sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=N347A; RCSB 4EU3/PMID 23030530 structure anchor and applied mutation signature N347A to reconstruct the assayed variant sequence.


enzyme_display_name: succinyl-CoA:acetate CoA-transferase

organism: Acetobacter aceti

substrate_name: Propanoate

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB:B3EY95 canonical sequence; RCSB 4EU3/PMID 23030530 structure anchor

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

smiles: CCC(=O)O

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

data_origin: experimental

enzyme: succinyl-CoA:acetate CoA-transferase

substrate: Propanoate

status: unverified

source: oed


substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=R228E; RCSB 4EU3/PMID 23030530 structure anchor and applied mutation signature R228E to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: Acetyl-CoA


substrate_name: Glutarate

smiles: O=C(O)CCCC(=O)O

substrate: Glutarate


substrate_name: Acetate

sequence_source: Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=R228E; RCSB 4EU3/PMID 23030530 structure anchor

smiles: CC(=O)O

substrate: Acetate


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=E435D; RCSB 4EU3/PMID 23030530 structure anchor and applied mutation signature E435D to reconstruct the assayed variant sequence.


substrate_name: Methylsuccinate

substrate: Methylsuccinate


sequence_source: Variant reconstructed from UniProtKB:B3EY95 canonical sequence using selected-row mutation_signature=E435D; RCSB 4EU3/PMID 23030530 structure anchor


sequence_source: UniProtKB reviewed entry B3EY95 canonical FASTA, direct check on 2026-06-04.

assay_conditions_summary: pH 5; 298.15 K; cofactor CoA


substrate_name: Succinyl-CoA; Acetoacetate

kcat_over_km_display: Not reported

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

source_databases_merged: sabio_rk brenda skid

source_db: brenda

substrate: Succinyl-CoA; Acetoacetate


substrate_name: succinyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry B3EY95 canonical FASTA, direct check on 2026-06-04. and applied mutation signature E435D to reconstruct the assayed variant sequence.

substrate: succinyl-CoA


substrate_name: Formate

smiles: O=CO

substrate: Formate


substrate_name: Succinyl-CoA; Acetate

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

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry B3EY95 canonical FASTA, direct check on 2026-06-04. and applied mutation signature S71A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines: SABIO-RK modifier species: succinyl-CoA:acetate CoA-transferase(Enzyme) mutant S71A AarC His6-tagged

proof_lines: mutant S71A, pH 8.0, temperature not specified in the publication

substrate: Succinyl-CoA; Acetate


substrate_name: D-Malate

substrate: D-Malate


substrate_name: Fumarate

substrate: Fumarate


enzyme_display_name: acetyl-CoA C-acyltransferase

organism: Rattus norvegicus

substrate_name: Acetoacetyl-CoA; Coenzyme A

kcat_display: Not reported

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

sequence_source: UniProtKB:P13437 direct accession lookup on 2026-06-04

assay_conditions_summary: cofactor CoA

enzyme: acetyl-CoA C-acyltransferase

substrate: Acetoacetyl-CoA; Coenzyme A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13437 direct accession lookup on 2026-06-04 and applied mutation signature H352Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant H352Y


substrate_name: Coenzyme A; Acetoacetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13437 direct accession lookup on 2026-06-04 and applied mutation signature H352K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant H352K

substrate: Coenzyme A; Acetoacetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13437 direct accession lookup on 2026-06-04 and applied mutation signature H352E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant H352E


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13437 direct accession lookup on 2026-06-04 and applied mutation signature H352A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant H352A


substrate_name: Coenzyme A; 3-Oxo-2-methylpalmitoyl-CoA

sequence_source: UniProtKB:P11915 direct accession lookup on 2026-06-04

substrate: Coenzyme A; 3-Oxo-2-methylpalmitoyl-CoA


sequence_source: UniProtKB:P21775 direct accession lookup on 2026-06-04


organism: Sus scrofa

substrate_name: Acetyldithio-CoA; Acetyl-CoA

sequence_source: UniProtKB:Q9TUF6 direct accession lookup on 2026-06-04

substrate: Acetyldithio-CoA; Acetyl-CoA


substrate_name: Acetate; Succinyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB REST B3EY95 canonical sequence with R228E reconstructed during review on 2026-06-04 and applied mutation signature R228E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: succinyl-CoA:acetate CoA-transferase(Enzyme) mutant R228E AarC His6-tagged

proof_lines: mutant R228E, pH 8.0, temperature not specified in the publication

substrate: Acetate; Succinyl-CoA


substrate_name: succinate

sequence_source: UniProtKB REST B3EY95 canonical sequence with R228E reconstructed during review on 2026-06-04

smiles: O=C(O)CCC(=O)O

substrate: succinate


km_display: Not reported

sequence_source: UniProtKB REST B3EY95 canonical sequence checked during review on 2026-06-04

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

proof_lines: pH 8.0, 30°C, His6-tagged wild-type enzyme and mutant E435D

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB REST B3EY95 canonical sequence with N347A reconstructed during review on 2026-06-04 and applied mutation signature N347A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: succinyl-CoA:acetate CoA-transferase(Enzyme) mutant N347A AarC His6-tagged

proof_lines: mutant N347A, pH 8.0, temperature not specified in the publication


substrate_name: L-Malate

substrate: L-Malate


sequence_source: UniProtKB REST B3EY95 canonical sequence with N347A reconstructed during review on 2026-06-04


substrate_name: oxaloacetate

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

substrate: oxaloacetate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST B3EY95 canonical sequence with S71A reconstructed during review on 2026-06-04 and applied mutation signature S71A to reconstruct the assayed variant sequence.


enzyme_display_name: trehalose-phosphatase

organism: Acinetobacter baumannii

substrate_name: alpha,alpha-trehalose 6-phosphate

sequence_source: UniProtKB:T2HRJ9 direct REST lookup on 2026-06-04; active UniProtKB unreviewed (TrEMBL) entry, organism Acinetobacter baumannii, EC 3.1.3.12.

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

enzyme: trehalose-phosphatase

substrate: alpha,alpha-trehalose 6-phosphate


organism: Arthrobacter sp.

substrate_name: trehalose 6-phosphate

sequence_source: UniProtKB:E9NR87 direct REST lookup on 2026-06-04; active UniProtKB unreviewed (TrEMBL) entry, organism Arthrobacter alpinus, EC 3.1.3.12.

substrate: trehalose 6-phosphate


proof_lines:
at pH 7.4 and 20°C
at pH 7.4 and 10°C
at pH 7.4 and 4°C


organism: Brugia malayi

sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=E386A; canonical residue E matched at 1-based position 386. and applied mutation signature E386A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=N228A; canonical residue N matched at 1-based position 228. and applied mutation signature N228A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=Q332A; canonical residue Q matched at 1-based position 332. and applied mutation signature Q332A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=K334A; canonical residue K matched at 1-based position 334. and applied mutation signature K334A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB:A8NS89 canonical sequence by applying selected mutation_signature=T339A; canonical residue T matched at 1-based position 339. and applied mutation signature T339A to reconstruct the assayed variant sequence.


enzyme_display_name: trehalose-6-phosphate phosphatase

sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature R337A to reconstruct the assayed variant sequence.

enzyme: trehalose-6-phosphate phosphatase


sequence_source: UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable

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

proof_lines: Ki above 10 mM, wild type enzyme, at pH 7.5 and 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature Q332A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature T339A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature E386A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature D378A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature S329A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct accession lookup on 2026-06-04; variant sequence reconstructed by residue-checked substitution when applicable and applied mutation signature K334A to reconstruct the assayed variant sequence.


