organism: Pasteurella multocida

substrate_name: 4-methylumbelliferyl beta-lactoside

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q15KI8 direct REST lookup 2026-06-18 and applied mutation signature M144H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 310.15 K; buffer Tris-HCl

proof_lines: mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: mutant enzyme M144H, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: mutant enzyme M144H, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

substrate: 4-methylumbelliferyl beta-lactoside


substrate_name: CMP-N-acetyl-beta-neuraminate

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q15KI8 and applied mutation signature H311A to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 1, enzyme row H311A; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 1.8 mM; kcat cell = 2.1 s^-1; kcat/Km cell = 1.1 s^-1 mM^-1; author manuscript page 17 (PDF page 17). captured primary segment: CMP-Neu5Ac | PmST1 H311A, the H311A single mutant of Pasteurella multocida sialyltransferase 1 | Table 1, enzyme row H311A: Km 1.8 mM | kcat 2.1 s^-1 | kcat/Km printed cell 1.1 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 1.8 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 1.8 mM. kcat: printed cell 2.1 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 2.1 s^(-1). kcat/Km: printed cell 1.1 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 1.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row H311A: Km = 1.8 mM; kcat = 2.1 s^-1; printed kcat/Km = 1.1 s^-1 mM^-1.

row_label: Table 1, enzyme row H311A

table_label: Table 1 (Apparent kinetics of the CMP-Neu5Ac hydrolysis activity of WT PmST1 and mutants), printed column heads enzyme | Km (mM) | kcat (s^-1) | kcat/Km (s^-1 mM^-1)

data_origin: experimental

substrate: CMP-N-acetyl-beta-neuraminate

status: corrected

source: oed


verification_status: unverified

mutation_signature: Unknown

kcat_over_km_origin: calculated

sequence_source: UniProtKB:Q15KI8 direct REST lookup 2026-06-18

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

status: unverified


source_db: brenda

kcat_over_km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q15KI8 direct REST lookup 2026-06-18 and applied mutation signature H311A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H311A, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

source: brenda


substrate_name: 4-methylumbelliferyl beta-Lewis x

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q15KI8 and applied mutation signature M144H to reconstruct the assayed variant sequence.

column_label: Table 2, acceptor row LexbMU, M144H column block; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 8.1 mM; kcat cell = 8.4 s^-1; kcat/Km cell = 1.0 s^-1 mM^-1; author manuscript page 18 (PDF page 18). captured primary segment: LexβMU | PmST1 M144H, the M144H single mutant of Pasteurella multocida sialyltransferase 1 | Table 2, acceptor row LexβMU, M144H column block: Km 8.1 mM | kcat 8.4 s^-1 | kcat/Km printed cell 1.0 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 8.1 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 8.1 mM. kcat: printed cell 8.4 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 8.4 s^(-1). kcat/Km: printed cell 1.0 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 1.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acceptor row LexbMU, M144H column block: Km = 8.1 mM; kcat = 8.4 s^-1; printed kcat/Km = 1.0 s^-1 mM^-1.

table_label: Table 2 (Apparent kinetics of the alpha2-3-sialyltransferase activity of WT PmST1 and mutants), printed column blocks Km (mM) | kcat (s^-1) | kcat/Km (s^-1 mM^-1), each block split into the sub-columns WT | M144D | M144H

substrate: 4-methylumbelliferyl beta-Lewis x


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q15KI8 and applied mutation signature D141A to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row D141A; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 1.4 mM; kcat cell = 2.5 x 10^-2 s^-1; kcat/Km cell = 1.8 x 10^-2 s^-1 mM^-1; author manuscript page 17 (PDF page 17). captured primary segment: CMP-Neu5Ac | PmST1 D141A, the D141A single mutant of Pasteurella multocida sialyltransferase 1 | Table 1, enzyme row D141A: Km 1.4 mM | kcat 2.5 x 10^-2 s^-1 | kcat/Km printed cell 1.8 x 10^-2 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 1.4 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 1.4 mM. kcat: printed cell 2.5 x 10^-2 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 0.025 s^(-1). kcat/Km: printed cell 1.8 x 10^-2 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 0.018 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row D141A: Km = 1.4 mM; kcat = 2.5 x 10^-2 s^-1; printed kcat/Km = 1.8 x 10^-2 s^-1 mM^-1.

row_label: Table 1, enzyme row D141A


source_db: skid

source_license: CC BY-NC-ND 4.0

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

source: skid


organism: Photobacterium phosphoreum

kcat_display: Not reported

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

sequence_source: UniProtKB:A5LHX0 direct REST lookup 2026-06-18

proof_lines:
pH 6.0, 25°C
Raw SKiD Env: Temp=25°C, pH=6

source_databases_merged: brenda skid


organism: Photobacterium sp. JT-ISH-224

sequence_source: UniProtKB:A8QYL0 direct REST lookup 2026-06-18


organism: Rattus norvegicus

sequence_source: UniProtKB:Q02734 direct REST lookup 2026-06-18

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: cathepsin V

organism: Homo sapiens

sequence_source: UniProtKB:O60911 direct REST lookup 2026-06-18

enzyme: cathepsin V


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

proof_lines: pH 5.5, 37°C, presence of dermatan sulfate

proof_lines: pH 5.5, 37°C, presence of heparan sulfate

proof_lines: in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C


enzyme_display_name: aminodeoxyfutalosine deaminase

organism: Acidothermus cellulolyticus

sequence_source: UniProtKB:A0LRH8 direct REST lookup 2026-06-18

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'AFL', Acel0264 column group; column 'kcat (s-1)' = 6.8; column 'Km (uM)' = 6.0; column 'kcat/Km (M-1 s-1)' = 1.1 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 6.8 s^-1; already in s^-1, no unit conversion applies; normalized 6.8 s^(-1). Km: printed cell 6.0 uM; 6.0 / 1000 = 0.006 mM; normalized 0.006 mM. kcat/Km: printed cell 1.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^6 / 1000 = 1100 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row AFL, Acel0264 column group: kcat = 6.8 s^-1; Km = 6.0 uM; kcat/Km = 1.1 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row 'AFL', Acel0264 column group

table_label: Table 2: Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429 (Biochemistry 2013, 52(37))

enzyme: aminodeoxyfutalosine deaminase


sequence_source: UniProtKB:A0LRH8 reviewed canonical sequence

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'NECA', Acel0264 column group; column 'kcat (s-1)' = 0.007; column 'Km (uM)' = 61; column 'kcat/Km (M-1 s-1)' = 110.

normalized_value_unit_evidence: kcat: printed cell 0.007 s^-1; already in s^-1, no unit conversion applies; normalized 0.007 s^(-1). Km: printed cell 61 uM; 61 / 1000 = 0.061 mM; normalized 0.061 mM. kcat/Km: printed cell 110 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 110 / 1000 = 0.11 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row NECA, Acel0264 column group: kcat = 0.007 s^-1; Km = 61 uM; kcat/Km = 110 M^-1 s^-1.

row_label: Table 2, substrate row 'NECA', Acel0264 column group


organism: Deinococcus radiodurans

sequence_source: UniProtKB:Q9RW45 reviewed canonical sequence

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'AFL', Dr0824 column group; column 'kcat (s-1)' = 8.6; column 'Km (uM)' = 1.8; column 'kcat/Km (M-1 s-1)' = 4.8 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 8.6 s^-1; already in s^-1, no unit conversion applies; normalized 8.6 s^(-1). Km: printed cell 1.8 uM; 1.8 / 1000 = 0.0018 mM; normalized 0.0018 mM. kcat/Km: printed cell 4.8 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.8 x 10^6 / 1000 = 4800 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row AFL, Dr0824 column group: kcat = 8.6 s^-1; Km = 1.8 uM; kcat/Km = 4.8 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row 'AFL', Dr0824 column group


column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row '2'-deoxyadenosine', Dr0824 column group; column 'kcat (s-1)' = 0.72; column 'Km (uM)' = 37; column 'kcat/Km (M-1 s-1)' = 1.9 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.72 s^-1; already in s^-1, no unit conversion applies; normalized 0.72 s^(-1). Km: printed cell 37 uM; 37 / 1000 = 0.037 mM; normalized 0.037 mM. kcat/Km: printed cell 1.9 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^4 / 1000 = 19 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row 2'-deoxyadenosine, Dr0824 column group: kcat = 0.72 s^-1; Km = 37 uM; kcat/Km = 1.9 x 10^4 M^-1 s^-1.

row_label: Table 2, substrate row '2'-deoxyadenosine', Dr0824 column group


organism: Nitratiruptor sp. SB155-2

sequence_source: UniProtKB:A6Q234 reviewed canonical sequence

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row '5'-deoxyadenosine', Nis0429 column group; column 'kcat (s-1)' = 0.017; column 'Km (uM)' = 42; column 'kcat/Km (M-1 s-1)' = 410.

normalized_value_unit_evidence: kcat: printed cell 0.017 s^-1; already in s^-1, no unit conversion applies; normalized 0.017 s^(-1). Km: printed cell 42 uM; 42 / 1000 = 0.042 mM; normalized 0.042 mM. kcat/Km: printed cell 410 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 410 / 1000 = 0.41 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row 5'-deoxyadenosine, Nis0429 column group: kcat = 0.017 s^-1; Km = 42 uM; kcat/Km = 410 M^-1 s^-1.

row_label: Table 2, substrate row '5'-deoxyadenosine', Nis0429 column group


column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'AFL', Nis0429 column group; column 'kcat (s-1)' = 1.2; column 'Km (uM)' = 0.9; column 'kcat/Km (M-1 s-1)' = 1.3 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 1.2 s^-1; already in s^-1, no unit conversion applies; normalized 1.2 s^(-1). Km: printed cell 0.9 uM; 0.9 / 1000 = 0.0009 mM; normalized 0.0009 mM. kcat/Km: printed cell 1.3 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^6 / 1000 = 1300 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row AFL, Nis0429 column group: kcat = 1.2 s^-1; Km = 0.9 uM; kcat/Km = 1.3 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row 'AFL', Nis0429 column group


organism: Streptomyces avermitilis

substrate_name: adenosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q82K09 canonical sequence with selected-batch R87M reconstruction and applied mutation signature R87M to reconstruct the assayed variant sequence.

