sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P45425 and applied mutation signature L84P to reconstruct the assayed variant sequence.

column_label: Table 1, L84P NanK column, N-acetyl-D-mannosamine block; kcat cell = 18 s-1; Km cell = 2.3 x 10^-4 M; kcat/Km cell = 7.8 x 10^4 M^-1 s^-1. captured primary segment: L84P NanK | N-acetyl-D-mannosamine | Table 1, L84P NanK column, N-acetyl-D-mannosamine block | 0.2 M Tris, pH 7.6 at 25 C | Table 1, L84P NanK column, N-acetyl-D-mannosamine block, kcat = 18 s-1 | Table 1, L84P NanK column, N-acetyl-D-mannosamine block, Km = 2.3 x 10^-4 M | Table 1, L84P NanK column, N-acetyl-D-mannosamine block, kcat/Km = 7.8 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 18 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 18.0 s^(-1). Km: printed cell 2.3 x 10^-4 M; 1 M is 1000 mM, so 2.3 x 10^-4 x 1000 = 0.23 mM. kcat/Km: printed cell 7.8 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.8 x 10^4 / 1000 = 78.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 18.0 / 0.23 = 78.26086956521739 s^-1 mM^-1, against the printed efficiency cell 78.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, L84P NanK column, N-acetyl-D-mannosamine block: kcat = 18 s-1; Km = 2.3 x 10^-4 M; kcat/Km = 7.8 x 10^4 M^-1 s^-1.

table_label: Table 1: Kinetic Parameters for Phosphorylation of Native and Ambiguous Substrates by Wild-Type NanK 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_display_name: N-acylmannosamine kinase

organism: Escherichia coli

substrate_name: D-Glucose

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

mutation_type: substitution

column_label: Table 1, L84P NanK column, D-glucose block; kcat cell = 84 s-1; Km cell = 6.4 x 10^-3 M; kcat/Km cell = 1.3 x 10^4 M^-1 s^-1. captured primary segment: L84P NanK | D-glucose | Table 1, L84P NanK column, D-glucose block | 0.2 M Tris, pH 7.6 at 25 C | Table 1, L84P NanK column, D-glucose block, kcat = 84 s-1 | Table 1, L84P NanK column, D-glucose block, Km = 6.4 x 10^-3 M | Table 1, L84P NanK column, D-glucose block, kcat/Km = 1.3 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 84 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 84.0 s^(-1). Km: printed cell 6.4 x 10^-3 M; 1 M is 1000 mM, so 6.4 x 10^-3 x 1000 = 6.4 mM. kcat/Km: printed cell 1.3 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^4 / 1000 = 13.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 84.0 / 6.4 = 13.125 s^-1 mM^-1, against the printed efficiency cell 13.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, L84P NanK column, D-glucose block: kcat = 84 s-1; Km = 6.4 x 10^-3 M; kcat/Km = 1.3 x 10^4 M^-1 s^-1.

data_origin: experimental

enzyme: N-acylmannosamine kinase

substrate: D-Glucose

status: corrected

source: oed


substrate_name: D-Mannose

mutation_signature: Unknown

sequence_source: UniProtKB:P45425 direct REST lookup on 2026-06-11

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

column_label: Table 4, wild-type NanK section, D-mannose row; kcat cell = 25 s-1; Km cell = 8.4 x 10^-2 M; kcat/Km cell = 3.0 x 10^2 M^-1 s^-1. captured primary segment: wild-type NanK | D-mannose | Table 4, wild-type NanK section, D-mannose row | 0.2 M Tris, pH 7.6 at 25 C | Table 4, wild-type NanK section, D-mannose row, kcat = 25 s-1 | Table 4, wild-type NanK section, D-mannose row, Km = 8.4 x 10^-2 M | Table 4, wild-type NanK section, D-mannose row, kcat/Km = 3.0 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 25 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 25.0 s^(-1). Km: printed cell 8.4 x 10^-2 M; 1 M is 1000 mM, so 8.4 x 10^-2 x 1000 = 84.0 mM. kcat/Km: printed cell 3.0 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.0 x 10^2 / 1000 = 0.3 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 25.0 / 84.0 = 0.2976190476190476 s^-1 mM^-1, against the printed efficiency cell 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, wild-type NanK section, D-mannose row: kcat = 25 s-1; Km = 8.4 x 10^-2 M; kcat/Km = 3.0 x 10^2 M^-1 s^-1.

table_label: Table 4: Specificity Profile of Wild-Type and L84P NanK (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-Mannose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P45425 and applied mutation signature V138M to reconstruct the assayed variant sequence.

column_label: Table 1, V138M NanK column, D-glucose block; kcat cell = 60 s-1; Km cell = 8.6 x 10^-3 M; kcat/Km cell = 7.0 x 10^3 M^-1 s^-1. captured primary segment: V138M NanK | D-glucose | Table 1, V138M NanK column, D-glucose block | 0.2 M Tris, pH 7.6 at 25 C | Table 1, V138M NanK column, D-glucose block, kcat = 60 s-1 | Table 1, V138M NanK column, D-glucose block, Km = 8.6 x 10^-3 M | Table 1, V138M NanK column, D-glucose block, kcat/Km = 7.0 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 60 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 60.0 s^(-1). Km: printed cell 8.6 x 10^-3 M; 1 M is 1000 mM, so 8.6 x 10^-3 x 1000 = 8.6 mM. kcat/Km: printed cell 7.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.0 x 10^3 / 1000 = 7.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 60.0 / 8.6 = 6.976744186046512 s^-1 mM^-1, against the printed efficiency cell 7.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, V138M NanK column, D-glucose block: kcat = 60 s-1; Km = 8.6 x 10^-3 M; kcat/Km = 7.0 x 10^3 M^-1 s^-1.


organism: Mus musculus

substrate_name: N-Acetyl-D-mannosamine; ATP

kcat_display: Not reported

kcat_over_km_display: Not reported

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

sequence_source: UniProtKB reviewed accession Q9QZ08 (NAGK_MOUSE) direct REST/FASTA lookup

assay_conditions_summary: cofactor ATP

substrate: N-Acetyl-D-mannosamine; ATP


organism: Rattus norvegicus

substrate_name: ATP; N-Acetyl-D-mannosamine

sequence_source: UniProtKB reviewed accession O35826 (GLCNE_RAT) direct REST/FASTA lookup

substrate: ATP; N-Acetyl-D-mannosamine


organism: Staphylococcus aureus

substrate_name: N-acetyl-D-glucosamine

source_db: brenda

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q2G159 and applied mutation signature Y160F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 298.15 K; buffer 22 mM Tris-HCl; cofactor ATP

column_label: Table 3 (Kinetic parameters for SaNanK substituted at Tyr-160), substrate-group head 'GlcNAc', enzyme-form column head 'SaNanK-Y160F'; row 'Vmax (umol/min/mg)' = 36.1 +/- 0.3 umol/min/mg; row 'kcat (s^-1)' = 19.1 +/- 0.2; row 'Km (mM)' = 0.049 +/- 0.002; row 'kcat/Km (s^-1/mM)' = 390 +/- 16.

normalized_value_unit_evidence: kcat: printed Table 3 cell 19.1 s^-1; already in s^-1, so no unit conversion applies; the paper-backed value is 19.1 s^(-1). Km: printed Table 3 cell 0.049 mM; already in mM, so no unit conversion applies; the paper-backed value is 0.049 mM. The Table 3 column also prints kcat/Km 390 s^-1/mM, which is typed as primary printed provenance for this measurement; this catalog row carries no exported kcat/Km, so no ratio value is written into it.

raw_value_unit_evidence: Table 3, substrate-group column GlcNAc, enzyme-form column SaNanK-Y160F: kcat = 19.1 +/- 0.2 s^-1; Km = 0.049 +/- 0.002 mM; kcat/Km = 390 +/- 16 s^-1/mM.

row_label: Table 3 decoded transcription, column SaNanK-Y160F under the GlcNAc substrate group

table_label: Table 3: Kinetic parameters for SaNanK substituted at Tyr-160 (J. Biol. Chem. 2020, 295(10):3301-3315)

substrate: N-acetyl-D-glucosamine

source: brenda


substrate_name: N-acetyl-D-mannosamine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q2G159 and applied mutation signature Y160A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters for SaNanK substituted at Tyr-160), substrate-group head 'N-Acetylmannosamine', enzyme-form column head 'SaNanK-Y160A'; row 'Vmax (umol/min/mg)' = 422 +/- 8 umol/min/mg; row 'kcat (s^-1)' = 223 +/- 4; row 'Km (mM)' = 1.34 +/- 0.1; row 'kcat/Km (s^-1/mM)' = 167 +/- 13.

normalized_value_unit_evidence: kcat: printed Table 3 cell 223 s^-1; already in s^-1, so no unit conversion applies; the paper-backed value is 223.0 s^(-1). Km: printed Table 3 cell 1.34 mM; already in mM, so no unit conversion applies; the paper-backed value is 1.34 mM. kcat/Km: printed Table 3 cell 167 s^-1/mM; s^-1/mM is the same scale as s^-1 mM^-1, so no unit conversion applies; the paper-backed value is 167.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate-group column N-Acetylmannosamine, enzyme-form column SaNanK-Y160A: kcat = 223 +/- 4 s^-1; Km = 1.34 +/- 0.1 mM; kcat/Km = 167 +/- 13 s^-1/mM.

row_label: Table 3 decoded transcription, column SaNanK-Y160A under the N-Acetylmannosamine substrate group

substrate: N-acetyl-D-mannosamine


normalized_value_unit_evidence: kcat: printed Table 3 cell 223 s^-1; already in s^-1, so no unit conversion applies; the paper-backed value is 223.0 s^(-1). Km: printed Table 3 cell 1.34 mM; already in mM, so no unit conversion applies; the paper-backed value is 1.34 mM. The Table 3 column also prints kcat/Km 167 s^-1/mM, which is typed as primary printed provenance for this measurement; this catalog row carries no exported kcat/Km, so no ratio value is written into it.


sequence_source: UniProtKB accession Q2G159 direct REST/FASTA lookup, supported by RCSB 6Q26/6Q27/6Q28 mapping

column_label: Table 1 (Kinetic parameters for wildtype SaNanK), column head 'GlcNAc'; row 'Vmax (umol/min/mg)' = 44.4 +/- 0.3 umol/min/mg; row 'kcat (s^-1)' = 23.4 +/- 0.2; row 'Km (mM)' = 0.260 +/- 0.005; row 'kcat/Km (s^-1/mM)' = 90 +/- 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 23.4 s^-1; already in s^-1, so no unit conversion applies; the paper-backed value is 23.4 s^(-1). Km: printed Table 1 cell 0.260 mM; already in mM, so no unit conversion applies; the paper-backed value is 0.26 mM. The Table 1 column also prints kcat/Km 90 s^-1/mM, which is typed as primary printed provenance for this measurement; this catalog row carries no exported kcat/Km, so no ratio value is written into it.