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB REST direct lookup A8NS89

source: skid


organism: Burkholderia pseudomallei

sequence_source: UniProtKB REST direct lookup Q63SB3


organism: Corynebacterium diphtheriae

sequence_source: UniProtKB REST direct lookup A0A811GD74


organism: Mycobacterium lentiflavum

sequence_source: UniProtKB REST direct lookup A0A0E4GVV3


organism: Mycobacterium triplex

sequence_source: UniProtKB REST direct lookup A0A024JUE5


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB REST direct lookup P9WFZ5


organism: Oryza sativa

sequence_source: UniProtKB REST direct lookup Q75WV3

assay_conditions_summary: 310.15 K; buffer 50mM Tris /HCl

proof_lines: in 50mM Tris /HCl buffer with 2mM MgCl2, at 37°C


organism: Oryza sativa Japonica Group

sequence_source: UniProtKB REST direct lookup Q9FWQ2

assay_conditions_summary: 310.15 K; buffer 50 mM Tris/HCl

proof_lines: in 50 mM Tris/HCl buffer with 2 mM MgCl2, at 37°C


enzyme_display_name: lacto-N-biosidase

organism: Bifidobacterium bifidum

substrate_name: H2O; p-Nitrophenyl lacto-N-bioside

sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature H263F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant H263F C-terminal His6-tagged

enzyme: lacto-N-biosidase

substrate: H2O; p-Nitrophenyl lacto-N-bioside


sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature D320N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant D320N C-terminal His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature D320A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant D320A C-terminal His6-tagged


sequence_source: UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04.

proof_lines: wild-type, transglycosylation reaction, pH 4.5, 30°C

proof_lines: wild-type, hydrolysis reaction, pH 4.5, 30°C


substrate_name: p-Nitrophenyl lacto-N-bioside; Lactose

sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature Q190L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant Q190L

proof_lines: mutant Q190L, transglycosylation reaction, pH 4.5, 30°C

proof_lines: mutant Q190L, hydrolysis reaction, pH 4.5, 30°C

substrate: p-Nitrophenyl lacto-N-bioside; Lactose


sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature H263A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant H263A

proof_lines: mutant H263A, hydrolysis reaction, pH 4.5, 30°C

proof_lines: mutant H263A, transglycosylation reaction, pH 4.5, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature N259Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant N259Q

proof_lines: mutant N259Q, transglycosylation reaction, pH 4.5, 30°C

proof_lines: mutant N259Q, hydrolysis reaction, pH 4.5, 30°C


substrate_name: p-Nitrophenyl lacto-N-bioside; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB B3TLD6 canonical sequence retrieved 2026-06-04; variant reconstructed from selected source mutation note. and applied mutation signature W394A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant W394A

proof_lines: mutant W394A, hydrolysis reaction, pH 4.5, 30°C

proof_lines: mutant W394A, transglycosylation reaction, pH 4.5, 30°C

substrate: p-Nitrophenyl lacto-N-bioside; H2O


organism: Escherichia coli

substrate_name: Xanthine

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A847 and applied mutation signature D143A to reconstruct the assayed variant sequence.

column_label: Table 4 (Xanthine Kinetic Parameters for TGTs), body row 'htTGT(D143A)': column 'kcat (x10-6 s-1)' = 5.5; column 'KM (uM)' = 13; column 'kcat/KM (x10-6 s-1 uM-1)' = 0.42; column 'relative KM' = 0.059; column 'relative kcat/KM' = 1.35. The number printed in parentheses beside each kinetic cell (0. 1, 1 and 0.04 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 4 cell 5.5 under the column head kcat (x10-6 s-1), so the cell is 5.5 x 10^-6 s^-1 and the value is 0.0000055 s^(-1). Km: printed Table 4 cell 13 under the column head KM (uM); 13 / 1000 = 0.013 mM. kcat/Km: printed Table 4 cell 0.42 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 0.42 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.42 x 10^-6 x 1000 = 0.00042 s^(-1)*mM^(-1). The exported values are kcat 0.000005 s^(-1), Km 0.013 mM and kcat_over_km 0.00038461538461538467 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, body row 'htTGT(D143A)': kcat = 5.5 in a column headed kcat (x10-6 s-1); KM = 13 in a column headed KM (uM); printed kcat/KM = 0.42 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 4, body row htTGT(D143A)

table_label: Table 4: Xanthine Kinetic Parameters for TGTs (Biochemistry 2006, 45(2):617-625). Printed column heads: enzyme; kcat (x10-6 s-1); KM (uM); kcat/KM (x10-6 s-1 uM-1); relative KM; relative kcat/KM.

substrate: Xanthine

status: corrected


substrate_name: tRNA guanine; Hypoxanthine

sequence_variant_note: Resolved canonical sequence from UniProtKB P0A847 FASTA checked directly; D143N reconstructed from the canonical D at residue 143. and applied mutation signature D143N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA-guanine transglycosylase(Enzyme) mutant htTGT(D143N)

substrate: tRNA guanine; Hypoxanthine


substrate_name: Hypoxanthine; tRNA guanine

sequence_variant_note: Resolved canonical sequence from UniProtKB P0A847 FASTA checked directly; D143A reconstructed from the canonical D at residue 143. and applied mutation signature D143A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA-guanine transglycosylase(Enzyme) mutant htTGT(D143A)

substrate: Hypoxanthine; tRNA guanine


substrate_name: Hypoxanthine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A847 and applied mutation signature D143N to reconstruct the assayed variant sequence.

column_label: Table 3 (Hypoxanthine Kinetic Parameters for TGTs), body row 'htTGT(D143N)': column 'kcat (x10-6 s-1)' = 120; column 'KM (uM)' = 490; column 'kcat/KM (x10-6 s-1 uM-1)' = 0.2; column 'relative KM' = 0.6; column 'relative kcat/KM' = 0.07. The number printed in parentheses beside each kinetic cell (05, 45 and 0.02 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 120 under the column head kcat (x10-6 s-1), so the cell is 120 x 10^-6 s^-1 and the value is 0.00012 s^(-1). Km: printed Table 3 cell 490 under the column head KM (uM); 490 / 1000 = 0.49 mM. kcat/Km: printed Table 3 cell 0.2 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 0.2 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.2 x 10^-6 x 1000 = 0.0002 s^(-1)*mM^(-1). The exported values are kcat 0.0001 s^(-1), Km 0.49 mM and kcat_over_km 0.00020408163265306123 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, body row 'htTGT(D143N)': kcat = 120 in a column headed kcat (x10-6 s-1); KM = 490 in a column headed KM (uM); printed kcat/KM = 0.2 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 3, body row htTGT(D143N)

table_label: Table 3: Hypoxanthine Kinetic Parameters for TGTs (Biochemistry 2006, 45(2):617-625). Printed column heads: enzyme; kcat (x10-6 s-1); KM (uM); kcat/KM (x10-6 s-1 uM-1); relative KM; relative kcat/KM.

substrate: Hypoxanthine


sequence_source: UniProtKB P0A847 FASTA checked directly.

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

column_label: Table 4 (Xanthine Kinetic Parameters for TGTs), body row 'htTGT(wt)': column 'kcat (x10-6 s-1)' = 69; column 'KM (uM)' = 224; column 'kcat/KM (x10-6 s-1 uM-1)' = 0.31; column 'relative KM' = 1.0; column 'relative kcat/KM' = 1.0. The number printed in parentheses beside each kinetic cell (3, 28 and 0.04 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 4 cell 69 under the column head kcat (x10-6 s-1), so the cell is 69 x 10^-6 s^-1 and the value is 0.000069 s^(-1). Km: printed Table 4 cell 224 under the column head KM (uM); 224 / 1000 = 0.224 mM. kcat/Km: printed Table 4 cell 0.31 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 0.31 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.31 x 10^-6 x 1000 = 0.00031 s^(-1)*mM^(-1). The exported values are kcat 0.00007 s^(-1), Km 0.224 mM and kcat_over_km 0.00031249999999999995 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, body row 'htTGT(wt)': kcat = 69 in a column headed kcat (x10-6 s-1); KM = 224 in a column headed KM (uM); printed kcat/KM = 0.31 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 4, body row htTGT(wt)


substrate_name: tRNA queuine; Guanine

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB P0A847 FASTA checked directly; D143S reconstructed from the canonical D at residue 143. and applied mutation signature D143S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA-guanine transglycosylase(Enzyme) mutant htTGT(D143S)

substrate: tRNA queuine; Guanine


column_label: Table 4 (Xanthine Kinetic Parameters for TGTs), body row 'htTGT(D143N)': column 'kcat (x10-6 s-1)' = 8.8; column 'KM (uM)' = 2.6; column 'kcat/KM (x10-6 s-1 uM-1)' = 3.4; column 'relative KM' = 0.012; column 'relative kcat/KM' = 10.9. The number printed in parentheses beside each kinetic cell (0.1, 0.2 and 0.3 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 4 cell 8.8 under the column head kcat (x10-6 s-1), so the cell is 8.8 x 10^-6 s^-1 and the value is 0.0000088 s^(-1). Km: printed Table 4 cell 2.6 under the column head KM (uM); 2.6 / 1000 = 0.0026 mM. kcat/Km: printed Table 4 cell 3.4 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 3.4 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.4 x 10^-6 x 1000 = 0.0034 s^(-1)*mM^(-1). The exported values are kcat 0.000009 s^(-1), Km 0.003 mM and kcat_over_km 0.003 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, body row 'htTGT(D143N)': kcat = 8.8 in a column headed kcat (x10-6 s-1); KM = 2.6 in a column headed KM (uM); printed kcat/KM = 3.4 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 4, body row htTGT(D143N)


