substrate_name: isopentenyl diphosphate

sequence_source: UniProtKB W0J9X7 REST direct sequence checked 2026-06-15.

substrate: isopentenyl diphosphate


enzyme_display_name: dimethylallylcistransferase

organism: Solanum habrochaites

source_db: oed

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

smiles: C=C(C)CCOP(=O)(O)OP(=O)(O)O

data_origin: experimental

enzyme: dimethylallylcistransferase

source: oed


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


organism: Solanum lycopersicum

sequence_source: UniProtKB C1K5M2 REST direct sequence checked 2026-06-15.


source_db: brenda

kcat_over_km_display: Not reported

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

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

source_databases_merged: brenda skid

source: brenda


enzyme_display_name: allose kinase

organism: Escherichia coli

substrate_name: D-Allose

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32718 and applied mutation signature F145L to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 2, F145L AlsK column, D-allose block; kcat cell = 49 s-1; Km cell = 1.5 x 10^-4 M; kcat/Km cell = 3.2 x 10^5 M^-1 s^-1. captured primary segment: F145L AlsK | D-allose | Table 2, F145L AlsK column, D-allose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, F145L AlsK column, D-allose block, kcat = 49 s-1 | Table 2, F145L AlsK column, D-allose block, Km = 1.5 x 10^-4 M | Table 2, F145L AlsK column, D-allose block, kcat/Km = 3.2 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 49 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 49.0 s^(-1). Km: printed cell 1.5 x 10^-4 M; 1 M is 1000 mM, so 1.5 x 10^-4 x 1000 = 0.15 mM. kcat/Km: printed cell 3.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.2 x 10^5 / 1000 = 320.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 49.0 / 0.15 = 326.6666666666667 s^-1 mM^-1, against the printed efficiency cell 320.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, F145L AlsK column, D-allose block: kcat = 49 s-1; Km = 1.5 x 10^-4 M; kcat/Km = 3.2 x 10^5 M^-1 s^-1.

table_label: Table 2: Kinetic Parameters for Phosphorylation of Native and Ambiguous Substrates by Wild-Type AlsK and Selected Variants (Biochemistry 2007, 46, 13564-13572); printed row heads kcat, sugar (s-1) | Km, sugar (M) | Km, ATP (M) | kcat/Km, sugar (M-1 s-1)

enzyme: allose kinase

substrate: D-Allose

status: corrected


substrate_name: D-Glucose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32718 and applied mutation signature A73G to reconstruct the assayed variant sequence.

column_label: Table 2, A73G AlsK column, D-glucose block; kcat cell = 13 s-1; Km cell = 6.5 x 10^-4 M; kcat/Km cell = 2.1 x 10^4 M^-1 s^-1. captured primary segment: A73G AlsK | D-glucose | Table 2, A73G AlsK column, D-glucose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, A73G AlsK column, D-glucose block, kcat = 13 s-1 | Table 2, A73G AlsK column, D-glucose block, Km = 6.5 x 10^-4 M | Table 2, A73G AlsK column, D-glucose block, kcat/Km = 2.1 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 13 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 13.0 s^(-1). Km: printed cell 6.5 x 10^-4 M; 1 M is 1000 mM, so 6.5 x 10^-4 x 1000 = 0.65 mM. kcat/Km: printed cell 2.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.1 x 10^4 / 1000 = 21.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 13.0 / 0.65 = 20.0 s^-1 mM^-1, against the printed efficiency cell 21.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, A73G AlsK column, D-glucose block: kcat = 13 s-1; Km = 6.5 x 10^-4 M; kcat/Km = 2.1 x 10^4 M^-1 s^-1.

substrate: D-Glucose


substrate_name: ATP

sequence_source: UniProtKB P32718 REST direct sequence checked 2026-06-15.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: ATP; D-Allose

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

column_label: Table 2, A73G AlsK column, D-allose block, ATP axis; kcat cell = 40 s-1; Km, ATP cell = 6.0 x 10^-5 M; kcat/Km cell: Table 2 carries none on the ATP axis. captured primary segment: A73G AlsK | ATP | Table 2, A73G AlsK column, D-allose block, ATP axis | 0.2 M Tris, pH 7.6 at 25 C | Table 2, A73G AlsK column, D-allose block, ATP axis, kcat = 40 s-1 | Table 2, A73G AlsK column, D-allose block, ATP axis, Km, ATP = 6.0 x 10^-5 M | kcat/Km: Table 2 prints no kcat/Km cell on the ATP axis of this measurement

normalized_value_unit_evidence: kcat: printed cell 40 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 40.0 s^(-1). Km: printed cell 6.0 x 10^-5 M; 1 M is 1000 mM, so 6.0 x 10^-5 x 1000 = 0.060000000000000005 mM. kcat/Km: the paper prints no efficiency cell on this ATP axis, so the ratio typed on this record is the arithmetic quotient of the two printed cells of this same measurement, 40.0 / 0.060000000000000005 = 666.6666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, A73G AlsK column, D-allose block, ATP axis: kcat = 40 s-1; Km, ATP = 6.0 x 10^-5 M; Table 2 carries no kcat/Km cell on the ATP axis.

substrate: ATP; D-Allose


sequence_source: UniProtKB P32718 direct FASTA/JSON lookup; reviewed Swiss-Prot D-allose kinase, EC 2.7.1.55, Escherichia coli K-12.

column_label: Table 2, wt AlsK column, D-allose block; kcat cell = 47 s-1; Km cell = 1.9 x 10^-4 M; kcat/Km cell = 2.5 x 10^5 M^-1 s^-1. captured primary segment: wt AlsK | D-allose | Table 2, wt AlsK column, D-allose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, wt AlsK column, D-allose block, kcat = 47 s-1 | Table 2, wt AlsK column, D-allose block, Km = 1.9 x 10^-4 M | Table 2, wt AlsK column, D-allose block, kcat/Km = 2.5 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 47 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 47.0 s^(-1). Km: printed cell 1.9 x 10^-4 M; 1 M is 1000 mM, so 1.9 x 10^-4 x 1000 = 0.19 mM. kcat/Km: printed cell 2.5 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 x 10^5 / 1000 = 250.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 47.0 / 0.19 = 247.3684210526316 s^-1 mM^-1, against the printed efficiency cell 250.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, wt AlsK column, D-allose block: kcat = 47 s-1; Km = 1.9 x 10^-4 M; kcat/Km = 2.5 x 10^5 M^-1 s^-1.

row_label: Table 2, wt AlsK column, D-allose block


column_label: Table 2, A73G AlsK column, D-glucose block, ATP axis; kcat cell = 13 s-1; Km, ATP cell = 4.5 x 10^-4 M; kcat/Km cell: Table 2 carries none on the ATP axis. captured primary segment: A73G AlsK | ATP | Table 2, A73G AlsK column, D-glucose block, ATP axis | 0.2 M Tris, pH 7.6 at 25 C | Table 2, A73G AlsK column, D-glucose block, ATP axis, kcat = 13 s-1 | Table 2, A73G AlsK column, D-glucose block, ATP axis, Km, ATP = 4.5 x 10^-4 M | kcat/Km: Table 2 prints no kcat/Km cell on the ATP axis of this measurement

normalized_value_unit_evidence: kcat: printed cell 13 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 13.0 s^(-1). Km: printed cell 4.5 x 10^-4 M; 1 M is 1000 mM, so 4.5 x 10^-4 x 1000 = 0.45 mM. kcat/Km: the paper prints no efficiency cell on this ATP axis, so the ratio typed on this record is the arithmetic quotient of the two printed cells of this same measurement, 13.0 / 0.45 = 28.88888888888889 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, A73G AlsK column, D-glucose block, ATP axis: kcat = 13 s-1; Km, ATP = 4.5 x 10^-4 M; Table 2 carries no kcat/Km cell on the ATP axis.


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

assay_conditions_summary: cofactor ATP


substrate_name: D-Altrose

column_label: Table 3, A73G AlsK section, D-altrose row; kcat cell = 94 s-1; Km cell = 4.8 x 10^-2 M; kcat/Km cell = 2.0 x 10^3 M^-1 s^-1. captured primary segment: A73G AlsK | D-altrose | Table 3, A73G AlsK section, D-altrose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, A73G AlsK section, D-altrose row, kcat = 94 s-1 | Table 3, A73G AlsK section, D-altrose row, Km = 4.8 x 10^-2 M | Table 3, A73G AlsK section, D-altrose row, kcat/Km = 2.0 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 94 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 94.0 s^(-1). Km: printed cell 4.8 x 10^-2 M; 1 M is 1000 mM, so 4.8 x 10^-2 x 1000 = 48.0 mM. kcat/Km: printed cell 2.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.0 x 10^3 / 1000 = 2.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 94.0 / 48.0 = 1.9583333333333333 s^-1 mM^-1, against the printed efficiency cell 2.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, A73G AlsK section, D-altrose row: kcat = 94 s-1; Km = 4.8 x 10^-2 M; kcat/Km = 2.0 x 10^3 M^-1 s^-1.

table_label: Table 3: Specificity Profiles of Wild-Type and A73G AlsK (Biochemistry 2007, 46, 13564-13572); printed column heads substrate | kcat (s-1) | Km (M) | kcat/Km (M-1 s-1) | x-fold change in kcat/Km

substrate: D-Altrose


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB P32718 direct FASTA/JSON lookup; reviewed Swiss-Prot D-allose kinase, EC 2.7.1.55, Escherichia coli K-12. Variant reconstructed by direct residue check for A73G. and applied mutation signature A73G to reconstruct the assayed variant sequence.

status: unverified


substrate_name: D-Mannose

column_label: Table 3, A73G AlsK section, D-mannose row; kcat cell = 9.5 s-1; Km cell = 2.1 x 10^-1 M; kcat/Km cell = 4.5 x 10^1 M^-1 s^-1. captured primary segment: A73G AlsK | D-mannose | Table 3, A73G AlsK section, D-mannose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, A73G AlsK section, D-mannose row, kcat = 9.5 s-1 | Table 3, A73G AlsK section, D-mannose row, Km = 2.1 x 10^-1 M | Table 3, A73G AlsK section, D-mannose row, kcat/Km = 4.5 x 10^1 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 9.5 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 9.5 s^(-1). Km: printed cell 2.1 x 10^-1 M; 1 M is 1000 mM, so 2.1 x 10^-1 x 1000 = 210.0 mM. kcat/Km: printed cell 4.5 x 10^1 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.5 x 10^1 / 1000 = 0.045 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 9.5 / 210.0 = 0.04523809523809524 s^-1 mM^-1, against the printed efficiency cell 0.045 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, A73G AlsK section, D-mannose row: kcat = 9.5 s-1; Km = 2.1 x 10^-1 M; kcat/Km = 4.5 x 10^1 M^-1 s^-1.

substrate: D-Mannose


column_label: Table 2, wt AlsK column, D-glucose block; kcat cell = 10 s-1; Km cell = 2.9 x 10^-2 M; kcat/Km cell = 3.4 x 10^2 M^-1 s^-1. captured primary segment: wt AlsK | D-glucose | Table 2, wt AlsK column, D-glucose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, wt AlsK column, D-glucose block, kcat = 10 s-1 | Table 2, wt AlsK column, D-glucose block, Km = 2.9 x 10^-2 M | Table 2, wt AlsK column, D-glucose block, kcat/Km = 3.4 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 10 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 10.0 s^(-1). Km: printed cell 2.9 x 10^-2 M; 1 M is 1000 mM, so 2.9 x 10^-2 x 1000 = 29.0 mM. kcat/Km: printed cell 3.4 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.4 x 10^2 / 1000 = 0.34 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 10.0 / 29.0 = 0.3448275862068966 s^-1 mM^-1, against the printed efficiency cell 0.34 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, wt AlsK column, D-glucose block: kcat = 10 s-1; Km = 2.9 x 10^-2 M; kcat/Km = 3.4 x 10^2 M^-1 s^-1.