raw_value_unit_evidence: Table 1, column GlcNAc (wild-type SaNanK): kcat = 23.4 +/- 0.2 s^-1; Km = 0.260 +/- 0.005 mM; kcat/Km = 90 +/- 3 s^-1/mM.

row_label: Table 1 decoded transcription, column GlcNAc, wild-type SaNanK

table_label: Table 1: Kinetic parameters for wildtype SaNanK (J. Biol. Chem. 2020, 295(10):3301-3315)


substrate_name: D-glucose

verification_status: verified

column_label: Table 1 (Kinetic parameters for wildtype SaNanK), column head 'Glucose'; row 'Vmax (umol/min/mg)' = 114 +/- 3 umol/min/mg; row 'kcat (s^-1)' = 60 +/- 1; row 'Km (mM)' = 15 +/- 1; row 'kcat/Km (s^-1/mM)' = 4.0 +/- 0.3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 60 s^-1; already in s^-1, so no unit conversion applies; the paper-backed value is 60.0 s^(-1). Km: printed Table 1 cell 15 mM; already in mM, so no unit conversion applies; the paper-backed value is 15.0 mM. kcat/Km: printed Table 1 cell 4.0 s^-1/mM; s^-1/mM is the same scale as s^-1 mM^-1, so no unit conversion applies; the paper-backed value is 4.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, column Glucose (wild-type SaNanK): kcat = 60 +/- 1 s^-1; Km = 15 +/- 1 mM; kcat/Km = 4.0 +/- 0.3 s^-1/mM.

row_label: Table 1 decoded transcription, column Glucose, wild-type SaNanK

substrate: D-glucose

status: verified


normalized_value_unit_evidence: kcat: printed Table 1 cell 23.4 s^-1; already in s^-1, so no unit conversion applies; the paper-backed value is 23.4 s^(-1). Km: printed Table 1 cell 0.260 mM; already in mM, so no unit conversion applies; the paper-backed value is 0.26 mM. kcat/Km: printed Table 1 cell 90 s^-1/mM; s^-1/mM is the same scale as s^-1 mM^-1, so no unit conversion applies; the paper-backed value is 90.0 s^(-1)*mM^(-1).


enzyme_display_name: triokinase

organism: Homo sapiens

substrate_name: ATP

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProt Q3LXA3 canonical sequence, reconstructed with selected mutation signature and applied mutation signature K204A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor FMN

enzyme: triokinase

substrate: ATP


substrate_name: D-glyceraldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3LXA3 and applied mutation signature S446A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of hTKFC and mutants (J. Biol. Chem. 2014, volume 289, number 15, pages 10620-10636); the table's stub column is 'Assay performed (substrate)' and its seven data column heads are 'Wild type', 'L domain', 'H221A', 'C404A', 'S446A', 'T112A' and 'K204A'; block 'GA kinase (GA) activity'; column 'S446A'; line 'kcat (s^-1)' = 0.74; line '10^6 Km (M)' = 7.1; line '10^-4 kcat/Km (M^-1 s^-1)' = 10.4.

normalized_value_unit_evidence: kcat: the printed cell 0.74 is already in s^-1, so no unit conversion applies and the canonical value is 0.74 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 7.1 is 7.1 x 10^-6 M = 7.1 uM, and 7.1 / 1000 gives 0.0071 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 10.4 is 10.4 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 104.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GA kinase (GA) activity block, column 'S446A': printed 'kcat (s^-1)' cell 0.74; printed '10^6 Km (M)' cell 7.1; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 10.4.

row_label: Table 1, GA kinase (GA) activity block, column head 'hTKFC forms' entry 'S446A' (hTKFC form S446A)

substrate: D-glyceraldehyde


sequence_variant_note: Resolved canonical sequence from UniProt Q3LXA3 canonical sequence, reconstructed with selected mutation signature and applied mutation signature C404A to reconstruct the assayed variant sequence.


substrate_name: dihydroxyacetone

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3LXA3 and applied mutation signature C404A to reconstruct the assayed variant sequence.

smiles: O=C(CO)CO

column_label: Table 1: Kinetic parameters of hTKFC and mutants (J. Biol. Chem. 2014, volume 289, number 15, pages 10620-10636); the table's stub column is 'Assay performed (substrate)' and its seven data column heads are 'Wild type', 'L domain', 'H221A', 'C404A', 'S446A', 'T112A' and 'K204A'; block 'DHA kinase (DHA) activity'; column 'C404A'; line 'kcat (s^-1)' = 2.26; line '10^6 Km (M)' = 1.91; line '10^-4 kcat/Km (M^-1 s^-1)' = 118.

normalized_value_unit_evidence: kcat: the printed cell 2.26 is already in s^-1, so no unit conversion applies and the canonical value is 2.26 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 1.91 is 1.91 x 10^-6 M = 1.91 uM, and 1.91 / 1000 gives 0.00191 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 118 is 118 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 1180.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, DHA kinase (DHA) activity block, column 'C404A': printed 'kcat (s^-1)' cell 2.26; printed '10^6 Km (M)' cell 1.91; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 118.

row_label: Table 1, DHA kinase (DHA) activity block, column head 'hTKFC forms' entry 'C404A' (hTKFC form C404A)

substrate: dihydroxyacetone


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3LXA3 and applied mutation signature T112A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of hTKFC and mutants (J. Biol. Chem. 2014, volume 289, number 15, pages 10620-10636); the table's stub column is 'Assay performed (substrate)' and its seven data column heads are 'Wild type', 'L domain', 'H221A', 'C404A', 'S446A', 'T112A' and 'K204A'; block 'GA kinase (GA) activity'; column 'T112A'; line 'kcat (s^-1)' = 0.16; line '10^6 Km (M)' = 13.7; line '10^-4 kcat/Km (M^-1 s^-1)' = 1.2.

normalized_value_unit_evidence: kcat: the printed cell 0.16 is already in s^-1, so no unit conversion applies and the canonical value is 0.16 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 13.7 is 13.7 x 10^-6 M = 13.7 uM, and 13.7 / 1000 gives 0.0137 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 1.2 is 1.2 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 12.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GA kinase (GA) activity block, column 'T112A': printed 'kcat (s^-1)' cell 0.16; printed '10^6 Km (M)' cell 13.7; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 1.2.

row_label: Table 1, GA kinase (GA) activity block, column head 'hTKFC forms' entry 'T112A' (hTKFC form T112A)


sequence_variant_note: Resolved canonical sequence from UniProt Q3LXA3 canonical sequence, reconstructed with selected mutation signature and applied mutation signature T112A to reconstruct the assayed variant sequence.


column_label: Table 1: Kinetic parameters of hTKFC and mutants (J. Biol. Chem. 2014, volume 289, number 15, pages 10620-10636); the table's stub column is 'Assay performed (substrate)' and its seven data column heads are 'Wild type', 'L domain', 'H221A', 'C404A', 'S446A', 'T112A' and 'K204A'; block 'GA kinase (ATP) activity'; column 'S446A'; line 'kcat (s^-1)' = 0.66; line '10^6 Km (M)' = 35.2; line '10^-4 kcat/Km (M^-1 s^-1)' = 1.9.

normalized_value_unit_evidence: kcat: the printed cell 0.66 is already in s^-1, so no unit conversion applies and the canonical value is 0.66 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 35.2 is 35.2 x 10^-6 M = 35.2 uM, and 35.2 / 1000 gives 0.0352 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 1.9 is 1.9 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 19.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GA kinase (ATP) activity block, column 'S446A': printed 'kcat (s^-1)' cell 0.66; printed '10^6 Km (M)' cell 35.2; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 1.9.

row_label: Table 1, GA kinase (ATP) activity block, column head 'hTKFC forms' entry 'S446A' (hTKFC form S446A)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3LXA3 and applied mutation signature K204A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of hTKFC and mutants (J. Biol. Chem. 2014, volume 289, number 15, pages 10620-10636); the table's stub column is 'Assay performed (substrate)' and its seven data column heads are 'Wild type', 'L domain', 'H221A', 'C404A', 'S446A', 'T112A' and 'K204A'; block 'GA kinase (GA) activity'; column 'K204A'; line 'kcat (s^-1)' = 2.09; line '10^6 Km (M)' = 15.0; line '10^-4 kcat/Km (M^-1 s^-1)' = 14.2.

normalized_value_unit_evidence: kcat: the printed cell 2.09 is already in s^-1, so no unit conversion applies and the canonical value is 2.09 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 15.0 is 15.0 x 10^-6 M = 15.0 uM, and 15.0 / 1000 gives 0.015 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 14.2 is 14.2 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 142.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GA kinase (GA) activity block, column 'K204A': printed 'kcat (s^-1)' cell 2.09; printed '10^6 Km (M)' cell 15.0; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 14.2.

row_label: Table 1, GA kinase (GA) activity block, column head 'hTKFC forms' entry 'K204A' (hTKFC form K204A)


enzyme_display_name: phosphoserine transaminase

organism: Ovis aries

verification_status: unverified

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

enzyme: phosphoserine transaminase

status: unverified


organism: Spinacia oleracea

substrate_name: L-Glutamate; 3-Phosphohydroxypyruvate

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

mutation_type: truncation

proof_lines: SABIO-RK modifier species: phosphoserine transaminase(Enzyme) wildtype truncated

substrate: L-Glutamate; 3-Phosphohydroxypyruvate


organism: Synechocystis sp.

substrate_name: L-glutamate

sequence_source: UniProtKB P74281 canonical sequence, direct accession lookup

substrate: L-glutamate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q3LXA3 canonical sequence with residue 204 K changed to A and applied mutation signature K204A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K204A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C

proof_lines: mutant enzyme K204A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C


column_label: Table 1: Kinetic parameters of hTKFC and mutants (J. Biol. Chem. 2014, volume 289, number 15, pages 10620-10636); the table's stub column is 'Assay performed (substrate)' and its seven data column heads are 'Wild type', 'L domain', 'H221A', 'C404A', 'S446A', 'T112A' and 'K204A'; block 'DHA kinase (DHA) activity'; column 'S446A'; line 'kcat (s^-1)' = 0.13; line '10^6 Km (M)' = 0.99; line '10^-4 kcat/Km (M^-1 s^-1)' = 13.1.

normalized_value_unit_evidence: kcat: the printed cell 0.13 is already in s^-1, so no unit conversion applies and the canonical value is 0.13 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 0.99 is 0.99 x 10^-6 M = 0.99 uM, and 0.99 / 1000 gives 0.00099 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 13.1 is 13.1 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 131.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, DHA kinase (DHA) activity block, column 'S446A': printed 'kcat (s^-1)' cell 0.13; printed '10^6 Km (M)' cell 0.99; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 13.1.