sequence_variant_note: Resolved canonical sequence from UniProtKB:B3TLD6 direct REST lookup plus one-based W394F substitution validated on 2026-06-04 and applied mutation signature W394F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant W394F

proof_lines: mutant W394F, transglycosylation reaction, pH 4.5, 30°C

proof_lines: mutant W394F, hydrolysis reaction, pH 4.5, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:B3TLD6 direct REST lookup plus one-based H263R substitution validated on 2026-06-04 and applied mutation signature H263R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant H263R

proof_lines: mutant H263R, hydrolysis reaction, pH 4.5, 30°C

proof_lines: mutant H263R, transglycosylation reaction, pH 4.5, 30°C


sequence_source: UniProtKB:B3TLD6 direct REST lookup on 2026-06-04


organism: Bifidobacterium longum

substrate_name: lacto-N-fucopentaose I

sequence_source: UniProtKB:A0A024QYS6 direct REST lookup on 2026-06-04

substrate: lacto-N-fucopentaose I


substrate_name: lacto-N-tetraose

substrate: lacto-N-tetraose


sequence_source: UniProtKB:P0DW93 direct REST lookup on 2026-06-04


organism: Zymomonas mobilis

substrate_name: [tRNA]-guanine

sequence_source: UniProtKB:P28720 direct lookup on 2026-06-04; reviewed Swiss-Prot entry TGT_ZYMMO, Zymomonas mobilis subsp. mobilis strain ZM4, EC 2.4.2.29.

proof_lines: wild type enzyme, in 200 mM HEPES, pH 7.3, 20 mM MgCl2

substrate: [tRNA]-guanine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P28720 direct lookup on 2026-06-04; reviewed Swiss-Prot entry TGT_ZYMMO, Zymomonas mobilis subsp. mobilis strain ZM4, EC 2.4.2.29. and applied mutation signature Y106F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12. and applied mutation signature Y221A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12.

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

mutation_type: deletion

proof_lines: mutant enzyme DELTA59, at pH 7.5 and 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12. and applied mutation signature D336A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12. and applied mutation signature S329A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 direct lookup on 2026-06-04; reviewed Swiss-Prot entry GOB1_BRUMA, Brugia malayi, EC 3.1.3.12. and applied mutation signature Y225A to reconstruct the assayed variant sequence.


column_label: Table 3 (Hypoxanthine Kinetic Parameters for TGTs), body row 'htTGT(D143A)': column 'kcat (x10-6 s-1)' = 190; column 'KM (uM)' = 1550; column 'kcat/KM (x10-6 s-1 uM-1)' = 0.1; column 'relative KM' = 1.9; column 'relative kcat/KM' = 0.03. The number printed in parentheses beside each kinetic cell (13, 170 and 0.02 on this line) is the printed standard error, which is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 190 under the column head kcat (x10-6 s-1), so the cell is 190 x 10^-6 s^-1 and the value is 0.00019 s^(-1). Km: printed Table 3 cell 1550 under the column head KM (uM); 1550 / 1000 = 1.55 mM. kcat/Km: printed Table 3 cell 0.1 under the column head kcat/KM (x10-6 s-1 uM-1), so the cell is 0.1 x 10^-6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.1 x 10^-6 x 1000 = 0.0001 s^(-1)*mM^(-1). The exported values are kcat 0.0002 s^(-1), Km 1.55 mM and kcat_over_km 0.00012903225806451613 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, body row 'htTGT(D143A)': kcat = 190 in a column headed kcat (x10-6 s-1); KM = 1550 in a column headed KM (uM); printed kcat/KM = 0.1 in a column headed kcat/KM (x10-6 s-1 uM-1).

row_label: Table 3, body row htTGT(D143A)


sequence_source: UniProtKB reviewed accession P0A847, direct REST/FASTA check 2026-06-04


substrate_name: Queuine; tRNA guanine

sequence_source: UniProtKB reviewed accessions P0A847, P0A848, and P0A849, direct REST check 2026-06-04; all three have identical canonical sequence

substrate: Queuine; tRNA guanine


organism: Shigella flexneri

substrate_name: Unknown

sequence_source: UniProtKB reviewed accession Q54177, direct REST/FASTA check 2026-06-04

substrate: Unknown


substrate_name: pre-queuine 0

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

sequence_source: UniProtKB reviewed accession P28720, direct REST/FASTA check 2026-06-04

assay_conditions_summary: pH 7.3; 310.15 K; buffer 200 mM HEPES

proof_lines: competitive inhibition, in 200 mM HEPES buffer (pH 7.3), 20 mM MgCl2

proof_lines: at 37°C, pH 7.3, in 200 mM HEPES buffer, 20 mM MgCl2, 2.95 mM Tween 20 containing both substrates

source_databases_merged: brenda skid

substrate: pre-queuine 0


substrate_name: pre-queuine 1

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P28720, direct REST/FASTA check 2026-06-04 and applied mutation signature E235Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E235Q, Km less than 0.0005 mM, in 200 mM HEPES, pH 7.3, 20 mM MgCl2

substrate: pre-queuine 1


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P28720, direct REST/FASTA check 2026-06-04 and applied mutation signature K52M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P28720, direct REST/FASTA check 2026-06-04 and applied mutation signature Y330F to reconstruct the assayed variant sequence.


sequence_source: UniProt REST direct lookup for P0DW93 on 2026-06-04

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

mutation_type: truncation

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant BlLnbXc C-terminal truncated (31-625)


organism: Bifidobacterium longum subsp. Longum

sequence_source: UniProt REST direct lookup for A0A024QYS6 on 2026-06-04

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


organism: Bifidobacterium saguini

sequence_source: UniProt REST direct lookup for A0A087D8U9 on 2026-06-04

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant BsaXc C-terminal truncated (34-640)


organism: Ruminococcus lactaris

sequence_source: UniProt REST direct lookup for B5CMC4 on 2026-06-04

proof_lines: SABIO-RK modifier species: lacto-N-biosidase(Enzyme) mutant RlXc C-terminal truncated (27-607)


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Candida albicans

substrate_name: Laminaripentaose

sequence_source: UniProt REST direct lookup for P29717 on 2026-06-04

enzyme: glucan 1,3-beta-glucosidase

substrate: Laminaripentaose


substrate_name: Laminariheptaose

substrate: Laminariheptaose


substrate_name: Laminaribiose; H2O

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

sequence_source: UniProtKB:P29717 reviewed Swiss-Prot direct REST/FASTA lookup

substrate: Laminaribiose; H2O


substrate_name: Laminarihexaose

substrate: Laminarihexaose


substrate_name: Laminaritriose

substrate: Laminaritriose


substrate_name: Laminaritetraose

substrate: Laminaritetraose


substrate_name: p-Nitrophenyl-beta-D-glucoside

substrate: p-Nitrophenyl-beta-D-glucoside


substrate_name: Gentiobiose

substrate: Gentiobiose


substrate_name: cellohexaose

substrate: cellohexaose


substrate_name: Cellobiose

substrate: Cellobiose


organism: Brugia malayi

substrate_name: trehalose 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB A8NS89 canonical sequence with Y225A reconstructed from PMID 24992307 Table 1/source mutation row and applied mutation signature Y225A to reconstruct the assayed variant sequence.

substrate: trehalose 6-phosphate


sequence_source: UniProtKB A8NS89 canonical reviewed Brugia malayi trehalose-phosphatase sequence


organism: Saccharomyces cerevisiae

substrate_name: trehalose 6-phosphate; H2O

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

substrate: trehalose 6-phosphate; H2O


organism: Stenotrophomonas maltophilia

substrate_name: alpha,alpha-trehalose 6-phosphate

substrate: alpha,alpha-trehalose 6-phosphate


organism: Stutzerimonas stutzeri

sequence_source: UniProtKB A0A4S2BAA8 unreviewed Stutzerimonas stutzeri trehalose 6-phosphate phosphatase sequence

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


organism: Thermoplasma acidophilum

sequence_source: UniProtKB Q9HIW7 reviewed Thermoplasma acidophilum trehalose-6-phosphate phosphatase-related protein sequence

proof_lines: in 50 mM Tris-HCl (pH 8.0), 5 mM dithiothreitol, and 20 mM MgCl2, at 50°C


organism: Thermus thermophilus

sequence_source: UniProtKB Q7WUI6 unreviewed Thermus thermophilus trehalose 6-phosphate phosphatase sequence


mutation_signature: Δ2

sequence_source: UniProtKB B3TLD6 canonical sequence retained as context only; row was not accepted as a reconstructed variant


enzyme_display_name: mitogen-activated protein kinase

organism: Homo sapiens

sequence_source: UniProtKB reviewed accession Q16539 direct lookup; primaryAccession=Q16539, organism=Homo sapiens, recommended name=Mitogen-activated protein kinase 14, EC=2.7.11.24.

enzyme: mitogen-activated protein kinase


sequence_source: UniProtKB reviewed accession P28482 direct lookup; primaryAccession=P28482, organism=Homo sapiens, recommended name=Mitogen-activated protein kinase 1, EC=2.7.11.24.

proof_lines: Ki below 0.000002 mM, potent, selective, and orally bioavailable inhibitor of ERK


organism: Mus musculus

substrate_name: ATP

sequence_source: UniProtKB reviewed accession P47811 direct lookup; primaryAccession=P47811, organism=Mus musculus, recommended name=Mitogen-activated protein kinase 14, EC=2.7.11.24.