substrate: adenosine


sequence_source: UniProtKB:Q82K09 reviewed canonical sequence

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'AFL', Sav2595 column group; column 'kcat (s-1)' = 3.8; column 'Km (uM)' = 4.8; column 'kcat/Km (M-1 s-1)' = 7.9 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 3.8 s^-1; already in s^-1, no unit conversion applies; normalized 3.8 s^(-1). Km: printed cell 4.8 uM; 4.8 / 1000 = 0.0048 mM; normalized 0.0048 mM. kcat/Km: printed cell 7.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.9 x 10^5 / 1000 = 790 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row AFL, Sav2595 column group: kcat = 3.8 s^-1; Km = 4.8 uM; kcat/Km = 7.9 x 10^5 M^-1 s^-1.

row_label: Table 2, substrate row 'AFL', Sav2595 column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q82K09 and applied mutation signature R87M to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Constants for Sav2595 mutants), variant row 'R87M', AFL column group; column 'kcat (s-1)' = 0.42; column 'Km (uM)' = 8; column 'kcat/Km (M-1 s-1)' = 5.3 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.42 s^-1; already in s^-1, no unit conversion applies; normalized 0.42 s^(-1). Km: printed cell 8 uM; 8 / 1000 = 0.008 mM; normalized 0.008 mM. kcat/Km: printed cell 5.3 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.3 x 10^4 / 1000 = 53 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row R87M, AFL column group: kcat = 0.42 s^-1; Km = 8 uM; kcat/Km = 5.3 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'R87M', AFL column group

table_label: Table 3: Kinetic Constants for Sav2595 mutants (Biochemistry 2013, 52(37))


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q82K09 and applied mutation signature R87A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Constants for Sav2595 mutants), variant row 'R87A', AFL column group; column 'kcat (s-1)' = 0.094; column 'Km (uM)' = 3.4; column 'kcat/Km (M-1 s-1)' = 2.7 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.094 s^-1; already in s^-1, no unit conversion applies; normalized 0.094 s^(-1). Km: printed cell 3.4 uM; 3.4 / 1000 = 0.0034 mM; normalized 0.0034 mM. kcat/Km: printed cell 2.7 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.7 x 10^4 / 1000 = 27 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row R87A, AFL column group: kcat = 0.094 s^-1; Km = 3.4 uM; kcat/Km = 2.7 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'R87A', AFL column group


enzyme_display_name: 2-isopropylmalate synthase

organism: Arabidopsis thaliana

source_db: uniprot

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 2.3 sec(-1) with 2-oxoisovalerate as substrate (PubMed:17189332). kcat is 1.9 sec(-1) with acetyl-CoA as substrate (PubMed:17189332).

enzyme: 2-isopropylmalate synthase

source: uniprot


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 3.5 sec(-1) for 3-methyl-2-oxobutanoate and 2.1 for acetyl-CoA.


organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)

proof_lines: kcat is 13 sec(-1) for 3-methyl-2-oxobutanoate, 3.4 sec(-1) for 2-oxobutanoate, 0.027 sec(-1) for 3-methyl-2-oxopentanoate.


enzyme_display_name: methylthioalkylmalate synthase

organism: Eutrema japonicum

proof_lines: MAM1-2 is 2000 time faster than MAM1-1 to catalyze the conversion of 6-(methylsulfinyl)hexylisothiocyanate into 2-(2-methylsulfanyl)ethylmalate.

enzyme: methylthioalkylmalate synthase


proof_lines: MAM1-1 is 2000 time slower than MAM1-2 to catalyze the conversion of 6-(methylsulfinyl)hexylisothiocyanate into 2-(2-methylsulfanyl)ethylmalate.


enzyme_display_name: cinnamate beta-D-glucosyltransferase

organism: Fragaria ananassa

substrate_name: cinnamic acid

proof_lines: The kinetic constants are determined for the recombinant His(6)-tagged protein.

enzyme: cinnamate beta-D-glucosyltransferase

substrate: cinnamic acid


organism: Punica granatum

substrate_name: gallic acid (at pH 5.0 and 30 degrees Celsius)

assay_conditions_summary: pH 5

proof_lines: kcat is 0.55 sec(-1) with gallic acid as substrate. kcat is 0.6 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec(-1) with caffeic acid as substrate. kcat is


proof_lines: kcat is 0.52 sec(-1) with gallic acid as substrate. kcat is 0.61 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 0.76 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.64 sec(-1) with caffeic acid as substrate. kcat is

substrate: gallic acid (at pH 5.0 and 30 degrees Celsius)


organism: Mus musculus

proof_lines: Relative Vmax is 4:2:1 for Gal-beta-1,3-GlcNAc, Gal-beta-1,4-GlcNAc and Gal-beta-1,3-GalNAc as substrate, respectively.


proof_lines: Relative Vmax is 2:5:1 for Gal-beta-1,3-GlcNAc, Gal-beta-1,4-GlcNAc and Gal-beta-1,3-GalNAc as substrate, respectively.


proof_lines: kcat is 32 sec(-1) for CMP-N-acetyl-beta-neuraminate (alpha2,3-sialyltransferase activity) (PubMed:16351087). kcat is 47 sec(-1) for LacMU (alpha2,3-sialyltransferase activity) (PubMed:16351087). kcat is 227 sec(-1) for alpha-Neu5Ac-(2->3)-


enzyme_display_name: cysteine desulfurase

organism: Bacillus subtilis (strain 168)

substrate_name: L-cysteine

proof_lines: In the presence of dithiothreitol, which regenerates the second reaction product SufU.S.

enzyme: cysteine desulfurase

substrate: L-cysteine


enzyme_display_name: mycothione reductase

organism: Mycobacterium tuberculosis

substrate_name: H+; Desmyoinositol mycothione; NADPH

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

assay_conditions_summary: cofactor NADPH

proof_lines: des-myo-inositol mycothione as second substrate

enzyme: mycothione reductase

substrate: H+; Desmyoinositol mycothione; NADPH


proof_lines: pH and temperature not specified in the publication


organism: myxoma virus


organism: Pasteurella multocida

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M144D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: mutant enzyme M144D, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: mutant enzyme M144D, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C


column_label: Table 2, acceptor row LacbMU, M144H column block; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 0.79 mM; kcat cell = 21 s^-1; kcat/Km cell = 27 s^-1 mM^-1; author manuscript page 18 (PDF page 18). captured primary segment: LacβMU | PmST1 M144H, the M144H single mutant of Pasteurella multocida sialyltransferase 1 | Table 2, acceptor row LacβMU, M144H column block: Km 0.79 mM | kcat 21 s^-1 | kcat/Km printed cell 27 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 0.79 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 0.79 mM. kcat: printed cell 21 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 21.0 s^(-1). kcat/Km: printed cell 27 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 27.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acceptor row LacbMU, M144H column block: Km = 0.79 mM; kcat = 21 s^-1; printed kcat/Km = 27 s^-1 mM^-1.


column_label: Table 2, acceptor row LexbMU, WT column block; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 17 mM; kcat cell = 6.7 s^-1; kcat/Km cell = 0.38 s^-1 mM^-1; author manuscript page 18 (PDF page 18). captured primary segment: LexβMU | wild-type PmST1, the recombinant Pasteurella multocida sialyltransferase 1 | Table 2, acceptor row LexβMU, WT column block: Km 17 mM | kcat 6.7 s^-1 | kcat/Km printed cell 0.38 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 17 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 17.0 mM. kcat: printed cell 6.7 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 6.7 s^(-1). kcat/Km: printed cell 0.38 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 0.38 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acceptor row LexbMU, WT column block: Km = 17 mM; kcat = 6.7 s^-1; printed kcat/Km = 0.38 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q15KI8 and applied mutation signature M144D to reconstruct the assayed variant sequence.

column_label: Table 2, acceptor row LacbMU, M144D column block; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 12 mM; kcat cell = 22 s^-1; kcat/Km cell = 1.9 s^-1 mM^-1; author manuscript page 18 (PDF page 18). captured primary segment: LacβMU | PmST1 M144D, the M144D single mutant of Pasteurella multocida sialyltransferase 1 | Table 2, acceptor row LacβMU, M144D column block: Km 12 mM | kcat 22 s^-1 | kcat/Km printed cell 1.9 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 12 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 12.0 mM. kcat: printed cell 22 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 22.0 s^(-1). kcat/Km: printed cell 1.9 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 1.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acceptor row LacbMU, M144D column block: Km = 12 mM; kcat = 22 s^-1; printed kcat/Km = 1.9 s^-1 mM^-1.


column_label: Table 2, acceptor row LexbMU, M144D column block; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 13 mM; kcat cell = 4.0 s^-1; kcat/Km cell = 0.32 s^-1 mM^-1; author manuscript page 18 (PDF page 18). captured primary segment: LexβMU | PmST1 M144D, the M144D single mutant of Pasteurella multocida sialyltransferase 1 | Table 2, acceptor row LexβMU, M144D column block: Km 13 mM | kcat 4.0 s^-1 | kcat/Km printed cell 0.32 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 13 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 13.0 mM. kcat: printed cell 4.0 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 4.0 s^(-1). kcat/Km: printed cell 0.32 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 0.32 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acceptor row LexbMU, M144D column block: Km = 13 mM; kcat = 4.0 s^-1; printed kcat/Km = 0.32 s^-1 mM^-1.