column_label: Table 2, F145L AlsK column, D-glucose block, ATP axis; kcat cell = 28 s-1; Km, ATP cell = 9.6 x 10^-4 M; kcat/Km cell: Table 2 carries none on the ATP axis. captured primary segment: F145L AlsK | ATP | Table 2, F145L AlsK column, D-glucose block, ATP axis | 0.2 M Tris, pH 7.6 at 25 C | Table 2, F145L AlsK column, D-glucose block, ATP axis, kcat = 28 s-1 | Table 2, F145L AlsK column, D-glucose block, ATP axis, Km, ATP = 9.6 x 10^-4 M | kcat/Km: Table 2 prints no kcat/Km cell on the ATP axis of this measurement

normalized_value_unit_evidence: kcat: printed cell 28 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 28.0 s^(-1). Km: printed cell 9.6 x 10^-4 M; 1 M is 1000 mM, so 9.6 x 10^-4 x 1000 = 0.9600000000000001 mM. kcat/Km: the paper prints no efficiency cell on this ATP axis, so the ratio typed on this record is the arithmetic quotient of the two printed cells of this same measurement, 28.0 / 0.9600000000000001 = 29.166666666666664 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, F145L AlsK column, D-glucose block, ATP axis: kcat = 28 s-1; Km, ATP = 9.6 x 10^-4 M; Table 2 carries no kcat/Km cell on the ATP axis.


column_label: Table 2, F145L AlsK column, D-glucose block; kcat cell = 28 s-1; Km cell = 7.2 x 10^-3 M; kcat/Km cell = 3.9 x 10^3 M^-1 s^-1. captured primary segment: F145L AlsK | D-glucose | Table 2, F145L AlsK column, D-glucose block | 0.2 M Tris, pH 7.6 at 25 C | Table 2, F145L AlsK column, D-glucose block, kcat = 28 s-1 | Table 2, F145L AlsK column, D-glucose block, Km = 7.2 x 10^-3 M | Table 2, F145L AlsK column, D-glucose block, kcat/Km = 3.9 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 28 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 28.0 s^(-1). Km: printed cell 7.2 x 10^-3 M; 1 M is 1000 mM, so 7.2 x 10^-3 x 1000 = 7.2 mM. kcat/Km: printed cell 3.9 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.9 x 10^3 / 1000 = 3.9 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 28.0 / 7.2 = 3.888888888888889 s^-1 mM^-1, against the printed efficiency cell 3.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, F145L AlsK column, D-glucose block: kcat = 28 s-1; Km = 7.2 x 10^-3 M; kcat/Km = 3.9 x 10^3 M^-1 s^-1.


column_label: Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row; kcat cell = 1.5 s-1; Km cell = 3.8 x 10^-1 M; kcat/Km cell = 4.1 M^-1 s^-1. captured primary segment: wild-type AlsK | 2'-deoxy-D-glucose | Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row, kcat = 1.5 s-1 | Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row, Km = 3.8 x 10^-1 M | Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row, kcat/Km = 4.1 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 1.5 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 1.5 s^(-1). Km: printed cell 3.8 x 10^-1 M; 1 M is 1000 mM, so 3.8 x 10^-1 x 1000 = 380.0 mM. kcat/Km: printed cell 4.1 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.1 / 1000 = 0.0040999999999999995 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 1.5 / 380.0 = 0.003947368421052632 s^-1 mM^-1, against the printed efficiency cell 0.0040999999999999995 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, wild-type AlsK section, 2'-deoxy-D-glucose row: kcat = 1.5 s-1; Km = 3.8 x 10^-1 M; kcat/Km = 4.1 M^-1 s^-1.


column_label: Table 3, A73G AlsK section, 2'-deoxy-D-glucose row; kcat cell = 19 s-1; Km cell = 5.1 x 10^-2 M; kcat/Km cell = 3.7 x 10^2 M^-1 s^-1. captured primary segment: A73G AlsK | 2'-deoxy-D-glucose | Table 3, A73G AlsK section, 2'-deoxy-D-glucose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, A73G AlsK section, 2'-deoxy-D-glucose row, kcat = 19 s-1 | Table 3, A73G AlsK section, 2'-deoxy-D-glucose row, Km = 5.1 x 10^-2 M | Table 3, A73G AlsK section, 2'-deoxy-D-glucose row, kcat/Km = 3.7 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 19 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 19.0 s^(-1). Km: printed cell 5.1 x 10^-2 M; 1 M is 1000 mM, so 5.1 x 10^-2 x 1000 = 51.0 mM. kcat/Km: printed cell 3.7 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.7 x 10^2 / 1000 = 0.37 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 19.0 / 51.0 = 0.37254901960784315 s^-1 mM^-1, against the printed efficiency cell 0.37 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, A73G AlsK section, 2'-deoxy-D-glucose row: kcat = 19 s-1; Km = 5.1 x 10^-2 M; kcat/Km = 3.7 x 10^2 M^-1 s^-1.


column_label: Table 3, wild-type AlsK section, D-altrose row; kcat cell = 34 s-1; Km cell = 2.1 x 10^-1 M; kcat/Km cell = 1.6 x 10^2 M^-1 s^-1. captured primary segment: wild-type AlsK | D-altrose | Table 3, wild-type AlsK section, D-altrose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, wild-type AlsK section, D-altrose row, kcat = 34 s-1 | Table 3, wild-type AlsK section, D-altrose row, Km = 2.1 x 10^-1 M | Table 3, wild-type AlsK section, D-altrose row, kcat/Km = 1.6 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 34 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 34.0 s^(-1). Km: printed cell 2.1 x 10^-1 M; 1 M is 1000 mM, so 2.1 x 10^-1 x 1000 = 210.0 mM. kcat/Km: printed cell 1.6 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^2 / 1000 = 0.16 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 34.0 / 210.0 = 0.1619047619047619 s^-1 mM^-1, against the printed efficiency cell 0.16 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, wild-type AlsK section, D-altrose row: kcat = 34 s-1; Km = 2.1 x 10^-1 M; kcat/Km = 1.6 x 10^2 M^-1 s^-1.


column_label: Table 3, wild-type AlsK section, D-mannose row; kcat cell = 0.5 s-1; Km cell = 3.9 x 10^-1 M; kcat/Km cell = 1.2 M^-1 s^-1. captured primary segment: wild-type AlsK | D-mannose | Table 3, wild-type AlsK section, D-mannose row | 0.2 M Tris, pH 7.6 at 25 C | Table 3, wild-type AlsK section, D-mannose row, kcat = 0.5 s-1 | Table 3, wild-type AlsK section, D-mannose row, Km = 3.9 x 10^-1 M | Table 3, wild-type AlsK section, D-mannose row, kcat/Km = 1.2 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.5 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.5 s^(-1). Km: printed cell 3.9 x 10^-1 M; 1 M is 1000 mM, so 3.9 x 10^-1 x 1000 = 390.0 mM. kcat/Km: printed cell 1.2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 / 1000 = 0.0012 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 0.5 / 390.0 = 0.001282051282051282 s^-1 mM^-1, against the printed efficiency cell 0.0012 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, wild-type AlsK section, D-mannose row: kcat = 0.5 s-1; Km = 3.9 x 10^-1 M; kcat/Km = 1.2 M^-1 s^-1.


substrate_name: D-Allose; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB P32718 direct FASTA/JSON lookup; reviewed Swiss-Prot D-allose kinase, EC 2.7.1.55, Escherichia coli K-12. Variant reconstructed by direct residue check for F145L. and applied mutation signature F145L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: allose kinase(Enzyme) mutant AlsK F145L

substrate: D-Allose; ATP


enzyme_display_name: inositol 3-kinase

organism: Thermococcus kodakarensis

substrate_name: D-Xylose

verification_status: verified

sequence_source: UniProtKB Q5JDA3 direct FASTA/JSON lookup; live TrEMBL TK2285 PfkB-family kinase from Thermococcus kodakarensis KOD1 with BRENDA cross-reference EC 2.7.1.64.

assay_conditions_summary: pH 7.5; 358.15 K; buffer solution; cofactor ATP

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Xylose': column 'kcat, s^-1' = 5.6; column 'Km, mM' = 418; column 'kcat/Km, s^-1 mM^-1' = 0.013. The kcat and Km cells are printed with their standard deviations (5.6 +/- 0.3 and 418 +/- 50); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.6 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 5.6 s^(-1). Km: printed Table 3 cell 418 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 418.0 mM. kcat/Km: printed Table 3 cell 0.013 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.013 s^(-1)*mM^(-1), which is the exact same-row quotient 5.6 / 418 = 0.013397129186602871 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Xylose': kcat = 5.6 s^-1; Km = 418 mM; printed kcat/Km = 0.013 s^-1 mM^-1.

table_label: Table 3: Kinetic parameters of TK2285 toward various monosaccharides and myo-inositol (J. Biol. Chem. 2013, 288(29):20856-20867)

enzyme: inositol 3-kinase

substrate: D-Xylose

status: verified


substrate_name: D-Talose

sequence_source: UniProtKB direct lookup Q5JDA3

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Talose': column 'kcat, s^-1' = 13.1; column 'Km, mM' = 438; column 'kcat/Km, s^-1 mM^-1' = 0.030. The kcat and Km cells are printed with their standard deviations (13.1 +/- 0.1 and 438 +/- 39); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 13.1 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 13.1 s^(-1). Km: printed Table 3 cell 438 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 438.0 mM. kcat/Km: printed Table 3 cell 0.030 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.03 s^(-1)*mM^(-1), which is the exact same-row quotient 13.1 / 438 = 0.029908675799086758 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Talose': kcat = 13.1 s^-1; Km = 438 mM; printed kcat/Km = 0.030 s^-1 mM^-1.

substrate: D-Talose


substrate_name: D-allose

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Allose': column 'kcat, s^-1' = 18.3; column 'Km, mM' = 863; column 'kcat/Km, s^-1 mM^-1' = 0.021. The kcat and Km cells are printed with their standard deviations (18.3 +/- 0.6 and 863 +/- 51); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 18.3 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 18.3 s^(-1). Km: printed Table 3 cell 863 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 863.0 mM. kcat/Km: printed Table 3 cell 0.021 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.021 s^(-1)*mM^(-1), which is the exact same-row quotient 18.3 / 863 = 0.021205098493626885 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Allose': kcat = 18.3 s^-1; Km = 863 mM; printed kcat/Km = 0.021 s^-1 mM^-1.

substrate: D-allose


substrate_name: D-Lyxose

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Lyxose': column 'kcat, s^-1' = 3.9; column 'Km, mM' = 171; column 'kcat/Km, s^-1 mM^-1' = 0.023. The kcat and Km cells are printed with their standard deviations (3.9 +/- 0.1 and 171 +/- 17); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.9 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 3.9 s^(-1). Km: printed Table 3 cell 171 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 171.0 mM. kcat/Km: printed Table 3 cell 0.023 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.023 s^(-1)*mM^(-1), which is the exact same-row quotient 3.9 / 171 = 0.02280701754385965 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Lyxose': kcat = 3.9 s^-1; Km = 171 mM; printed kcat/Km = 0.023 s^-1 mM^-1.