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: pH 7.0, 30°C, wild-type p38 isozyme alpha

substrate: ATP


sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB reviewed accession P47811 after direct coordinate check of canonical residue 110=G and batch mutation_signature=G110A. and applied mutation signature G110A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant G110A of p38 isozyme alpha


sequence_variant_note: Resolved canonical sequence from Variant sequence reconstructed from UniProtKB reviewed accession P47811 after direct coordinate check of canonical residue 110=G and batch mutation_signature=G110D. and applied mutation signature G110D to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant G110D of p38 isozyme alpha


substrate_name: ATP; Protein

substrate: ATP; Protein


substrate_name: Protein

substrate: Protein


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


substrate_name: Cellotetraose

sequence_source: UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04

substrate: Cellotetraose


substrate_name: laminaribiose

substrate: laminaribiose


substrate_name: Gentiotriose

substrate: Gentiotriose


substrate_name: Laminarin

substrate: Laminarin


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04 and applied mutation signature F144A with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04 and applied mutation signature F258W with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04 and applied mutation signature F144A/F258Y with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 reviewed entry; retrieved via UniProt REST on 2026-06-04 and applied mutation signature F258I with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.


organism: Rhizomucor miehei

sequence_source: UniProtKB:A0A0B4RUW2 direct REST lookup, accessed 2026-06-04


substrate_name: Laminaran

substrate: Laminaran


substrate_name: laminaritriose

substrate: laminaritriose


substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


organism: uncultured bacterium

substrate_name: 4-nitrophenyl beta-L-fucoside

substrate: 4-nitrophenyl beta-L-fucoside


organism: Escherichia coli

sequence_source: UniProtKB:P17411 direct REST lookup, accessed 2026-06-04


sequence_source: UniProtKB:P11988 direct REST lookup, accessed 2026-06-04

column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row PNPG-6-P; the Michaelis constant 2.5 comes from the printed column K_m (mM), the turnover number 7 from the printed column k_cat (1/s), and the catalytic efficiency 3.0 x 10^3 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 2.5 mM; already in mM, no unit conversion applies; the exported value is 2.5 mM. kcat: printed cell 7 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 7.0 s^(-1). kcat/Km: printed cell 3.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.0 x 10^3 / 1000 = 3.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 2.8 s^(-1)*mM^(-1), the quotient 7 / 2.5 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 3.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row PNPG-6-P: Km = 2.5 mM; kcat = 7 1/s; printed kcat/Km = 3.0 x 10^3 M^-1 s^-1.


enzyme_display_name: 8-amino-7-oxononanoate synthase

organism: Arabidopsis thaliana

substrate_name: pimeloyl-CoA

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

enzyme: 8-amino-7-oxononanoate synthase

substrate: pimeloyl-CoA


substrate_name: L-Alanine; 6-Carboxyhexanoyl-CoA

proof_lines: 5-aminolevulinate synthase-fusion protein (single chain chimeric dimer), pH 7.5, 30°C

substrate: L-Alanine; 6-Carboxyhexanoyl-CoA


substrate_name: L-alanine

substrate: L-alanine


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


organism: Lysinibacillus sphaericus

substrate_name: 6-Carboxyhexanoyl-CoA; L-Alanine

substrate: 6-Carboxyhexanoyl-CoA; L-Alanine


assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


substrate_name: L-Alanine

substrate: L-Alanine


substrate_name: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate


organism: Lactobacillus gasseri


organism: Streptococcus pneumoniae

substrate_name: cellobiose 6-phosphate

verification_status: verified

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM NaH2PO4. The Enzymatic Activity Assays section states this

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'Wild type', Cellobiose-6'P column group: column 'Km (uM)' = 1135; column 'kcat (s^-1)' = 170; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 1.5. The other three numeric cells of the same printed row belong to the pNP-beta-Glc6P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 1135 uM; 1135 / 1000 = 1.135 mM. kcat: printed Table 2 cell 170 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 1.5 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 1.5 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 150.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 170.0 / 1.135 = 149.7797356828194 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'Wild type', Cellobiose-6'P column group: Km = 1135 uM; kcat = 170 s^-1; printed kcat/Km = 1.5 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Wild type', the three Cellobiose-6'P cells (Km, kcat, kcat/Km x10^-1)

table_label: Table 2: Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P (J. Biol. Chem. 2013, 288(21):14949-14958)

substrate: cellobiose 6-phosphate

status: verified


column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'Wild type', pNP-beta-Glc6P column group: column 'Km (uM)' = 478; column 'kcat (s^-1)' = 195; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 4.1. The other three numeric cells of the same printed row belong to the Cellobiose-6'P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 478 uM; 478 / 1000 = 0.478 mM. kcat: printed Table 2 cell 195 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 4.1 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 4.1 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 410.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 195.0 / 0.478 = 407.9497907949791 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'Wild type', pNP-beta-Glc6P column group: Km = 478 uM; kcat = 195 s^-1; printed kcat/Km = 4.1 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Wild type', the three pNP-beta-Glc6P cells (Km, kcat, kcat/Km x10^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0H2UP35 and applied mutation signature Y126F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'Y126F', Cellobiose-6'P column group: column 'Km (uM)' = 1515; column 'kcat (s^-1)' = 138; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 0.9. The other three numeric cells of the same printed row belong to the pNP-beta-Glc6P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 1515 uM; 1515 / 1000 = 1.515 mM. kcat: printed Table 2 cell 138 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 0.9 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 0.9 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 90.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 138.0 / 1.515 = 91.0891089108911 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'Y126F', Cellobiose-6'P column group: Km = 1515 uM; kcat = 138 s^-1; printed kcat/Km = 0.9 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Y126F', the three Cellobiose-6'P cells (Km, kcat, kcat/Km x10^-1)


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0H2UP35 and applied mutation signature M423A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'M423A', Cellobiose-6'P column group: column 'Km (uM)' = 1320; column 'kcat (s^-1)' = 145; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 1.1. The other three numeric cells of the same printed row belong to the pNP-beta-Glc6P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 1320 uM; 1320 / 1000 = 1.32 mM. kcat: printed Table 2 cell 145 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 1.1 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 1.1 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 110.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 145.0 / 1.32 = 109.84848484848484 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'M423A', Cellobiose-6'P column group: Km = 1320 uM; kcat = 145 s^-1; printed kcat/Km = 1.1 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'M423A', the three Cellobiose-6'P cells (Km, kcat, kcat/Km x10^-1)


substrate_name: UDP-GlcNAc

sequence_source: UniProtKB REST P17443 FASTA/JSON checked 2026-06-04

proof_lines:
wild type enzyme
wild-type enzyme

substrate: UDP-GlcNAc


sequence_source: UniProtKB P17443 canonical sequence used only as mutation context; row-specific variant sequence not resolved

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

proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant N198A C-terminal His-tag


proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant Y105A C-terminal His-tag


proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant H124A C-terminal His-tag


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


organism: Klebsiella pneumoniae subsp. pneumoniae

substrate_name: Unknown

sequence_source: UniProtKB A6T4N3 FASTA/JSON direct lookup, reviewed Swiss-Prot entry MURG_KLEP7.