column_label: Table 2, acceptor row LacbMU, WT column block; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 1.4 mM; kcat cell = 47 s^-1; kcat/Km cell = 34 s^-1 mM^-1; author manuscript page 18 (PDF page 18). captured primary segment: LacβMU | wild-type PmST1, the recombinant Pasteurella multocida sialyltransferase 1 | Table 2, acceptor row LacβMU, WT column block: Km 1.4 mM | kcat 47 s^-1 | kcat/Km printed cell 34 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 1.4 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 1.4 mM. kcat: printed cell 47 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 47.0 s^(-1). kcat/Km: printed cell 34 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 34.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acceptor row LacbMU, WT column block: Km = 1.4 mM; kcat = 47 s^-1; printed kcat/Km = 34 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D141A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D141A, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C


column_label: Table 1, enzyme row M144H; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 13 mM; kcat cell = 71 s^-1; kcat/Km cell = 5.5 s^-1 mM^-1; author manuscript page 17 (PDF page 17). captured primary segment: CMP-Neu5Ac | PmST1 M144H, the M144H single mutant of Pasteurella multocida sialyltransferase 1 | Table 1, enzyme row M144H: Km 13 mM | kcat 71 s^-1 | kcat/Km printed cell 5.5 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 13 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 13.0 mM. kcat: printed cell 71 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 71.0 s^(-1). kcat/Km: printed cell 5.5 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 5.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row M144H: Km = 13 mM; kcat = 71 s^-1; printed kcat/Km = 5.5 s^-1 mM^-1.

row_label: Table 1, enzyme row M144H


proof_lines: wild type enzyme, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: wild type enzyme, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: wild type enzyme, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C


column_label: Table 1, enzyme row M144D; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 7.3 mM; kcat cell = 6.5 s^-1; kcat/Km cell = 0.89 s^-1 mM^-1; author manuscript page 17 (PDF page 17). captured primary segment: CMP-Neu5Ac | PmST1 M144D, the M144D single mutant of Pasteurella multocida sialyltransferase 1 | Table 1, enzyme row M144D: Km 7.3 mM | kcat 6.5 s^-1 | kcat/Km printed cell 0.89 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 7.3 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 7.3 mM. kcat: printed cell 6.5 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 6.5 s^(-1). kcat/Km: printed cell 0.89 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 0.89 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row M144D: Km = 7.3 mM; kcat = 6.5 s^-1; printed kcat/Km = 0.89 s^-1 mM^-1.

row_label: Table 1, enzyme row M144D


enzyme_display_name: 3-hydroxybenzoate 6-monooxygenase

organism: Burkholderia cepacia

substrate_name: NADH

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

proof_lines:
cosubstrate 3-hydroxybenzoate
cosubstrate NADPH
cosubstrate NADH

enzyme: 3-hydroxybenzoate 6-monooxygenase

substrate: NADH


organism: Klebsiella pneumoniae

substrate_name: NADH; 3-Hydroxybenzoate; O2; H+

substrate: NADH; 3-Hydroxybenzoate; O2; H+


organism: Martelella sp. AD-3

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH


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


organism: Micrococcus sp.

assay_conditions_summary: cofactor NADH


organism: Polaromonas naphthalenivorans

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines: pH 8.0, 30°C, recombinant NagX, with NADH


organism: Pseudomonas aeruginosa


organism: Rhodococcus jostii

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines:
in 50 mM Tris-SO4 (pH 8.0), at 25°C
in 100 mM Tris-H2SO4 (pH 8.0), at 4°C


enzyme_display_name: thiol S-methyltransferase

organism: Physcomitrium patens

substrate_name: thiobenzoic acid

enzyme: thiol S-methyltransferase

substrate: thiobenzoic acid


organism: Rattus norvegicus

substrate_name: S-Aristeromycinyl-L-methionine

substrate: S-Aristeromycinyl-L-methionine


enzyme_display_name: bile acid-CoA:amino acid N-acyltransferase

organism: Bos taurus

substrate_name: Choloyl-CoA; Glycine

ki_unit: mM

substrate: Choloyl-CoA; Glycine


organism: Gallus gallus

substrate_name: Taurine; Choloyl-CoA

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

enzyme: bile acid-CoA:amino acid N-acyltransferase

substrate: Taurine; Choloyl-CoA


organism: Homo sapiens

substrate_name: choloyl-CoA

assay_conditions_summary: pH 8.4; 310.15 K; cofactor CoA

substrate: choloyl-CoA


proof_lines: mutant enzyme BAAT-S, at pH 8.4 and 37°C

proof_lines: mutant enzyme BAAT-SKL, at pH 8.4 and 37°C


proof_lines:
+ 60 mM glycine
+ 40 mM taurine


organism: Mus musculus

substrate_name: taurine

proof_lines: recombinant enzyme, expressed in Escherichia coli

substrate: taurine


proof_lines:
+ 0.05 mM deoxycholoyl-CoA
rats fed with cellulose
rats fed with pectin


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; cofactor CoA

proof_lines:
pH 8.0, isoform IPMS2
pH 8.0, isoform IPMS1


organism: Candida maltosa

substrate_name: acetyl-CoA

proof_lines: non-competitive, with respect to acetyl-CoA

proof_lines: competitive, with respect to 2-oxo-3-methylbutanoate

substrate: acetyl-CoA


organism: Cupriavidus necator

substrate_name: pyruvate

assay_conditions_summary: pH 8.1; cofactor CoA

proof_lines:
with acetyl-CoA as cosubstrate
with respect to acetyl-CoA
pH 8.1, acetyl-CoA varied

substrate: pyruvate


organism: Lachancea kluyveri

proof_lines: LkLeu4, pH and temperature not specified in the publication

proof_lines: LkLeu4BIS, pH and temperature not specified in the publication


organism: Malus domestica

proof_lines: cosubstrate: 2-oxobutanoate, pH and temperature not specified in the publication

proof_lines: cosubstrate: pyruvate, pH and temperature not specified in the publication


organism: Methanocaldococcus jannaschii

assay_conditions_summary: pH 7.8; 310.15 K; cofactor CoA

proof_lines:
at pH 7.8 and 37°C
at pH 7.8 and 37 °C


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA

proof_lines: cosubstrate 2-oxo-3-methylbutanoate, pH 7.4, 25°C


substrate_name: Unknown

km_display: Not reported

proof_lines: mutant enzyme D563A, pH and temperature not specified in the publication

substrate: Unknown


proof_lines: mutant enzyme Q566A, pH and temperature not specified in the publication


proof_lines: mutant enzyme S560W, pH and temperature not specified in the publication


proof_lines: mutant enzyme H540A, pH and temperature not specified in the publication


proof_lines: mutant enzyme M559A, pH and temperature not specified in the publication


proof_lines: mutant enzyme D564A, pH and temperature not specified in the publication


proof_lines: mutant enzyme D563N, pH and temperature not specified in the publication


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


enzyme_display_name: CoA-disulfide reductase

organism: Bacillus anthracis

substrate_name: CoA-disulfide

assay_conditions_summary: 298.15 K; cofactor NADH

proof_lines: 25°C, mutant enzyme Y25F. Cosubstrate: NADH

enzyme: CoA-disulfide reductase

substrate: CoA-disulfide


substrate_name: NADPH

sequence_source: NCBI RefSeq NP_843735.1; PMID 18399646 full text

assay_conditions_summary: 298.15 K; cofactor NADPH

proof_lines: 25°C, wild-type enzyme, cosubstrate: NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from Reconstructed from NCBI RefSeq NP_843735.1 using PMID 18399646 Y367F BACoADR evidence and applied mutation signature Y367F to reconstruct the assayed variant sequence.

proof_lines: 25°C, mutant enzyme Y367F. Cosubstrate: NADH


sequence_variant_note: Resolved canonical sequence from Reconstructed from NCBI RefSeq NP_843735.1 using PMID 18399646 Y425F BACoADR evidence and applied mutation signature Y425F to reconstruct the assayed variant sequence.


organism: Staphylococcus aureus

substrate_name: CoA-ethyl disulfide

assay_conditions_summary: pH 7.8; 298.15 K; cofactor CoA

proof_lines: temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4

substrate: CoA-ethyl disulfide


sequence_source: UniProtKB/Swiss-Prot P9WHH3; identical strict M. tuberculosis candidates P9WHH2/A5U6K7 share this sequence

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADPH


organism: Rhodococcus erythropolis

sequence_source: UniProtKB/TrEMBL C0ZY75; RefSeq WP_020907415.1; PMID 33377161 PR4 paper anchor

proof_lines: in PBS at pH 7.4, temperature not specified in the publication

proof_lines: in 20 mM HEPES, at pH 7.0, temperature not specified in the publication

proof_lines: in 20 mM TEA-HCl, at pH 7.6, temperature not specified in the publication


organism: Catharanthus roseus

substrate_name: S-adenosyl-L-methionine

proof_lines: when assayed with benzene thiol and furfuryl thiol

substrate: S-adenosyl-L-methionine


organism: Euglena gracilis


substrate_name: dihydroziprasidone

substrate: dihydroziprasidone


organism: Oryza sativa

substrate_name: thiocyanate

proof_lines: 0.5 mM S-adenosyl-L-methionine, pH 7.5, 25°C

substrate: thiocyanate


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


proof_lines: mutant enzyme D81E/N321I, at pH 7.5 and 25°C


organism: Neurospora crassa

assay_conditions_summary: pH 7; cofactor CoA


organism: Salmonella enterica subsp. enterica serovar Typhimurium

assay_conditions_summary: pH 6.8; cofactor CoA

proof_lines: pH 6.8, 0.4 mM acetyl-CoA, 0.1 mM 2-oxo-3-methylbutanoate, wild-type enzyme

proof_lines: pH 6.8, 0.8 mM acetyl-CoA, 4 mM 2-oxo-3-methylbutanoate, wild-type enzyme


proof_lines: pH 6.8, 0.4 mM acetyl-CoA, 0.1 mM 2-oxo-3-methylbutanoate, feedback-resistent enzyme

proof_lines: pH 6.8, 0.8 mM acetyl-CoA, 4 mM 2-oxo-3-methylbutanoate, feedback-resistent enzyme


