residues of ST0452

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

proof_lines: pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein


proof_lines:
pH 7.5, 80°C, wild-type ST0452 protein
pH 7.5, 80°C, wild-type enzyme


sequence_source: Reconstructed from UniProt Q975F9 canonical sequence using selected note: DC005 deletion of the C-terminal 5 residues of ST0452

proof_lines: pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein


organism: Yersinia pestis

sequence_source: UniProt direct accession lookup: Q8Z9S7 / GLMU_YERPE


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


substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


organism: Pseudomonas fluorescens

proof_lines:
pH 7.5, 30°C
pH 8, 30°C
pH 7.5, 30°C, pH-dependent


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: above, pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, R339A mutant

substrate: NADPH


proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439F mutant


proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439A mutant


proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439N mutant


proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, K439P mutant


substrate_name: NADH

proof_lines: pH 7.5, 25°C, cosubstrate 4-hydroxyacetophenone, wild-type HAPMO

substrate: NADH


organism: Pseudomonas putida

proof_lines: pH 8, 30°C, 4-hydroxyacetophenone as substrate


organism: Bos taurus

proof_lines:
5 mM tyramine
in presence of tyramine
pH 6.0, 28°C, 1.0 mM tyramine


organism: Drosophila melanogaster

substrate_name: tyramine

proof_lines: at 10 mM ascorbate, 0.058 mM O2, pH 6 and 35°C

proof_lines: at 50 mM ascorbate, 1.04 mM O2, pH 6 and 35°C

substrate: tyramine


organism: Felis catus

substrate_name: ascorbate

proof_lines:
with or without Cu2+
in the absence of Cu2+
in the presence of Cu2+

substrate: ascorbate


organism: Gallus gallus

substrate_name: dopamine

substrate: dopamine


organism: Escherichia coli (strain K12)

substrate_name: N-acetylglucosamine 1-phosphate

substrate: N-acetylglucosamine 1-phosphate


substrate_name: GlcNAc-1-P (at pH 7.6)

assay_conditions_summary: pH 7.6; cofactor CoA

substrate: GlcNAc-1-P (at pH 7.6)


organism: Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1)

substrate_name: phosphate

substrate: phosphate


organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)


organism: Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)

substrate_name: diphosphate

substrate: diphosphate


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)


organism: Treponema pallidum (strain DSM 117211 / Nichols)


organism: Winmispira thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1)


organism: Xanthomonas campestris pv. campestris (strain B100)


organism: Homo sapiens


organism: Mus musculus

substrate_name: pNppp (isoform 1)

substrate: pNppp (isoform 1)


enzyme_display_name: uracil-DNA glycosylase

substrate_name: ATP

enzyme: uracil-DNA glycosylase

substrate: ATP


organism: Escherichia coli

substrate_name: D-Glucosamine 1-phosphate

sequence_source: direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P0ACC7.json

substrate: D-Glucosamine 1-phosphate


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

proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant GlmU C324A N-terminal His6-tagged

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


sequence_variant_note: Resolved canonical sequence from direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P0ACC7.json and applied mutation signature C385A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P0ACC7.json and applied mutation signature C324A to reconstruct the assayed variant sequence.


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

proof_lines: SABIO-RK modifier species: glucosamine-1-phosphate N-acetyltransferase(Enzyme) mutant GlmU C296A N-terminal His6-tagged

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


organism: Mycobacterium tuberculosis

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

sequence_source: direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P9WMN3.json

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines:
pH 7.5, 37°C, recombinant enzyme
Raw SKiD Env: Temp=30°C, pH=7.6
Raw SKiD Env: Temp=37°C, pH=7.5

source_databases_merged: sabio_rk brenda skid


substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P9WMN3.json and applied mutation signature N397A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 303.15 K; cofactor CoA

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P9WMN3.json and applied mutation signature H374A to reconstruct the assayed variant sequence.


substrate_name: alpha-D-glucosamine 1-phosphate

sequence_variant_note: Resolved canonical sequence from direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/P9WMN3.json and applied mutation signature S416A to reconstruct the assayed variant sequence.

substrate: alpha-D-glucosamine 1-phosphate


substrate_name: propionyl-CoA

sequence_source: direct UniProtKB REST lookup: https://rest.uniprot.org/uniprotkb/A5U161.json

assay_conditions_summary: pH 7.5; 303.15 K; buffer containing 10 mM MgCl2 throughout the purification process; cofactor CoA

column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'Pro-CoA', fixed-substrate column value 'GlcN-1P'; column 'K_m (uM)' = 60; column 'k_cat (s^-1)' = 0.5; column 'k_cat/K_m (M^-1 s^-1)' = 8.3 x 10^3; column 'K_d (uM)' = 500 uM.

normalized_value_unit_evidence: Km: printed Table 1 cell 60 uM; 60 / 1000 = 0.06 mM. kcat: printed Table 1 cell 0.5 s^-1; already in s^-1, no unit conversion applies, so the paper value is 0.5 s^(-1). kcat/Km: printed Table 1 cell 8.3 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.3 x 10^3 / 1000 = 8.3 s^-1 mM^-1. The catalog carries 8.333333333333334 s^(-1)*mM^(-1) for this metric, which is the exact quotient 0.5 / 0.06 of the same table line's printed kcat and Km cells; the printed efficiency cell reproduces that quotient at the two-significant-figure precision the paper uses, so the exact quotient is kept.