row_label: Table 1, DHA kinase (DHA) activity block, column head 'hTKFC forms' entry 'S446A' (hTKFC form S446A)


sequence_variant_note: Resolved canonical sequence from UniProtKB Q3LXA3 canonical sequence with residue 112 T changed to A and applied mutation signature T112A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T112A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C

proof_lines: mutant enzyme T112A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q3LXA3 canonical sequence with residue 446 S changed to A and applied mutation signature S446A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S446A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C

proof_lines: mutant enzyme S446A, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P45425 direct accession check plus L84P reconstruction and applied mutation signature L84P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB P45425 direct accession check plus V138M reconstruction and applied mutation signature V138M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P45425 and applied mutation signature L84P to reconstruct the assayed variant sequence.

column_label: Table 4, L84P NanK section, D-mannose row; kcat cell = 62 s-1; Km cell = 2.3 x 10^-2 M; kcat/Km cell = 2.8 x 10^3 M^-1 s^-1. captured primary segment: L84P NanK | D-mannose | Table 4, L84P NanK section, D-mannose row | 0.2 M Tris, pH 7.6 at 25 C | Table 4, L84P NanK section, D-mannose row, kcat = 62 s-1 | Table 4, L84P NanK section, D-mannose row, Km = 2.3 x 10^-2 M | Table 4, L84P NanK section, D-mannose row, kcat/Km = 2.8 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 62 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 62.0 s^(-1). Km: printed cell 2.3 x 10^-2 M; 1 M is 1000 mM, so 2.3 x 10^-2 x 1000 = 23.0 mM. kcat/Km: printed cell 2.8 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.8 x 10^3 / 1000 = 2.8 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 62.0 / 23.0 = 2.6956521739130435 s^-1 mM^-1, against the printed efficiency cell 2.8 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, L84P NanK section, D-mannose row: kcat = 62 s-1; Km = 2.3 x 10^-2 M; kcat/Km = 2.8 x 10^3 M^-1 s^-1.


substrate_name: D-Glucose; ATP

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB P45425 direct accession check plus L84P/V138M reconstruction and applied mutation signature L84P/V138M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: N-acylmannosamine kinase(Enzyme) mutant NanK L84P/V138M

substrate: D-Glucose; ATP


column_label: Table 1, L84P NanK column, N-acetyl-D-mannosamine block, ATP axis; kcat cell = 18 s-1; Km, ATP cell = 8.4 x 10^-5 M; kcat/Km cell: Table 1 carries none on the ATP axis. captured primary segment: L84P NanK | ATP | Table 1, L84P NanK column, N-acetyl-D-mannosamine block, ATP axis | 0.2 M Tris, pH 7.6 at 25 C | Table 1, L84P NanK column, N-acetyl-D-mannosamine block, ATP axis, kcat = 18 s-1 | Table 1, L84P NanK column, N-acetyl-D-mannosamine block, ATP axis, Km, ATP = 8.4 x 10^-5 M | kcat/Km: Table 1 prints no kcat/Km cell on the ATP axis of this measurement

normalized_value_unit_evidence: kcat: printed cell 18 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 18.0 s^(-1). Km: printed cell 8.4 x 10^-5 M; 1 M is 1000 mM, so 8.4 x 10^-5 x 1000 = 0.08399999999999999 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, 18.0 / 0.08399999999999999 = 214.2857142857143 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, L84P NanK column, N-acetyl-D-mannosamine block, ATP axis: kcat = 18 s-1; Km, ATP = 8.4 x 10^-5 M; Table 1 carries no kcat/Km cell on the ATP axis.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P45425 and applied mutation signature V138M to reconstruct the assayed variant sequence.

column_label: Table 1, V138M NanK column, N-acetyl-D-mannosamine block, ATP axis; kcat cell = 20 s-1; Km, ATP cell = 1.1 x 10^-4 M; kcat/Km cell: Table 1 carries none on the ATP axis. captured primary segment: V138M NanK | ATP | Table 1, V138M NanK column, N-acetyl-D-mannosamine block, ATP axis | 0.2 M Tris, pH 7.6 at 25 C | Table 1, V138M NanK column, N-acetyl-D-mannosamine block, ATP axis, kcat = 20 s-1 | Table 1, V138M NanK column, N-acetyl-D-mannosamine block, ATP axis, Km, ATP = 1.1 x 10^-4 M | kcat/Km: Table 1 prints no kcat/Km cell on the ATP axis of this measurement

normalized_value_unit_evidence: kcat: printed cell 20 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 20.0 s^(-1). Km: printed cell 1.1 x 10^-4 M; 1 M is 1000 mM, so 1.1 x 10^-4 x 1000 = 0.11 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, 20.0 / 0.11 = 181.8181818181818 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, V138M NanK column, N-acetyl-D-mannosamine block, ATP axis: kcat = 20 s-1; Km, ATP = 1.1 x 10^-4 M; Table 1 carries no kcat/Km cell on the ATP axis.


substrate_name: N-Acetyl-D-mannosamine

column_label: Table 1, V138M NanK column, N-acetyl-D-mannosamine block; kcat cell = 20 s-1; Km cell = 1.6 x 10^-4 M; kcat/Km cell = 1.2 x 10^5 M^-1 s^-1. captured primary segment: V138M NanK | N-acetyl-D-mannosamine | Table 1, V138M NanK column, N-acetyl-D-mannosamine block | 0.2 M Tris, pH 7.6 at 25 C | Table 1, V138M NanK column, N-acetyl-D-mannosamine block, kcat = 20 s-1 | Table 1, V138M NanK column, N-acetyl-D-mannosamine block, Km = 1.6 x 10^-4 M | Table 1, V138M NanK column, N-acetyl-D-mannosamine block, kcat/Km = 1.2 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 20 s-1; the printed turnover column is already per second, so no unit conversion applies and the value is 20.0 s^(-1). Km: printed cell 1.6 x 10^-4 M; 1 M is 1000 mM, so 1.6 x 10^-4 x 1000 = 0.16 mM. kcat/Km: printed cell 1.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^5 / 1000 = 120.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 20.0 / 0.16 = 125.0 s^-1 mM^-1, against the printed efficiency cell 120.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, V138M NanK column, N-acetyl-D-mannosamine block: kcat = 20 s-1; Km = 1.6 x 10^-4 M; kcat/Km = 1.2 x 10^5 M^-1 s^-1.

substrate: N-Acetyl-D-mannosamine


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

sequence_source: UniProtKB Q9Y223 direct accession check

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

assay_conditions_summary: pH 8.1; 310.15 K; cofactor ATP

proof_lines:
pH 8.1, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=8.1

source_databases_merged: brenda skid


enzyme_display_name: tryprostatin B synthase

organism: Aspergillus fumigatus

substrate_name: cyclo-(L-Trp-Gly)

sequence_source: UniProtKB REST Q4WAW7 canonical sequence, direct lookup on 2026-06-11

enzyme: tryprostatin B synthase

substrate: cyclo-(L-Trp-Gly)


substrate_name: cyclo-(L-Trp-L-Pro)

substrate: cyclo-(L-Trp-L-Pro)


substrate_name: cyclo-(D-Trp-L-Pro)

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q4WAW7 canonical sequence; reconstructed by applying Y205L and applied mutation signature Y205L to reconstruct the assayed variant sequence.

substrate: cyclo-(D-Trp-L-Pro)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q4WAW7 canonical sequence; reconstructed by applying Y205N and applied mutation signature Y205N to reconstruct the assayed variant sequence.


substrate_name: cyclo-(D-Trp-D-Pro)

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4WAW7 and applied mutation signature Y205L to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme block 'Y205L', substrate row 'cyclo-D-Trp-D-Pro (2a)'; column 'KM [mM]' = 0.28; column 'kcat [s-1]' = 1.39; column 'kcat/KM [s-1 M-1]' = 4964; column 'Protein amount and incubation time' = 2.5 ug, 10 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.28 mM; the printed unit is already mM, so the value carries over as 0.28 mM and equals the exported value 0.28 mM. kcat: printed Table 3 cell 1.39 s^-1; the printed unit is already s^-1, so the value carries over as 1.39 s^(-1) and equals the exported value 1.39 s^(-1). kcat/Km: printed Table 3 cell 4964 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4964 / 1000 = 4.964 s^-1 mM^-1, the printed-precision rendering of the exact same-measurement quotient 1.39 / 0.28 = 4.9642857142857135 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 3, enzyme block 'Y205L', substrate row 'cyclo-D-Trp-D-Pro (2a)': KM = 0.28 mM; kcat = 1.39 s^-1; printed kcat/KM = 4964 M^-1 s^-1.

table_label: Table 3: Kinetic parameters of FtmPT1, Y205N, and Y205L reactions (Appl Microbiol Biotechnol 2016, 100:9943-9953)

substrate: cyclo-(D-Trp-D-Pro)


column_label: Table 3, enzyme block 'Y205L', substrate row 'cyclo-D-Trp-L-Pro (4a)'; column 'KM [mM]' = 0.46; column 'kcat [s-1]' = 0.41; column 'kcat/KM [s-1 M-1]' = 891; column 'Protein amount and incubation time' = 2.5 ug, 45 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.46 mM; the printed unit is already mM, so the value carries over as 0.46 mM and equals the exported value 0.46 mM. kcat: printed Table 3 cell 0.41 s^-1; the printed unit is already s^-1, so the value carries over as 0.41 s^(-1) and equals the exported value 0.41 s^(-1). kcat/Km: printed Table 3 cell 891 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 891 / 1000 = 0.891 s^-1 mM^-1, the printed-precision rendering of the exact same-measurement quotient 0.41 / 0.46 = 0.8913043478260869 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 3, enzyme block 'Y205L', substrate row 'cyclo-D-Trp-L-Pro (4a)': KM = 0.46 mM; kcat = 0.41 s^-1; printed kcat/KM = 891 M^-1 s^-1.


column_label: Table 3, enzyme block 'Y205L', substrate row 'cyclo-L-Trp-L-Pro (1a)'; column 'KM [mM]' = 0.19; column 'kcat [s-1]' = 4.26; column 'kcat/KM [s-1 M-1]' = 22,421; column 'Protein amount and incubation time' = 1.0 ug, 30 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.19 mM; the printed unit is already mM, so the value carries over as 0.19 mM and equals the exported value 0.19 mM. kcat: printed Table 3 cell 4.26 s^-1; the printed unit is already s^-1, so the value carries over as 4.26 s^(-1) and equals the exported value 4.26 s^(-1). kcat/Km: printed Table 3 cell 22,421 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 22421 / 1000 = 22.421 s^-1 mM^-1, the printed-precision rendering of the exact same-measurement quotient 4.26 / 0.19 = 22.421052631578945 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 3, enzyme block 'Y205L', substrate row 'cyclo-L-Trp-L-Pro (1a)': KM = 0.19 mM; kcat = 4.26 s^-1; printed kcat/KM = 22,421 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4WAW7 and applied mutation signature Y205N to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme block 'Y205N', substrate row 'cyclo-D-Trp-L-Pro (4a)'; column 'KM [mM]' = 0.40; column 'kcat [s-1]' = 0.21; column 'kcat/KM [s-1 M-1]' = 525; column 'Protein amount and incubation time' = 5.0 ug, 30 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.40 mM; the printed unit is already mM, so the value carries over as 0.4 mM and equals the exported value 0.4 mM. kcat: printed Table 3 cell 0.21 s^-1; the printed unit is already s^-1, so the value carries over as 0.21 s^(-1) and equals the exported value 0.21 s^(-1). kcat/Km: printed Table 3 cell 525 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 525 / 1000 = 0.525 s^-1 mM^-1, the printed-precision rendering of the exact same-measurement quotient 0.21 / 0.40 = 0.5249999999999999 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 3, enzyme block 'Y205N', substrate row 'cyclo-D-Trp-L-Pro (4a)': KM = 0.40 mM; kcat = 0.21 s^-1; printed kcat/KM = 525 M^-1 s^-1.