substrate: D-Lyxose


substrate_name: D-ribose

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Ribose': column 'kcat, s^-1' = 5.1; column 'Km, mM' = 951; column 'kcat/Km, s^-1 mM^-1' = 0.005. The kcat and Km cells are printed with their standard deviations (5.1 +/- 0.4 and 951 +/- 119); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.1 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 5.1 s^(-1). Km: printed Table 3 cell 951 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 951.0 mM. kcat/Km: printed Table 3 cell 0.005 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.005 s^(-1)*mM^(-1), which is the exact same-row quotient 5.1 / 951 = 0.005362776025236593 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Ribose': kcat = 5.1 s^-1; Km = 951 mM; printed kcat/Km = 0.005 s^-1 mM^-1.

substrate: D-ribose


substrate_name: D-tagatose

substrate: D-tagatose


substrate_name: myo-inositol

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'myo-Inositol': column 'kcat, s^-1' = 23.2; column 'Km, mM' = 0.36; column 'kcat/Km, s^-1 mM^-1' = 64.9. The kcat and Km cells are printed with their standard deviations (23.2 +/- 0.5 and 0.36 +/- 0.03); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 23.2 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 23.2 s^(-1). Km: printed Table 3 cell 0.36 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 0.36 mM. kcat/Km: printed Table 3 cell 64.9 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 64.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'myo-Inositol': kcat = 23.2 s^-1; Km = 0.36 mM; printed kcat/Km = 64.9 s^-1 mM^-1.

substrate: myo-inositol


column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Tagatose': column 'kcat, s^-1' = 1.5; column 'Km, mM' = 53; column 'kcat/Km, s^-1 mM^-1' = 0.028. The kcat and Km cells are printed with their standard deviations (1.5 +/- 0.1 and 53 +/- 9); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.5 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 1.5 s^(-1). Km: printed Table 3 cell 53 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 53.0 mM. kcat/Km: printed Table 3 cell 0.028 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.028 s^(-1)*mM^(-1), which is the exact same-row quotient 1.5 / 53 = 0.02830188679245283 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Tagatose': kcat = 1.5 s^-1; Km = 53 mM; printed kcat/Km = 0.028 s^-1 mM^-1.


substrate_name: D-Xylulose

column_label: Table 3 carries one phosphate-acceptor label column and three numeric columns. The metric head line prints kcat | Km | kcat/Km and the unit line under it prints s^-1 | mM | s^-1 mM^-1. The cited cell set is Table 3, row 'D-Xylulose': column 'kcat, s^-1' = 11.6; column 'Km, mM' = 524; column 'kcat/Km, s^-1 mM^-1' = 0.022. The kcat and Km cells are printed with their standard deviations (11.6 +/- 0.4 and 524 +/- 38); the kcat/Km cell is printed on its own.

normalized_value_unit_evidence: kcat: printed Table 3 cell 11.6 under the column head 'kcat, s^-1'; the column is already per second, so no unit conversion applies and the paper value is 11.6 s^(-1). Km: printed Table 3 cell 524 under the column head 'Km, mM'; the column is already in mM, so no unit conversion applies and the paper value is 524.0 mM. kcat/Km: printed Table 3 cell 0.022 under the column head 'kcat/Km, s^-1 mM^-1'; the column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.022 s^(-1)*mM^(-1), which is the exact same-row quotient 11.6 / 524 = 0.022137404580152672 rendered at the precision the table prints.

raw_value_unit_evidence: Table 3, phosphate-acceptor row 'D-Xylulose': kcat = 11.6 s^-1; Km = 524 mM; printed kcat/Km = 0.022 s^-1 mM^-1.

substrate: D-Xylulose


organism: Zea mays

substrate_name: myo-Inositol; ATP

kcat_display: Not reported

sequence_source: UniProtKB direct lookup Q5GA22

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

substrate: myo-Inositol; ATP


enzyme_display_name: propionate kinase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: GTP

sequence_source: UniProtKB direct lookup O06961

enzyme: propionate kinase

substrate: GTP


substrate_name: CTP

substrate: CTP


substrate_name: propanoate

smiles: CCC(=O)O

substrate: propanoate


substrate_name: UTP

substrate: UTP


substrate_name: Butyrate

smiles: CCCC(=O)O

substrate: Butyrate


substrate_name: ATP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ATP


proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5


enzyme_display_name: teichoic acid poly(glycerol phosphate) polymerase

organism: Bacillus subtilis

substrate_name: CDPglycerol

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13485 direct accession lookup on 2026-06-15 and applied mutation signature D645A to reconstruct the assayed variant sequence.

substrate: CDPglycerol


substrate_name: (Glycerophosphate)n; CDPglycerol

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13485 direct accession lookup on 2026-06-15 and applied mutation signature E639A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant E639A

enzyme: teichoic acid poly(glycerol phosphate) polymerase

substrate: (Glycerophosphate)n; CDPglycerol


substrate_name: CDPglycerol; (Glycerophosphate)n

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13485 direct accession lookup on 2026-06-15 and applied mutation signature D630A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant D630A

substrate: CDPglycerol; (Glycerophosphate)n


substrate_name: acetate

smiles: CC(=O)O

substrate: acetate


organism: Salmonella typhimurium

substrate_name: Propanoate; ATP

substrate: Propanoate; ATP


substrate_name: Propanoate

substrate: Propanoate


substrate_name: Acetate

substrate: Acetate


enzyme_display_name: 2'-5' oligoadenylate synthase

organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D408A/D410A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

enzyme: 2'-5' oligoadenylate synthase


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

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E639A to reconstruct the assayed variant sequence.


km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H474A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant H474A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D645A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant D645A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E604A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D630A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant E604A


substrate_name: isopentenyl diphosphate

source_db: uniprot

substrate: isopentenyl diphosphate

source: uniprot


substrate_name: myo-inositol

substrate: myo-inositol


organism: Klebsiella aerogenes

substrate_name: D-allose

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

substrate: D-allose


organism: Bacillus licheniformis

substrate_name: CDP-glycerol

substrate: CDP-glycerol


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


enzyme_display_name: sedoheptulose-bisphosphatase

organism: Cyberlindnera jadinii

substrate_name: sedoheptulose 1,7-bisphosphate

assay_conditions_summary: pH 6

enzyme: sedoheptulose-bisphosphatase

substrate: sedoheptulose 1,7-bisphosphate


organism: Lathyrus oleraceus


organism: Spinacia oleracea

substrate_name: sedoheptulose 1,7-diphosphate

proof_lines:
reduced enzyme
oxidized enzyme

substrate: sedoheptulose 1,7-diphosphate


organism: Triticum aestivum

proof_lines:
at pH 8.2, in presence of 10 mM Mg2+
with 5 mM phosphate
with 10 mM phosphate


organism: Escherichia coli (strain K12)

substrate_name: D-allose (at 25 degrees Celsius and pH 7.6)

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

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: Catalytic efficiency with D-allose as substrate is 735-fold higher than that with D-glucose.


organism: Mus musculus

proof_lines: kcat is 0.39 sec(-1) with ATP as substrate.


organism: Bacillus subtilis (strain 168)

proof_lines: kcat for CDP-glycerol is 14 min(-1) (PubMed:16141206). kcat for lipid III analog is 26 sec(-1) (PubMed:18465758).


substrate_name: Fructose 1,6-bisphosphate; H2O

sequence_source: UniProtKB:O20252 FASTA direct lookup

substrate: Fructose 1,6-bisphosphate; H2O


organism: Synechococcus elongatus

substrate_name: Sedoheptulose 1,7-bisphosphate; H2O

sequence_source: UniProtKB:Q31QY2 FASTA direct lookup

substrate: Sedoheptulose 1,7-bisphosphate; H2O


organism: Synechocystis sp.

sequence_source: UniProtKB:P73922 FASTA direct lookup

assay_conditions_summary: pH 8

proof_lines: in 50 mM Tris/HCl, pH 8.0, 15 mM MgCl2, 10 mM dithiothreitol, at 289°C


sequence_source: UniProtKB:P46285 FASTA direct lookup


organism: Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)

substrate_name: L-glytamate

substrate: L-glytamate


enzyme_display_name: 3-hydroxyisobutyryl-CoA hydrolase

organism: Rattus norvegicus

assay_conditions_summary: cofactor CoA

enzyme: 3-hydroxyisobutyryl-CoA hydrolase


enzyme_display_name: N-acetylneuraminate synthase

organism: Campylobacter jejuni

substrate_name: N-Acetyl-D-mannosamine; H2O; Phosphoenolpyruvate; N-Acetyl-D-mannosamine; H2O; Phosphoenolpyruvate; N-Acetylneuraminate; Phosphate; N-Propanoylmannosamine; Phosphoenolpyruvate; H2O; N-Propanoylmannosamine; N-Propanoylneuraminate; Phosphoenolpyruvate; H2O; N-Butanoylmannosamine; N-Butanoylmannosamine; N-Butanoylneuraminate

enzyme: N-acetylneuraminate synthase


substrate_name: N-Propanoylmannosamine

substrate: N-Propanoylmannosamine


substrate_name: N-Butanoylmannosamine

substrate: N-Butanoylmannosamine


substrate_name: N-Acetyl-D-mannosamine

substrate: N-Acetyl-D-mannosamine


substrate_name: N-Pentanoylmannosamine

substrate: N-Pentanoylmannosamine


substrate_name: Phosphoenolpyruvate

substrate: Phosphoenolpyruvate


organism: Moritella viscosa


organism: Neisseria meningitidis

substrate_name: phosphoenolpyruvate

proof_lines: 37°C, 100 mM Tris-HCl buffer, pH 7.0, 1 mM MnCl2, 50 microM to 1 mM phosphoenolpyruvate, His-tagged enzyme, purine nucleoside phosphorylase, 200 mircoM 2-amino-6-mercapto-7-methylpurine ribonucleoside

proof_lines: 4.5/1 mixture of 2S-inhibitor/2R-inhibitor, a 1.2/1 mixture of 2S-inhibitor/2R-inhibitor requires a 2.5-fold lower total inhibitor concentration, 37°C, 100 mM Tris-HCl buffer, pH 7.0, 1 mM MnCl2, 50 microM to 1 mM phosphoenolpyruvate, His-t

substrate: phosphoenolpyruvate


organism: Halomonas elongata

substrate_name: L-2,4-diaminobutanoate; 2-oxoglutarate

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature D180V to reconstruct the assayed variant sequence.

substrate: L-2,4-diaminobutanoate; 2-oxoglutarate


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature D180V/F320Y/Q325R to reconstruct the assayed variant sequence.