raw_value_unit_evidence: Table 1, varied-substrate row 'Pro-CoA', fixed substrate 'GlcN-1P': Km = 60 uM; kcat = 0.5 s^-1; printed kcat/Km = 8.3 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate-analogue row with varied substrate 'Pro-CoA' and fixed substrate 'GlcN-1P'

table_label: Table 1: Steady-State Kinetic Parameters for GlmU (Biochemistry 2018, 57, 3387-3401)

substrate: propionyl-CoA


substrate_name: acetoacetyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines:
pH 7.5, 30°C
cosubstrate propionyl-CoA, pH 7.5, 30°C
cosubstrate acetyl-CoA, pH 7.5, 30°C

substrate: acetoacetyl-CoA


column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'AAc-CoA', fixed-substrate column value 'GlcN-1P'; column 'K_m (uM)' = 1800; column 'k_cat (s^-1)' = 0.5; column 'k_cat/K_m (M^-1 s^-1)' = 2.8 x 10^2; column 'K_d (uM)' = ND.

normalized_value_unit_evidence: Km: printed Table 1 cell 1800 uM; 1800 / 1000 = 1.8 mM. kcat: printed Table 1 cell 0.5 s^-1; already in s^-1, no unit conversion applies, so the paper value is 0.5 s^(-1). kcat/Km: printed Table 1 cell 2.8 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.8 x 10^2 / 1000 = 0.28 s^-1 mM^-1. The catalog carries 0.2777777777777778 s^(-1)*mM^(-1) for this metric, which is the exact quotient 0.5 / 1.8 of the same table line's printed kcat and Km cells; the printed efficiency cell reproduces that quotient at the two-significant-figure precision the paper uses, so the exact quotient is kept.

raw_value_unit_evidence: Table 1, varied-substrate row 'AAc-CoA', fixed substrate 'GlcN-1P': Km = 1800 uM; kcat = 0.5 s^-1; printed kcat/Km = 2.8 x 10^2 M^-1 s^-1.

row_label: Table 1, substrate-analogue row with varied substrate 'AAc-CoA' and fixed substrate 'GlcN-1P'


substrate_name: succinyl-CoA

column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'Suc-CoA', fixed-substrate column value 'GlcN-1P'; column 'K_m (uM)' = 1100; column 'k_cat (s^-1)' = 0.9; column 'k_cat/K_m (M^-1 s^-1)' = 8.2 x 10^2; column 'K_d (uM)' = ND.

normalized_value_unit_evidence: Km: printed Table 1 cell 1100 uM; 1100 / 1000 = 1.1 mM. kcat: printed Table 1 cell 0.9 s^-1; already in s^-1, no unit conversion applies, so the paper value is 0.9 s^(-1). kcat/Km: printed Table 1 cell 8.2 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.2 x 10^2 / 1000 = 0.82 s^-1 mM^-1. The catalog carries 0.8181818181818181 s^(-1)*mM^(-1) for this metric, which is the exact quotient 0.9 / 1.1 of the same table line's printed kcat and Km cells; the printed efficiency cell reproduces that quotient at the two-significant-figure precision the paper uses, so the exact quotient is kept.

raw_value_unit_evidence: Table 1, varied-substrate row 'Suc-CoA', fixed substrate 'GlcN-1P': Km = 1100 uM; kcat = 0.9 s^-1; printed kcat/Km = 8.2 x 10^2 M^-1 s^-1.

row_label: Table 1, substrate-analogue row with varied substrate 'Suc-CoA' and fixed substrate 'GlcN-1P'

substrate: succinyl-CoA


substrate_name: n-propionyl-CoA

substrate: n-propionyl-CoA


enzyme_display_name: chitosanase

organism: Aspergillus fumigatus

enzyme: chitosanase


organism: Bacillus amyloliquefaciens

substrate_name: chitosan

substrate: chitosan


organism: Bacillus cereus


organism: Bacillus sp.

substrate_name: H2O; Chitosan

unit: lgwedgeoneswedgeone

substrate: H2O; Chitosan


organism: Bacillus sp. MN


substrate_name: chitopentaose

substrate: chitopentaose


organism: Bacillus subtilis


substrate_name: dUMP-carrying ssDNA and dsDNA

substrate: dUMP-carrying ssDNA and dsDNA


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


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: G/U dsDNA

substrate: G/U dsDNA


organism: Arabidopsis thaliana

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


substrate_name: L-threonine

substrate: L-threonine


enzyme_display_name: homoserine dehydrogenase

organism: Mycobacterium leprae

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

enzyme: homoserine dehydrogenase

substrate: Unknown


organism: Pyrococcus horikoshii

substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58802 and applied mutation signature K57A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 323.15 K; cofactor NADP+

column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'K57A', NADP header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.06; column 'kcat s-1' = 26.7; column 'kcat/Km s-1 mM-1' = 518.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.06 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.06 mM. kcat: printed Table 2 cell 26.7 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 26.7 s^(-1). kcat/Km: printed Table 2 cell 518 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the paper-side value carried here is 518.0 s^(-1)*mM^(-1), the paper's own fitted efficiency cell for this same block.