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

substrate: Unknown


substrate_name: trehalose 6-phosphate

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution N228A. and applied mutation signature N228A to reconstruct the assayed variant sequence.

substrate: trehalose 6-phosphate


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution E384A. and applied mutation signature E384A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution W280A. and applied mutation signature W280A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution D336A. and applied mutation signature D336A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution D378A. and applied mutation signature D378A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution R337A. and applied mutation signature R337A to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution E384A.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed E125A substitution and applied mutation signature E125A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed S191A substitution and applied mutation signature S191A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed T15A substitution and applied mutation signature T15A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant T15A C-terminal His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed Y105A substitution and applied mutation signature Y105A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P17443 canonical sequence with reconstructed S191A substitution

proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant S191A C-terminal His-tag


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed R260A substitution and applied mutation signature R260A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed N291A substitution and applied mutation signature N291A to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

substrate_name: 4-Nitrophenyl beta-D-glucopyranoside 6-phosphate; H2O

sequence_source: UniProtKB Q9X108 direct lookup on 2026-06-04

proof_lines:
pH 7.5, 50°C
pH 7.5
Raw SKiD Env: Temp=50°C, pH=7.5


organism: uncultured organism

sequence_source: UniProtKB L7Y2Z6 direct lookup on 2026-06-04


enzyme_display_name: beta-ureidopropionase

substrate_name: H2O; N-Carbamoyl-beta-alanine

sequence_source: UniProtKB Q8H183 direct lookup on 2026-06-04

enzyme: beta-ureidopropionase

substrate: H2O; N-Carbamoyl-beta-alanine


organism: Caenorhabditis elegans

substrate_name: 3-ureidopropionic acid

sequence_source: UniProtKB Q19437 direct lookup on 2026-06-04

substrate: 3-ureidopropionic acid


sequence_source: UniProtKB Q9UBR1 direct lookup on 2026-06-04


smiles: N=C(O)NCCC(=O)O


organism: Lachancea kluyveri

substrate_name: N-Carbamoyl-beta-alanine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct lookup plus E159D one-based substitution computed on 2026-06-04 and applied mutation signature E159D to reconstruct the assayed variant sequence.

substrate: N-Carbamoyl-beta-alanine


sequence_source: UniProtKB Q96W94 direct lookup on 2026-06-04


enzyme_display_name: ribokinase

substrate_name: ATP

sequence_source: UniProtKB Q9H477 direct REST lookup, release 2026_01

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

enzyme: ribokinase

substrate: ATP


substrate_name: D-ribose

substrate: D-ribose


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9H477 direct REST lookup plus explicit N199L reconstruction and applied mutation signature N199L to reconstruct the assayed variant sequence.

proof_lines: mutant N199L, presence of Mg2+, pH 7.2, 37°C


proof_lines: wild-type, presence of Mg2+, pH 7.2, 37°C

proof_lines: wild-type, presence of Mn2+, pH 7.2, 37°C


organism: Leishmania donovani

sequence_source: UniProtKB E9BIX7 direct REST lookup redirects to A0A3S7X0F5, release 2026_01

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP


organism: Staphylococcus aureus

sequence_source: UniProtKB A0A0H2WZY4 direct REST lookup, release 2026_01

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0H2UP35 canonical sequence; Y126F reconstructed by replacing canonical residue 126 Y with F and applied mutation signature Y126F to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His-tagged mutant Y126F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0H2UP35 and applied mutation signature M423A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'M423A', pNP-beta-Glc6P column group: column 'Km (uM)' = 512; column 'kcat (s^-1)' = 168; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 3.3. The other three numeric cells of the same printed row belong to the Cellobiose-6'P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 512 uM; 512 / 1000 = 0.512 mM. kcat: printed Table 2 cell 168 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 3.3 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 3.3 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 330.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 168.0 / 0.512 = 328.125 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'M423A', pNP-beta-Glc6P column group: Km = 512 uM; kcat = 168 s^-1; printed kcat/Km = 3.3 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'M423A', the three pNP-beta-Glc6P cells (Km, kcat, kcat/Km x10^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0H2UP35 and applied mutation signature Y126F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'Y126F', pNP-beta-Glc6P column group: column 'Km (uM)' = 598; column 'kcat (s^-1)' = 146; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 2.4. The other three numeric cells of the same printed row belong to the Cellobiose-6'P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 598 uM; 598 / 1000 = 0.598 mM. kcat: printed Table 2 cell 146 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 2.4 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 2.4 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 240.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 146.0 / 0.598 = 244.14715719063545 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'Y126F', pNP-beta-Glc6P column group: Km = 598 uM; kcat = 146 s^-1; printed kcat/Km = 2.4 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Y126F', the three pNP-beta-Glc6P cells (Km, kcat, kcat/Km x10^-1)


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0H2UP35 canonical sequence; M423A reconstructed by replacing canonical residue 423 M with A and applied mutation signature M423A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His-tagged mutant M423A


organism: Streptococcus pyogenes

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


substrate_name: 4-nitrophenyl 6-phospho-beta-glucoside

sequence_source: UniProtKB:Q99YP9 canonical sequence; RCSB 4B3K/4B3L/5FOO SIFTS mapping supports the same accession

proof_lines:
at pH 6.0 and 37°C
Raw SKiD Env: Temp=37°C, pH=6

substrate: 4-nitrophenyl 6-phospho-beta-glucoside


sequence_source: UniProtKB:Q9X108 reviewed canonical sequence; RCSB 1UP4/1UP6/1UP7 SIFTS mapping supports the same accession


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WQ87; direct REST check on 2026-06-04; P0A4X4 is listed as a secondary accession of P9WQ87.

assay_conditions_summary: pH 7.7; 298.15 K; cofactor CoA


sequence_source: UniProtKB reviewed accession P9WQ87; direct REST check on 2026-06-04.


substrate_name: D-Alanine

substrate: D-Alanine


organism: Thermus thermophilus

sequence_source: UniProtKB reviewed accession Q5SHZ8; direct REST check on 2026-06-04.


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

proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant E125A C-terminal His-tag


proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant N291A C-terminal His-tag


proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant R260A C-terminal His-tag


enzyme_display_name: angiotensin-converting enzyme 2

organism: Homo sapiens

sequence_source: UniProtKB reviewed accession Q9BYF1 direct lookup on 2026-06-04

proof_lines:
pH 6.5, room temperature
pH 7.4, 37°C
Ki above 0.01 mM

enzyme: angiotensin-converting enzyme 2


substrate_name: Angiotensin I

substrate: Angiotensin I


substrate_name: Dynorphin A (1-13)

substrate: Dynorphin A (1-13)


substrate_name: Angiotensin II

substrate: Angiotensin II


substrate_name: Neurotensin (1-8)

substrate: Neurotensin (1-8)


substrate_name: H2O; Angiotensin II

substrate: H2O; Angiotensin II


enzyme_display_name: adenosyl-fluoride synthase

organism: Nocardia brasiliensis

substrate_name: fluoride

sequence_source: UniProtKB W8JNL4 direct REST lookup; reviewed Swiss-Prot entry FLA_NOCB7, last annotation update 2026-01-28.

enzyme: adenosyl-fluoride synthase

substrate: fluoride


organism: Streptantibioticus cattleyicolor

sequence_source: UniProtKB Q70GK9 direct REST lookup; reviewed Swiss-Prot entry FLA_STRCT, last annotation update 2025-02-05.

proof_lines: 37°C, direct displacement reaction in the absence of L-methionine or S-adenosyl-L-methionine, pH not specified in the publication

proof_lines: about, during turnover, pH and temperature not specified in the publication


organism: Streptomyces cattleya

substrate_name: S-Adenosyl-L-methionine; F-

proof_lines:
Raw SKiD Env: Temp=26°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=-----, pH=-----

substrate: S-Adenosyl-L-methionine; F-


organism: Streptomyces sp. MA37

substrate_name: S-adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB W0W999 direct REST lookup plus direct A279Y reconstruction from the canonical sequence. and applied mutation signature A279Y to reconstruct the assayed variant sequence.

proof_lines: mutant A279Y, pH not specified in the publication, temperature not specified in the publication

substrate: S-adenosyl-L-methionine


sequence_source: UniProtKB W0W999 direct REST lookup; reviewed Swiss-Prot entry FLA_STRSQ, last annotation update 2026-01-28.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB W0W999 direct REST lookup plus direct F213Y/A279L reconstruction from the canonical sequence. and applied mutation signature F213Y/A279L to reconstruct the assayed variant sequence.

proof_lines: mutant F213Y/A279L, pH not specified in the publication, temperature not specified in the publication


organism: Streptomyces xinghaiensis

sequence_source: UniProtKB A0A068VNW5 direct REST lookup; unreviewed TrEMBL entry A0A068VNW5_9ACTN, last annotation update 2026-01-28.