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:Q2G159 REST/FASTA, accessed 2026-06-11

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP

source: skid


enzyme_display_name: GDP-L-galactose/GDP-D-glucose: hexose 1-phosphate guanylyltransferase

organism: Arabidopsis thaliana

substrate_name: D-Glucose 1-phosphate

sequence_source: UniProtKB:Q8RWE8 REST/FASTA, accessed 2026-06-11

column_label: Table 1B Reverse reaction, from TABLE 1: Substrate specificity of the A. thaliana VTC2 phosphorylase (J Biol Chem 2007, 282(26):18879-18885); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 M-1). Table 1B Reverse reaction, substrate row D-Glc-1-P; column kcat (s-1) = 12; column Km (mM) = 29; column kcat/Km (s-1 M-1) = 412. captured primary segment: D-Glc-1-P | kcat 12 s^-1 | Km 29 mM | kcat/Km 412 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed TABLE 1 kcat cell 12 s^-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 12.0 s^(-1), which is what the export carries. Km: printed TABLE 1 Km cell 29 mM; the cell is already in mM, so no unit conversion applies and the paper value is 29.0 mM, which is what the export carries. kcat/Km: printed TABLE 1 kcat/Km cell 412 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 412.0 / 1000 = 0.412 s^(-1)*mM^(-1). Quotient disclosure for this row: 12.0 / 29.0 = 0.41379310344827586 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.412 s^-1 mM^-1. The export carries 0.41379310344827586 s^(-1)*mM^(-1); the printed efficiency cell is the paper's own independently fitted primary value, and this pass adopts it.

raw_value_unit_evidence: Table 1B Reverse reaction, substrate row D-Glc-1-P: kcat = 12 s^-1; Km = 29 mM; printed kcat/Km = 412 s^-1 M^-1.

substrate: D-Glucose 1-phosphate


substrate_name: GDP-L-galactose; Phosphate

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

proof_lines: presence of GDP-alpha-L-galactose, pH 7.5, 26°C

enzyme: GDP-L-galactose/GDP-D-glucose: hexose 1-phosphate guanylyltransferase

substrate: GDP-L-galactose; Phosphate


substrate_name: D-Galactose 1-phosphate

column_label: Table 1B Reverse reaction, from TABLE 1: Substrate specificity of the A. thaliana VTC2 phosphorylase (J Biol Chem 2007, 282(26):18879-18885); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 M-1). Table 1B Reverse reaction, substrate row D-Gal-1-P; column kcat (s-1) = 0.023; column Km (mM) = 67; column kcat/Km (s-1 M-1) = 0.34. captured primary segment: D-Gal-1-P | kcat 0.023 s^-1 | Km 67 mM | kcat/Km 0.34 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed TABLE 1 kcat cell 0.023 s^-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 0.023 s^(-1), which is what the export carries. Km: printed TABLE 1 Km cell 67 mM; the cell is already in mM, so no unit conversion applies and the paper value is 67.0 mM, which is what the export carries. kcat/Km: printed TABLE 1 kcat/Km cell 0.34 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 0.34 / 1000 = 0.00034 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.023 / 67.0 = 0.00034328358208955223 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.00034 s^-1 mM^-1. The export carries 0.00034328358208955223 s^(-1)*mM^(-1), the exact full-precision quotient of the two printed component cells, and the printed cell is that same quotient written to the precision TABLE 1 uses, so no metric changes.

raw_value_unit_evidence: Table 1B Reverse reaction, substrate row D-Gal-1-P: kcat = 0.023 s^-1; Km = 67 mM; printed kcat/Km = 0.34 s^-1 M^-1.

substrate: D-Galactose 1-phosphate


substrate_name: L-Galactose 1-phosphate

column_label: Table 1B Reverse reaction, from TABLE 1: Substrate specificity of the A. thaliana VTC2 phosphorylase (J Biol Chem 2007, 282(26):18879-18885); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 M-1). Table 1B Reverse reaction, substrate row L-Gal-1-P; column kcat (s-1) = 6.0; column Km (mM) = 45; column kcat/Km (s-1 M-1) = 133. captured primary segment: L-Gal-1-P | kcat 6.0 s^-1 | Km 45 mM | kcat/Km 133 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed TABLE 1 kcat cell 6.0 s^-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 6.0 s^(-1), which is what the export carries. Km: printed TABLE 1 Km cell 45 mM; the cell is already in mM, so no unit conversion applies and the paper value is 45.0 mM, which is what the export carries. kcat/Km: printed TABLE 1 kcat/Km cell 133 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 133.0 / 1000 = 0.133 s^(-1)*mM^(-1). Quotient disclosure for this row: 6.0 / 45.0 = 0.13333333333333333 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.133 s^-1 mM^-1. The export carries 0.13333333333333333 s^(-1)*mM^(-1), the exact full-precision quotient of the two printed component cells, and the printed cell is that same quotient written to the precision TABLE 1 uses, so no metric changes.

raw_value_unit_evidence: Table 1B Reverse reaction, substrate row L-Gal-1-P: kcat = 6.0 s^-1; Km = 45 mM; printed kcat/Km = 133 s^-1 M^-1.

substrate: L-Galactose 1-phosphate


substrate_name: GDP-D-mannose

column_label: Table 1A Forward reaction, from TABLE 1: Substrate specificity of the A. thaliana VTC2 phosphorylase (J Biol Chem 2007, 282(26):18879-18885); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 M-1). Table 1A Forward reaction, substrate row GDP-D-Man; column kcat (s-1) = 0.093; column Km (mM) = 0.52; column kcat/Km (s-1 M-1) = 1.9 x 10^2. captured primary segment: GDP-D-Man | kcat 0.093 s^-1 | Km 0.52 mM | kcat/Km 1.9 x 10^2 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed TABLE 1 kcat cell 0.093 s^-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 0.093 s^(-1), which is what the export carries. Km: printed TABLE 1 Km cell 0.52 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.52 mM, which is what the export carries. kcat/Km: printed TABLE 1 kcat/Km cell 1.9 x 10^2 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 190.0 / 1000 = 0.19 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.093 / 0.52 = 0.17884615384615385 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.19 s^-1 mM^-1. The export carries 0.17884615384615385 s^(-1)*mM^(-1); the printed efficiency cell is the paper's own independently fitted primary value, and this pass adopts it.

raw_value_unit_evidence: Table 1A Forward reaction, substrate row GDP-D-Man: kcat = 0.093 s^-1; Km = 0.52 mM; printed kcat/Km = 1.9 x 10^2 s^-1 M^-1.

substrate: GDP-D-mannose


substrate_name: D-Mannose 1-phosphate

substrate: D-Mannose 1-phosphate


substrate_name: GDP-D-glucose

column_label: Table 1A Forward reaction, from TABLE 1: Substrate specificity of the A. thaliana VTC2 phosphorylase (J Biol Chem 2007, 282(26):18879-18885); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 M-1). Table 1A Forward reaction, substrate row GDP-D-Glc; column kcat (s-1) = 23; column Km (mM) = 0.0044; column kcat/Km (s-1 M-1) = 5.7 x 10^6. captured primary segment: GDP-D-Glc | kcat 23 s^-1 | Km 0.0044 mM | kcat/Km 5.7 x 10^6 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed TABLE 1 kcat cell 23 s^-1; the cell is already in s^-1, so no unit conversion applies and the paper value is 23.0 s^(-1), which is what the export carries. Km: printed TABLE 1 Km cell 0.0044 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.0044 mM; the export carries 0.004 mM, and this pass adopts the printed cell. kcat/Km: printed TABLE 1 kcat/Km cell 5.7 x 10^6 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 5700000.0 / 1000 = 5700.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 23.0 / 0.0044 = 5227.272727272727 s^-1 mM^-1, against the printed catalytic-efficiency cell 5700.0 s^-1 mM^-1. The export carries 5750.0 s^(-1)*mM^(-1); the printed efficiency cell is the paper's own independently fitted primary value, and this pass adopts it.

raw_value_unit_evidence: Table 1A Forward reaction, substrate row GDP-D-Glc: kcat = 23 s^-1; Km = 0.0044 mM; printed kcat/Km = 5.7 x 10^6 s^-1 M^-1.

substrate: GDP-D-glucose


enzyme_display_name: GDP-L-galactose phosphorylase 1

substrate_name: Phosphate

sequence_source: UniProtKB:Q8RWE8 direct REST lookup on 2026-06-11; reviewed Swiss-Prot GGAP1_ARATH; organism Arabidopsis thaliana; EC 2.7.7.69