raw_value_unit_evidence: Table 2, enzyme row 'K57A', NADP header block: Km = 0.06 mM; kcat = 26.7 s-1; printed kcat/Km = 518 s-1 mM-1.

table_label: Table 2: kinetic parameters for the NAD and NADP coenzyme blocks (Scientific Reports 2015, volume 5, article 11674)

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from UniProtKB:O58802 and applied mutation signature R40A to reconstruct the assayed variant sequence.


substrate_name: NAD+

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

assay_conditions_summary: pH 9; 323.15 K; cofactor NAD+

column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'Wild type', NAD header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.32; column 'kcat s-1' = 70.1; column 'kcat/Km s-1 mM-1' = 219.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.32 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.32 mM. kcat: printed Table 2 cell 70.1 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 70.1 s^(-1). kcat/Km: printed Table 2 cell 219 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the printed cell normalizes to 219.0 s^(-1)*mM^(-1); the catalog carries the full-precision quotient of the same two printed cells, 70.1 / 0.32 = 219.0625 s^(-1)*mM^(-1), which the printed cell renders at integer precision.

raw_value_unit_evidence: Table 2, enzyme row 'Wild type', NAD header block: Km = 0.32 mM; kcat = 70.1 s-1; printed kcat/Km = 219 s-1 mM-1.

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from UniProtKB:O58802 and applied mutation signature K57A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58802 and applied mutation signature R40A to reconstruct the assayed variant sequence.

column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'R40A', NADP header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.04; column 'kcat s-1' = 3.4; column 'kcat/Km s-1 mM-1' = 89.1.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.04 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.04 mM. kcat: printed Table 2 cell 3.4 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 3.4 s^(-1). kcat/Km: printed Table 2 cell 89.1 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the paper-side value carried here is 89.1 s^(-1)*mM^(-1), the paper's own fitted efficiency cell for this same block.

raw_value_unit_evidence: Table 2, enzyme row 'R40A', NADP header block: Km = 0.04 mM; kcat = 3.4 s-1; printed kcat/Km = 89.1 s-1 mM-1.


column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'K57A', NAD header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.05; column 'kcat s-1' = 48.5; column 'kcat/Km s-1 mM-1' = 1020.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.05 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.05 mM. kcat: printed Table 2 cell 48.5 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 48.5 s^(-1). kcat/Km: printed Table 2 cell 1020 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the paper-side value carried here is 1020.0 s^(-1)*mM^(-1), the paper's own fitted efficiency cell for this same block.

raw_value_unit_evidence: Table 2, enzyme row 'K57A', NAD header block: Km = 0.05 mM; kcat = 48.5 s-1; printed kcat/Km = 1020 s-1 mM-1.


column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'R40A', NAD header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.95; column 'kcat s-1' = 96.1; column 'kcat/Km s-1 mM-1' = 102.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.95 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.95 mM. kcat: printed Table 2 cell 96.1 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 96.1 s^(-1). kcat/Km: printed Table 2 cell 102 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the paper-side value carried here is 102.0 s^(-1)*mM^(-1), the paper's own fitted efficiency cell for this same block.

raw_value_unit_evidence: Table 2, enzyme row 'R40A', NAD header block: Km = 0.95 mM; kcat = 96.1 s-1; printed kcat/Km = 102 s-1 mM-1.


proof_lines: pH 9.0, 50°C, recombinant wild-type enzyme


substrate_name: L-homoserine

proof_lines:
pH 9.0, 50°C, recombinant enzyme
Raw SKiD Env: Temp=50°C, pH=9

substrate: L-homoserine


organism: Saccharomyces cerevisiae

substrate_name: L-Aspartate 4-semialdehyde

column_label: Retained supplementary PDF Supplementary Table 2, Sc-Hom6 natural-substrate row: kcat 126 +/- 23; Km 0.22 +/- 0.04; kcat/Km 573.

normalized_value_unit_evidence: At retained catalog units, kcat is 126 s^-1, Km is 0.22 mM, and the independently printed kcat/Km is 573 s^-1 mM^-1.

raw_value_unit_evidence: Supplementary Table 2 Sc-Hom6 natural-substrate row: kcat 126 +/- 23 s^-1; Km 0.22 +/- 0.04 mM; independently printed kcat/Km 573 s^-1 mM^-1.

row_label: Sc-Hom6 / Natural substrate

table_label: Supplementary Table 2. Kinetic parameters of wild-type homoserine pathway enzymes on their natural substrates and the corresponding intermediates of the synthetic DHB pathway

substrate: L-Aspartate 4-semialdehyde


substrate_name: H+; L-Aspartate 4-semialdehyde; NADPH

assay_conditions_summary: cofactor NADP+

substrate: H+; L-Aspartate 4-semialdehyde; NADPH


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines:
pH 8.0, 30°C, oxidized enzyme
pH 8.0, 30°C, reduced enzyme
pH 8.0, 30°C


organism: Thermotoga maritima

assay_conditions_summary: pH 10.5; 328.15 K; cofactor NADP+


organism: Thermus thermophilus

assay_conditions_summary: pH 10; 323.15 K; cofactor NADP+


proof_lines: pH 9.5, 50°C, recombinant enzyme, with NAD+


substrate_name: L-Aspartate 4-semialdehyde; H+; NADPH; L-Aspartate 4-semialdehyde; H+; ...