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

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


substrate_name: angiotensin II

sequence_variant_note: Resolved canonical sequence from UniProt REST direct check for Q9BYF1 on 2026-06-04; R514Q reconstructed from the canonical sequence. and applied mutation signature R514Q to reconstruct the assayed variant sequence.

substrate: angiotensin II


sequence_source: UniProt REST direct check for Q9BYF1 on 2026-06-04.


substrate_name: hDPP4; MERS-CoV pseudovirus

substrate: hDPP4; MERS-CoV pseudovirus


substrate_name: hACE2; SARS-CoV-2 pseudovirus

substrate: hACE2; SARS-CoV-2 pseudovirus


substrate_name: hACE2; SARS-CoV pseudovirus

substrate: hACE2; SARS-CoV pseudovirus


organism: Mus musculus

substrate_name: Angiotensin II; H2O

sequence_source: UniProt REST direct check for Q8R0I0 on 2026-06-04.

substrate: Angiotensin II; H2O


enzyme_display_name: serine--glyoxylate transaminase

organism: Oryza sativa Japonica Group

substrate_name: L-serine

proof_lines:
cosubstrate pyruvate, pH 7.6, 30°C
cosubstrate glyoxylate, pH 7.6, 30°C
cosubstrate L-alanine, pH 7.6, 30°C

enzyme: serine--glyoxylate transaminase

substrate: L-serine


enzyme_display_name: rhodopsin kinase

organism: Bos taurus

substrate_name: rhodopsin

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with S5A reconstructed after residue check and applied mutation signature S5A to reconstruct the assayed variant sequence.

enzyme: rhodopsin kinase

substrate: rhodopsin


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with L166K reconstructed after residue check and applied mutation signature L166K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with D164A reconstructed after residue check and applied mutation signature D164A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with T8E reconstructed after residue check and applied mutation signature T8E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed P28327 canonical sequence

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with D164A/L166K reconstructed after residue check and applied mutation signature D164A/L166K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with T8A reconstructed after residue check and applied mutation signature T8A to reconstruct the assayed variant sequence.


substrate_name: ACE2; Spike glycoprotein

substrate: ACE2; Spike glycoprotein


substrate_name: N-Carbamoyl-beta-alanine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct accession lookup plus selected-record mutation reconstruction and applied mutation signature E159A to reconstruct the assayed variant sequence.

substrate: N-Carbamoyl-beta-alanine


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct accession lookup plus selected-record mutation reconstruction and applied mutation signature H262A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct accession lookup plus selected-record mutation reconstruction and applied mutation signature R322A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct accession lookup plus selected-record mutation reconstruction and applied mutation signature H397N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q96W94 direct accession lookup


organism: Rattus norvegicus

substrate_name: N-Carbamoyl-beta-alanine; H2O

sequence_source: UniProtKB Q03248 direct accession lookup

substrate: N-Carbamoyl-beta-alanine; H2O


organism: Zea mays

substrate_name: H2O; N-Carbamoyl-beta-alanine

sequence_source: UniProtKB B4FSZ8 direct accession lookup

substrate: H2O; N-Carbamoyl-beta-alanine


sequence_source: UniProtKB:A0A068VNW5 direct REST lookup on 2026-06-04


organism: Arabidopsis thaliana

substrate_name: ATP

sequence_source: UniProtKB:A1A6H3 direct REST lookup on 2026-06-04

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, temperature not specified in the publication

substrate: ATP


substrate_name: ATP; D-Ribose

sequence_source: UniProtKB:Q9H477 direct REST lookup on 2026-06-04

assay_conditions_summary: cofactor ATP

substrate: ATP; D-Ribose


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9H477 direct REST lookup on 2026-06-04 plus E202L reconstruction and applied mutation signature E202L to reconstruct the assayed variant sequence.

proof_lines: mutant E202L, presence of Mg2+, pH 7.2, 37°C


sequence_source: UniProtKB:Q9H477 direct REST lookup on 2026-06-04 plus E202L reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9H477 direct REST lookup on 2026-06-04 plus N199L reconstruction and applied mutation signature N199L to reconstruct the assayed variant sequence.


substrate_name: D-ribose

sequence_source: UniProtKB:Q9H477 direct REST lookup on 2026-06-04 plus N199L reconstruction

substrate: D-ribose


substrate_name: Rhodopsin; ATP

sequence_source: UniProtKB:P28327 canonical FASTA direct lookup on 2026-06-04

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: Rhodopsin; ATP


organism: Danio rerio

sequence_source: UniProtKB:Q1XHM0 canonical FASTA direct lookup on 2026-06-04


sequence_source: UniProtKB:Q49HM9 canonical FASTA direct lookup on 2026-06-04


substrate_name: ATP; Rhodopsin

substrate: ATP; Rhodopsin


sequence_source: UniProtKB:Q15835 canonical FASTA direct lookup on 2026-06-04


sequence_source: UniProtKB:Q8WTQ7 canonical FASTA direct lookup on 2026-06-04


sequence_source: UniProt REST direct check for Q9M336 on 2026-06-04.


enzyme_display_name: Uracil phosphoribosyltransferase

organism: [Bacillus] caldolyticus

substrate_name: Uracil

sequence_source: UniProt REST direct check for P70881 on 2026-06-04.

assay_conditions_summary: pH 8

proof_lines:
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: Uracil phosphoribosyltransferase

substrate: Uracil


enzyme_display_name: Bifunctional protein PyrR

organism: Bacillus subtilis

substrate_name: Diphosphate; UMP

sequence_source: UniProt REST direct check for P39765 on 2026-06-04.

enzyme: Bifunctional protein PyrR

substrate: Diphosphate; UMP


substrate_name: UMP

substrate: UMP


organism: Escherichia coli

substrate_name: 5-Phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProt REST direct check for P0A8F0 on 2026-06-04.

substrate: 5-Phospho-alpha-D-ribose 1-diphosphate


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check for P0A8F0 on 2026-06-04 plus direct P131D substitution reconstruction. and applied mutation signature P131D to reconstruct the assayed variant sequence.


enzyme_display_name: dimethylargininase

substrate_name: N(omega)-methyl-L-Arginine

sequence_source: UniProtKB:P56965 FASTA fetched during exact accession review

smiles: CN=C(N)NCCCC(N)C(=O)O

enzyme: dimethylargininase

substrate: N(omega)-methyl-L-Arginine


substrate_name: NG-monomethyl-L-arginine

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

substrate: NG-monomethyl-L-arginine


substrate_name: Nomega,Nomega-dimethyl-L-arginine

sequence_variant_note: Resolved canonical sequence from UniProtKB:O94760 FASTA with E78A reconstructed during review and applied mutation signature E78A to reconstruct the assayed variant sequence.

proof_lines: mutant E78A, pH 7.3, temperature not specified in the publication

substrate: Nomega,Nomega-dimethyl-L-arginine


substrate_name: S-methyl-L-thiocitrulline

sequence_source: UniProtKB:O94760 FASTA used only as canonical context

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 E78AA, pH 7.3, temperature not specified in the publication

substrate: S-methyl-L-thiocitrulline


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94760 FASTA with L30A reconstructed during review and applied mutation signature L30A to reconstruct the assayed variant sequence.

proof_lines: mutant L30A, pH 7.3, temperature not specified in the publication


sequence_source: UniProtKB:O94760 FASTA fetched during exact accession review

proof_lines: wild-type, pH 7.3, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94760 FASTA with L271G reconstructed during review and applied mutation signature L271G to reconstruct the assayed variant sequence.

proof_lines: mutant L271G, pH 7.3, temperature not specified in the publication


proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed accession Q9I4E3 direct REST lookup, accessed 2026-06-04


substrate_name: H2O; NG,NG-Dimethyl-L-arginine

sequence_source: UniProtKB reviewed accession O08557 direct REST lookup, accessed 2026-06-04

substrate: H2O; NG,NG-Dimethyl-L-arginine


enzyme_display_name: thiamine-triphosphatase

substrate_name: thiamine triphosphate

sequence_source: UniProtKB reviewed accession Q8MKF1 direct REST lookup, accessed 2026-06-04

enzyme: thiamine-triphosphatase

substrate: thiamine triphosphate


organism: Homo sapiens

sequence_source: UniProtKB reviewed accession Q9BU02 direct REST lookup, accessed 2026-06-04


proof_lines:
wild type enzyme
GST-fused wild type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9BU02 direct REST lookup, accessed 2026-06-04 and applied mutation signature E63Q to reconstruct the assayed variant sequence.