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

enzyme: GDP-L-galactose phosphorylase 1

substrate: Phosphate


enzyme_display_name: GDP-L-galactose phosphorylase 2

sequence_source: UniProtKB:Q9FLP9 direct REST lookup on 2026-06-11; reviewed Swiss-Prot GGAP2_ARATH; organism Arabidopsis thaliana; EC 2.7.7.69

enzyme: GDP-L-galactose phosphorylase 2


substrate_name: GDP-L-galactose

substrate: GDP-L-galactose


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8RWE8 canonical sequence with row-specific S290F reconstruction on 2026-06-11 and applied mutation signature S290F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: GDP-L-galactose phosphorylase(Enzyme) mutant Ser290Phe VTC2-3 his-tagged


substrate_name: Phosphate; GDP-L-galactose

proof_lines: presence of GDP-L-galactose, pH 7.5, 26°C

substrate: Phosphate; GDP-L-galactose


column_label: Table 3, enzyme block 'Y205N', substrate row 'cyclo-D-Trp-D-Pro (2a)'; column 'KM [mM]' = 0.32; column 'kcat [s-1]' = 0.25; column 'kcat/KM [s-1 M-1]' = 781; column 'Protein amount and incubation time' = 2.5 ug, 60 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.32 mM; the printed unit is already mM, so the value carries over as 0.32 mM and equals the exported value 0.32 mM. kcat: printed Table 3 cell 0.25 s^-1; the printed unit is already s^-1, so the value carries over as 0.25 s^(-1) and equals the exported value 0.25 s^(-1). kcat/Km: printed Table 3 cell 781 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 781 / 1000 = 0.781 s^-1 mM^-1, the printed-precision rendering of the exact same-measurement quotient 0.25 / 0.32 = 0.78125 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 3, enzyme block 'Y205N', substrate row 'cyclo-D-Trp-D-Pro (2a)': KM = 0.32 mM; kcat = 0.25 s^-1; printed kcat/KM = 781 M^-1 s^-1.


substrate_name: cyclo-(L-Trp-D-Pro)

column_label: Table 3, enzyme block 'Y205L', substrate row 'cyclo-L-Trp-D-Pro (3a)'; column 'KM [mM]' = 0.083; column 'kcat [s-1]' = 0.18; column 'kcat/KM [s-1 M-1]' = 2169; column 'Protein amount and incubation time' = 2.5 ug, 10 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.083 mM; the printed unit is already mM, so the value carries over as 0.083 mM and equals the exported value 0.083 mM. kcat: printed Table 3 cell 0.18 s^-1; the printed unit is already s^-1, so the value carries over as 0.18 s^(-1) and equals the exported value 0.18 s^(-1). kcat/Km: printed Table 3 cell 2169 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2169 / 1000 = 2.169 s^-1 mM^-1, the printed-precision rendering of the exact same-measurement quotient 0.18 / 0.083 = 2.1686746987951806 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 3, enzyme block 'Y205L', substrate row 'cyclo-L-Trp-D-Pro (3a)': KM = 0.083 mM; kcat = 0.18 s^-1; printed kcat/KM = 2169 M^-1 s^-1.

substrate: cyclo-(L-Trp-D-Pro)


column_label: Table 3, enzyme block 'Y205N', substrate row 'cyclo-L-Trp-L-Pro (1a)'; column 'KM [mM]' = 0.11; column 'kcat [s-1]' = 1.36; column 'kcat/KM [s-1 M-1]' = 12,364; column 'Protein amount and incubation time' = 1.0 ug, 45 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.11 mM; the printed unit is already mM, so the value carries over as 0.11 mM and equals the exported value 0.11 mM. kcat: printed Table 3 cell 1.36 s^-1; the printed unit is already s^-1, so the value carries over as 1.36 s^(-1) and equals the exported value 1.36 s^(-1). kcat/Km: printed Table 3 cell 12,364 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12364 / 1000 = 12.364 s^-1 mM^-1, the printed-precision rendering of the exact same-measurement quotient 1.36 / 0.11 = 12.363636363636365 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 3, enzyme block 'Y205N', substrate row 'cyclo-L-Trp-L-Pro (1a)': KM = 0.11 mM; kcat = 1.36 s^-1; printed kcat/KM = 12,364 M^-1 s^-1.


column_label: Table 3, enzyme block 'Y205N', substrate row 'cyclo-L-Trp-D-Pro (3a)'; column 'KM [mM]' = 0.62; column 'kcat [s-1]' = 0.32; column 'kcat/KM [s-1 M-1]' = 516; column 'Protein amount and incubation time' = 1.0 ug, 5 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.62 mM; the printed unit is already mM, so the value carries over as 0.62 mM and equals the exported value 0.62 mM. kcat: printed Table 3 cell 0.32 s^-1; the printed unit is already s^-1, so the value carries over as 0.32 s^(-1) and equals the exported value 0.32 s^(-1). kcat/Km: printed Table 3 cell 516 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 516 / 1000 = 0.516 s^-1 mM^-1, the printed-precision rendering of the exact same-measurement quotient 0.32 / 0.62 = 0.5161290322580645 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 3, enzyme block 'Y205N', substrate row 'cyclo-L-Trp-D-Pro (3a)': KM = 0.62 mM; kcat = 0.32 s^-1; printed kcat/KM = 516 M^-1 s^-1.


substrate_name: N-acetyl-D-mannosamine

sequence_source: UniProtKB Q2G159 canonical FASTA direct fetch, 2026-06-11

assay_conditions_summary: pH 8.5; 298.15 K; buffer 22 mM Tris-HCl; cofactor NADH

column_label: Table 1 (Kinetic parameters for wildtype SaNanK), column head 'N-Acetylmannosamine'; row 'Vmax (umol/min/mg)' = 497 +/- 7 umol/min/mg; row 'kcat (s^-1)' = 263 +/- 3; row 'Km (mM)' = 0.30 +/- 0.01; row 'kcat/Km (s^-1/mM)' = 871 +/- 34; row 'ATP Km (mM)' = 0.73 +/- 0.02 mM.

normalized_value_unit_evidence: kcat: the Results text prints 262.6 s^-1 for this measurement; the value is already in s^-1, so no unit conversion applies; the paper-backed value is 262.6 s^(-1). Km: printed Table 1 cell 0.30 mM; already in mM, so no unit conversion applies; the paper-backed value is 0.3 mM. kcat/Km: printed Table 1 cell 871 s^-1/mM; s^-1/mM is the same scale as s^-1 mM^-1, so no unit conversion applies; the paper-backed value is 871.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, column N-Acetylmannosamine (wild-type SaNanK): the Results text states kcat = 262.6 s^-1 and Km N-acetylmannosamine = 0.30 mM for this measurement, and the Table 1 cells for the same column print kcat 263 +/- 3 s^-1, Km 0.30 +/- 0.01 mM and kcat/Km 871 +/- 34 s^-1/mM.

row_label: Table 1 decoded transcription, column N-Acetylmannosamine, wild-type SaNanK

substrate: N-acetyl-D-mannosamine


substrate_name: N-acetyl-D-glucosamine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q2G159 and applied mutation signature Y160A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters for SaNanK substituted at Tyr-160), substrate-group head 'GlcNAc', enzyme-form column head 'SaNanK-Y160A'; row 'Vmax (umol/min/mg)' = 33.6 +/- 0.3 umol/min/mg; row 'kcat (s^-1)' = 17.8 +/- 0.2; row 'Km (mM)' = 0.057 +/- 0.003; row 'kcat/Km (s^-1/mM)' = 310 +/- 16.

normalized_value_unit_evidence: kcat: printed Table 3 cell 17.8 s^-1; already in s^-1, so no unit conversion applies; the paper-backed value is 17.8 s^(-1). Km: printed Table 3 cell 0.057 mM; already in mM, so no unit conversion applies; the paper-backed value is 0.057 mM. kcat/Km: printed Table 3 cell 310 s^-1/mM; s^-1/mM is the same scale as s^-1 mM^-1, so no unit conversion applies; the paper-backed value is 310.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate-group column GlcNAc, enzyme-form column SaNanK-Y160A: kcat = 17.8 +/- 0.2 s^-1; Km = 0.057 +/- 0.003 mM; kcat/Km = 310 +/- 16 s^-1/mM.

row_label: Table 3 decoded transcription, column SaNanK-Y160A under the GlcNAc substrate group

substrate: N-acetyl-D-glucosamine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q2G159 and applied mutation signature Y160F to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters for SaNanK substituted at Tyr-160), substrate-group head 'N-Acetylmannosamine', enzyme-form column head 'SaNanK-Y160F'; row 'Vmax (umol/min/mg)' = 408 +/- 5 umol/min/mg; row 'kcat (s^-1)' = 216 +/- 3; row 'Km (mM)' = 1.27 +/- 0.1; row 'kcat/Km (s^-1/mM)' = 171 +/- 13.

normalized_value_unit_evidence: kcat: printed Table 3 cell 216 s^-1; already in s^-1, so no unit conversion applies; the paper-backed value is 216.0 s^(-1). Km: printed Table 3 cell 1.27 mM; already in mM, so no unit conversion applies; the paper-backed value is 1.27 mM. kcat/Km: printed Table 3 cell 171 s^-1/mM; s^-1/mM is the same scale as s^-1 mM^-1, so no unit conversion applies; the paper-backed value is 171.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate-group column N-Acetylmannosamine, enzyme-form column SaNanK-Y160F: kcat = 216 +/- 3 s^-1; Km = 1.27 +/- 0.1 mM; kcat/Km = 171 +/- 13 s^-1/mM.

row_label: Table 3 decoded transcription, column SaNanK-Y160F under the N-Acetylmannosamine substrate group


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q2G159 canonical FASTA by Y160F, direct fetch 2026-06-11 and applied mutation signature Y160F to reconstruct the assayed variant sequence.


enzyme_display_name: pectinesterase

organism: Acetivibrio thermocellus

substrate_name: Pectin

sequence_source: UniProtKB A3DJL8 direct accession lookup (reviewed 2026-06-11)

proof_lines: Citrus pectin (50% esterified), recombinant enzyme, pH 8.5, 50°C

proof_lines: Citrus pectin (25% esterified), recombinant enzyme, pH 8.5, 50°C

proof_lines: Citrus pectin (85% esterified), recombinant enzyme, pH 8.5, 50°C

enzyme: pectinesterase

substrate: Pectin


organism: Aspergillus niger

sequence_source: UniProtKB A0A345K402 direct accession lookup (reviewed 2026-06-11)


organism: Bacteroides thetaiotaomicron

substrate_name: apple pectin

sequence_source: UniProtKB Q8A900 direct accession lookup (reviewed 2026-06-11)

proof_lines: isolated recombinant protein lacking signal peptide, pH not specified in the publication, temperature not specified in the publication

proof_lines: isolated central module, pH not specified in the publication, temperature not specified in the publication

substrate: apple pectin


organism: Carica papaya

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


organism: Erwinia chrysanthemi

substrate_name: Pectin; n n n n n n H2O

sequence_variant_note: Resolved canonical sequence from P0C1A8 canonical sequence from UniProtKB with direct T272A reconstruction (reviewed 2026-06-11) and applied mutation signature T272A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pectinesterase(Enzyme) mutant T272A

substrate: Pectin; n n n n n n H2O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0C1A8 and applied mutation signature Q177A to reconstruct the assayed variant sequence.

column_label: Table III (Steady-state kinetic analyses of mutant PMEs) prints one enzyme-label column followed by three numeric columns whose heads are kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1) in that printed order. The cited cell set is Table III, enzyme row Q177A: kcat (s^-1) = 40; Km (mM) = 0.22; kcat/Km (s^-1 mM^-1) = 181.