sequence_source: UniProtKB:O81852 direct accession sequence

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

proof_lines: pH 8.0, 37°C, purified recombinant soluble enzyme


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


substrate_name: NADP+; L-Homoserine; NADP+; L-Homoserine; ...

sequence_variant_note: Resolved canonical sequence from UniProtKB:O81852 canonical sequence with Q443A reconstruction and applied mutation signature Q443A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: homoserine dehydrogenase(Enzyme) mutant Q443A


substrate_name: L-Homoserine; NADP+; L-Homoserine; NADP+; ...

sequence_variant_note: Resolved canonical sequence from UniProtKB:O81852 canonical sequence with Q524A reconstruction and applied mutation signature Q524A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: homoserine dehydrogenase(Enzyme) mutant Q524A


assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

column_label: J. Biol. Chem. 280(50):41178-41183 (2005); journal page 41179 (PDF page 2), RESULTS, 'Comparison of AK-HSDH Isoform Kinetic Properties': RESULTS prose pair for HSDH II: Km for aspartate semialdehyde 311 +/- 6 uM; catalytic constant 196 +/- 21 s^-1: kcat (catalytic constant v/[E]0) = 196 +/- 21 s^-1; Km = 311 +/- 6 uM.

normalized_value_unit_evidence: Printed catalytic constant 196 +/- 21 s^-1 is already in the catalog unit s^(-1); no conversion needed; catalog kcat = 196.0. Printed Km 311 +/- 6 uM / 1000 = 0.311 mM, matching the catalog km 0.311 mM exactly. The paper prints no kcat/Km value for this measurement. The catalog kcat_over_km 630.225080385852 s^(-1)*mM^(-1) is the exact full-precision quotient of this same printed pair, 196.0 / 0.311 = 630.225080385852.

raw_value_unit_evidence: RESULTS prose pair for HSDH II: Km for aspartate semialdehyde 311 +/- 6 uM; catalytic constant 196 +/- 21 s^-1: printed kcat (catalytic constant v/[E]0) 196 +/- 21 s^-1; printed Km 311 +/- 6 uM; no printed kcat/Km.

table_label: RESULTS prose, 'Comparison of AK-HSDH Isoform Kinetic Properties' (no numbered table; values printed in the running text)


sequence_source: UniProtKB:Q9SA18 direct accession sequence

column_label: J. Biol. Chem. 280(50):41178-41183 (2005); journal page 41179 (PDF page 2), RESULTS, 'Comparison of AK-HSDH Isoform Kinetic Properties': RESULTS prose pair for HSDH I: Km for aspartate semialdehyde 290 +/- 17 uM; catalytic constant 245 +/- 19 s^-1: kcat (catalytic constant v/[E]0) = 245 +/- 19 s^-1; Km = 290 +/- 17 uM.

normalized_value_unit_evidence: Printed catalytic constant 245 +/- 19 s^-1 is already in the catalog unit s^(-1); no conversion needed; catalog kcat = 245.0. Printed Km 290 +/- 17 uM / 1000 = 0.29 mM, matching the catalog km 0.29 mM exactly. The paper prints no kcat/Km value for this measurement. The catalog kcat_over_km 844.8275862068966 s^(-1)*mM^(-1) is the exact full-precision quotient of this same printed pair, 245.0 / 0.29 = 844.8275862068966.

raw_value_unit_evidence: RESULTS prose pair for HSDH I: Km for aspartate semialdehyde 290 +/- 17 uM; catalytic constant 245 +/- 19 s^-1: printed kcat (catalytic constant v/[E]0) 245 +/- 19 s^-1; printed Km 290 +/- 17 uM; no printed kcat/Km.


assay_conditions_summary: cofactor NADPH

substrate: L-Aspartate 4-semialdehyde; H+; NADPH; L-Aspartate 4-semialdehyde; H+; ...


sequence_source: UniProtKB:P19582 direct accession sequence

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+


substrate_name: NADP+; L-homoserine

substrate: NADP+; L-homoserine


substrate_name: L-Homoserine

substrate: L-Homoserine


organism: Escherichia coli

sequence_source: UniProtKB:P00561 direct accession sequence

substrate: L-Homoserine; NADP+; L-Homoserine; NADP+; ...


organism: Glycine max

substrate_name: L-homoserine; L-aspartate 4-semialdehyde; NADH; ...

sequence_source: UniProtKB:O65027 direct accession sequence

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines:
cosubstrate NAD+, pH 8.0, 25°C
cosubstrate NADP+, pH 8.0, 25°C
cosubstrate NADH, pH 8.0, 25°C


sequence_source: UniProtKB:O63067 direct accession sequence

proof_lines:
cosubstrate NADP+, pH 8.0, 25°C
cosubstrate NAD+, pH 8.0, 25°C
cosubstrate NADH, pH 8.0, 25°C

substrate: L-homoserine; L-aspartate 4-semialdehyde; NADH; ...


substrate_name: L-aspartate 4-semialdehyde

substrate: L-aspartate 4-semialdehyde


substrate_name: L-aspartate 4-semialdehyde; L-homoserine; NADPH; ...