organism: Spinacia oleracea

assay_conditions_summary: cofactor CoA


organism: Brassica juncea

proof_lines: pH 7.5, 25°C, wild-type enzyme, Mn2+ as metal cofactor

proof_lines: pH 7.5, 25°C, wild-type enzyme, Mg2+ as metal cofactor


substrate_name: 4-methylthio-2-oxobutanoic acid

proof_lines: pH 7.5, 25°C, mutant enzyme H388N, Mg2+ as metal cofactor

proof_lines: pH 7.5, 25°C, mutant enzyme H388N, Mn2+ as metal cofactor

substrate: 4-methylthio-2-oxobutanoic acid


proof_lines: pH 7.5, 25°C, mutant enzyme E227Q, Mg2+ as metal cofactor

proof_lines: pH 7.5, 25°C, mutant enzyme E227Q, Mn2+ as metal cofactor


enzyme_display_name: glycogen(starch) synthase

organism: Ascaris suum

substrate_name: UDP-glucose

proof_lines: value independent of glucose 6-phosphate concentration

enzyme: glycogen(starch) synthase

substrate: UDP-glucose


organism: Bos taurus

proof_lines:
without glucose-6-phosphate
with glucose-6-phosphate


organism: Calyptocephallela gayi


organism: Crypthecodinium cohnii

substrate_name: amylopectin

assay_conditions_summary: cofactor ADP

proof_lines:
high-mobility isoform
low-mobility isoform

substrate: amylopectin


organism: Dictyostelium discoideum


organism: Homo sapiens

proof_lines: value dependent on the presence of glucose 6-phosphate


organism: Mytilus edulis

proof_lines:
UDP-glucose, synthase D
synthase I


organism: Oryctolagus cuniculus

proof_lines:
with Na2SO4, form I
presence of glucose 6-phosphate
absence of glucose 6-phosphate


organism: Pelophylax ridibundus


organism: Pyrococcus furiosus

substrate_name: ADP-glucose

assay_conditions_summary: pH 5; 353.15 K; cofactor ADP

substrate: ADP-glucose


organism: Rattus norvegicus

substrate_name: UDPglucose; (1,4-alpha-D-Glucosyl)n

substrate: UDPglucose; (1,4-alpha-D-Glucosyl)n


organism: Saccharomyces cerevisiae

proof_lines:
value dependent on glucose 6-phosphate
dependent on glucose-6-phosphate


organism: Streptomyces avermitilis

sequence_source: UniProtKB Q82K09 canonical sequence retrieved directly for the wild-type accession.


substrate_name: adenosine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q82K09 canonical sequence with R87A reconstruction from PMID 23972005 mutation context. and applied mutation signature R87A to reconstruct the assayed variant sequence.

substrate: adenosine


organism: Sus scrofa

proof_lines: synthase I, 25°C, presence of glucose 6-phosphate

proof_lines: synthase I, 37°C, presence of glucose 6-phosphate

proof_lines: synthase I, 25°C, absence of glucose 6-phosphate


organism: Trichomonas vaginalis

sequence_source: UniProtKB reviewed entry A2E926 fetched by direct EC 2.4.1.11 + Trichomonas vaginalis lookup on 2026-06-18

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

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


organism: Fragaria x ananassa

substrate_name: trans-3-(2-furyl)acrylic acid

substrate: trans-3-(2-furyl)acrylic acid


organism: Ipomoea batatas


organism: Phaseolus vulgaris

substrate_name: Cinnamic acid

substrate: Cinnamic acid


organism: Bifidobacterium bifidum

substrate_name: phosphate

substrate: phosphate


organism: Bifidobacterium longum subsp. Longum

sequence_source: UniProtKB reviewed entry E8MF13 fetched by direct EC 2.4.1.211 + Bifidobacterium longum lookup on 2026-06-18


organism: Clostridium perfringens ATCC 13124


organism: Escherichia coli

substrate_name: hypoxanthine

substrate: hypoxanthine


substrate_name: guanine

substrate: guanine


proof_lines:
37°C, pH 7.3, wild-type enzyme
pH 7.3, 37°C, wild-type


substrate_name: queuine

proof_lines: pH and temperature not specified in the publication

substrate: queuine


organism: Triticum aestivum


organism: Zymomonas mobilis

substrate_name: Unknown

substrate: Unknown


organism: Gallus gallus


organism: Helicobacter bizzozeronii

substrate_name: FCHASE beta-D-Gal-(1->4)-beta-D-GlcNAc

substrate: FCHASE beta-D-Gal-(1->4)-beta-D-GlcNAc


enzyme_display_name: [myosin light-chain] kinase

organism: Bos taurus

substrate_name: myosin light chain

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ATP

enzyme: [myosin light-chain] kinase

substrate: myosin light chain


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Homo sapiens

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: at 25Â°C, pH not specified in the publication


organism: Limulus sp.

substrate_name: Limulus myosin light chain

substrate: Limulus myosin light chain


organism: Meleagris gallopavo

assay_conditions_summary: pH 7.3; 297.15 K; cofactor ATP


organism: Mus musculus

substrate_name: unphosphorylated myosin II regulatory light chain


organism: Oryctolagus cuniculus

substrate_name: myosin regulatory light chain

assay_conditions_summary: pH 7

substrate: myosin regulatory light chain


assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines: 25°C, pH 7.6, isolated, freshly prepared


organism: Ovis aries

substrate_name: turkey gizzard myosin light chain

substrate: turkey gizzard myosin light chain


organism: Rattus norvegicus

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Sus scrofa


enzyme_display_name: inositol-trisphosphate 3-kinase

substrate_name: 1D-myo-inositol 1,4,5-trisphosphate

proof_lines: pH 7.2, 37°C, in presence or absence of 50 nM calmodulin

enzyme: inositol-trisphosphate 3-kinase

substrate: 1D-myo-inositol 1,4,5-trisphosphate


organism: Calyptocephallela gayi


proof_lines: recombinant wild-type catalytic/CaM binding domain, pH 7.5, 30°C


proof_lines: recombinant mutant K272D catalytic/CaM binding domain, pH 7.5, 30°C


proof_lines: recombinant mutant K268E catalytic/CaM binding domain, pH 7.5, 30°C


proof_lines: recombinant enzyme fragment comprising calmodulin binding domain

proof_lines: IP3K-A, non-competitive with respect to Ins(1,4,5)P3


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines:
pH 7.4, 37°C, platelet enzyme
pH 7.4, 37°C
pH 7.4


proof_lines: pH 7.5, 30°C, recombinant, catalytically active fragment of isoform C

proof_lines: recombinant catalytic/CaM binding domain, pH 7.5, 30°C


enzyme_display_name: polynucleotide 5'-hydroxyl-kinase

substrate_name: oligo (dT)25

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: polymin P precipitable enzyme, pH 7.5, 37°C

enzyme: polynucleotide 5'-hydroxyl-kinase

substrate: oligo (dT)25


organism: Escherichia phage T2

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


assay_conditions_summary: pH 8.4; 310.15 K; cofactor ATP


organism: Kostyavirus CJW1

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP


substrate_name: [gamma-S]ATP

substrate: [gamma-S]ATP


organism: Omegavirus omega


assay_conditions_summary: pH 5.5; 310.15 K; cofactor ATP

proof_lines:
pH 5.5, 37°C
pH 5.5
competitive versus ATP, pH 5.5, 37°C


organism: Rhodothermus phage RM378

assay_conditions_summary: pH 6; 338.15 K; cofactor ATP


organism: Runella slithyformis

assay_conditions_summary: pH 6; cofactor ATP

proof_lines:
at pH 6.0 and 37Â°C
at pH 8.0 and 37Â°C


organism: synthetic ribozyme

assay_conditions_summary: pH 6; 303.15 K; cofactor ATP

proof_lines: pH-independent in the range pH 6.0-8.5, 30°C


organism: Tequatrovirus T4

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: phosphate exchange reaction between nucleotides, forward reaction, pH 7.6, 37°C

proof_lines: dephosphorylation of single-stranded oligonucleotides, pH 7.6, 37°C


proof_lines:
mutant pseT 1, pH 7.6, 37°C
mutant pseT 47, pH 7.6, 37°C


organism: unidentified baculovirus

assay_conditions_summary: pH 5; 303.15 K; cofactor ATP


organism: Arabidopsis thaliana

substrate_name: myo-inositol

substrate: myo-inositol


organism: Bos taurus

substrate_name: CDP-didecanoyl-sn-glycerol

substrate: CDP-didecanoyl-sn-glycerol


organism: Candida albicans


organism: Canis familiaris

substrate_name: myo-Inositol; CDP-1,2-diacylglycerol

substrate: myo-Inositol; CDP-1,2-diacylglycerol


organism: Canis lupus familiaris


organism: Cavia porcellus


organism: Chlamydomonas reinhardtii

proof_lines:
pH 8.5, 37°C, exchange reaction
pH 8.5, 37°C


organism: Homo sapiens


organism: Oryctolagus cuniculus


organism: Plasmodium knowlesi

substrate_name: CDP-diacylglycerol

substrate: CDP-diacylglycerol


organism: Rattus norvegicus


organism: Ricinus communis


organism: Saccharomyces cerevisiae

proof_lines:
pH 8.0, 37°C
pH 8.0, 30°C
pH 8.0, 30°C, forward reaction


organism: Acidithiobacillus ferrooxidans

substrate_name: L-cysteine

proof_lines: in 50 mM Tris-HCl (pH 8.0), 10 mM MgCl2, 5 mM dithiothreitol, at 25°C

substrate: L-cysteine


proof_lines: 25°C, pH 7.4, presence of chloroplast protein CpSufE


organism: Azotobacter vinelandii


organism: Bacillus subtilis

substrate_name: Acceptor; L-Cysteine

proof_lines: in 50 mM MOPS (pH 7.4), temperature not specified in the publication

substrate: Acceptor; L-Cysteine


organism: Dickeya chrysanthemi

substrate_name: L-selenocysteine

substrate: L-selenocysteine


organism: Escherichia coli

assay_conditions_summary: pH 8

proof_lines:
pH 8, CSD in the presence of pyruvate
pH 8, IcsS in the presence of pyruvate
pH 8, IcsS in the absence of pyruvate