normalized_value_unit_evidence: kcat: printed Table III cell 40 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 40.0 s^(-1). Km: printed Table III cell 0.22 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.22 mM. kcat/Km: printed Table III cell 181 s-1 mM-1; the printed column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 181.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, enzyme row Q177A: kcat = 40 s-1; Km = 0.22 mM; printed kcat/Km = 181 s-1 mM-1.

row_label: Table III, enzyme row Q177A

table_label: Table III: Steady-state kinetic analyses of mutant PMEs (The EMBO Journal 2007, 26:3879-3887)


sequence_variant_note: Resolved canonical sequence from P0C1A8 canonical sequence from UniProtKB with direct Q153A reconstruction (reviewed 2026-06-11) and applied mutation signature Q153A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pectinesterase(Enzyme) mutant Q153A


sequence_source: UniProtKB:P0C1A8 REST FASTA

column_label: Table III (Steady-state kinetic analyses of mutant PMEs) prints one enzyme-label column followed by three numeric columns whose heads are kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1) in that printed order. The cited cell set is Table III, enzyme row PME3937 wild-type: kcat (s^-1) = 450; Km (mM) = 0.13; kcat/Km (s^-1 mM^-1) = 3462.

normalized_value_unit_evidence: kcat: printed Table III cell 450 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 450.0 s^(-1). Km: printed Table III cell 0.13 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.13 mM. kcat/Km: printed Table III cell 3462 s-1 mM-1; the printed column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 3462.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, enzyme row PME3937 wild-type: kcat = 450 s-1; Km = 0.13 mM; printed kcat/Km = 3462 s-1 mM-1.

row_label: Table III, enzyme row PME3937 wild-type


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0C1A8 and applied mutation signature Q153A to reconstruct the assayed variant sequence.

column_label: Table III (Steady-state kinetic analyses of mutant PMEs) prints one enzyme-label column followed by three numeric columns whose heads are kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1) in that printed order. The cited cell set is Table III, enzyme row Q153A: kcat (s^-1) = 232; Km (mM) = 2.2; kcat/Km (s^-1 mM^-1) = 106.

normalized_value_unit_evidence: kcat: printed Table III cell 232 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 232.0 s^(-1). Km: printed Table III cell 2.2 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 2.2 mM. kcat/Km: printed Table III cell 106 s-1 mM-1; the printed column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 106.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, enzyme row Q153A: kcat = 232 s-1; Km = 2.2 mM; printed kcat/Km = 106 s-1 mM-1.

row_label: Table III, enzyme row Q153A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0C1A8 REST FASTA plus single-substitution reconstruction and applied mutation signature M306A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pectinesterase(Enzyme) mutant M306A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0C1A8 and applied mutation signature T272A to reconstruct the assayed variant sequence.

column_label: Table III (Steady-state kinetic analyses of mutant PMEs) prints one enzyme-label column followed by three numeric columns whose heads are kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1) in that printed order. The cited cell set is Table III, enzyme row T272A: kcat (s^-1) = 425; Km (mM) = 0.77; kcat/Km (s^-1 mM^-1) = 552.

normalized_value_unit_evidence: kcat: printed Table III cell 425 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 425.0 s^(-1). Km: printed Table III cell 0.77 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.77 mM. kcat/Km: printed Table III cell 552 s-1 mM-1; the printed column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 552.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, enzyme row T272A: kcat = 425 s-1; Km = 0.77 mM; printed kcat/Km = 552 s-1 mM-1.

row_label: Table III, enzyme row T272A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0C1A8 and applied mutation signature V198A to reconstruct the assayed variant sequence.

column_label: Table III (Steady-state kinetic analyses of mutant PMEs) prints one enzyme-label column followed by three numeric columns whose heads are kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1) in that printed order. The cited cell set is Table III, enzyme row V198A: kcat (s^-1) = 68; Km (mM) = 0.06; kcat/Km (s^-1 mM^-1) = 1133.

normalized_value_unit_evidence: kcat: printed Table III cell 68 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 68.0 s^(-1). Km: printed Table III cell 0.06 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.06 mM. kcat/Km: printed Table III cell 1133 s-1 mM-1; the printed column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 1133.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, enzyme row V198A: kcat = 68 s-1; Km = 0.06 mM; printed kcat/Km = 1133 s-1 mM-1.

row_label: Table III, enzyme row V198A


substrate_name: n n n n n n H2O; Pectin

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0C1A8 REST FASTA plus single-substitution reconstruction and applied mutation signature Q177A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pectinesterase(Enzyme) mutant Q177A

substrate: n n n n n n H2O; Pectin


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0C1A8 and applied mutation signature M306A to reconstruct the assayed variant sequence.

column_label: Table III (Steady-state kinetic analyses of mutant PMEs) prints one enzyme-label column followed by three numeric columns whose heads are kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1) in that printed order. The cited cell set is Table III, enzyme row M306A: kcat (s^-1) = 59; Km (mM) = 0.53; kcat/Km (s^-1 mM^-1) = 111.

normalized_value_unit_evidence: kcat: printed Table III cell 59 s-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 59.0 s^(-1). Km: printed Table III cell 0.53 mM; the printed column is already in mM, so no unit conversion applies and the paper value is 0.53 mM. kcat/Km: printed Table III cell 111 s-1 mM-1; the printed column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 111.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, enzyme row M306A: kcat = 59 s-1; Km = 0.53 mM; printed kcat/Km = 111 s-1 mM-1.

row_label: Table III, enzyme row M306A


enzyme_display_name: histidinol-phosphatase

organism: Lactococcus lactis subsp. lactis

substrate_name: L-histidinol phosphate

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

enzyme: histidinol-phosphatase

substrate: L-histidinol phosphate


sequence_source: UniProtKB Q02150 direct FASTA lookup

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


proof_lines:
at pH 9.0 and 22°C
Raw SKiD Env: Temp=22°C, pH=9


sequence_variant_note: Resolved canonical sequence from UniProtKB P0C1A8 direct accession lookup; V198A reconstructed from canonical residue 198. and applied mutation signature V198A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pectinesterase(Enzyme) mutant V198A


organism: Linum usitatissimum

substrate_name: citrus pectin

sequence_source: UniProtKB Q94FS6 direct accession lookup

proof_lines:
pH 7.5, neutral isoform
pH 7.5, very basic isoform, i.e. luPME5
pH 7.5, basic isoform

substrate: citrus pectin


organism: Prunus armeniaca

sequence_source: UniProtKB A0A0N9LQL8 direct accession lookup


organism: Vigna radiata

substrate_name: Unknown

ki_unit: mM

sequence_source: UniProtKB Q9M5J0 direct accession lookup

substrate: Unknown


substrate_name: L-histidinol 1-phosphate

sequence_source: UniProtKB Q6NPM8 direct accession lookup

substrate: L-histidinol 1-phosphate


organism: Corynebacterium glutamicum

sequence_source: UniProtKB Q8NS80 direct accession lookup

proof_lines:
pH 7.4, 30°C
pH 7.4, 30°C, Hill coefficient 1.47


sequence_source: UniProtKB reviewed Q4WAW7 / FTMB_ASPFU direct REST and FASTA check on 2026-06-11

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


substrate_name: cyclo-(L-Trp-L-His)

substrate: cyclo-(L-Trp-L-His)


substrate_name: brevianamide F

substrate: brevianamide F


substrate_name: cyclo-(D-Trp-L-Ala)

substrate: cyclo-(D-Trp-L-Ala)


substrate_name: cyclo-(L-Trp-L-Tyr)

substrate: cyclo-(L-Trp-L-Tyr)


substrate_name: cyclo-(L-Trp-L-Ala)

substrate: cyclo-(L-Trp-L-Ala)


substrate_name: cyclo-(L-Trp-D-Ala)

substrate: cyclo-(L-Trp-D-Ala)


substrate_name: cyclo-(D-Trp-D-Pro)

substrate: cyclo-(D-Trp-D-Pro)


sequence_source: UniProtKB:Q02150 direct REST lookup on 2026-06-11 provided the canonical sequence only.


organism: Medicago truncatula

sequence_source: UniProtKB:G7J7Q5 direct REST lookup on 2026-06-11.

proof_lines:
pH 8.4, 22°C
Raw SKiD Env: Temp=22°C, pH=8.4


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P95189 direct REST lookup on 2026-06-11.

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


enzyme_display_name: sphingomyelin phosphodiesterase

organism: Bacillus cereus

substrate_name: H2O; Arachidoyllysophosphatidylcholine

enzyme: sphingomyelin phosphodiesterase

substrate: H2O; Arachidoyllysophosphatidylcholine


substrate_name: Palmitoyllysophosphatidylcholine; H2O

substrate: Palmitoyllysophosphatidylcholine; H2O


substrate_name: Myristoyllysophosphatidylcholine; H2O

substrate: Myristoyllysophosphatidylcholine; H2O


organism: Homo sapiens

substrate_name: CDP-choline

assay_conditions_summary: pH 5; 310.15 K; cofactor ATP

proof_lines:
at pH 5.0 and 37°C
Raw SKiD Env: Temp=37°C, pH=5

substrate: CDP-choline


organism: Mus musculus

substrate_name: sphingomyelin

sequence_source: UniProtKB direct accession lookup Q9JJY3 on 2026-06-11

proof_lines: 37°C, pH 7.4, recombinant nSMase2 in yeast microsomes

substrate: sphingomyelin


substrate_name: Sphingomyelin; H2O

sequence_source: UniProtKB direct accession lookup P9WKQ1 on 2026-06-11

substrate: Sphingomyelin; H2O


organism: Rattus norvegicus

substrate_name: H2O; Sphingomyelin

substrate: H2O; Sphingomyelin


sequence_source: UniProtKB direct accession lookup Q5XIA6 on 2026-06-11


enzyme_display_name: alpha-D-xyloside xylohydrolase

organism: Bacteroides ovatus

substrate_name: XLLG

sequence_source: UniProtKB direct accession lookup A7LXT0 on 2026-06-11

assay_conditions_summary: pH 7.6; 310.15 K; buffer and pH optimum

column_label: Extended Data Table ED1; row Bo GH31A / XLLG; columns k cat (s -1 ), K m (mM), and same-row kcat/Km quotient; raw kcat 31.0 ± 1.9; raw Km 0.378 ± 0.075.

row_label: Bo GH31A / XLLG

table_label: Extended Data Table ED1: Summary of kinetic analyses of XyGUL glycoside hydrolases

enzyme: alpha-D-xyloside xylohydrolase

substrate: XLLG


substrate_name: p-Nitrophenol alpha-D-glucopyranoside

assay_conditions_summary: pH 6; 310.15 K; buffer and pH optimum

column_label: Extended Data Table ED1; row Bo GH31A / Glc-α-PNP; columns k cat (s -1 ), K m (mM), and same-row kcat/Km quotient; raw kcat 0.071 ± 0.015; raw Km 31.8 ± 5.1.