sequence_source: UniProtKB:Q3S3F6 direct accession sequence

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines:
cosubstrate NADPH, pH 8.0, 25°C
cosubstrate NADP+, pH 8.0, 25°C
cosubstrate NAD+, pH 8.0, 25°C


organism: Hordeum vulgare

proof_lines:
isozyme I
isozyme II


organism: Lathyrus oleraceus

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines:
threonine sensitive isozyme
isozyme II
threonine insensitive isozyme


organism: Triticum aestivum

substrate_name: NADPH

proof_lines:
threonine sensitive isozyme
threonine resistant isozyme

substrate: NADPH


organism: Zea mays

proof_lines: threonine-sensitive enzyme, pH and temperature not specified in the publication


organism: Unknown

substrate_name: beta-glycinamide ribonucleotide

substrate: beta-glycinamide ribonucleotide


sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/Q5SL04.json

assay_conditions_summary: pH 9.5; 323.15 K; cofactor NAD+


sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/P08179.json


organism: Homo sapiens

sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/P22102.json

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


organism: Mus musculus

sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/Q64737.json


enzyme_display_name: acylaminoacyl-peptidase

organism: Aeropyrum pernix

substrate_name: p-nitrophenyl caprylate

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526K to reconstruct the assayed variant sequence.

enzyme: acylaminoacyl-peptidase

substrate: p-nitrophenyl caprylate


substrate_name: N-acetyl-Leu-p-nitroanilide

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526A to reconstruct the assayed variant sequence.

substrate: N-acetyl-Leu-p-nitroanilide


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526I to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST accession check https://rest.uniprot.org/uniprotkb/Q9YBQ2.json

proof_lines:
80°C, wild-type enzyme
pH 7.0, 70°C, wild-type enzyme
wild-type


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature R526L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature H367A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature D524N to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 70°C, mutant enzyme D524N, measured under first-order conditions


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json) and applied mutation signature D524A to reconstruct the assayed variant sequence.


sequence_source: reconstructed from UniProtKB Q9YBQ2 canonical sequence (https://rest.uniprot.org/uniprotkb/Q9YBQ2.json)


proof_lines: pH 7.0, 70°C, mutant enzyme D524A, measured under first-order conditions


sequence_source: UniProtKB:Q9YBQ2 direct REST lookup


organism: Aeropyrum pernix K1

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature H367A and applied mutation signature H367A to reconstruct the assayed variant sequence.

proof_lines:
mutant H367A, larger than 0.1
mutant H367A


substrate_name: Ac-Leu-p-nitroanilide

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature D15A/R18A and applied mutation signature D15A/R18A to reconstruct the assayed variant sequence.

substrate: Ac-Leu-p-nitroanilide


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature R18A and applied mutation signature R18A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature ΔN21 could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature D15A and applied mutation signature D15A to reconstruct the assayed variant sequence.


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

proof_lines: wild-type, in the presence of 1 M sodium chloride


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature E88A/R526V and applied mutation signature E88A/R526V to reconstruct the assayed variant sequence.

proof_lines: mutant E88A/R526V, in the presence of 1 M sodium chloride


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature E88A and applied mutation signature E88A to reconstruct the assayed variant sequence.

proof_lines: mutant E88A, in the presence of 1 M sodium chloride


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9YBQ2 direct REST lookup; variant reconstructed from mutation signature R526V and applied mutation signature R526V to reconstruct the assayed variant sequence.

proof_lines: mutant R526V, in the presence of 1 M sodium chloride


organism: Arabidopsis thaliana

substrate_name: N-acetyl-Ala-p-nitroanilide

sequence_source: UniProtKB:Q84LM4 direct REST lookup

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

substrate: N-acetyl-Ala-p-nitroanilide


organism: Bombyx mori

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

proof_lines:
pH 7.5, 25°C, recombinant enzyme
pH 7.5, 45°C, recombinant enzyme


organism: Saccharolobus solfataricus

substrate_name: N-acetyl-L-leucyl 4-nitroanilide

sequence_source: UniProtKB:Q7LX61 direct REST lookup

substrate: N-acetyl-L-leucyl 4-nitroanilide


proof_lines: pH 7.5, 80°C, substrate: N-acetyl-L-leucyl 4-nitroanilide


substrate_name: N-acetyl-L-alanyl 4-nitroanilide

substrate: N-acetyl-L-alanyl 4-nitroanilide


sequence_source: UniProtKB Q97VD6 direct REST lookup


proof_lines: in 25 mM Tris-HCl buffer pH 7.5, at 90°C

proof_lines: pH 7.5, 90°C, substrate: acetyl-Leu-4-nitroanilide


organism: Trematomus bernacchii

sequence_source: UniProtKB V5QZ74 direct REST lookup

proof_lines:
15°C, pH 8
50°C, pH 8
37°C, pH 8


substrate_name: Ac-Ala-pNA

assay_conditions_summary: pH 7

substrate: Ac-Ala-pNA


organism: Escherichia coli (strain K12)

proof_lines: kcat is 20.7 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 8.5). kcat is 13.5 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 7.5).