organism: Lentinula edodes


organism: Streptomyces lividans


enzyme_display_name: juvenile-hormone esterase

organism: Bombyx mori

substrate_name: juvenile hormone III

enzyme: juvenile-hormone esterase

substrate: juvenile hormone III


organism: Drosophila melanogaster

substrate_name: Alpha-naphthyl acetate

substrate: Alpha-naphthyl acetate


organism: Galleria mellonella

substrate_name: juvenile hormone I

substrate: juvenile hormone I


organism: Elizabethkingia meningoseptica

proof_lines:
mutant with T152C
mutant enzyme T152C


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant D66N


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant D183E


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant T152S


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant W11S


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant T170S


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant D183N


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant T170C


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant T203A


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant R180L


organism: Leptinotarsa decemlineata

proof_lines:
pH 8, major enzyme form with pI 5.6
pH 8, minor enzyme form with pI 5.5


organism: Lymantria dispar

proof_lines: racemic, (10R,11S)-enantiomer of juvenile hormone II


organism: Rhyparobia maderae

substrate_name: Juvenile hormone

proof_lines: during vitellogenesis, kcat at ovulation time is 2-3times higher than earlier during vitellogenesis

proof_lines: at ovulation time, kcat at ovulation time is 2-3times higher than earlier during vitellogenesis

substrate: Juvenile hormone


organism: Spodoptera frugiperda

proof_lines: pH not specified in the publication, 30°C


organism: Spodoptera littoralis


organism: Trichoplusia ni

proof_lines: second value 0.0025 mM, enzyme in crude hemolymph

proof_lines: second value 0.00034 mM, enzyme in crude hemolymph


enzyme_display_name: fluoroacetyl-CoA thioesterase

organism: Streptantibioticus cattleyicolor

substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB Q1EMV2 canonical sequence; V23A variant reconstructed from selected BRENDA mutation note and UniProt/PubMed 20836570 mutagenesis evidence. and applied mutation signature V23A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor CoA

enzyme: fluoroacetyl-CoA thioesterase

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1EMV2 canonical sequence; F36A variant reconstructed from selected BRENDA mutation note and UniProt/PubMed 20836570 mutagenesis evidence. and applied mutation signature F36A to reconstruct the assayed variant sequence.


substrate_name: fluoroacetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB Q1EMV2 canonical sequence; H76A variant reconstructed from selected BRENDA mutation note and UniProt/PubMed 20836570 mutagenesis evidence. and applied mutation signature H76A to reconstruct the assayed variant sequence.

substrate: fluoroacetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1EMV2 canonical sequence; T42S variant reconstructed from selected BRENDA mutation note and UniProt/PubMed 20836570 mutagenesis evidence. and applied mutation signature T42S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1EMV2 canonical sequence; L26A variant reconstructed from selected BRENDA mutation note and UniProt/PubMed 20836570 mutagenesis evidence. and applied mutation signature L26A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1EMV2 canonical sequence; E50Q variant reconstructed from selected BRENDA mutation note and UniProt/PubMed 20836570 mutagenesis evidence. and applied mutation signature E50Q to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant T203S


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant R180Q


proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant R180K


organism: Gallus gallus


organism: Homo sapiens

proof_lines: at 37°C and pH 7.7, pH- and temperature dependend


organism: Rattus sp.


organism: Sus scrofa

proof_lines: amidase-1 and amidase-2, value depending on enzyme concentration


enzyme_display_name: dCMP deaminase

organism: Bacillus subtilis

substrate_name: dCMP

enzyme: dCMP deaminase

substrate: dCMP


organism: Equus asinus


organism: Escherichia phage T2

assay_conditions_summary: pH 6

proof_lines: pH 8.3, in the presence of dCTP or 5-hydroxymethyl-dCTP. Decreasing the pH to 6.0 lowers the apparent Km


organism: Herpes simplex virus

proof_lines: in the presence of dCTP and presence of 2 mM Mg2+

proof_lines: in the presence of dCTP and absence of 2 mM Mg2+


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1EMV2 with row-specific F33A reconstruction and applied mutation signature F33A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1EMV2 with row-specific T42A reconstruction and applied mutation signature T42A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1EMV2 with row-specific T42C reconstruction and applied mutation signature T42C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q1EMV2


enzyme_display_name: cathepsin V

substrate_name: Z-Phe-Arg-4-methyl-7-coumaryl amide

sequence_source: UniProtKB O60911

assay_conditions_summary: pH 5.5; 298.15 K; buffer 100 mM sodium acetate

proof_lines: recombinant enzyme, pH 5.5, 25°C, in presence of 0.3 M NaCl

enzyme: cathepsin V

substrate: Z-Phe-Arg-4-methyl-7-coumaryl amide


substrate_name: Ac-DVAD-p-nitroanilide

proof_lines:
pH 7.0
wid-type protein
pH 7.2, 37°C

substrate: Ac-DVAD-p-nitroanilide


substrate_name: N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide

sequence_source: UniProtKB P55210

substrate: N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide


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

proof_lines: mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and 195-200, processed with thrombin

proof_lines: mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and inserted after Asp-203, processed with thrombin


enzyme_display_name: N(4)-acetylcytidine amidohydrolase

organism: Buttiauxella agrestis

enzyme: N(4)-acetylcytidine amidohydrolase


organism: Cronobacter universalis


organism: Klebsiella pneumoniae


organism: Shewanella loihica


enzyme_display_name: fructose-6-phosphate phosphoketolase

organism: Bifidobacterium animalis subsp. lactis

substrate_name: D-xylulose 5-phosphate, D-fructose 6-phosphate

sequence_source: UniProtKB reviewed accession Q9AEM9 REST/FASTA direct check on 2026-06-18

enzyme: fructose-6-phosphate phosphoketolase


organism: Bifidobacterium breve

substrate_name: phosphate, D-fructose 6-phosphate

proof_lines: in 40 mM potassium phosphate pH 6.5, 25 mM MES buffer pH 6.5, 0.02 mM ThDP and 0.1 mM MgCl2, at 22°C

substrate: phosphate, D-fructose 6-phosphate


organism: Bifidobacterium dentium

substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


organism: Bifidobacterium pseudolongum subsp. globosum


organism: Komagataeibacter xylinus

substrate_name: phosphate, fructose 6-phosphate

substrate: phosphate, fructose 6-phosphate


organism: Lactiplantibacillus paraplantarum

substrate_name: D-fructose 6-phosphate

proof_lines: in 71 mM sodium fluoride and 24 mM sodium iodoacetate, at 37°C

substrate: D-fructose 6-phosphate


organism: Lactiplantibacillus plantarum

substrate_name: D-fructose 6-phosphate, phosphate

substrate: D-fructose 6-phosphate, phosphate


organism: Lactococcus lactis

substrate: D-xylulose 5-phosphate, D-fructose 6-phosphate


organism: Leuconostoc mesenteroides


organism: Leuconostoc mesenteroides subsp. mesenteroides

substrate_name: D-fructose 6-phosphate, D-xylulose 5-phosphate


organism: Pseudomonas aeruginosa


organism: Homo sapiens


organism: Mycoplasma mycoides


organism: Rattus norvegicus

substrate_name: deoxycytidine

proof_lines: pH 8.1, 37°C, NM-16 fibroblasts in presence of 0.02 mM docosahexanoic acid

proof_lines: pH 8.1, 37°C, Rat-2 fibroblasts in presence of 0.02 mM docosahexanoic acid

substrate: deoxycytidine


organism: Saccharomyces cerevisiae


organism: Tequatrovirus T4

proof_lines:
R115E
mutant R115E, pH 8.0, 30°C
R115E, absence of dCTP


proof_lines:
wild-type
wild-type enzyme, pH 8.0, 30°C
wild-type, presence of dCTP and Mg2+


proof_lines:
R115Q dimer
mutant R115Q, pH 8.0, 30°C
R115Q hexamer


organism: African swine fever virus

substrate_name: diphosphoinositol pentakisphosphate

substrate: diphosphoinositol pentakisphosphate


organism: Drosophila melanogaster

substrate_name: guanosine tetraphosphate

proof_lines: in the presence of 10 mM Mg2+, at pH 9.0 and 26°C

substrate: guanosine tetraphosphate


organism: Mus musculus


substrate_name: 5-diphosphoinositol pentakisphosphate

substrate: 5-diphosphoinositol pentakisphosphate


substrate_name: L-cysteine (when in complex with bcn92, IscU and fh)

proof_lines: kcat is 2.6 min(-1) with L-cysteine as a substrate (when in complex with bcn92, IscU and fh).


organism: Escherichia coli (strain K12)

substrate_name: L-cysteine

substrate: L-cysteine


proof_lines: Kinetic parameter was determined for the protein lacking the 55 N-terminal amino acids and in a complex with LYRM4.


enzyme_display_name: aminodeoxyfutalosine deaminase

organism: Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B)

substrate_name: aminodeoxyfutalosine

verification_status: verified

enzyme: aminodeoxyfutalosine deaminase

substrate: aminodeoxyfutalosine

status: verified


organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)


organism: Nitratiruptor sp. (strain SB155-2)

proof_lines: kcat is 1.28 sec(-1) with aminodeoxyfutalosine as substrate. kcat is 0.31 sec(-1) with 5'-methylthioadenosine as substrate. kcat is 0.017 sec(-1) with 5'-deoxyadenosine as substrate.


organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)


enzyme_display_name: thyroxine 5-deiodinase

organism: Aquarana catesbeiana

sequence_source: UniProtKB reviewed accession P49898

assay_conditions_summary: pH 7

enzyme: thyroxine 5-deiodinase


organism: Bacillus subtilis


organism: Gallus gallus

proof_lines:
pH 7.2, 37°C
isozyme type III


proof_lines:
pH 7.4, 37°C, isozyme Dio2
pH 7.4, 37°C, isozyme Dio3
pH 7.4, 37°C, isozyme Dio1


substrate_name: L-thyroxine

proof_lines:
pH 7.4, 37°C
not influenced by selenium-deficiency
pH 7.5, 37°C, isozyme type III

substrate: L-thyroxine


organism: Chiloscyllium punctatum

sequence_source: UniProtKB:A9QW70 REST lookup on 2026-06-18

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

assay_conditions_summary: buffer phosphate

proof_lines: recombinant enzyme, in phosphate buffer, in presence of 400 mM urea


organism: Homo sapiens

substrate_name: Reduced acceptor; L-Thyroxine

sequence_source: UniProtKB:P55073 REST lookup on 2026-06-18

substrate: Reduced acceptor; L-Thyroxine


proof_lines: SABIO-RK modifier species: thyroxine 5-deiodinase(Enzyme) mutant SeC144C

proof_lines: recombinant mutant SeC144C, pH 7.2, 37°C, in presence of 0.3 mM DTT

proof_lines: recombinant mutant SeC144C, pH 7.2, 37°C, in presence of 1 mM DTT


proof_lines: native wild-type, pH 7.2, 37°C, in presence of 10 mM DTT

proof_lines: native wild-type, pH 7.2, 37°C, in presence of 1 mM DTT

proof_lines: recombinant wild-type, pH 7.2, 37°C, in presence of 0.3 mM DTT


substrate_name: Triiodothyronine; Reduced acceptor

proof_lines: SABIO-RK modifier species: thyroxine 5-deiodinase(Enzyme) mutant P146S

substrate: Triiodothyronine; Reduced acceptor


organism: Oreochromis niloticus

sequence_source: UniProtKB:Q9I966 REST lookup on 2026-06-18


organism: Pituophis deppei

sequence_source: UniProtKB:D2J363 REST lookup on 2026-06-18

proof_lines: recombinant enzyme, at 30°C, at pH 7.0, with 50 mM dithiothreitol

proof_lines: native enzyme, at 30°C, at pH 7.0, with 50 mM dithiothreitol


organism: Arabidopsis thaliana

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

assay_conditions_summary: pH 8; 303.15 K; cofactor FMN


sequence_source: UniProtKB:Q9LDD5 REST lookup on 2026-06-18


substrate_name: FMN

substrate: FMN


sequence_source: UniProtKB:P42962 REST lookup on 2026-06-18


substrate_name: Riboflavin-5-phosphate; H2O

substrate: Riboflavin-5-phosphate; H2O


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


substrate_name: H2O; Riboflavin-5-phosphate

sequence_source: UniProtKB:P96741 REST lookup on 2026-06-18

substrate: H2O; Riboflavin-5-phosphate


organism: Bacillus subtilis (strain 168)


assay_conditions_summary: pH 9; cofactor FMN


organism: Bacteroides thetaiotaomicron

substrate_name: D-ribitol 5-phosphate

substrate: D-ribitol 5-phosphate


substrate_name: D-ribitol 1-phosphate

substrate: D-ribitol 1-phosphate


substrate_name: octyl acetate

proof_lines: isozyme Ib, (alpha1)2 subunit, pH 7.5, 22°C

proof_lines: isozyme Ib, (alpha2)2 subunit, pH 7.5, 22°C

substrate: octyl acetate


assay_conditions_summary: cofactor FMN

proof_lines: kcat is 0.59 sec(-1) for FMN (PubMed:22002057). kcat is 2.80 sec(-1) for 5-amino-6-(5-phospho-D-ribitylamino)uracil (PubMed:27490826).


proof_lines: kcat is 0.13 sec(-1) for 5-amino-6-(5-phospho-D-ribitylamino)uracil.


organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

proof_lines: kcat is 1.8 sec(-1) with D-ribitol-1-phosphate as substrate. kcat is 1.5 sec(-1) with D-ribitol-5-phosphate as substrate. kcat is 0.016 sec(-1) with 5-amino-6-(5-phospho-D-ribitylamino)uracil as substrate.


organism: Bos taurus

substrate_name: acetylated platelet-activation factor

substrate: acetylated platelet-activation factor


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

proof_lines: SABIO-RK modifier species: 1-alkyl-2-acetylglycerophosphocholine esterase(Enzyme) mutant H92/T198 (PAF4/7) N-terminally His-tagged

proof_lines: SABIO-RK modifier species: 1-alkyl-2-acetylglycerophosphocholine esterase(Enzyme) mutant H92/V379 (PAF4/11) N-terminally His-tagged

proof_lines: SABIO-RK modifier species: 1-alkyl-2-acetylglycerophosphocholine esterase(Enzyme) mutant H92/T198/V379 (PAF4/7/11) N-terminally His-tagged


organism: Thermus thermophilus

substrate_name: S-Adenosyl-L-methionine; tRNA containing guanosine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16; source accession Q5SM16; reconstructed S150A and applied mutation signature S150A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant S150A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16; source accession Q5SM16; reconstructed R41K and applied mutation signature R41K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant R41K

substrate: S-Adenosyl-L-methionine; tRNA containing guanosine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16; source accession Q5SM16; reconstructed E124A and applied mutation signature E124A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant E124A


sequence_source: UniProtKB reviewed Q29460

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


sequence_source: UniProtKB reviewed Q13093


substrate_name: tRNA containing guanosine; S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed primary accession Q5SM16; Q9FAC4 resolves to Q5SM16 where present in source evidence. and applied mutation signature N152A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant N152A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed primary accession Q5SM16; Q9FAC4 resolves to Q5SM16 where present in source evidence. and applied mutation signature L151A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant L151A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed primary accession Q5SM16; Q9FAC4 resolves to Q5SM16 where present in source evidence. and applied mutation signature I142A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant I142A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed primary accession Q5SM16; Q9FAC4 resolves to Q5SM16 where present in source evidence. and applied mutation signature V128A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant V128A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed primary accession Q5SM16; Q9FAC4 resolves to Q5SM16 where present in source evidence. and applied mutation signature M144A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant M144A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed primary accession Q5SM16; Q9FAC4 resolves to Q5SM16 where present in source evidence. and applied mutation signature T99A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant T99A

substrate: tRNA containing guanosine; S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed primary accession Q5SM16; Q9FAC4 resolves to Q5SM16 where present in source evidence. and applied mutation signature L101A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanosine18-2'-O)-methyltransferase(Enzyme) mutant L101A


sequence_source: UniProtKB reviewed primary accession Q5SM16; Q9FAC4 resolves to Q5SM16 where present in source evidence.

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


organism: Rattus norvegicus


organism: Canis lupus familiaris


organism: Felis catus


organism: Mus musculus


organism: Suncus murinus


organism: Sus scrofa


organism: Xenopus laevis

substrate_name: L-thyroxine (outer-ring deiodination activity)


organism: Acidothermus cellulolyticus

sequence_source: UniProtKB REST FASTA/TSV direct check on 2026-06-18; reviewed accession with EC 3.5.4.40 and aminodeoxyfutalosine deaminase annotation.


organism: Deinococcus radiodurans


organism: Nitratiruptor sp. SB155-2


organism: Streptomyces avermitilis


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA/TSV direct check on 2026-06-18; reviewed accession with EC 3.5.4.40 and aminodeoxyfutalosine deaminase annotation. and applied mutation signature R87A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R87A, at pH 7.5 and at 30°C


substrate_name: adenosine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA/TSV direct check on 2026-06-18; reviewed accession with EC 3.5.4.40 and aminodeoxyfutalosine deaminase annotation. and applied mutation signature R87M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R87M, at pH 7.5 and at 30°C

substrate: adenosine


organism: Homo sapiens

substrate_name: LDL

proof_lines: Affinity for LDL is 2.3 to 4-fold lower than for HDL. Relative reactivities are 16% for HDL(3), 1.3% for HDL(2) and 6.5% for LDL.

substrate: LDL


enzyme_display_name: sterol O-acyltransferase

assay_conditions_summary: cofactor CoA

enzyme: sterol O-acyltransferase


enzyme_display_name: gamma-glutamyltransferase

organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_reconstruction and applied mutation signature S463T to reconstruct the assayed variant sequence.

enzyme: gamma-glutamyltransferase


organism: Bacillus licheniformis

sequence_source: UniProtKB:Q65KZ6 (queried via source accession Q62WE3 on 2026-06-18)


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q65KZ6 (queried via source accession Q62WE3 on 2026-06-18) and applied mutation signature N450Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A9YTT0 (queried via source accession A9YTT0 on 2026-06-18) and applied mutation signature R109F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A9YTT0 (queried via source accession A9YTT0 on 2026-06-18) and applied mutation signature R109M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A9YTT0 (queried via source accession A9YTT0 on 2026-06-18)


sequence_variant_note: Resolved canonical sequence from UniProtKB:A9YTT0 (queried via source accession A9YTT0 on 2026-06-18) and applied mutation signature R109E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A9YTT0 (queried via source accession A9YTT0 on 2026-06-18) and applied mutation signature R109L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A9YTT0 (queried via source accession A9YTT0 on 2026-06-18) and applied mutation signature R109K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A9YTT0 (queried via source accession A9YTT0 on 2026-06-18) and applied mutation signature R109S to reconstruct the assayed variant sequence.