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


substrate_name: 2-oxoglutarate; L-2,4-diaminobutanoate

substrate: 2-oxoglutarate; L-2,4-diaminobutanoate


substrate_name: N-butanoyl-D-mannosamine

substrate: N-butanoyl-D-mannosamine


organism: Escherichia coli


substrate_name: N-acetyl-D-mannosamine

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM Tris-acetate

proof_lines: the reaction mixture contains 1 mM MgCl2 in 50 mM Tris-acetate buffer, pH 7.5, at 37°C

substrate: N-acetyl-D-mannosamine


organism: Homo sapiens

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


organism: Pseudomonas aeruginosa


proof_lines: wild-type enzyme, a deuterium isotope of the substrate is used


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_O52250_D180V and applied mutation signature D180V to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9I168 direct lookup, release 2026_02


substrate_name: L-2,4-Diaminobutanoate; 2-Oxoglutarate

substrate: L-2,4-Diaminobutanoate; 2-Oxoglutarate


organism: Arabidopsis thaliana

substrate_name: H2O; 3-Hydroxy-2-methylpropanoyl-CoA

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

sequence_source: UniProtKB Q9LKJ1 direct lookup, release 2026_02

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM Tris/HCl; cofactor CoA

proof_lines: at 30°C, in 50 mM Tris/HCl buffer, pH 7.0

substrate: H2O; 3-Hydroxy-2-methylpropanoyl-CoA


substrate_name: H2O; (S)-3-Hydroxyisobutyryl-CoA

sequence_source: UniProtKB Q6NVY1 direct lookup, release 2026_02

substrate: H2O; (S)-3-Hydroxyisobutyryl-CoA


substrate_name: 3-Hydroxypropanoyl-CoA; H2O

sequence_source: UniProtKB Q5XIE6 direct lookup, release 2026_02

substrate: 3-Hydroxypropanoyl-CoA; H2O


enzyme_display_name: pantoate kinase

organism: Thermococcus kodakaraensis

substrate_name: D-Pantoate

sequence_source: UniProtKB Q5JHF1 direct accession lookup

enzyme: pantoate kinase

substrate: D-Pantoate


substrate_name: ATP

assay_conditions_summary: pH 8; 315.15 K; cofactor ATP

substrate: ATP


organism: Thermococcus kodakarensis

substrate_name: GTP

assay_conditions_summary: pH 7.5; 315.15 K; cofactor ATP

substrate: GTP


substrate_name: CTP

substrate: CTP


substrate_name: UTP

substrate: UTP


enzyme_display_name: guanidinobutyrase

organism: Arthrobacter sp. (strain KUJ 8602)

enzyme: guanidinobutyrase


organism: Aspergillus niger


organism: Brevibacterium helvolum


organism: Candida parapsilosis

proof_lines: 4-guanidinobutyrase activity, pH and temperature not specified in the publication


organism: Gallus sp.


sequence_source: UniProtKB reviewed accession Q9I3S3/GBUA_PSEAE; EC evidence cites PubMed 12029055; sequence fetched 2026-06-15.

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


sequence_source: UniProtKB reviewed accession Q9I3S3/GBUA_PSEAE; EC evidence cites PubMed 21600989; sequence fetched 2026-06-15.


organism: Pseudomonas putida

assay_conditions_summary: pH 9

proof_lines:
at pH 10
at pH 11
at pH 9


organism: Pseudomonas sp.


organism: Tinca tinca

substrate_name: 4-Guanidinobutanoate; H2O

substrate: 4-Guanidinobutanoate; H2O


substrate_name: H2O; 4-Guanidinobutanoate

sequence_source: UniProtKB reviewed entry Q9I3S3 / GBUA_PSEAE FASTA and REST accession check

substrate: H2O; 4-Guanidinobutanoate


smiles: NC(N)=NCCCC(=O)O


enzyme_display_name: coniferyl-alcohol glucosyltransferase

substrate_name: sinapate

enzyme: coniferyl-alcohol glucosyltransferase

substrate: sinapate


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)


organism: Mus musculus


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: inositol hexakisphosphate

substrate: inositol hexakisphosphate


enzyme_display_name: molybdenum cofactor guanylyltransferase

organism: Escherichia coli (strain K12)

enzyme: molybdenum cofactor guanylyltransferase


enzyme_display_name: carbon disulfide hydrolase

organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: carbon disulfide

enzyme: carbon disulfide hydrolase

substrate: carbon disulfide


enzyme_display_name: inositol-1,4-bisphosphate 1-phosphatase

substrate_name: adenosine 3',5'-bisphosphate

enzyme: inositol-1,4-bisphosphate 1-phosphatase

substrate: adenosine 3',5'-bisphosphate


organism: Bos taurus

substrate_name: 1D-myo-inositol 1,4-bisphosphate

substrate: 1D-myo-inositol 1,4-bisphosphate


enzyme_display_name: pterin deaminase

organism: Unknown prokaryotic organism

substrate_name: isoxanthopterin

enzyme: pterin deaminase

substrate: isoxanthopterin


enzyme_display_name: 4-hydroxyphenylacetate decarboxylase

organism: Clostridium scatologenes

substrate_name: H+; 4-Hydroxyphenylacetate

enzyme: 4-hydroxyphenylacetate decarboxylase

substrate: H+; 4-Hydroxyphenylacetate


organism: Tractidigestivibacter scatoligenes

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: 5-dehydro-4-deoxyglucarate dehydratase

organism: Acinetobacter baylyi

sequence_source: UniProtKB:Q6FFQ1 direct REST lookup on 2026-06-15

enzyme: 5-dehydro-4-deoxyglucarate dehydratase


enzyme_display_name: isomaltose glucohydrolase

organism: Kribbella flavida

substrate_name: isomaltotriose

sequence_source: UniProtKB REST direct accession lookup, checked 2026-06-15

enzyme: isomaltose glucohydrolase

substrate: isomaltotriose


substrate_name: panose

proof_lines:
pH 6.0, 35°C
Raw SKiD Env: Temp=35°C, pH=6

substrate: panose


substrate_name: isomaltose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, checked 2026-06-15 and applied mutation signature W350A to reconstruct the assayed variant sequence.

substrate: isomaltose


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, checked 2026-06-15 and applied mutation signature F290Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, checked 2026-06-15 and applied mutation signature W354A to reconstruct the assayed variant sequence.


organism: Agrobacterium tumefaciens

substrate_name: 6-Formylpterin; H2O

substrate: 6-Formylpterin; H2O


organism: unidentified prokaryotic organism


organism: unknown prokaryotic organism

substrate_name: 2-Amino-4,7-dihydroxypteridine; H2O

substrate: 2-Amino-4,7-dihydroxypteridine; H2O


organism: Clostridium difficile


enzyme_display_name: S-methyl-5'-thioinosine phosphorylase

organism: Pseudomonas aeruginosa

substrate_name: Inosine

sequence_source: UniProtKB direct lookup Q9HZK1

enzyme: S-methyl-5'-thioinosine phosphorylase

substrate: Inosine


substrate_name: adenine

substrate: adenine


enzyme_display_name: AMP phosphorylase

organism: Thermococcus kodakarensis

substrate_name: CMP

sequence_source: UniProtKB direct lookup Q5JCX3

enzyme: AMP phosphorylase

substrate: CMP


substrate_name: UMP

substrate: UMP


substrate_name: phosphate

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

proof_lines:
pH 7.5, 85°C
pH 7.5, 85°C, cosubstrate: AMP
Raw SKiD Env: Temp=85°C, pH=7.5

substrate: phosphate


substrate_name: GMP

substrate: GMP


smiles: O=P(O)(O)O


organism: Halomonas elongata

sequence_source: UniProtKB direct lookup O52250

sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup O52250 and applied mutation signature D180V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup O52250 and applied mutation signature D180V/F320Y/Q325R to reconstruct the assayed variant sequence.


substrate_name: L-aspartate 4-semialdehyde

substrate: L-aspartate 4-semialdehyde


organism: Paenibacillus lautus


organism: Thermococcus kodakaraensis

substrate_name: ATP; D-Pantoate

sequence_source: UniProtKB direct lookup Q5JHF1

substrate: ATP; D-Pantoate


substrate_name: pantothenate

substrate: pantothenate


organism: Homo sapiens

substrate_name: 5-PP-InsP5; ATP

sequence_source: UniProtKB direct lookup Q6PFW1

assay_conditions_summary: pH 6.2; 310.15 K; cofactor ATP

substrate: 5-PP-InsP5; ATP


sequence_source: UniProtKB direct lookup O43314

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C

proof_lines: isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 m MKCl, at 37°C


organism: Arabidopsis thaliana

substrate_name: Sinapyl alcohol; UDPglucose

sequence_source: UniProtKB:O81498 direct REST/FASTA lookup

substrate: Sinapyl alcohol; UDPglucose


substrate_name: Coniferaldehyde

sequence_source: UniProtKB:Q9LVR1 direct REST/FASTA lookup

column_label: Table label: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2. Row: Coniferyl aldehyde. Enzyme column group: 72E2. Columns read: K m (mM) cell 0.02, k cat (s^-1) cell 1.37, k cat/K m (mM^-1 s^-1) cell 68.50. metric: kcat; raw value: 1.37; raw unit: s^-1; normalized value: 1.37 s^(-1); metric: Km; raw value: 0.02; raw unit: mM; normalized value: 0.02 mM; metric: kcat/Km; raw value: 68.50; raw unit: mM^-1 s^-1; normalized value: 68.5 s^-1 mM^-1; assay condition: Steady-state kinetic parameters of UGT72E2 (UDP-glycosyltransferase 72E2, UniProt Q9LVR1, Arabidopsis thaliana) from Table 2 of the primary article, PMID 15907484. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: 7200 columns of Table 2 row Coniferyl aldehyde: Km 0.02 mM = 0.02 mM (export unit); kcat 1.37 s^-1 = 1.37 s^(-1); kcat/Km 68.50 mM^-1 s^-1 corresponds to 68.5 s^-1 mM^-1. In the table asset the superscript minus one renders as −, so the header cell `k cat (s−1)` is the paper's k cat (s^-1) and `k cat/K m (mM−1 s−1)` is the paper's k cat/K m (mM^-1 s^-1); absent UGT720 cells render as – dashes. mM^-1 s^-1 and the export unit s^(-1)*mM^(-1) are the same unit written in either order, so no numeric conversion is applied; the paper's K m is already in mM.

raw_value_unit_evidence: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2 | column group header row of Table 2: 72E1	72E2 | metric header row: K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1)	K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1) | row: Coniferyl aldehyde	0.27	1.22	4.52	0.02	1.37	68.50 | 72E2 cells read: K m = 0.02 mM; k cat = 1.37 s^-1; k cat/K m = 68.50 mM^-1 s^-1

row_label: 72E2 | Coniferyl aldehyde

substrate: Coniferaldehyde


substrate_name: coniferyl alcohol

column_label: Table label: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2. Row: Coniferyl alcohol. Enzyme column group: 72E2. Columns read: K m (mM) cell 0.06, k cat (s^-1) cell 3.17, k cat/K m (mM^-1 s^-1) cell 52.83. metric: kcat; raw value: 3.17; raw unit: s^-1; normalized value: 3.17 s^(-1); metric: Km; raw value: 0.06; raw unit: mM; normalized value: 0.06 mM; metric: kcat/Km; raw value: 52.83; raw unit: mM^-1 s^-1; normalized value: 52.833333333333336 s^-1 mM^-1; assay condition: Steady-state kinetic parameters of UGT72E2 (UDP-glycosyltransferase 72E2, UniProt Q9LVR1, Arabidopsis thaliana) from Table 2 of the primary article, PMID 15907484. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: 7200 columns of Table 2 row Coniferyl alcohol: Km 0.06 mM = 0.06 mM (export unit); kcat 3.17 s^-1 = 3.17 s^(-1); kcat/Km 52.83 mM^-1 s^-1 corresponds to 52.833333333333336 s^-1 mM^-1. In the table asset the superscript minus one renders as −, so the header cell `k cat (s−1)` is the paper's k cat (s^-1) and `k cat/K m (mM−1 s−1)` is the paper's k cat/K m (mM^-1 s^-1); absent UGT720 cells render as – dashes. mM^-1 s^-1 and the export unit s^(-1)*mM^(-1) are the same unit written in either order, so no numeric conversion is applied; the paper's K m is already in mM. The printed Table 2 7200 kcat/Km cell 52.83 mM^-1 s^-1 is this same row's own quotient stated at two decimal places: 3.17 s^-1 / 0.06 mM = 52.833333333333336 s^-1 mM^-1, which is the export's stored value. The quotient rounds to the printed cell at the printed cell's own precision, so the printed cell and the exported value agree and the difference is printed precision only.