organism: Rattus norvegicus

substrate_name: N(alpha)-formyl-L-methionyl-L-leucyl-L-phenylalanine (f-MLF) (at pH 7)

proof_lines: kcat is 4.6 sec(-1) with N(alpha)-formyl-L-methionyl-L-leucyl-L-phenylalanine (f-MLF) as substrate (at pH 7). kcat is 14 sec(-1) with N(alpha)-formyl-L-methionyl-L-leucyl-L-phenylalanine (f-MLF) as substrate (at pH 8). kcat is 5.6 sec(-1) w


mutation_signature: deletion construct with amino acids 68-354 / donor UDP-GalNAc deletion construct with amino acids 68-354

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

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, donor UDP-GalNAc


mutation_signature: deletion construct with amino acids 68-354 / co-substrate: donor UDP-GalNAc deletion construct with amino acids 68-354

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc


proof_lines: mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose

proof_lines: mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc

proof_lines: mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, donor UDP-GalNAc


organism: Oryctolagus cuniculus

substrate_name: UDP-galactose

proof_lines:
in reaction with N-acetyllactosamine
in reaction with 2-fucosyllactose

substrate: UDP-galactose


enzyme_display_name: non-specific protein-tyrosine kinase

proof_lines: pH 8.0, 30°C, recombinant mutant E338A Csk

enzyme: non-specific protein-tyrosine kinase


proof_lines: pH 8.0, 30°C, recombinant Csk residue-339-deletion mutant


substrate_name: [kdSrc kinase]-L-tyrosine

proof_lines: pH 8.0, 30°C, recombinant mutant R281A/R283A

substrate: [kdSrc kinase]-L-tyrosine


proof_lines: pH 8.0, 30°C, recombinant mutant S280A/R281A/R283A/F381A


proof_lines: pH 8.0, 30°C, recombinant W188A Csk mutant


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, 30°C, recombinant DSH3 Csk mutant

proof_lines: pH 8.0, 30°C, recombinant DSH2 Csk mutant


proof_lines: pH 8.0, 30°C, recombinant K361G/K362A Csk mutant


proof_lines: pH 8.0, 30°C, recombinant W188F Csk mutant


substrate_name: tyramine

proof_lines: enzyme from serum of 27-weeks-old rats, at 37°C, pH not specified in the publication

proof_lines: enzyme from serum of 15-weeks-old rats, at 37°C, pH not specified in the publication

proof_lines: enzyme from serum of 8-weeks-old rats, at 37°C, pH not specified in the publication

substrate: tyramine


organism: Escherichia coli

substrate_name: NADP+; L-Homoserine

proof_lines: recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity

proof_lines: recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity

proof_lines: recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity

substrate: NADP+; L-Homoserine


substrate_name: L-homoserine

proof_lines: recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity

substrate: L-homoserine


organism: Spinacia oleracea

substrate_name: DL-aspartate 4-semialdehyde

assay_conditions_summary: cofactor NADH

substrate: DL-aspartate 4-semialdehyde


proof_lines:
mutant 13N + 13C 1:1
mutant B13


proof_lines:
pH 7.5
pH 8.5
purT gene product


proof_lines:
mutant H108A
strain H108A


organism: Yersinia pseudotuberculosis

substrate_name: alpha-D-glucosamine 1-phosphate

assay_conditions_summary: pH 8.2; 310.15 K; cofactor CoA

proof_lines: pH 8.2, 37°C, recombinant His6-tagged enzyme

substrate: alpha-D-glucosamine 1-phosphate


organism: Dictyostelium discoideum


substrate_name: UDP-N-acetylgalactosamine

proof_lines: with L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3 as acceptor

substrate: UDP-N-acetylgalactosamine


substrate_name: UDP-D-galactose

substrate: UDP-D-galactose


substrate_name: UDP-Gal

substrate: UDP-Gal


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


mutation_signature: deletion construct with amino acids 68-354 / co-substrate: donor UDP-alpha-D-galactose deletion construct with amino acids 68-354

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose


mutation_signature: deletion construct with amino acids 68-354 / donor UDP-alpha-D-galactose deletion construct with amino acids 68-354

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, donor UDP-alpha-D-galactose


substrate_name: UDP-GalNAc

proof_lines: deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication

substrate: UDP-GalNAc


proof_lines: mutant C80S/C196S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc

proof_lines: mutant C80S/C196S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose

proof_lines: mutant C80S/C196S, pH 7.0, temperature not specified in the publication, donor UDP-GalNAc


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08179 plus direct D144A reconstruction and applied mutation signature D144A to reconstruct the assayed variant sequence.

proof_lines:
mutant D144A
strain D144A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08179 plus direct N106G reconstruction and applied mutation signature N106G to reconstruct the assayed variant sequence.


organism: Gallus gallus


substrate_name: beta-glycinamide ribonucleotide

proof_lines: chimeric enzyme GPX-M55 (hGART1-56/PurN58-212)

proof_lines: chimeric enzyme GPX-M24 (hGART1-54/PurN55-212)

proof_lines: chimeric enzyme GPG-N11 (hGART1-56/PurN57-131/hGART132-202)

substrate: beta-glycinamide ribonucleotide


proof_lines:
wild type enzyme
wild-type enzyme


substrate_name: N-acetyl-D-glucosamine 1-phosphate

sequence_source: UniProtKB:P0ACC7 canonical wild-type sequence

assay_conditions_summary: cofactor CoA

proof_lines:
GmlU uridyltransferase
uridyltransferase activity

substrate: N-acetyl-D-glucosamine 1-phosphate


substrate_name: D-glucosamine 1-phosphate

substrate: D-glucosamine 1-phosphate


substrate_name: acetyl-CoA

proof_lines: mutant His6GlmU, mutant His6-GlmU C296A, mutant His6-GlmU C385A

substrate: acetyl-CoA


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines:
pH 7.5, 25°C
pH 7.5, 37°C
Vmax: 4.489 microM/min/pmol enzyme