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9BU02 direct REST lookup, accessed 2026-06-04 and applied mutation signature E78K to reconstruct the assayed variant sequence.

substrate: Unknown


substrate_name: Thiamine triphosphate; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 direct REST lookup, accessed 2026-06-04 and applied mutation signature K11A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant K11A His-tagged

substrate: Thiamine triphosphate; H2O


enzyme_display_name: arsenate reductase (thioredoxin)

substrate_name: arsenate

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

proof_lines: wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

enzyme: arsenate reductase (thioredoxin)

substrate: arsenate


organism: Bacillus thuringiensis


organism: Corynebacterium glutamicum


mutation_signature: N-terminally truncated mutant

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

proof_lines: N-terminally truncated mutant, pH 8.0, 37°C


organism: Staphylococcus aureus


substrate_name: Reduced thioredoxin; Arsenate

proof_lines: SABIO-RK modifier species: arsenate reductase (thioredoxin)(Enzyme) mutant ArsC C15A

proof_lines: pH 7.5, 37°C, mutant enzyme C15A, at 10 mM arsenate

substrate: Reduced thioredoxin; Arsenate


substrate_name: D-ribose

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9H477 canonical sequence plus selected-row mutation E202L and applied mutation signature E202L to reconstruct the assayed variant sequence.

substrate: D-ribose


substrate_name: ATP

substrate: ATP


enzyme_display_name: trehalose-phosphatase

organism: Brugia malayi

substrate_name: trehalose 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 canonical sequence plus selected-row mutation W280A and applied mutation signature W280A to reconstruct the assayed variant sequence.

enzyme: trehalose-phosphatase

substrate: trehalose 6-phosphate


organism: Candida albicans

substrate_name: Laminarin

sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 canonical sequence plus selected-row mutation F229A and applied mutation signature F229A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

substrate: Laminarin


organism: Cellulomonas fimi


organism: Hordeum vulgare

substrate_name: 4-nitrophenyl beta-D-glucoside

substrate: 4-nitrophenyl beta-D-glucoside


organism: Xanthomonas campestris

substrate_name: UDP-glucuronate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8GCH2 and applied mutation signature K307A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.2; 293.15 K; buffer 75 mM MgCl2

column_label: Table 2 (Kinetic parameters for wild-type and mutant GumK), enzyme row 'K307A'; column 'Km UDPGlcA (uM)' = 440; column 'Vmax (pmol/ug min)' = 15.2; column 'Kcat (min^-1)' = 0.68. The table has no kcat/Km column.

normalized_value_unit_evidence: Km: printed Table 2 cell 440 uM; 1 uM is 1/1000 mM, so 440 / 1000 = 0.44 mM. kcat: printed Table 2 cell 0.68 min^-1; the printed turnover column is per minute, so 0.68 / 60 = 0.011333333333333334 s^(-1). Vmax: printed Table 2 cell 15.2 pmol/ug min; 1 pmol/(ug min) is 0.000000000001 mol per 0.000001 g per 60 s, so 15.2 / 60 x 0.000001 = 0.00000025333333333333327 mol*s^(-1)*g^(-1). kcat/Km: Table 2 prints no efficiency cell, so the same-measurement quotient of the two printed cells is 0.011333333333333334 / 0.44 = 0.02575757575757576 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row K307A: column 'Km UDPGlcA (uM)' printed 440; column 'Vmax (pmol/ug min)' printed 15.2; column 'Kcat (min^-1)' printed 0.68. Table 2 carries no catalytic efficiency column.

row_label: Table 2, row K307A, donor UDP-GlcA columns

table_label: Table 2: Kinetic parameters for wild-type and mutant GumK (J. Biol. Chem. 2008, 283(36):25027-25035)

substrate: UDP-glucuronate


enzyme_display_name: uracil phosphoribosyltransferase

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A8F0; direct REST/FASTA lookup 2026-06-04 and applied mutation signature P131D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: uracil phosphoribosyltransferase(Enzyme) mutant P131D

enzyme: uracil phosphoribosyltransferase


substrate_name: 5-Phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProtKB reviewed accession P0A8F0; direct REST/FASTA lookup 2026-06-04

substrate: 5-Phospho-alpha-D-ribose 1-diphosphate


organism: Toxoplasma gondii

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProtKB reviewed accession Q26998; direct REST/FASTA lookup 2026-06-04

proof_lines:
recombinant wild-type, with GTP
recombinant wild-type, without GTP

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


substrate_name: Glyoxylate; L-Serine

sequence_source: UniProtKB reviewed accession Q56YA5; direct REST/FASTA lookup 2026-06-04

proof_lines:
at 10 mM glyoxylate
cosubstrate glyoxylate, pH 8.0, 30°C
at 30 mM L-alanine

substrate: Glyoxylate; L-Serine


substrate_name: L-Serine

substrate: L-Serine


substrate_name: L-Alanine

substrate: L-Alanine


sequence_source: UniProt REST P0A006 canonical sequence checked 2026-06-04

proof_lines:
high affinity
pH 7.5, 37°C
Raw SKiD Env: Temp=-----, pH=-----


proof_lines: wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A006 canonical sequence with H62Q substitution reconstructed during worker review and applied mutation signature H62Q to reconstruct the assayed variant sequence.

proof_lines: H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters


sequence_variant_note: Resolved canonical sequence from UniProt REST Q8GCH2 canonical sequence with Q310A substitution reconstructed during worker review and applied mutation signature Q310A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q8GCH2 canonical sequence with E192A substitution reconstructed during worker review and applied mutation signature E192A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant E192A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProt REST Q8GCH2 canonical sequence with D234A substitution reconstructed during worker review and applied mutation signature D234A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant D234A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProt REST Q8GCH2 canonical sequence with E272A substitution reconstructed during worker review and applied mutation signature E272A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant E272A His-tagged


organism: Rhizomucor miehei

substrate_name: cellobiose

substrate: cellobiose


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row ONPG-6-P; the Michaelis constant 0.6 comes from the printed column K_m (mM), the turnover number 11 from the printed column k_cat (1/s), and the catalytic efficiency 1.9 x 10^4 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.6 mM; already in mM, no unit conversion applies; the exported value is 0.6 mM. kcat: printed cell 11 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 11.0 s^(-1). 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 = 19.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 18.333333333333336 s^(-1)*mM^(-1), the quotient 11 / 0.6 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 19.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row ONPG-6-P: Km = 0.6 mM; kcat = 11 1/s; printed kcat/Km = 1.9 x 10^4 M^-1 s^-1.


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row ONPGlc-6-P; the Michaelis constant 0.06 comes from the printed column K_m (mM), the turnover number 70 from the printed column k_cat (1/s), and the catalytic efficiency 1.16 x 10^6 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.06 mM; already in mM, no unit conversion applies; the exported value is 0.06 mM. kcat: printed cell 70 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 70.0 s^(-1). kcat/Km: printed cell 1.16 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.16 x 10^6 / 1000 = 1160.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 1166.6666666666667 s^(-1)*mM^(-1), the quotient 70 / 0.06 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 1160.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row ONPGlc-6-P: Km = 0.06 mM; kcat = 70 1/s; printed kcat/Km = 1.16 x 10^6 M^-1 s^-1.


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row PNPGlc-6-P; the Michaelis constant 0.08 comes from the printed column K_m (mM), the turnover number 58 from the printed column k_cat (1/s), and the catalytic efficiency 7.29 x 10^5 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.08 mM; already in mM, no unit conversion applies; the exported value is 0.08 mM. kcat: printed cell 58 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 58.0 s^(-1). kcat/Km: printed cell 7.29 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.29 x 10^5 / 1000 = 729.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 725.0 s^(-1)*mM^(-1), the quotient 58 / 0.08 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 729.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row PNPGlc-6-P: Km = 0.08 mM; kcat = 58 1/s; printed kcat/Km = 7.29 x 10^5 M^-1 s^-1.


substrate_name: beta-Casomorphin

substrate: beta-Casomorphin


organism: SARS coronavirus

substrate_name: ACE2; Spike glycoprotein RBD-SD1

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

substrate: ACE2; Spike glycoprotein RBD-SD1


organism: Bos taurus

substrate_name: H2O; NG,NG-Dimethyl-L-arginine

proof_lines: in the presence of 5 mM EDTA, at pH 7.3 and 37°C

substrate: H2O; NG,NG-Dimethyl-L-arginine


organism: Hyphomicrobium methylovorum


organism: Methylococcus capsulatus

substrate_name: L-alanine

proof_lines: pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate

proof_lines: pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine

proof_lines: pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-alanine

substrate: L-alanine


organism: Methylotuvimicrobium alcaliphilum

substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: Rhodopsin; ATP

substrate: Rhodopsin; ATP


substrate_name: ATP

substrate: ATP


substrate_name: cellotriose

substrate: cellotriose


substrate_name: gentobiose

substrate: gentobiose


substrate_name: cellotetraose

substrate: cellotetraose


substrate_name: NG,NG-Dimethyl-L-arginine

sequence_source: UniProtKB:P56965 reviewed Swiss-Prot direct lookup

substrate: NG,NG-Dimethyl-L-arginine


organism: Mus musculus

substrate_name: thiamine triphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus W53A reconstruction and applied mutation signature W53A to reconstruct the assayed variant sequence.

substrate: thiamine triphosphate


sequence_source: UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus K65A reconstruction and applied mutation signature K65A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus Y79A reconstruction and applied mutation signature Y79A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus K11A reconstruction and applied mutation signature K11A to reconstruct the assayed variant sequence.


substrate_name: Thiamine triphosphate; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus D37A reconstruction and applied mutation signature D37A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant D37A His-tagged

substrate: Thiamine triphosphate; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus E81A reconstruction and applied mutation signature E81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; D207A reconstructed after confirming residue 207 is D. and applied mutation signature D207A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant D207A His-tagged


substrate_name: UDP-glucuronate

sequence_source: UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04.