raw_value_unit_evidence: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2 | column group header row of Table 2: 72E1	72E2 | metric header row: K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1)	K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1) | row: Coniferyl alcohol	–	–	–	0.06	3.17	52.83 | 72E2 cells read: K m = 0.06 mM; k cat = 3.17 s^-1; k cat/K m = 52.83 mM^-1 s^-1

row_label: 72E2 | Coniferyl alcohol

substrate: coniferyl alcohol


substrate_name: Sinapoyl aldehyde

substrate: Sinapoyl aldehyde


substrate_name: UDPglucose; Coniferaldehyde

substrate: UDPglucose; Coniferaldehyde


substrate_name: sinapyl alcohol

column_label: Table label: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2. Row: Sinapyl alcohol. Enzyme column group: 72E2. Columns read: K m (mM) cell 0.15, k cat (s^-1) cell 4.52, k cat/K m (mM^-1 s^-1) cell 30.13. metric: kcat; raw value: 4.52; raw unit: s^-1; normalized value: 4.52 s^(-1); metric: Km; raw value: 0.15; raw unit: mM; normalized value: 0.15 mM; metric: kcat/Km; raw value: 30.13; raw unit: mM^-1 s^-1; normalized value: 30.133333333333333 s^-1 mM^-1; assay condition: Steady-state kinetic parameters of UGT72E2 (UDP-glycosyltransferase 72E2, UniProt Q9LVR1, Arabidopsis thaliana) from Table 2 of the primary article, PMID 15907484. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: 7200 columns of Table 2 row Sinapyl alcohol: Km 0.15 mM = 0.15 mM (export unit); kcat 4.52 s^-1 = 4.52 s^(-1); kcat/Km 30.13 mM^-1 s^-1 corresponds to 30.133333333333333 s^-1 mM^-1. In the table asset the superscript minus one renders as −, so the header cell `k cat (s−1)` is the paper's k cat (s^-1) and `k cat/K m (mM−1 s−1)` is the paper's k cat/K m (mM^-1 s^-1); absent UGT720 cells render as – dashes. mM^-1 s^-1 and the export unit s^(-1)*mM^(-1) are the same unit written in either order, so no numeric conversion is applied; the paper's K m is already in mM. The printed Table 2 7200 kcat/Km cell 30.13 mM^-1 s^-1 is this same row's own quotient stated at two decimal places: 4.52 s^-1 / 0.15 mM = 30.133333333333333 s^-1 mM^-1, which is the export's stored value. The quotient rounds to the printed cell at the printed cell's own precision, so the printed cell and the exported value agree and the difference is printed precision only.

raw_value_unit_evidence: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2 | column group header row of Table 2: 72E1	72E2 | metric header row: K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1)	K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1) | row: Sinapyl alcohol	–	–	–	0.15	4.52	30.13 | 72E2 cells read: K m = 0.15 mM; k cat = 4.52 s^-1; k cat/K m = 30.13 mM^-1 s^-1

row_label: 72E2 | Sinapyl alcohol

substrate: sinapyl alcohol


enzyme_display_name: aklavinone 7-L-rhodosaminyltransferase

organism: Streptomyces galilaeus

substrate_name: dTDP-2-deoxyfucose; Aklavinone

enzyme: aklavinone 7-L-rhodosaminyltransferase

substrate: dTDP-2-deoxyfucose; Aklavinone


substrate_name: Aklavinone; dTDP-2-deoxyfucose

sequence_source: UniProtKB:Q9L4U6 direct REST/FASTA lookup

substrate: Aklavinone; dTDP-2-deoxyfucose


substrate_name: aklavinone

substrate: aklavinone


substrate_name: epsilon-Rhodomycinone

substrate: epsilon-Rhodomycinone


substrate_name: 5'-Methylthioinosine; Phosphate

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

sequence_source: UniProtKB:Q9HZK1 direct REST/FASTA lookup

proof_lines:
pH 7.4, 25°C
Raw SKiD Env: Temp=25°C, pH=7.4

source_databases_merged: sabio_rk brenda skid

substrate: 5'-Methylthioinosine; Phosphate


organism: Escherichia coli

substrate_name: GTP

sequence_source: UniProtKB REST exact accession P32173, accessed 2026-06-15

proof_lines: pH 7.2, temperature not specified in the publication, wild-type

substrate: GTP


organism: Acidianus sp.

substrate_name: H2O; Carbon disulfide

sequence_source: UniProtKB REST exact accession G0WXL9, accessed 2026-06-15

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: carbon disulfide hydrolase(Enzyme) mutant Gly199Stop

substrate: H2O; Carbon disulfide


substrate_name: Carbon disulfide; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession G0WXL9, accessed 2026-06-15 and applied mutation signature F77A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carbon disulfide hydrolase(Enzyme) mutant Phe77Ala

substrate: Carbon disulfide; H2O


substrate_name: Carbonyl sulfide

smiles: O=C=S

substrate: Carbonyl sulfide


substrate_name: Carbon disulfide

smiles: S=C=S

substrate: Carbon disulfide


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession G0WXL9, accessed 2026-06-15 and applied mutation signature F96S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carbon disulfide hydrolase(Enzyme) mutant Phe96Ser


organism: Acidithiobacillus thiooxidans

substrate_name: carbonyl sulfide

sequence_source: UniProtKB REST exact accession S5FT07, accessed 2026-06-15

substrate: carbonyl sulfide


sequence_source: UniProtKB REST exact accession S5FU55, accessed 2026-06-15


organism: Sulfolobus solfataricus

sequence_source: UniProtKB REST exact accession Q97YU3, accessed 2026-06-15


organism: Bos taurus

substrate_name: 1D-myo-Inositol 1,4-bisphosphate; H2O

sequence_source: UniProtKB REST exact accession P21327, accessed 2026-06-15

substrate: 1D-myo-Inositol 1,4-bisphosphate; H2O


substrate_name: inositol 1,3,4-trisphosphate

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

substrate: inositol 1,3,4-trisphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession P21327, accessed 2026-06-15 and applied mutation signature D54A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D54A, pH and temperature not specified in the publication


organism: Rattus norvegicus

substrate_name: inositol 1,4-bisphosphate

sequence_source: UniProtKB REST exact accession Q9Z1N4, accessed 2026-06-15

substrate: inositol 1,4-bisphosphate


organism: Kribbella flavida

substrate_name: isomaltose

sequence_source: UniProtKB REST exact accession D2PPM8, accessed 2026-06-15

substrate: isomaltose


substrate_name: panose

substrate: panose


sequence_source: UniProt REST accession lookup for O43314


substrate_name: TorD; MobA-M1-M2

substrate: TorD; MobA-M1-M2


sequence_variant_note: Resolved canonical sequence from P32173 UniProt canonical sequence with explicit mutation reconstruction from the selected BRENDA note and applied mutation signature P79L/A81T/G82S to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, temperature not specified in the publication, mutant P79L/A81T/G82S


sequence_source: UniProt REST accession lookup for P32173


substrate_name: Mo-Molybdopterin; GTP

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: molybdenum cofactor guanylyltransferase(Enzyme) mutant fusion of N-terminal MobA domain and C-terminal MocA domain

substrate: Mo-Molybdopterin; GTP


substrate_name: apoTorA; MobA-M1

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

substrate: apoTorA; MobA-M1


substrate_name: apoTorA; MobA-M1-M2

substrate: apoTorA; MobA-M1-M2


substrate_name: TorD; MobA-M2

substrate: TorD; MobA-M2


sequence_variant_note: Resolved canonical sequence from P32173 UniProt canonical sequence with explicit mutation reconstruction from the selected BRENDA note and applied mutation signature L12T/G14A/P79L/A81T/G82S to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, temperature not specified in the publication, mutant L12T/G14A/P79L/A81T/G82S


substrate_name: PaoD; N-MobA-C-MocA

substrate: PaoD; N-MobA-C-MocA


substrate_name: Mo-Molybdopterin; CTP

proof_lines: SABIO-RK modifier species: molybdenum cofactor guanylyltransferase(Enzyme) mutant MobA with M1 and M2 motifs of MocA

proof_lines: SABIO-RK modifier species: molybdenum cofactor guanylyltransferase(Enzyme) mutant MobA with M1 motif of MocA

proof_lines: SABIO-RK modifier species: molybdenum cofactor guanylyltransferase(Enzyme) mutant MobA with M2 motif of MocA

substrate: Mo-Molybdopterin; CTP


substrate_name: N-MobA-C-MocA; GTP

substrate: N-MobA-C-MocA; GTP


substrate_name: GTP

sequence_variant_note: Resolved canonical sequence from P32173 UniProt canonical sequence with explicit mutation reconstruction from the selected BRENDA note and applied mutation signature L12T/G14A to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, temperature not specified in the publication, mutant L12T/G14A

substrate: GTP


enzyme_display_name: Pro-Pro endopeptidase

organism: Clostridioides difficile

substrate_name: Dabcyl-Lys-EVNPPPPD-EdansGlu

sequence_source: UniProtKB reviewed entry Q183R7, fetched 2026-06-15

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

enzyme: Pro-Pro endopeptidase

substrate: Dabcyl-Lys-EVNPPPPD-EdansGlu


organism: Paenibacillus alvei

substrate_name: YPSSKPLPPVPPVQPLPPVPKLETS; H2O

sequence_source: UniProtKB reviewed entry K4ZRC1, fetched 2026-06-15

substrate: YPSSKPLPPVPPVQPLPPVPKLETS; H2O


substrate_name: H2O; YPSSKPLPPVPPVQPLPPVPKLETS

sequence_source: Reconstructed from UniProtKB K4ZRC1 canonical sequence plus UniProtKB mutagenesis feature SERV112-115GGST supported by PMID 29794027

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

proof_lines: SABIO-RK modifier species: Pro-Pro endopeptidase(Enzyme) mutant PPEP-2-GGST

substrate: H2O; YPSSKPLPPVPPVQPLPPVPKLETS


substrate_name: YPSSKPLPPVPPVQPLPPVPKLETS

proof_lines: wild type enzyme PPEP-2, at pH 7.0 and 37°C

proof_lines: recombinant enzyme PPEP-2GGST, where residues 112-115 of the wild type enzyme (SERV) are replaced by residues 91-94 of Pro-Pro endopeptidase-1 (GGST), at pH 7.0 and 37°C

substrate: YPSSKPLPPVPPVQPLPPVPKLETS


enzyme_display_name: isoleucine N-monooxygenase

organism: Lotus japonicus

substrate_name: isoleucine

proof_lines: kcat is 120 min(-1) with isoleucine as substrate (PubMed:15122013). kcat is 44 min(-1) with valine as substrate (PubMed:15122013).

enzyme: isoleucine N-monooxygenase

substrate: isoleucine


proof_lines: kcat is 220 min(-1) with isoleucine as substrate (PubMed:15122013). kcat is 50 min(-1) with valine as substrate (PubMed:15122013).


organism: Manihot esculenta

substrate_name: valine

proof_lines: kcat is 2.3 min(-1) with isoleucine as substrate (PubMed:10636899). kcat is 4.3 min(-1) with valine as substrate (PubMed:10636899).

substrate: valine


enzyme_display_name: tryptophan 7-halogenase

organism: Kutzneria sp. (strain 744)

substrate_name: Unknown

proof_lines: kcat is 0.19 min(-1) with L-Trp as substrate (PubMed:18828589). kcat is 0.07 min(-1) with 6-chloro-L-tryptophan as substrate (PubMed:18828589).

enzyme: tryptophan 7-halogenase

substrate: Unknown


organism: Lentzea aerocolonigenes

substrate_name: tryptophan (with FAD)

assay_conditions_summary: cofactor FAD

substrate: tryptophan (with FAD)


enzyme_display_name: nicotinate N-methyltransferase

substrate_name: nicotinate

proof_lines: kcat is 3.52 sec(-1) with nicotinate as substrate (PubMed:28533213). kcat is 3.01 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:28533213).