row_label: Bo GH31A / Glc-α-PNP

substrate: p-Nitrophenol alpha-D-glucopyranoside


substrate_name: H2O; Palmitoyllysophosphatidylcholine

substrate: H2O; Palmitoyllysophosphatidylcholine


sequence_source: UniProt REST FASTA for Q9NXE4 checked 2026-06-11


substrate_name: ATP

substrate: ATP


substrate_name: ADP

assay_conditions_summary: pH 5; 310.15 K; cofactor ADP

substrate: ADP


substrate_name: CDP-ethanolamine

substrate: CDP-ethanolamine


substrate_name: ADP-ribose

substrate: ADP-ribose


substrate_name: Isoprimeverose

sequence_source: UniProtKB:A7LXT0 canonical sequence, checked 2026-06-11

column_label: Extended Data Table ED1; row Bo GH31A / Isoprimeverose; columns k cat (s -1 ), K m (mM), and same-row kcat/Km quotient; raw kcat 1.78 ± 0.21; raw Km 38.1 ± 7.1.

raw_value_unit_evidence: kcat 1.78 ± 0.21 s^-1; Km 38.1 ± 7.1 mM; same-row kcat/Km derived as 1.78 / 38.1.

row_label: Bo GH31A / Isoprimeverose

substrate: Isoprimeverose


substrate_name: p-Nitrophenol alpha-D-xylopyranoside

column_label: Extended Data Table ED1; row Bo GH31A / Xyl-α-PNP; columns k cat (s -1 ), K m (mM), and same-row kcat/Km quotient; raw kcat 1.60 ± 0.031; raw Km 7.7 ± 0.273.

raw_value_unit_evidence: kcat 1.60 ± 0.031 s^-1; Km 7.7 ± 0.273 mM; same-row kcat/Km derived as 1.6 / 7.7.

row_label: Bo GH31A / Xyl-α-PNP

substrate: p-Nitrophenol alpha-D-xylopyranoside


substrate_name: XXXG

column_label: Extended Data Table ED1; row label: BoGH31A / XXXG; column label: kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1), Assay; raw value: 32.6 +/- 2.1, 0.223 +/- 0.046, and 146.2; raw unit: s^-1, mM, and s^-1 mM^-1; normalized value: 32.6 s^-1, 0.223 mM, and 146.2 s^-1 mM^-1; assay HPLC; condition: 37 C in 50 mM buffer at or near the BoGH31A pH optimum with HPAEC-PAD analysis.

normalized_value_unit_evidence: kcat normalized_value=32.6 normalized_unit=s^(-1); Km normalized_value=0.223 normalized_unit=mM; kcat/Km normalized_value=146.2 normalized_unit=s^(-1)*mM^(-1).

raw_value_unit_evidence: Extended Data Table ED1 BoGH31A XXXG cells: kcat raw_value=32.6 +/- 2.1 raw_unit=s^-1; Km raw_value=0.223 +/- 0.046 raw_unit=mM; kcat/Km raw_value=146.2 raw_unit=s^-1 mM^-1; assay HPLC.

row_label: BoGH31A / XXXG

table_label: Extended Data Table ED1. Summary of kinetic analyses of XyGUL glycoside hydrolases

substrate: XXXG


organism: Cellvibrio japonicus

sequence_source: UniProtKB:B3PBD9 canonical sequence, checked 2026-06-11


source_db: brenda;skid

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

source: brenda;skid


organism: Escherichia coli

sequence_source: UniProtKB:P31434 canonical sequence, checked 2026-06-11


organism: Sulfolobus solfataricus

substrate_name: 4-Nitrophenyl alpha-D-xyloside

substrate: 4-Nitrophenyl alpha-D-xyloside


substrate_name: Maltotriose

substrate: Maltotriose


substrate_name: p-Nitrophenyl-alpha-D-glucoside

substrate: p-Nitrophenyl-alpha-D-glucoside


substrate_name: Maltose

substrate: Maltose


substrate_name: H2O; Maltose

substrate: H2O; Maltose


organism: uncultured microorganism

substrate_name: 4-nitrophenyl alpha-D-xylopyranoside

substrate: 4-nitrophenyl alpha-D-xylopyranoside


substrate_name: L-histidinol phosphate

sequence_variant_note: Resolved canonical sequence from UniProt Q02150 canonical sequence; RCSB 4GC3/4GK8 construct coordinate offset -2; PMID 23327428 Table 2 mutation row and applied mutation signature H42N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: L-histidinol phosphate


sequence_variant_note: Resolved canonical sequence from UniProt Q02150 canonical sequence; RCSB 4GC3/4GK8 construct coordinate offset -2; PMID 23327428 Table 2 mutation row and applied mutation signature R160M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q02150 canonical sequence; RCSB 4GC3/4GK8 construct coordinate offset -2; PMID 23327428 Table 2 mutation row and applied mutation signature Y157F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q02150 canonical sequence; RCSB 4GC3/4GK8 construct coordinate offset -2; PMID 23327428 Table 2 mutation row and applied mutation signature Y117A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q02150 canonical sequence; RCSB 4GC3/4GK8 construct coordinate offset -2; PMID 23327428 Table 2 mutation row and applied mutation signature D228N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q02150 canonical sequence; RCSB 4GC3/4GK8 construct coordinate offset -2; PMID 23327428 Table 2 mutation row and applied mutation signature Y161F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q02150 canonical sequence; RCSB 4GC3/4GK8 construct coordinate offset -2; PMID 23327428 Table 2 mutation row and applied mutation signature R197M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme HY157F, at pH 9.0 and 22°C


enzyme_display_name: flavonol 3-sulfotransferase

organism: Flaveria chloraefolia

substrate_name: 3'-Phosphoadenylyl sulfate; Quercetin

proof_lines: SABIO-RK modifier species: flavonol 3-sulfotransferase(Enzyme) mutant K277R

enzyme: flavonol 3-sulfotransferase

substrate: 3'-Phosphoadenylyl sulfate; Quercetin


substrate_name: 3'-Phosphoadenylyl sulfate

substrate: 3'-Phosphoadenylyl sulfate


sequence_variant_note: Resolved canonical sequence from UniProtKB P52836 FASTA direct lookup on 2026-06-11; K59R reconstructed from the canonical sequence. and applied mutation signature K59R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: flavonol 3-sulfotransferase(Enzyme) mutant K59R


substrate_name: quercetin

substrate: quercetin


substrate_name: Quercetin; 3'-Phosphoadenylyl sulfate

proof_lines: SABIO-RK modifier species: flavonol 3-sulfotransferase(Enzyme) mutant G281A

substrate: Quercetin; 3'-Phosphoadenylyl sulfate


sequence_source: UniProtKB:P52836 reviewed canonical sequence


substrate_name: Rhamnetin

substrate: Rhamnetin


substrate_name: isorhamnetin

substrate: isorhamnetin


proof_lines: SABIO-RK modifier species: flavonol 3-sulfotransferase(Enzyme) mutant K101

proof_lines: SABIO-RK modifier species: flavonol 3-sulfotransferase(Enzyme) mutant c111

proof_lines: SABIO-RK modifier species: flavonol 3-sulfotransferase(Enzyme) mutant K118


substrate_name: kaempferol

substrate: kaempferol


substrate_name: H2O; L-Histidinol phosphate

proof_lines: SABIO-RK modifier species: histidinol-phosphatase(Enzyme) mutant N-terminal domain (residues 3-166) fused to MGSS(H)6GS

substrate: H2O; L-Histidinol phosphate


substrate_name: HisB-N; Mg2+

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

substrate: HisB-N; Mg2+


organism: Lactococcus lactis subsp. lactis

sequence_variant_note: Resolved canonical sequence from uniprot:Q02150 and applied mutation signature Y117F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q02150 and applied mutation signature R160M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q02150 and applied mutation signature Y161F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q02150 and applied mutation signature E115Q with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q02150 and applied mutation signature Y161A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q02150 and applied mutation signature H42N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


substrate_name: alpha-D-xylopyranosyl fluoride

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

substrate: alpha-D-xylopyranosyl fluoride


proof_lines: pH 7.0, 37°C, mechanism-based inactivator


enzyme_display_name: endopeptidase La

organism: Thermoplasma acidophilum

substrate_name: H2O; ATP

enzyme: endopeptidase La

substrate: H2O; ATP


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q9HJ89 and applied mutation signature K568A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: endopeptidase La(Enzyme) mutant K568A


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q9HJ89 and applied mutation signature S525A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: endopeptidase La(Enzyme) mutant S525A


organism: Pseudomonas sp. ADP

substrate_name: ammelide

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:O52063 and applied mutation signature D303N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 301.15 K; cofactor ADP

substrate: ammelide


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:O52063 and applied mutation signature D303A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:O52063 and applied mutation signature K65A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O52063 and applied mutation signature K65R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 301.15 K; buffer 200 mM sodium phosphate; cofactor ADP

column_label: Table 2 (Steady state kinetic characterization of AtzC and its variants), body row 'K65R'; column 'k cat (s-1)' = 332.3; column 'K M (mM)' = 2.4; column 'K cat/K M (s-1.M-1)' = 1.4 x 10^5. The uncertainty printed beside the k cat and K M cells of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 332.3 in a column headed k cat (s-1); s-1 is already the canonical s^-1, so no conversion is applied and the value is 332.3 s^(-1). Km: printed Table 2 cell 2.4 in a column headed K M (mM); mM is already canonical, so no conversion is applied and the value is 2.4 mM. kcat/Km: printed Table 2 cell 1.4 x 10^5 in a column headed K cat/K M (s-1.M-1), that is 140000 s^(-1)*M^(-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 140000 / 1000 = 140 s^-1 mM^-1. The exported values are kcat 332.2 s^(-1), Km 2.4 mM and kcat_over_km 138.41666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'K65R': k cat = 332.3 s-1; K M = 2.4 mM; printed K cat/K M = 1.4 x 10^5 in a column headed (s-1.M-1), that is 140000 s^(-1)*M^(-1).