substrate_name: PEA

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

substrate: PEA


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: phosphocholine

substrate: phosphocholine


organism: Candida albicans

substrate_name: cholesterol

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

substrate: cholesterol


organism: Chlorocebus aethiops

proof_lines: pyripyropene A-insensitive chimera A2:1-428

proof_lines: pyripyropene A-insensitive chimera A2:1-479


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

proof_lines: pyripyropene A-insensitive mutant A2Q492L

proof_lines: pyripyropene A-insensitive mutant A2V493L

proof_lines: pyripyropene A-insensitive mutant A2S494C


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


proof_lines:
HisACAT1, mutant HisACAT1/P64
mutant HisACAT1/1-65


proof_lines: in the absence of acyl-CoA binding protein

proof_lines: pH and temperature not specified in the publication


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


organism: Oryctolagus cuniculus

substrate_name: Unknown

proof_lines:
liver enzyme
greater than, liver enzyme
less than, aortic enzyme

substrate: Unknown


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


organism: Arabidopsis thaliana


substrate_name: Phosphoethanolamine

smiles: NCCOP(=O)(O)O

substrate: Phosphoethanolamine


organism: Pseudomonas aeruginosa

substrate_name: p-nitrophenyl phosphate

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

substrate: p-nitrophenyl phosphate


substrate_name: 4-nitrophenyl phosphate

proof_lines: purified recombinant mutant E43A, pH 5.0, 37°C

substrate: 4-nitrophenyl phosphate


proof_lines: purified recombinant mutant E42A, pH 5.0, 37°C


proof_lines: pH 5.0, 37°C, recombinant wild-type enzyme

proof_lines: purified recombinant wild-type enzyme, pH 5.0, 37°C


proof_lines: pH 5.0, 37°C, recombinant mutant Y82A/Y83A/Y84A

proof_lines: purified recombinant mutant Y82A/Y83A/Y84A, pH 5.0, 37°C


organism: Beta vulgaris

proof_lines:
37°C, pH 7.0, enzyme BvPECP2L
37°C, pH 7.0, enzyme BvPECP1S


substrate_name: O-Phosphoethanolamine

substrate: O-Phosphoethanolamine


assay_conditions_summary: pH 5

proof_lines: at pH 5 and pH 7.4, without signal peptide

proof_lines: at pH 5, with and without signal peptide


proof_lines: recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+

proof_lines: recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+

proof_lines: recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+


proof_lines: recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+

proof_lines: recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+

proof_lines: recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+


proof_lines: recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+

proof_lines: recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+

proof_lines: recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+


proof_lines: recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+

proof_lines: recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+

proof_lines: recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+


proof_lines: recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+

proof_lines: recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+


sequence_source: UniProt REST 2026_02 O77760


sequence_source: UniProt REST 2026_02 O77759


substrate_name: Oleoyl-CoA; Cholesterol

mutation_signature: Δ1

sequence_source: UniProt REST 2026_02 P35610

mutation_type: deletion

proof_lines: SABIO-RK modifier species: sterol O-acyltransferase(Enzyme) mutant delta 1-65 His-tagged

substrate: Oleoyl-CoA; Cholesterol


substrate_name: Cholesterol; Oleoyl-CoA

proof_lines: SABIO-RK modifier species: sterol O-acyltransferase(Enzyme) mutant P64A His-tagged

substrate: Cholesterol; Oleoyl-CoA


assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: pH 7.4, 37°C, with cholesterol (0.32 mM). Without cholesterol, the Km for pregnenolone is too high to be measurable


sequence_source: UniProt REST 2026_02 O75908


sequence_source: UniProt REST 2026_02 Q65KZ6


sequence_source: UniProt REST 2026_02 Q62WE3 -> Q65KZ6

sequence_variant_note: Resolved canonical sequence from UniProt REST 2026_02 Q62WE3 -> Q65KZ6 and applied mutation signature N450A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST 2026_02 Q62WE3 -> Q65KZ6 and applied mutation signature N450K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST 2026_02 Q62WE3 -> Q65KZ6 and applied mutation signature N450D to reconstruct the assayed variant sequence.


enzyme_display_name: shikimate kinase

organism: Helicobacter pylori

substrate_name: shikimate

assay_conditions_summary: pH 7.7; 298.15 K; buffer text; cofactor NADH

proof_lines: in 100 mM Tris–HCl (pH 8.0), 50 mM KCl, 5 mM MgCl2, 2 mM ATP, 2 mM phosphoenolpyruvate, 0.7 mM NADH, 3 U/ml proteinase K, 2.5 U/ml lactate dehydrogenase, and 2 mM shikimate, at 25°C

enzyme: shikimate kinase

substrate: shikimate


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

assay_conditions_summary: cofactor ATP


organism: Dickeya chrysanthemi


organism: Escherichia coli (strain K12)


organism: Helicobacter pylori (strain ATCC 700392 / 26695)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Thermus thermophilus

substrate_name: guanosine18 in yeast tRNA-Phe

sequence_source: UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4

substrate: guanosine18 in yeast tRNA-Phe


substrate_name: S-adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature I142A to reconstruct the assayed variant sequence.

substrate: S-adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature T99A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature L151A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature L101A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature M144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature N152A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature S150A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature E124A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature V128A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature R41K to reconstruct the assayed variant sequence.


substrate_name: guanosine18 in yeast tRNAPhe

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature D190A to reconstruct the assayed variant sequence.

proof_lines: mutant D190A, pH not specified in the publication, temperature not specified in the publication

substrate: guanosine18 in yeast tRNAPhe


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature K186A to reconstruct the assayed variant sequence.

proof_lines: mutant K186A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature Y184A to reconstruct the assayed variant sequence.

proof_lines: mutant Y184A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q5SM16/TRMH_THET8, reached by direct lookup of source accession Q9FAC4 and applied mutation signature E182A to reconstruct the assayed variant sequence.

proof_lines: mutant E182A, pH not specified in the publication, temperature not specified in the publication


organism: Escherichia coli

substrate_name: guanosine18 in Escherichia coli tRNASer/CGA

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


sequence_variant_note: Resolved canonical sequence from UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature N35D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature P143Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature S150T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature E124D to reconstruct the assayed variant sequence.


sequence_source: UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical.

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 Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature S150C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature S37G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature N35Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature R41M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature N35A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5SM16/Q72GI1 direct EC+organism lookup; reviewed Thermus TrmH sequences are identical. and applied mutation signature R168A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names R8A. and applied mutation signature R8A to reconstruct the assayed variant sequence.


substrate_name: guanosine18 in tRNATyr

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names R176A. and applied mutation signature R176A to reconstruct the assayed variant sequence.

substrate: guanosine18 in tRNATyr


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names L179ter. and applied mutation signature L179ter to reconstruct the assayed variant sequence.

mutation_type: truncation


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names H71A. and applied mutation signature H71A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names K90A. and applied mutation signature K90A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names H34A. and applied mutation signature H34A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names R19A. and applied mutation signature R19A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names K32A. and applied mutation signature K32A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names R109A. and applied mutation signature R109A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence. Source row note names R166A. and applied mutation signature R166A to reconstruct the assayed variant sequence.


substrate_name: guanosine18 in yeast tRNAPhe-AGA mutant transcript

sequence_source: UniProtKB REST Q5SM16 and Q72GI1; both reviewed Thermus thermophilus TrmH entries have EC 2.1.1.34 and the same canonical 194-aa sequence.

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

proof_lines: pH and temperature not specified in the publication, Vmax: 0.00675 micromol/mg/h

proof_lines: pH and temperature not specified in the publication, Vmax: 0.18 micromol/mg/h

proof_lines: pH and temperature not specified in the publication, Vmax: 0.135 micromol/mg/h


organism: Methanocaldococcus jannaschii

substrate_name: ATP

sequence_source: UniProtKB:Q58835 direct lookup 2026-06-18

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


organism: Mycobacterium tuberculosis

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

assay_conditions_summary: pH 7.7; 298.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5SM16 direct lookup 2026-06-18 (replacement for source accession Q9FAC4) and applied mutation signature Q185A to reconstruct the assayed variant sequence.

proof_lines: mutant Q185A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5SM16 direct lookup 2026-06-18 (replacement for source accession Q9FAC4) and applied mutation signature D180A to reconstruct the assayed variant sequence.

proof_lines: mutant D180A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5SM16 direct lookup 2026-06-18 (replacement for source accession Q9FAC4) and applied mutation signature V187A to reconstruct the assayed variant sequence.

proof_lines: mutant V187A, pH not specified in the publication, temperature not specified in the publication


organism: Erwinia chrysanthemi

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10880 and applied mutation signature C162S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer Table 1 | condition 50 mM triethanolamine hydrochloride/KOH; cofactor ATP

column_label: Table 1 body row 'C162S', column 'Km or Kd (ATP) (uM)' = 670, column 'kcat (s-1)' = 40. The kcat/Km column of Table 1 is headed 'kcat/Km (shikimate) (M-1 sec-1)' and prints no ATP value. The 'Kd (ADP) (uM)' column of this row is blank.

normalized_value_unit_evidence: kcat: printed Table 1 cell 40 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 40.0 s^(-1). Km: printed Table 1 cell 670 in a column headed Km or Kd (ATP) (uM); 1 uM is 0.001 mM, so 670 / 1000 = 0.67 mM. kcat/Km: Table 1 prints its catalytic-efficiency column for shikimate only, so the efficiency of this ATP measurement is the quotient of the two printed cells of the same table line, 40.0 / 0.67 = 59.70149253731343 s^-1 mM^-1. The exported values are kcat 40.0 s^(-1), Km 0.67 mM and kcat_over_km 59.70149253731343 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'C162S', substrate ATP: Km = 670 in a column headed Km or Kd (ATP) (uM), kcat = 40 in a column headed kcat (s-1). Table 1 prints its catalytic-efficiency column for shikimate only.

row_label: Table 1, body row C162S, substrate ATP

table_label: Table 1: The kinetic parameters of native and mutant shikimate kinase from Erwinia chrysanthemi in comparison to the Escherichia coli isoenzymes I and II (Protein Science 2001, 10(6):1137-1149). Printed column heads: Km or Kd (shikimate) (uM); Km or Kd (ATP) (uM); Kd (ADP) (uM); kcat (s-1); kcat/Km (shikimate) (M-1 sec-1).


assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

column_label: Table 1 body row 'C162S', column 'Km or Kd (shikimate) (uM)' = 280, column 'kcat (s-1)' = 40, column 'kcat/Km (shikimate) (M-1 sec-1)' = 1.6 x 10^5. The 'Kd (ADP) (uM)' column of this row is blank.