enzyme: nicotinate N-methyltransferase

substrate: nicotinate


organism: Glycine max

proof_lines: kcat is 4.81 sec(-1) with nicotinate as substrate (PubMed:28533213). kcat is 4.14 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:28533213).


organism: Oryza sativa subsp. japonica

proof_lines: kcat is 2.25 sec(-1) with nicotinate as substrate (PubMed:28533213). kcat is 2.07 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:28533213).


substrate_name: aklavinone (with dTDP-4-amino-2-deoxyrhamnose as sugar donor)

proof_lines: kcat is 9.6 sec(-1) for glycosyltransferase activity with aklavinone as sugar acceptor and TDP-L-rhodosamine as sugar donor. kcat is 0.05 sec(-1) for glycosyltransferase activity without AknT and with aklavinone as sugar acceptor and TDP-L-


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: inosine (at 25 degrees Celsius and pH 7.5)

proof_lines: kcat is 1.7 sec(-1) with inosine as substrate (PubMed:14982926, PubMed:24416224). kcat is 2.63 sec(-1) with inosine as substrate (PubMed:29440412). kcat is 1.1 sec(-1) with guanosine as substrate (PubMed:19575810). kcat is 1.5 sec(-1) with

proof_lines: kcat is 0.34 sec(-1) with inosine as substrate (PubMed:11707439). kcat is 0.14 sec(-1) with guanosine as substrate (PubMed:11707439). kcat is 0.64 sec(-1) with 2'-deoxyinosine as substrate (PubMed:11707439). kcat is 0.2 sec(-1) with 2'-deox


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

proof_lines: kcat is 4.8 sec(-1) with S-methyl-5'-thioinosine as substrate (PubMed:21197954). kcat is 0.57 sec(-1) with inosine as substrate (PubMed:21197954). kcat is 0.0549 sec(-1) with adenosine as substrate (PubMed:21197954).


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: CMP (in the presence of AMP, at 85 degrees Celsius)

proof_lines: kcat is 39.1 sec(-1), 15.0 sec(-1), 10.5 sec(-1) and 2.7 sec(-1), with CMP, AMP, UMP, and GMP as substrate, respectively (at 85 degrees Celsius). KM for AMP was not determined because the reaction does not follow Michaelis-Menten kinetics.


enzyme_display_name: N-acetylneuraminate synthase

organism: Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)

substrate_name: ManNAc

enzyme: N-acetylneuraminate synthase

substrate: ManNAc


organism: Homo sapiens

proof_lines: The catalytic efficiency is 80 folds higher for 5-PP-InsP5 (InsP7) compared to InsP6.


enzyme_display_name: 3-sulfinopropanoyl-CoA desulfinase

organism: Advenella mimigardefordensis (strain DSM 17166 / LMG 22922 / DPN7)

enzyme: 3-sulfinopropanoyl-CoA desulfinase


organism: Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)


organism: Paraburkholderia xenovorans (strain LB400)


organism: Variovorax paradoxus


organism: Acidianus sp. (strain A1-3)

substrate_name: carbon disulfide

proof_lines: kcat is 952 sec(-1) with carbon disulfide as substrate. kcat is 1800 sec(-1) with the intermediate carbonyl sulfide as substrate.

substrate: carbon disulfide


organism: Acidithiobacillus thiooxidans

proof_lines: kcat is 780 sec(-1) with carbon disulfide as substrate. kcat is 814 sec(-1) with the intermediate carbonyl sulfide as substrate.


proof_lines: kcat is 3000 sec(-1) with carbon disulfide as substrate. kcat is 22400 sec(-1) with the intermediate carbonyl sulfide as substrate.


enzyme_display_name: 3-hydroxyisobutyryl-CoA hydrolase

organism: Arabidopsis thaliana

proof_lines: Can also use 3-hydroxy-3-phenoylpropionoyl-CoA and p-coumaroyl-CoA as substrates, but not benzoyl-CoA.

enzyme: 3-hydroxyisobutyryl-CoA hydrolase


substrate_name: 1D-myo-inositol 1,4-bisphosphate

proof_lines: KM for adenosine 3',5'-bisphosphate is between 2 and 10 uM.

substrate: 1D-myo-inositol 1,4-bisphosphate


proof_lines: KM for adenosine 3',5'-bisphosphate is below 1 uM.


substrate_name: Nicotinate; S-Adenosyl-L-methionine

sequence_source: UniProtKB:I1M2U5; sequence_version=1

substrate: Nicotinate; S-Adenosyl-L-methionine


organism: Oryza sativa

substrate_name: S-Adenosyl-L-methionine; Nicotinate

sequence_source: UniProtKB:Q6K9X3; sequence_version=1

substrate: S-Adenosyl-L-methionine; Nicotinate


organism: Advenella mimigardefordensis

sequence_source: UniProtKB:K4L7X3; sequence_version=1

sequence_variant_note: Resolved canonical sequence from UniProtKB:K4L7X3; sequence_version=1 and applied mutation signature Q246E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

proof_lines: recombinant His6-tagged mutant Q246E, pH 7.4, 30°C


proof_lines: recombinant His6-tagged wild-type enzyme, pH 7.4, 30°C


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Clostridioides difficile

sequence_source: UniProtKB:Q183R7; sequence_version=1


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q183R7; sequence_version=1 and applied mutation signature E184A to reconstruct the assayed variant sequence.


organism: Mus musculus

substrate_name: adenosine 3',5'-bisphosphate (PAP)

proof_lines: The different methodology used for determination of the hydrolysis of inositol-1,4-bisphosphate might account for the discrepancy obtained with protein homologs from human and rat, which show much more efficiency with this substrate.

substrate: adenosine 3',5'-bisphosphate (PAP)


organism: Rattus norvegicus

substrate_name: 3'-phosphoadenylyl sulfate

proof_lines: KM for adenosine 3',5'-bisphosphate is below 2 uM.

substrate: 3'-phosphoadenylyl sulfate


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

proof_lines: KM for adenosine 3',5'-bisphosphate is below 10 uM.


organism: Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399)

substrate_name: panose

proof_lines: kcat is 11.4 sec(-1) for isomaltose as substrate. kcat is 1.17 sec(-1) for panose as substrate. kcat is 1.07 sec(-1) for isomaltotriose as substrate.

substrate: panose


organism: Clostridioides difficile (strain 630)

proof_lines: kcat is 19 sec(-1) with synthetic FRET peptide DabcylLys-EVNPPPPD-EdansGlu as substrate.


organism: Paenibacillus alvei (strain ATCC 6344 / DSM 29 / NBRC 3343 / NCIMB 9371 / NCTC 6352)

substrate_name: a FRET peptide containing PLPPVP

proof_lines: kcat is 8 sec(-1) with a FRET peptide containing PLPPVP as substrate. kcat is 3 sec(-1) with a FRET peptide containing VLPPVP as substrate.

substrate: a FRET peptide containing PLPPVP


enzyme_display_name: guanidinobutyrase

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

enzyme: guanidinobutyrase


organism: Rhizobium rhizogenes (strain K84 / ATCC BAA-868)

substrate_name: formylpterin

proof_lines: kcat is 64 sec(-1) with formylpterin as substrate. kcat is 110 sec(-1) with pterin-6-carboxylate as substrate. kcat is 48 sec(-1) with pterin-7-carboxylate as substrate. kcat is 131 sec(-1) with pterin as substrate. kcat is 28 sec(-1) with

substrate: formylpterin


proof_lines: kcat is 110 sec(-1) for the decarboxylation of 4-hydroxyphenylacetate. kcat is 65 sec(-1) for the decarboxylation of 3,4-hydroxyphenylacetate.


organism: Clostridium scatologenes

proof_lines: kcat is 135 sec(-1) for the decarboxylation of 4-hydroxyphenylacetate. kcat is 67 sec(-1) for the decarboxylation of 3,4-hydroxyphenylacetate.


organism: Lotus japonicus

substrate_name: NADPH; O2; L-Isoleucine; H+

sequence_source: UniProtKB reviewed accession Q6J541

assay_conditions_summary: pH 7.5; 301.15 K; cofactor NADPH

substrate: NADPH; O2; L-Isoleucine; H+


substrate_name: L-Isoleucine

substrate: L-Isoleucine


substrate_name: O2; H+; NADPH; L-Isoleucine

sequence_source: UniProtKB reviewed accession Q6J540

substrate: O2; H+; NADPH; L-Isoleucine


substrate_name: L-Valine

substrate: L-Valine


organism: Kutzneria sp. 744

sequence_source: UniProtKB reviewed accession A8CF75

assay_conditions_summary: pH 7

proof_lines: about, pH 7.0, temperature not specified in the publication, recombinant His-tagged enzyme


organism: Lentzea aerocolonigenes

substrate_name: L-tryptophan

sequence_source: UniProtKB reviewed accession Q8KHZ8

proof_lines:
pH 7.5
Raw SKiD Env: Temp=-----, pH=7.5

substrate: L-tryptophan


organism: Pseudomonas fluorescens

substrate_name: O2; Cl-; FADH2; L-Tryptophan; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature S347A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant S347A

substrate: O2; Cl-; FADH2; L-Tryptophan; H+


substrate_name: FADH2; O2; Cl-; H+; L-Tryptophan

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature W272A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant W272A

substrate: FADH2; O2; Cl-; H+; L-Tryptophan


substrate_name: L-Tryptophan; H+; O2; Cl-; FADH2

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature W272F/W274F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant W272F_W274F

substrate: L-Tryptophan; H+; O2; Cl-; FADH2


substrate_name: FADH2; H+; Cl-; O2; L-Tryptophan

sequence_source: UniProtKB reviewed accession P95480

substrate: FADH2; H+; Cl-; O2; L-Tryptophan


substrate_name: L-Tryptophan; FADH2; Cl-; O2; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature W274F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant W274F

substrate: L-Tryptophan; FADH2; Cl-; O2; H+


substrate_name: FADH2; L-Tryptophan; H+; O2; Cl-

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature W272F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant W272F

substrate: FADH2; L-Tryptophan; H+; O2; Cl-


enzyme_display_name: carminomycin 4-O-methyltransferase

organism: Streptomyces peucetius

sequence_source: UniProtKB reviewed accession Q06528

enzyme: carminomycin 4-O-methyltransferase


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


proof_lines:
pH 8.0, 37°C
Raw SKiD Env: Temp=37°C, pH=8


substrate_name: tryptophan

sequence_source: UniProtKB Q8KHZ8 official REST lookup on 2026-06-15

proof_lines: ranges from 0.02 s-1 to 0.05 s-1 for different preparations, 25°C

substrate: tryptophan


sequence_variant_note: Resolved canonical sequence from UniProtKB P95480 official REST lookup on 2026-06-15 plus direct 1-indexed H101A substitution reconstruction and applied mutation signature H101A to reconstruct the assayed variant sequence.

proof_lines: His-tagged recombinant mutant enzyme H101A, at 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P95480 official REST lookup on 2026-06-15 plus direct 1-indexed W455A substitution reconstruction and applied mutation signature W455A to reconstruct the assayed variant sequence.

proof_lines: His-tagged recombinant mutant enzyme W455A, at 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P95480 official REST lookup on 2026-06-15 plus direct 1-indexed F103A substitution reconstruction and applied mutation signature F103A to reconstruct the assayed variant sequence.