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S474A


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant N456A


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged wild-type GlmU


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant K403A


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant E458A


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant R463A


proof_lines: pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S416A


organism: Yersinia pestis


organism: Homo sapiens

substrate_name: EEEEY

substrate: EEEEY


substrate_name: ATP

proof_lines: pH 8.0, 30°C, recombinant mutant H384Q/Y416F

substrate: ATP


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


proof_lines: pH 8.0, 30°C, recombinant mutant H384Y/Y527F


proof_lines: pH 8.0, 30°C, recombinant mutant H384Y/Y416F


assay_conditions_summary: cofactor ATP

proof_lines: recombinant GST-fusion Chk, 12 mM Mg2+, no Mn2+

proof_lines: non-receptor tyrosine kinase Src, pH and temperature not specified in the publication


organism: Monosiga brevicollis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Acholeplasma laidlawii

substrate_name: Diphosphate; D-Fructose 6-phosphate

substrate: Diphosphate; D-Fructose 6-phosphate


organism: Ananas comosus

substrate_name: D-fructose 1,6-bisphosphate

proof_lines: pH 7.7, 25°C, in presence of fructose 2,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


organism: Brassica nigra

proof_lines: pH 6.8, 25°C, in presence of fructose 2,6-bisphosphate


organism: Bacillus subtilis

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


sequence_variant_note: Mutation signature K133A matches the mutant residue at offset +0 and the reference residue at offset +6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature R140A matches the mutant residue at offset +0 and the reference residue at offset -6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature R134A matches the mutant residue at offset +0 and the reference residue at offset +6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: adenine2085 in 23S rRNA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature R134A to reconstruct the assayed variant sequence.

substrate: adenine2085 in 23S rRNA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature M196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature N192A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature K197A/N200A/E202A/K204A/K205A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature K197A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature T108A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature R140A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13956 canonical sequence with row-specific mutation reconstruction and applied mutation signature F163A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed F163A single substitution and applied mutation signature F163A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed K168A single substitution and applied mutation signature K168A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed N11A single substitution and applied mutation signature N11A to reconstruct the assayed variant sequence.


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed N11A single substitution


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed E128A single substitution and applied mutation signature E128A to reconstruct the assayed variant sequence.


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed E128A single substitution


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed K166A single substitution and applied mutation signature K166A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P13956 canonical sequence with reviewer-reconstructed P165A single substitution and applied mutation signature P165A to reconstruct the assayed variant sequence.


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed K168A single substitution


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed K166A single substitution


sequence_source: UniProt P13956 reviewed canonical 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 UniProt P13956 canonical sequence with reviewer-reconstructed N101A single substitution and applied mutation signature N101A to reconstruct the assayed variant sequence.


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed N101A single substitution


sequence_source: UniProt P13956 canonical sequence with reviewer-reconstructed P165A single substitution


substrate_name: 23S rRNA; S-Adenosyl-L-methionine

proof_lines: pH 7.5, 37°C, a 262-nucleotide RNA fragment within domain V of Bacillus subtilis 23S rRNA

substrate: 23S rRNA; S-Adenosyl-L-methionine


organism: Streptomyces fradiae

substrate_name: S-Adenosyl-L-methionine; rRNA

sequence_source: UniProt P45439 reviewed canonical sequence

substrate: S-Adenosyl-L-methionine; rRNA


enzyme_display_name: arylsulfatase (type I)

organism: Clostridium perfringens

substrate_name: 4-Nitrophenyl sulfate; H2O

sequence_source: UniProtKB REST direct accession lookup for Q0TUK6

enzyme: arylsulfatase (type I)

substrate: 4-Nitrophenyl sulfate; H2O


substrate_name: 4-Nitrocatechol sulfate; H2O

sequence_source: UniProtKB REST direct accession lookup for Q96EG1

substrate: 4-Nitrocatechol sulfate; H2O


substrate_name: 4-nitrocatechol sulfate

sequence_source: UniProtKB REST direct accession lookup for Q6UWY0

substrate: 4-nitrocatechol sulfate


substrate_name: Unknown

sequence_source: UniProtKB REST direct accession lookup for Q8IWU6

substrate: Unknown


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


organism: Marinomonas sp. FW-1

substrate_name: 4-nitrophenyl sulfate

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

substrate: 4-nitrophenyl sulfate


organism: Pseudoalteromonas atlantica


organism: Pseudoalteromonas carrageenovora

sequence_source: UniProtKB REST direct accession lookup for P28607


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for P28607 plus row mutation reconstruction and applied mutation signature H260L to reconstruct the assayed variant sequence.