normalized_value_unit_evidence: kcat: printed Table 1 cell 40 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 40.0 s^(-1). Km: printed Table 1 cell 280 in a column headed Km or Kd (shikimate) (uM); 1 uM is 0.001 mM, so 280 / 1000 = 0.28 mM. kcat/Km: printed Table 1 cell 1.6 x 10^5 in a column headed kcat/Km (shikimate) (M-1 sec-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^5 / 1000 = 160.0 s^-1 mM^-1. The exported values are kcat 40.0 s^(-1), Km 0.28 mM and kcat_over_km 142.85714285714283 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'C162S', substrate shikimate: Km = 280 in a column headed Km or Kd (shikimate) (uM), kcat = 40 in a column headed kcat (s-1), printed kcat/Km = 1.6 x 10^5 in a column headed kcat/Km (shikimate) (M-1 sec-1).

row_label: Table 1, body row C162S, substrate shikimate


sequence_source: UniProtKB:P10880 direct lookup 2026-06-18

column_label: Table 1 body row 'Wild type', column 'Km or Kd (shikimate) (uM)' = 310/700c, column 'kcat (s-1)' = 35, column 'kcat/Km (shikimate) (M-1 sec-1)' = 1.3 x 10^5. Table 1 footnote c states that the second number of a slash-separated cell is the fluorescence-quenching dissociation constant, so the Michaelis constant of this cell is 310 uM. The 'Kd (ADP) (uM)' column of this row prints 1680.

normalized_value_unit_evidence: kcat: printed Table 1 cell 35 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 35.0 s^(-1). Km: printed Table 1 cell 310 in a column headed Km or Kd (shikimate) (uM); 1 uM is 0.001 mM, so 310 / 1000 = 0.31 mM. kcat/Km: printed Table 1 cell 1.3 x 10^5 in a column headed kcat/Km (shikimate) (M-1 sec-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^5 / 1000 = 130.0 s^-1 mM^-1. The exported values are kcat 35.0 s^(-1), Km 0.31 mM and kcat_over_km 112.90322580645162 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'Wild type', substrate shikimate: Km = 310 in a column headed Km or Kd (shikimate) (uM), kcat = 35 in a column headed kcat (s-1), printed kcat/Km = 1.3 x 10^5 in a column headed kcat/Km (shikimate) (M-1 sec-1).

row_label: Table 1, body row Wild type, substrate shikimate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10880 and applied mutation signature C13S to reconstruct the assayed variant sequence.

column_label: Table 1 body row 'C13S', column 'Km or Kd (ATP) (uM)' = 235/1530c, column 'kcat (s-1)' = 23. The kcat/Km column of Table 1 is headed 'kcat/Km (shikimate) (M-1 sec-1)' and prints no ATP value. Table 1 footnote c states that the second number of a slash-separated cell is the fluorescence-quenching dissociation constant, so the Michaelis constant of this cell is 235 uM. The 'Kd (ADP) (uM)' column of this row prints 1450.

normalized_value_unit_evidence: kcat: printed Table 1 cell 23 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 23.0 s^(-1). Km: printed Table 1 cell 235 in a column headed Km or Kd (ATP) (uM); 1 uM is 0.001 mM, so 235 / 1000 = 0.235 mM. kcat/Km: Table 1 prints its catalytic-efficiency column for shikimate only, so the efficiency of this ATP measurement is the quotient of the two printed cells of the same table line, 23.0 / 0.235 = 97.87234042553192 s^-1 mM^-1. The exported values are kcat 23.0 s^(-1), Km 0.235 mM and kcat_over_km 97.87234042553192 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'C13S', substrate ATP: Km = 235 in a column headed Km or Kd (ATP) (uM), kcat = 23 in a column headed kcat (s-1). Table 1 prints its catalytic-efficiency column for shikimate only.

row_label: Table 1, body row C13S, substrate ATP


column_label: Table 1 body row 'Wild type', column 'Km or Kd (ATP) (uM)' = 620/2560c, column 'kcat (s-1)' = 35. The kcat/Km column of Table 1 is headed 'kcat/Km (shikimate) (M-1 sec-1)' and prints no ATP value. Table 1 footnote c states that the second number of a slash-separated cell is the fluorescence-quenching dissociation constant, so the Michaelis constant of this cell is 620 uM. The 'Kd (ADP) (uM)' column of this row prints 1680.

normalized_value_unit_evidence: kcat: printed Table 1 cell 35 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 35.0 s^(-1). Km: printed Table 1 cell 620 in a column headed Km or Kd (ATP) (uM); 1 uM is 0.001 mM, so 620 / 1000 = 0.62 mM. kcat/Km: Table 1 prints its catalytic-efficiency column for shikimate only, so the efficiency of this ATP measurement is the quotient of the two printed cells of the same table line, 35.0 / 0.62 = 56.45161290322581 s^-1 mM^-1. The exported values are kcat 35.0 s^(-1), Km 0.62 mM and kcat_over_km 56.45161290322581 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'Wild type', substrate ATP: Km = 620 in a column headed Km or Kd (ATP) (uM), kcat = 35 in a column headed kcat (s-1). Table 1 prints its catalytic-efficiency column for shikimate only.

row_label: Table 1, body row Wild type, substrate ATP


column_label: Table 1 body row 'C13S', column 'Km or Kd (shikimate) (uM)' = 75, column 'kcat (s-1)' = 23, column 'kcat/Km (shikimate) (M-1 sec-1)' = 3.4 x 10^5. The 'Kd (ADP) (uM)' column of this row prints 1450.

normalized_value_unit_evidence: kcat: printed Table 1 cell 23 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 23.0 s^(-1). Km: printed Table 1 cell 75 in a column headed Km or Kd (shikimate) (uM); 1 uM is 0.001 mM, so 75 / 1000 = 0.075 mM. kcat/Km: printed Table 1 cell 3.4 x 10^5 in a column headed kcat/Km (shikimate) (M-1 sec-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.4 x 10^5 / 1000 = 340.0 s^-1 mM^-1. The exported values are kcat 23.0 s^(-1), Km 0.075 mM and kcat_over_km 306.6666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'C13S', substrate shikimate: Km = 75 in a column headed Km or Kd (shikimate) (uM), kcat = 23 in a column headed kcat (s-1), printed kcat/Km = 3.4 x 10^5 in a column headed kcat/Km (shikimate) (M-1 sec-1).

row_label: Table 1, body row C13S, substrate shikimate


sequence_source: UniProtKB:P0A6D7 direct lookup 2026-06-18

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


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


sequence_source: UniProtKB reviewed accession P0A6D7 (AROK_ECOLI), fetched by direct UniProt REST check on 2026-06-18.


substrate_name: GlcNAc-Ins

proof_lines: MSmB is a monobromobimane derivative of mycothiol, CySmB-GlcNAc-Ins is a bimane derivative of mycothiol.

substrate: GlcNAc-Ins


organism: Bacillus licheniformis

sequence_variant_note: Resolved canonical sequence from UniProtKB Q65KZ6 canonical sequence reconstructed with N450A after direct residue check on 2026-06-18 and applied mutation signature N450A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q65KZ6 canonical sequence reconstructed with N450Q after direct residue check on 2026-06-18 and applied mutation signature N450Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A9YTT0 canonical sequence reconstructed with R109K after direct residue check on 2026-06-18 and applied mutation signature R109K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A9YTT0 canonical sequence reconstructed with R109E after direct residue check on 2026-06-18 and applied mutation signature R109E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB A9YTT0 canonical sequence direct REST lookup on 2026-06-18

proof_lines: recombinant wild-type enzyme, pH 9.0, 60°C


sequence_variant_note: Resolved canonical sequence from UniProtKB A9YTT0 canonical sequence reconstructed with R109S after direct residue check on 2026-06-18 and applied mutation signature R109S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A9YTT0 canonical sequence reconstructed with R109F after direct residue check on 2026-06-18 and applied mutation signature R109F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A9YTT0 canonical sequence reconstructed with R109L after direct residue check on 2026-06-18 and applied mutation signature R109L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A9YTT0 canonical sequence reconstructed with R109M after direct residue check on 2026-06-18 and applied mutation signature R109M to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

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


sequence_source: UniProtKB P54422 canonical sequence direct REST lookup on 2026-06-18


organism: Corynebacterium glutamicum

sequence_source: UniProtKB Q8NRT7 canonical sequence direct REST lookup on 2026-06-18


organism: Equus caballus

proof_lines: versus L-gamma-glutamyl-4-nitroanilide, pH 7.4, 37°C


sequence_source: UniProtKB P18956 canonical sequence direct REST lookup on 2026-06-18


enzyme_display_name: hercynylcysteine S-oxide synthase

organism: Chloracidobacterium thermophilum

substrate_name: L-cysteine

sequence_source: UniProtKB REST direct check on 2026-06-18: G2LET6

enzyme: hercynylcysteine S-oxide synthase

substrate: L-cysteine


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct check on 2026-06-18: G2LET6 and applied mutation signature Y93F to reconstruct the assayed variant sequence.

proof_lines:
mutant Y93F, pH 8, 26°C
mutant Y93F/94F, pH 8, 26°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct check on 2026-06-18: G2LET6 and applied mutation signature Y94F to reconstruct the assayed variant sequence.


substrate_name: Unknown

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


substrate_name: hercynine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct check on 2026-06-18: G2LET6 and applied mutation signature D52L/A420Y to reconstruct the assayed variant sequence.

proof_lines: mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication

substrate: hercynine


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct check on 2026-06-18: G2LET6 and applied mutation signature A420Y to reconstruct the assayed variant sequence.

proof_lines: mutant A420Y, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct check on 2026-06-18: G2LET6 and applied mutation signature D52L to reconstruct the assayed variant sequence.

proof_lines: mutant D52L, pH not specified in the publication, temperature not specified in the publication


organism: Methylobacterium brachiatum

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

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


organism: Methylobacterium pseudosasicola

sequence_source: UniProtKB REST direct check on 2026-06-18: A0A1I4PM45


substrate_name: L-Cysteine

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

substrate: L-Cysteine