proof_lines: His-tagged recombinant mutant enzyme F103A, at 30°C, pH not specified in the publication


sequence_source: UniProtKB P95480 official REST lookup on 2026-06-15

proof_lines: His-tagged recombinant wild type enzyme, at 30°C, pH not specified in the publication


proof_lines: pH 7.2, 30°C, in vitro two-component system of enzyme and flavin reductase to provide FADH2


sequence_source: UniProtKB Q06528 official REST lookup on 2026-06-15


organism: Lathyrus oleraceus

substrate_name: nicotinate

substrate: nicotinate


organism: Lemna aequinoctialis


enzyme_display_name: coniferyl-alcohol glucosyltransferase

organism: Forsythia ovata

substrate_name: UDPglucose

enzyme: coniferyl-alcohol glucosyltransferase

substrate: UDPglucose


substrate_name: tryptophan (with FAD at pH 7.2 and 30 degrees Celsius)

assay_conditions_summary: pH 7.2; cofactor FAD


organism: Picea abies

substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


organism: Pinus strobus

substrate_name: sinapyl alcohol

substrate: sinapyl alcohol


organism: Rosa sp.


organism: Streptomyces galilaeus

substrate_name: dTDP-beta-L-rhodosamine

sequence_source: UniProtKB REST reviewed accession Q9L4U6

proof_lines: with dTDP-L-2-deoxyfucose as cosubstrate, in 75 mM Tris (pH 7.5), 10 mM MgCl2, at 25°C

proof_lines: with aklavinone as cosubstrate, in 75 mM Tris (pH 7.5), 10 mM MgCl2, at 25°C

substrate: dTDP-beta-L-rhodosamine


organism: Acinetobacter baumannii

substrate_name: L-2,4-diaminobutyric acid

substrate: L-2,4-diaminobutyric acid


organism: Rattus norvegicus

substrate_name: diphosphoinositol pentakisphosphate

assay_conditions_summary: pH 6.8; 310.15 K; cofactor ATP

substrate: diphosphoinositol pentakisphosphate


organism: Advenella mimigardefordensis

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: pH 7.4, 37°C, with a Vmax of 4.19 micromol/min*mg


organism: Cupriavidus necator

proof_lines: pH 7.4, 37°C, with a Vmax of 6.1 micromol/min*mg


organism: Paraburkholderia xenovorans

proof_lines: pH 7.4, 37°C, with a Vmax of 1.58 micromol/min*mg


organism: Variovorax paradoxus

proof_lines: pH 7.4, 37°C, with a Vmax of 3.47 micromol/min*mg


enzyme_display_name: carbon disulfide hydrolase

organism: Acidianus sp.

substrate_name: carbon disulfide

proof_lines: pH and temperature not specified in the publication, mutant enzyme G199stop

enzyme: carbon disulfide hydrolase

substrate: carbon disulfide


sequence_source: UniProtKB REST reviewed accession G0WXL9

proof_lines: pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:G0WXL9 plus row-specific F77A reconstruction and applied mutation signature F77A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme F77A


sequence_variant_note: Resolved canonical sequence from UniProtKB:G0WXL9 plus row-specific F96S reconstruction and applied mutation signature F96S to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme F96S


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


enzyme_display_name: inositol-1,4-bisphosphate 1-phosphatase

organism: Bos taurus

substrate_name: inositol 1,4-bisphosphate

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

enzyme: inositol-1,4-bisphosphate 1-phosphatase

substrate: inositol 1,4-bisphosphate


substrate_name: H2O; 1D-myo-Inositol 1,4-bisphosphate

substrate: H2O; 1D-myo-Inositol 1,4-bisphosphate


enzyme_display_name: pterin deaminase

organism: Priestia megaterium

enzyme: pterin deaminase


organism: unknown prokaryotic organism

substrate_name: 2-Amino-4,7-dihydroxypteridine; H2O

substrate: 2-Amino-4,7-dihydroxypteridine; H2O


enzyme_display_name: 4-hydroxyphenylacetate decarboxylase

organism: Clostridioides difficile

proof_lines: in 100 mM Tris-HCl, pH 7.5, 40 mM NaCl, 5 mM MgCl2, 5 mM (NH4)2SO4, 5 mM cysteine, 25 mM substrate, and 5 mM dithiothreitol, at 30°C

enzyme: 4-hydroxyphenylacetate decarboxylase


organism: Clostridium scatologenes


organism: Streptomyces sp. (strain C5)

substrate_name: carminomycin

sequence_source: source_record; UniProt Q55216 direct sequence check

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

substrate: carminomycin


organism: Streptomyces peucetius


organism: Arabidopsis thaliana


organism: Bacillus subtilis


column_label: Table 1: Apparent Km and kcat of lipid I analogs at 600 uM UDP-ManNAc (Biochemistry 2006, 45(36):10895-10904, NIH public-access author manuscript, PDF page 21); printed column heads Lipid I analog | Km (uM) | kcat (min-1) | kcat/Km (min-1 uM-1). Table 1, lipid I analog row 5; column Km (uM) = 35; column kcat (min-1) = 517; column kcat/Km (min-1 uM-1) = 14.77. captured primary segment: Table 1 Apparent Km and kcat of lipid I analogs at 600 uM UDP-ManNAc | Bacillus subtilis TagA | lipid I analog 5 | Km 35 uM | kcat 517 min^-1 | kcat/Km 14.77 min^-1 uM^-1 | assay 50 mM Tris, pH 7.8, and 250 mM NaCl, room temperature

raw_value_unit_evidence: Table 1, lipid I analog row 5: Km cell = 35 uM; kcat cell = 517 min^-1; printed kcat/Km cell = 14.77 min^-1 uM^-1.

row_label: Table 1, lipid I analog row 5


column_label: Table 1: Apparent Km and kcat of lipid I analogs at 600 uM UDP-ManNAc (Biochemistry 2006, 45(36):10895-10904, NIH public-access author manuscript, PDF page 21); printed column heads Lipid I analog | Km (uM) | kcat (min-1) | kcat/Km (min-1 uM-1). Table 1, lipid I analog row 2; column Km (uM) = 258; column kcat (min-1) = 52; column kcat/Km (min-1 uM-1) = 0.20. captured primary segment: Table 1 Apparent Km and kcat of lipid I analogs at 600 uM UDP-ManNAc | Bacillus subtilis TagA | lipid I analog 2 | Km 258 uM | kcat 52 min^-1 | kcat/Km 0.20 min^-1 uM^-1 | assay 50 mM Tris, pH 7.8, and 250 mM NaCl, room temperature

raw_value_unit_evidence: Table 1, lipid I analog row 2: Km cell = 258 uM; kcat cell = 52 min^-1; printed kcat/Km cell = 0.20 min^-1 uM^-1.

row_label: Table 1, lipid I analog row 2


column_label: Table 1: Apparent Km and kcat of lipid I analogs at 600 uM UDP-ManNAc (Biochemistry 2006, 45(36):10895-10904, NIH public-access author manuscript, PDF page 21); printed column heads Lipid I analog | Km (uM) | kcat (min-1) | kcat/Km (min-1 uM-1). Table 1, lipid I analog row 1; column Km (uM) = 193; column kcat (min-1) = 551; column kcat/Km (min-1 uM-1) = 2.85. captured primary segment: Table 1 Apparent Km and kcat of lipid I analogs at 600 uM UDP-ManNAc | Bacillus subtilis TagA | lipid I analog 1 | Km 193 uM | kcat 551 min^-1 | kcat/Km 2.85 min^-1 uM^-1 | assay 50 mM Tris, pH 7.8, and 250 mM NaCl, room temperature

raw_value_unit_evidence: Table 1, lipid I analog row 1: Km cell = 193 uM; kcat cell = 551 min^-1; printed kcat/Km cell = 2.85 min^-1 uM^-1.

row_label: Table 1, lipid I analog row 1


enzyme_display_name: benzoyl-CoA reductase

organism: Pseudomonas sp.

substrate_name: benzoyl-CoA

enzyme: benzoyl-CoA reductase

substrate: benzoyl-CoA


organism: Thauera aromatica

assay_conditions_summary: cofactor ATP


sequence_source: UniProtKB reviewed accession P27620 FASTA and metadata; TAGA_BACSU, Bacillus subtilis strain 168 TagA, EC 2.4.1.187, with PMID 16953575 evidence.

proof_lines:
apparent Kcat at 600 microM UDP-ManNAc
apparent Km at 600 microM UDP-ManNAc


organism: Escherichia coli

substrate_name: 7,8-dihydroneopterin 3'-triphosphate

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

substrate: 7,8-dihydroneopterin 3'-triphosphate


organism: Bacillus subtilis (strain 168)

substrate_name: UDP-N-acetyl-alpha-D-mannosamine

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

substrate: UDP-N-acetyl-alpha-D-mannosamine


enzyme_display_name: sucrose-phosphate phosphatase

organism: Unknown

substrate_name: sucrose 6-phosphate

enzyme: sucrose-phosphate phosphatase

substrate: sucrose 6-phosphate


organism: Daucus carota

substrate_name: sucrose phosphate

substrate: sucrose phosphate


organism: Lathyrus oleraceus


organism: Methylobacillus flagellatus


organism: Oryza sativa


organism: Spinacia oleracea

substrate_name: Sucrose 6-phosphate; H2O

substrate: Sucrose 6-phosphate; H2O


organism: Synechocystis sp.

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: Benzoyl-CoA; H2O; ATP; Reduced acceptor

substrate: Benzoyl-CoA; H2O; ATP; Reduced acceptor


substrate_name: ATP

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: Benzoyl-CoA

assay_conditions_summary: pH 7.3; 310.15 K; cofactor CoA

substrate: Benzoyl-CoA


substrate_name: Benzoyl-CoA; Reduced acceptor; ATP

substrate: Benzoyl-CoA; Reduced acceptor; ATP


sequence_source: UniProtKB:Q9CA40 direct accession lookup on 2026-06-15

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


sequence_source: UniProtKB:P0AFC0 direct accession lookup on 2026-06-15

proof_lines:
pH 8.5, 37°C
Raw SKiD Env: Temp=37°C, pH=8.5
Raw SKiD Env: Temp=42°C, pH=8.5


substrate_name: dATP

substrate: dATP


organism: Lactococcus lactis

sequence_source: UniProtKB:D8KIT5 direct accession lookup on 2026-06-15


enzyme_display_name: acetate CoA-transferase

substrate_name: Acetoacetyl-CoA; Acetate

assay_conditions_summary: cofactor CoA

enzyme: acetate CoA-transferase

substrate: Acetoacetyl-CoA; Acetate


enzyme_display_name: hydroquinone glucosyltransferase

enzyme: hydroquinone glucosyltransferase


organism: Escherichia coli (strain K12)

substrate_name: acetyl-CoA (for acetoacetyl-CoA formation)


substrate: acetyl-CoA (for acetoacetyl-CoA formation)


organism: Oryza sativa subsp. japonica

substrate_name: sucrose 6(F)-phosphate

substrate: sucrose 6(F)-phosphate


organism: Zea mays


organism: Arabidopsis thaliana

substrate_name: NADH (in the presence of 5 mM of manganese)

assay_conditions_summary: cofactor NADH


substrate_name: dihydroneopterin triphosphate

substrate: dihydroneopterin triphosphate


substrate_name: 3,4-Dichlorophenol; UDPglucose

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: hydroquinone glucosyltransferase(Enzyme) mutant Y315F N-terminal streptactin-tagged

substrate: 3,4-Dichlorophenol; UDPglucose


proof_lines: SABIO-RK modifier species: hydroquinone glucosyltransferase(Enzyme) mutant H19Q N-terminal streptactin-tagged


proof_lines: SABIO-RK modifier species: hydroquinone glucosyltransferase(Enzyme) mutant N312D-Y315F N-terminal streptactin-tagged


organism: Brassica napus

proof_lines: SABIO-RK modifier species: hydroquinone glucosyltransferase(Enzyme) mutant F317Y N-terminal streptactin-tagged


substrate_name: UDPglucose; 3,4-Dichlorophenol

proof_lines: SABIO-RK modifier species: hydroquinone glucosyltransferase(Enzyme) mutant D314N-F317Y N-terminal streptactin-tagged

substrate: UDPglucose; 3,4-Dichlorophenol


organism: Rauvolfia serpentina

substrate_name: hydroquinone

substrate: hydroquinone


organism: Acetobacter aceti

substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot:B3EY95:direct_reconstructed_variant and applied mutation signature N347A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines: mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C

substrate: acetyl-CoA


substrate_name: acetate

column_label: AarC acetate saturation, decoded plain-numeral measurement-bound row: kcat = 290 s^-1; Km = 110 mM; kcat/Km = 2.6 x 10^3 M^-1 s^-1; Ki = 1600 mM. The article prints these four constants for the one acetate-saturation measurement in running prose, and prints no kcat column and no Km column for any enzyme form anywhere in the article body.