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

substrate: UDP-glucuronate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; M231A reconstructed after confirming residue 231 is M. and applied mutation signature M231A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; Y292A reconstructed after confirming residue 292 is Y. and applied mutation signature Y292A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; K307A reconstructed after confirming residue 307 is K. and applied mutation signature K307A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant K307A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; E272A reconstructed after confirming residue 272 is E. and applied mutation signature E272A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; Y39A sequence reconstructed from the canonical sequence. and applied mutation signature Y39A to reconstruct the assayed variant sequence.


substrate_name: H2O; Thiamine triphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; K65A sequence reconstructed from the canonical sequence. and applied mutation signature K65A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant K65A His-tagged

substrate: H2O; Thiamine triphosphate


sequence_source: UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; Y39A sequence reconstructed from the canonical sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant Y39A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; D37A sequence reconstructed from the canonical sequence. and applied mutation signature D37A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; Y79A sequence reconstructed from the canonical sequence. and applied mutation signature Y79A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant Y79A His-tagged


sequence_source: UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04.


substrate_name: Triphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; W53A sequence reconstructed from the canonical sequence. and applied mutation signature W53A to reconstruct the assayed variant sequence.

substrate: Triphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; K193A sequence reconstructed from the canonical sequence. and applied mutation signature K193A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q8JZL3

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature K193A reconstruction and applied mutation signature K193A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant K193A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature E81A reconstruction and applied mutation signature E81A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant E81A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature W53A reconstruction and applied mutation signature W53A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant W53A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature D147A reconstruction and applied mutation signature D147A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant D147A His-tagged


sequence_source: UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature D147A reconstruction


enzyme_display_name: 2-hydroxy-dATP diphosphatase

organism: Homo sapiens

sequence_source: UniProtKB reviewed accession P36639

enzyme: 2-hydroxy-dATP diphosphatase


sequence_source: UniProtKB reviewed accession P36639 direct REST/FASTA lookup


substrate_name: dGTP

substrate: dGTP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P36639 direct REST/FASTA lookup plus D119A substitution reconstruction and applied mutation signature D119A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P36639 direct REST/FASTA lookup plus F27A substitution reconstruction and applied mutation signature F27A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P36639 direct REST/FASTA lookup plus F27A substitution reconstruction


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


sequence_source: UniProtKB:P36639 direct lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:P36639 direct lookup and applied mutation signature D119A to reconstruct the assayed variant sequence.


substrate_name: 8-oxo-dGTP; H2O

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

substrate: 8-oxo-dGTP; H2O


sequence_source: UniProtKB:Q8BG93 direct lookup

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: oxaloacetate decarboxylase

organism: Enterococcus faecalis

substrate_name: oxaloacetate

sequence_source: UniProtKB:Q82YW6 direct lookup

proof_lines: calculated value at pH 4.5, temperature not specified in the publication

enzyme: oxaloacetate decarboxylase

substrate: oxaloacetate


substrate_name: Oxaloacetate

sequence_source: UniProtKB:P48163 direct lookup

substrate: Oxaloacetate


sequence_source: UniProtKB:Q6P587 direct lookup


enzyme_display_name: pyridoxal phosphatase

substrate_name: Pyridoxal phosphate; H2O

sequence_source: UniProtKB reviewed entry Q96GD0 direct REST lookup

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

enzyme: pyridoxal phosphatase

substrate: Pyridoxal phosphate; H2O


substrate_name: Pyridoxamine phosphate

substrate: Pyridoxamine phosphate


substrate_name: Pyridoxine phosphate

substrate: Pyridoxine phosphate


substrate_name: Pyridoxal phosphate

substrate: Pyridoxal phosphate


substrate_name: H2O; Pyridoxal phosphate

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

substrate: H2O; Pyridoxal phosphate


substrate_name: pyridoxal 5'-phosphate

sequence_source: UniProtKB reviewed entry P60487 direct REST lookup

substrate: pyridoxal 5'-phosphate


proof_lines:
pH 7.4, 22°C
Raw SKiD Env: Temp=22°C, pH=7.4


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed entry F4KEV7 direct REST lookup from source accession Q9LVM4

proof_lines:
pH 6.8, 30°C
pH 6.8, 30°C, in presence of Mg2+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P49789 and applied mutation signature H96G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5.8; 299.65 K; cofactor NADH

column_label: Table 2: Kinetic Parameters for Catalysis by H96G-Fhit (Biochemistry 2004, 43(23):7637-7642); Table 2, substrate row 'AMP-Im' (footnote a); column 'substrate'; column 'kcat (s-1)'; column 'Km (uM)'; column 'kcat/Km (M-1 s-1)'; the printed cells for this row are kcat 0.91 s-1, Km 26 uM and kcat/Km 3.5 x 10^4 M-1 s-1.

normalized_value_unit_evidence: kcat: printed cell 0.91 s-1; already in s^-1, no unit conversion applies; normalized value 0.91 s^(-1). Km: printed cell 26 uM; 1 uM is 0.001 mM, so 26 / 1000 = 0.026 mM; normalized value 0.026 mM. kcat/Km: printed cell 3.5 x 10^4 M-1 s-1 = 35000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 35000 / 1000 = 35 s^-1 mM^-1; normalized value 35 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row 'AMP-Im': kcat = 0.91 s-1; Km = 26 uM; printed kcat/Km = 3.5 x 10^4 M-1 s-1.


sequence_source: UniProtKB:P49789 canonical FASTA

assay_conditions_summary: pH 7; 299.65 K; cofactor NADH

column_label: Table 3: Kinetic Parameters for Catalysis by Wild-Type Fhit (Biochemistry 2004, 43(23):7637-7642); Table 3, substrate row 'AMP-Im' (footnote a); column 'substrate'; column 'kcat (s-1)'; column 'Km (uM)'; column 'kcat/Km (M-1 s-1)'; the printed cells for this row are kcat 4.4 s-1, Km 6.2 uM and kcat/Km 6.4 x 10^5 M-1 s-1.

normalized_value_unit_evidence: kcat: printed cell 4.4 s-1; already in s^-1, no unit conversion applies; normalized value 4.4 s^(-1). Km: printed cell 6.2 uM; 1 uM is 0.001 mM, so 6.2 / 1000 = 0.0062 mM; normalized value 0.0062 mM. kcat/Km: printed cell 6.4 x 10^5 M-1 s-1 = 640000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 640000 / 1000 = 640 s^-1 mM^-1; normalized value 640 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row 'AMP-Im': kcat = 4.4 s-1; Km = 6.2 uM; printed kcat/Km = 6.4 x 10^5 M-1 s-1.


substrate_name: P1,P3-Bis(5'-adenosyl) triphosphate

assay_conditions_summary: pH 7.3; 299.65 K; cofactor ADP

column_label: Table 3: Kinetic Parameters for Catalysis by Wild-Type Fhit (Biochemistry 2004, 43(23):7637-7642); Table 3, substrate row 'Ap3A' (footnote b); column 'substrate'; column 'kcat (s-1)'; column 'Km (uM)'; column 'kcat/Km (M-1 s-1)'; the printed cells for this row are kcat 3.5 s-1, Km 2.9 uM and kcat/Km 11.6 x 10^5 M-1 s-1.

normalized_value_unit_evidence: kcat: printed cell 3.5 s-1; already in s^-1, no unit conversion applies; normalized value 3.5 s^(-1). Km: printed cell 2.9 uM; 1 uM is 0.001 mM, so 2.9 / 1000 = 0.0029 mM; normalized value 0.0029 mM. kcat/Km: printed cell 11.6 x 10^5 M-1 s-1 = 1160000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1160000 / 1000 = 1160 s^-1 mM^-1; normalized value 1160 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row 'Ap3A': kcat = 3.5 s-1; Km = 2.9 uM; printed kcat/Km = 11.6 x 10^5 M-1 s-1.

substrate: P1,P3-Bis(5'-adenosyl) triphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49789 canonical FASTA with H96G reconstruction and applied mutation signature H96G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bis(5'-adenosyl)-triphosphatase(Enzyme) mutant H96G Fhit