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

proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260F


proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260I


proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260Q


proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260R


proof_lines: 55°C, pH not specified in the publication, wild-type enzyme


proof_lines: 55°C, pH not specified in the publication, mutant enzyme H260L


organism: Bruguiera sexangula

substrate_name: D-fructose 6-phosphate

proof_lines:
pH 7.2, 30°C
pH 7.2, 30°C, presence of 0.15 mM NaCl

substrate: D-fructose 6-phosphate


organism: Citrus sinensis

assay_conditions_summary: pH 7.2; 298.15 K; buffer + NaCl, pH 7

proof_lines: forward reaction, HEPES-NaOH buffer + NaCl, pH 7.2, 25°C

proof_lines: forward reaction, Tris-HCl buffer, pH 7.2, 25°C


organism: Clostridium thermosuccinogenes


organism: Daucus carota

proof_lines:
forward reaction, pH 8.0, 25°C
reverse reaction, pH 8.0, 25°C
pH 8.0, 25°C


organism: Dictyoglomus thermophilum


organism: Entamoeba histolytica

substrate_name: diphosphate

proof_lines:
wild-type, pH 7.2, 30°C
wild-type enzyme, pH 7.2, 30°C

substrate: diphosphate


substrate_name: D-Fructose 6-phosphate; Diphosphate

proof_lines:
37°C, pH 7.0
forward reaction, pH 7.0, 30°C
pH 7.0, 30°C

substrate: D-Fructose 6-phosphate; Diphosphate


organism: Giardia duodenalis

substrate_name: phosphate

proof_lines: substrate is a Mg2+-chelated complexe of phosphate, not uncomplexed ligand

substrate: phosphate


organism: Glycine max

proof_lines:
pH 7.5, 25°C
with diphosphate


organism: Pseudomonas aeruginosa

substrate_name: testosterone 17-sulfate

sequence_source: UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta

substrate: testosterone 17-sulfate


substrate_name: etiocholanolonesulfate

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/P161A/A323D/L325F/K330V/W358Y to reconstruct the assayed variant sequence.

substrate: etiocholanolonesulfate


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/P161A/L325F/K330V to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme R155P/P161A/L325F/K330V


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/I156V/P161A/A323D/L325F/K330V/W358N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/I156V/L325F/K330V to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme R155P/I156V/L325F/K330V


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/P161A/P329R/L325F/K330V to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme R155P/P161A/P329R/L325F/K330V


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P51691 (SV=3); https://rest.uniprot.org/uniprotkb/P51691.fasta and applied mutation signature R155P/P161A/A323Q/L325F/K330V to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme R155P/P161A/A323Q/L325F/K330V


enzyme_display_name: aqualysin 1

organism: Thermus aquaticus

sequence_source: UniProtKB direct accession lookup P08594 (SV=2); https://rest.uniprot.org/uniprotkb/P08594.fasta

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

enzyme: aqualysin 1


column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row Wild-type; column 'k cat (s -1 )' = 91.6 ± 2.75; column 'K m (mM)' = 0.79 ± 0.04; column 'k cat / K m (mM -1 s -1 )' = 116.

normalized_value_unit_evidence: kcat: printed Table 3 cell 91.6 ± 2.75 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 91.6 s^(-1). Km: printed Table 3 cell 0.79 ± 0.04 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.79 mM. kcat/Km: printed Table 3 cell 116 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 116.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row Wild-type: k_cat = 91.6 ± 2.75 s^-1; K_m = 0.79 ± 0.04 mM; printed k_cat/K_m = 116 mM^-1 s^-1.

row_label: Table 3, enzyme row Wild-type

table_label: Table 3: Kinetic parameters of the wild-type and mutant enzymes (AMB Express 2014, 4:59)


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature D138N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row D138N; column 'k cat (s -1 )' = 59.5 ± 6.14; column 'K m (mM)' = 0.77 ± 0.01; column 'k cat / K m (mM -1 s -1 )' = 77.3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 59.5 ± 6.14 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 59.5 s^(-1). Km: printed Table 3 cell 0.77 ± 0.01 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.77 mM. kcat/Km: printed Table 3 cell 77.3 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 77.3 s^-1 mM^-1.

row_label: Table 3, enzyme row D138N


organism: Hexamita inflata


organism: Methylococcus capsulatus

proof_lines: using D-fructose 6-phosphate as cosubstrate, in 0.1 M HEPES-HCl, pH 7.0, at 30°C

proof_lines: using D-fructose 1,6-bisphosphate as cosubstrate, in 0.1 M HEPES-HCl, pH 7.0, at 30°C


organism: Methylosinus trichosporium


organism: Methylotuvimicrobium alcaliphilum

proof_lines: in 50 mM Tris-HCl, pH 7.5, 5 mM MgCl2, at 30°C


organism: Musa acuminata


organism: Musa cavendishii

proof_lines: pH 7.0, 25°C, presence of 0.005 mM D-fructose 1,6-diphosphate


organism: Naegleria fowleri


organism: Oryza sativa

proof_lines: versus fructose 6-phosphate, pH 7.5, 25°C, in presence of fructose 2,6-bisphosphate at saturating concentration

proof_lines: versus diphosphate, pH 7.5, 25°C, in presence of fructose 2,6-bisphosphate at saturating concentration


organism: Phaseolus coccineus


organism: Phaseolus vulgaris