normalized_value_unit_evidence: kcat: printed value 290 s^-1; the printed unit is already s^-1, so no unit conversion applies and the exported value is 290.0 s^(-1). Km: printed value 110 mM; the printed unit is already mM, so no unit conversion applies and the exported value is 110.0 mM. kcat/Km: printed value 2.6 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.6 x 10^3 x 0.001 = 2.6 s^-1 mM^-1; the export row holds no kcat_over_km value, so this converted figure is kept as typed provenance only and no ratio metric is written.

raw_value_unit_evidence: AarC acetate saturation, decoded plain-numeral measurement-bound row: kcat = 290 s^-1; Km = 110 mM; printed kcat/Km = 2.6 x 10^3 M^-1 s^-1; printed Ki = 1600 mM.

row_label: AarC acetate saturation, decoded plain-numeral measurement-bound row, substrate acetate, enzyme form wild-type AarC

table_label: Results, 'Protein Production, Isolation, and Biophysical Characterization', journal page 8424: the AarC acetate-saturation steady-state constants stated in running prose

substrate: acetate


substrate_name: succinate

proof_lines: mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C

substrate: succinate


substrate_name: succinyl-CoA

proof_lines: mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C

substrate: succinyl-CoA


proof_lines: mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C


organism: Anabaena sp.

substrate_name: sucrose 6-phosphate

substrate: sucrose 6-phosphate


sequence_source: UniProtKB reviewed direct accession lookup Q9SJ66


sequence_source: UniProtKB reviewed direct accession lookup Q93XN8


substrate_name: Sucrose 6-phosphate; H2O

sequence_source: UniProtKB reviewed direct accession lookup Q6YXW6

substrate: Sucrose 6-phosphate; H2O


organism: Saccharum officinarum

sequence_source: UniProtKB TrEMBL direct accession lookup Q4FCW1


enzyme_display_name: D(-)-tartrate dehydratase

organism: Bradyrhizobium diazoefficiens

substrate_name: D-Tartrate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q89FH0 canonical FASTA plus selected mutation_signature H322Q; residue check performed 2026-06-15 and applied mutation signature H322Q to reconstruct the assayed variant sequence.

enzyme: D(-)-tartrate dehydratase

substrate: D-Tartrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q89FH0 canonical FASTA plus selected mutation_signature K184R; residue check performed 2026-06-15 and applied mutation signature K184R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q89FH0 and applied mutation signature H322N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

column_label: Table 2 (Kinetic Parameters of TarD) carries one enzyme-label column and exactly three kinetic columns, printed once as the column heads kcat (s-1), KM (mM) and kcat/KM (M-1 s-1). The cited cell set is Table 2, enzyme row H322N: kcat (s-1) = (6.9 +/- 0.4) x 10^-3; KM (mM) = 0.048 +/- 0.019; kcat/KM (M-1 s-1) = 1.4 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 6.9 x 10^-3 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 0.0069 s^(-1). Km: printed Table 2 cell 0.048 under the column head KM (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.048 mM. kcat/Km: printed Table 2 cell 1.4 x 10^2 under the column head kcat/KM (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 140.0 / 1000 = 0.14 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 (Kinetic Parameters of TarD), enzyme row H322N: kcat printed as (6.9 +/- 0.4) x 10^-3 under the column head kcat (s-1); KM printed as 0.048 +/- 0.019 under the column head KM (mM); kcat/KM printed as 1.4 x 10^2 under the column head kcat/KM (M-1 s-1).

row_label: Table 2, enzyme row H322N

table_label: Table 2: Kinetic Parameters of TarD (Biochemistry 2006, 45, 14598-14608)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q89FH0 and applied mutation signature H322A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters of TarD) carries one enzyme-label column and exactly three kinetic columns, printed once as the column heads kcat (s-1), KM (mM) and kcat/KM (M-1 s-1). The cited cell set is Table 2, enzyme row H322A: kcat (s-1) = (2.7 +/- 0.2) x 10^-3; KM (mM) = 6.2 +/- 2.5; kcat/KM (M-1 s-1) = 4.4 x 10^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.7 x 10^-3 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 0.0027 s^(-1). Km: printed Table 2 cell 6.2 under the column head KM (mM); the column is already in mM, so no unit conversion applies and the paper value is 6.2 mM. kcat/Km: printed Table 2 cell 4.4 x 10^-1 under the column head kcat/KM (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.44 / 1000 = 0.00044 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 (Kinetic Parameters of TarD), enzyme row H322A: kcat printed as (2.7 +/- 0.2) x 10^-3 under the column head kcat (s-1); KM printed as 6.2 +/- 2.5 under the column head KM (mM); kcat/KM printed as 4.4 x 10^-1 under the column head kcat/KM (M-1 s-1).

row_label: Table 2, enzyme row H322A


substrate_name: D-tartrate

substrate: D-tartrate


organism: Bradyrhizobium japonicum

substrate_name: (S,S)-Tartrate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q89FH0 and applied mutation signature H322Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters of TarD) carries one enzyme-label column and exactly three kinetic columns, printed once as the column heads kcat (s-1), KM (mM) and kcat/KM (M-1 s-1). The cited cell set is Table 2, enzyme row H322Q: kcat (s-1) = (1.9 +/- 0.4) x 10^-3; KM (mM) = 7.7 +/- 5.5; kcat/KM (M-1 s-1) = 2.5 x 10^-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.9 x 10^-3 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 0.0019 s^(-1). Km: printed Table 2 cell 7.7 under the column head KM (mM); the column is already in mM, so no unit conversion applies and the paper value is 7.7 mM. kcat/Km: printed Table 2 cell 2.5 x 10^-1 under the column head kcat/KM (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.25 / 1000 = 0.00025 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 (Kinetic Parameters of TarD), enzyme row H322Q: kcat printed as (1.9 +/- 0.4) x 10^-3 under the column head kcat (s-1); KM printed as 7.7 +/- 5.5 under the column head KM (mM); kcat/KM printed as 2.5 x 10^-1 under the column head kcat/KM (M-1 s-1).

row_label: Table 2, enzyme row H322Q

substrate: (S,S)-Tartrate


sequence_source: RCSB 2DW7 / UniProt Q89FH0

column_label: Table 2 (Kinetic Parameters of TarD) carries one enzyme-label column and exactly three kinetic columns, printed once as the column heads kcat (s-1), KM (mM) and kcat/KM (M-1 s-1). The cited cell set is Table 2, enzyme row wild type: kcat (s-1) = 7.3 +/- 0.1; KM (mM) = 0.086 +/- 0.007; kcat/KM (M-1 s-1) = 8.5 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 7.3 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 7.3 s^(-1). Km: printed Table 2 cell 0.086 under the column head KM (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.086 mM. kcat/Km: printed Table 2 cell 8.5 x 10^4 under the column head kcat/KM (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 85000.0 / 1000 = 85.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 (Kinetic Parameters of TarD), enzyme row wild type: kcat printed as 7.3 +/- 0.1 under the column head kcat (s-1); KM printed as 0.086 +/- 0.007 under the column head KM (mM); kcat/KM printed as 8.5 x 10^4 under the column head kcat/KM (M-1 s-1).

row_label: Table 2, enzyme row wild type


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q89FH0 and applied mutation signature K184R to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters of TarD) carries one enzyme-label column and exactly three kinetic columns, printed once as the column heads kcat (s-1), KM (mM) and kcat/KM (M-1 s-1). The cited cell set is Table 2, enzyme row K184R: kcat (s-1) = (5.8 +/- 0.5) x 10^-3; KM (mM) = 0.035 +/- 0.016; kcat/KM (M-1 s-1) = 1.7 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.8 x 10^-3 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 0.0058 s^(-1). Km: printed Table 2 cell 0.035 under the column head KM (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.035 mM. kcat/Km: printed Table 2 cell 1.7 x 10^2 under the column head kcat/KM (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 170.0 / 1000 = 0.17 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 (Kinetic Parameters of TarD), enzyme row K184R: kcat printed as (5.8 +/- 0.5) x 10^-3 under the column head kcat (s-1); KM printed as 0.035 +/- 0.016 under the column head KM (mM); kcat/KM printed as 1.7 x 10^2 under the column head kcat/KM (M-1 s-1).

row_label: Table 2, enzyme row K184R


organism: Cereibacter sphaeroides


organism: Pseudomonas sp.

proof_lines:
strain Ch
strain G2


sequence_variant_note: Resolved canonical sequence from UniProtKB Q89FH0 direct lookup plus selected mutation_signature H322N reconstruction and applied mutation signature H322N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q89FH0 direct lookup plus selected mutation_signature H322A reconstruction and applied mutation signature H322A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q89FH0 direct lookup

normalized_value_unit_evidence: kcat: printed Table 2 cell 7.3 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 7.3 s^(-1). Km: printed Table 2 cell 0.086 under the column head KM (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.086 mM. kcat/Km: printed Table 2 cell 8.5 x 10^4 under the column head kcat/KM (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 85000.0 / 1000 = 85.0 s^-1 mM^-1, which is the printed efficiency at the two significant figures the paper prints; the catalog holds the full-precision quotient of the same two printed component cells, 7.3 / 0.086 = 84.88372093023256 s^(-1)*mM^(-1).


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


organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)

sequence_source: source_record; direct UniProt Q89FH0 check


substrate_name: Vanillin

sequence_source: UniProtKB/Swiss-Prot Q9AR73 (HQGT_RAUSE), linked to PMID 11937332 and DOI 10.1016/S0968-0896(02)00029-9

substrate: Vanillin


enzyme_display_name: 5-dehydro-4-deoxyglucarate dehydratase

organism: Acinetobacter baylyi

sequence_source: UniProtKB REST direct lookup on 2026-06-15 for accession Q6FFQ1

enzyme: 5-dehydro-4-deoxyglucarate dehydratase


organism: Agrobacterium fabrum

sequence_source: UniProtKB REST direct lookup on 2026-06-15 for accession Q8UB77

proof_lines:
pH 7.5, 22°C
Raw SKiD Env: Temp=22°C, pH=7.5


organism: Comamonas testosteroni


assay_conditions_summary: pH 7; 310.15 K; buffer 25 mM potassium phosphate

proof_lines: in 25 mM potassium phosphate buffer, at pH 7.0 and 37°C


organism: Polaromonas naphthalenivorans

sequence_source: UniProtKB REST direct lookup on 2026-06-15 for accession A1VMN2


organism: Polaromonas naphthalenivorans CJ2