row_label: Table 2, row K65R

table_label: Table 2: Steady state kinetic characterization of AtzC and its variants. NDA: no detectable activity. Printed column heads: Variant; k cat (s-1); K M (mM); K cat/K M (s-1.M-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O52063 and applied mutation signature N304A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady state kinetic characterization of AtzC and its variants), body row 'N304A'; column 'k cat (s-1)' = 29.3; column 'K M (mM)' = 4.2; column 'K cat/K M (s-1.M-1)' = 7.0 x 10^3. The uncertainty printed beside the k cat and K M cells of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 29.3 in a column headed k cat (s-1); s-1 is already the canonical s^-1, so no conversion is applied and the value is 29.3 s^(-1). Km: printed Table 2 cell 4.2 in a column headed K M (mM); mM is already canonical, so no conversion is applied and the value is 4.2 mM. kcat/Km: printed Table 2 cell 7.0 x 10^3 in a column headed K cat/K M (s-1.M-1), that is 7000 s^(-1)*M^(-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7000 / 1000 = 7 s^-1 mM^-1. The exported values are kcat 29.3 s^(-1), Km 4.2 mM and kcat_over_km 6.976190476190476 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'N304A': k cat = 29.3 s-1; K M = 4.2 mM; printed K cat/K M = 7.0 x 10^3 in a column headed (s-1.M-1), that is 7000 s^(-1)*M^(-1).

row_label: Table 2, row N304A


sequence_source: UniProtKB:P31434 reviewed canonical sequence fetched 2026-06-11


substrate_name: Isoprimeverose

substrate: Isoprimeverose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9M0 reviewed canonical sequence plus direct K722A reconstruction fetched/computed 2026-06-11 and applied mutation signature K722A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: endopeptidase La(Enzyme) mutant K722A


substrate_name: ATP; H2O

sequence_source: UniProtKB:P0A9M0 reviewed canonical sequence fetched 2026-06-11

substrate: ATP; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9M0 reviewed canonical sequence plus direct S679A reconstruction fetched/computed 2026-06-11 and applied mutation signature S679A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: endopeptidase La(Enzyme) mutant S679A


substrate_name: FRETN 89-98

sequence_source: UniProtKB:P36776 reviewed canonical sequence fetched 2026-06-11

substrate: FRETN 89-98


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O52063 and applied mutation signature N304D to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady state kinetic characterization of AtzC and its variants), PDF page 11 of 15. Variant row N304D; column kcat (s-1) cell = 189.0; column KM (mM) cell = 25.0; column Kcat/KM (s-1.M-1) cell = 7.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 189.0 s-1; the printed unit is already canonical, so kcat = 189.0 s^(-1); the exported value is 189.0 s^(-1), identical. Km: printed Table 2 cell 25.0 mM; the printed unit is already canonical, so Km = 25.0 mM; the exported value is 25.0 mM, identical. kcat/Km: printed Table 2 cell 7.6 x 10^3 under the printed column head Kcat/KM (s-1.M-1), i.e. 7600 s^(-1)*M^(-1); 1 M^(-1) = 1/1000 mM^(-1), so the printed cell is 7600 / 1000 = 7.6 s^(-1)*mM^(-1); the exported value is 7600 s^(-1)*mM^(-1), which is the printed number carried over without the M-to-mM conversion.

raw_value_unit_evidence: Table 2, PDF page 11 of 15, variant row N304D: kcat cell = 189.0 s-1; KM cell = 25.0 mM; Kcat/KM cell = 7.6 x 10^3 under the printed column head Kcat/KM (s-1.M-1), i.e. 7600 s^(-1)*M^(-1).

table_label: Table 2. Steady state kinetic characterization of AtzC and its variants. NDA: no detectable activity. Printed column heads: Variant; kcat (s-1); KM (mM); Kcat/KM (s-1.M-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O52063 and applied mutation signature H219A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady state kinetic characterization of AtzC and its variants), PDF page 11 of 15. Variant row H219A; column kcat (s-1) cell = 16.8; column KM (mM) cell = 1.6; column Kcat/KM (s-1.M-1) cell = 1.1 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 16.8 s-1; the printed unit is already canonical, so kcat = 16.8 s^(-1); the exported value is 16.8 s^(-1), identical. Km: printed Table 2 cell 1.6 mM; the printed unit is already canonical, so Km = 1.6 mM; the exported value is 1.6 mM, identical. kcat/Km: printed Table 2 cell 1.1 x 10^4 under the printed column head Kcat/KM (s-1.M-1), i.e. 11000 s^(-1)*M^(-1); 1 M^(-1) = 1/1000 mM^(-1), so the printed cell is 11000 / 1000 = 11 s^(-1)*mM^(-1); the exported value is 11000 s^(-1)*mM^(-1), which is the printed number carried over without the M-to-mM conversion.

raw_value_unit_evidence: Table 2, PDF page 11 of 15, variant row H219A: kcat cell = 16.8 s-1; KM cell = 1.6 mM; Kcat/KM cell = 1.1 x 10^4 under the printed column head Kcat/KM (s-1.M-1), i.e. 11000 s^(-1)*M^(-1).


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O52063 and applied mutation signature Q160A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady state kinetic characterization of AtzC and its variants), PDF page 11 of 15. Variant row Q160A; column kcat (s-1) cell = 23.0; column KM (mM) cell = 1.8; column Kcat/KM (s-1.M-1) cell = 1.3 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 23.0 s-1; the printed unit is already canonical, so kcat = 23.0 s^(-1); the exported value is 23.0 s^(-1), identical. Km: printed Table 2 cell 1.8 mM; the printed unit is already canonical, so Km = 1.8 mM; the exported value is 1.8 mM, identical. kcat/Km: printed Table 2 cell 1.3 x 10^4 under the printed column head Kcat/KM (s-1.M-1), i.e. 13000 s^(-1)*M^(-1); 1 M^(-1) = 1/1000 mM^(-1), so the printed cell is 13000 / 1000 = 13 s^(-1)*mM^(-1); the exported value is 13000 s^(-1)*mM^(-1), which is the printed number carried over without the M-to-mM conversion.

raw_value_unit_evidence: Table 2, PDF page 11 of 15, variant row Q160A: kcat cell = 23.0 s-1; KM cell = 1.8 mM; Kcat/KM cell = 1.3 x 10^4 under the printed column head Kcat/KM (s-1.M-1), i.e. 13000 s^(-1)*M^(-1).


row_label: Table 2, PDF page 11 of 15, variant row Q160A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O52063 and applied mutation signature D303A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady state kinetic characterization of AtzC and its variants), PDF page 11 of 15. Variant row D303A; column kcat (s-1) cell = 35.8; column KM (mM) cell = 1.7; column Kcat/KM (s-1.M-1) cell = 2.1 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 35.8 s-1; the printed unit is already canonical, so kcat = 35.8 s^(-1); the exported value is 35.8 s^(-1), identical. Km: printed Table 2 cell 1.7 mM; the printed unit is already canonical, so Km = 1.7 mM; the exported value is 1.7 mM, identical. kcat/Km: printed Table 2 cell 2.1 x 10^4 under the printed column head Kcat/KM (s-1.M-1), i.e. 21000 s^(-1)*M^(-1); 1 M^(-1) = 1/1000 mM^(-1), so the printed cell is 21000 / 1000 = 21 s^(-1)*mM^(-1); the exported value is 21000 s^(-1)*mM^(-1), which is the printed number carried over without the M-to-mM conversion.

raw_value_unit_evidence: Table 2, PDF page 11 of 15, variant row D303A: kcat cell = 35.8 s-1; KM cell = 1.7 mM; Kcat/KM cell = 2.1 x 10^4 under the printed column head Kcat/KM (s-1.M-1), i.e. 21000 s^(-1)*M^(-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O52063 and applied mutation signature D188N to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady state kinetic characterization of AtzC and its variants), PDF page 11 of 15. Variant row D188N; column kcat (s-1) cell = 14.1; column KM (mM) cell = 1.9; column Kcat/KM (s-1.M-1) cell = 7.4 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 14.1 s-1; the printed unit is already canonical, so kcat = 14.1 s^(-1); the exported value is 14.1 s^(-1), identical. Km: printed Table 2 cell 1.9 mM; the printed unit is already canonical, so Km = 1.9 mM; the exported value is 1.9 mM, identical. kcat/Km: printed Table 2 cell 7.4 x 10^3 under the printed column head Kcat/KM (s-1.M-1), i.e. 7400 s^(-1)*M^(-1); 1 M^(-1) = 1/1000 mM^(-1), so the printed cell is 7400 / 1000 = 7.4 s^(-1)*mM^(-1); the exported value is 7400 s^(-1)*mM^(-1), which is the printed number carried over without the M-to-mM conversion.

raw_value_unit_evidence: Table 2, PDF page 11 of 15, variant row D188N: kcat cell = 14.1 s-1; KM cell = 1.9 mM; Kcat/KM cell = 7.4 x 10^3 under the printed column head Kcat/KM (s-1.M-1), i.e. 7400 s^(-1)*M^(-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O52063 and applied mutation signature W309A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady state kinetic characterization of AtzC and its variants), PDF page 11 of 15. Variant row W309A; column kcat (s-1) cell = 42.4; column KM (mM) cell = 5.6; column Kcat/KM (s-1.M-1) cell = 7.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 42.4 s-1; the printed unit is already canonical, so kcat = 42.4 s^(-1); the exported value is 42.4 s^(-1), identical. Km: printed Table 2 cell 5.6 mM; the printed unit is already canonical, so Km = 5.6 mM; the exported value is 5.6 mM, identical. kcat/Km: printed Table 2 cell 7.6 x 10^3 under the printed column head Kcat/KM (s-1.M-1), i.e. 7600 s^(-1)*M^(-1); 1 M^(-1) = 1/1000 mM^(-1), so the printed cell is 7600 / 1000 = 7.6 s^(-1)*mM^(-1); the exported value is 7600 s^(-1)*mM^(-1), which is the printed number carried over without the M-to-mM conversion.

raw_value_unit_evidence: Table 2, PDF page 11 of 15, variant row W309A: kcat cell = 42.4 s-1; KM cell = 5.6 mM; Kcat/KM cell = 7.6 x 10^3 under the printed column head Kcat/KM (s-1.M-1), i.e. 7600 s^(-1)*M^(-1).


enzyme_display_name: mRNA (guanine-N(7))-methyltransferase

organism: Chikungunya virus

substrate_name: S-adenosyl-L-methionine

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

enzyme: mRNA (guanine-N(7))-methyltransferase

substrate: S-adenosyl-L-methionine


substrate_name: GTP

substrate: GTP


enzyme_display_name: mRNA cap guanine-N(7) methyltransferase

organism: Encephalitozoon cuniculi

substrate_name: GTP; S-Adenosyl-L-methionine

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:Q8SR66 direct REST lookup on 2026-06-11

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

source_databases_merged: sabio_rk brenda skid

enzyme: mRNA cap guanine-N(7) methyltransferase

substrate: GTP; S-Adenosyl-L-methionine


sequence_source: UniProtKB:O43148 direct REST lookup on 2026-06-11


enzyme_display_name: Flavonol 3-sulfotransferase

substrate_name: Rhamnetin; 3'-Phosphoadenylyl sulfate

sequence_source: UniProtKB:P52836 direct REST lookup on 2026-06-11

enzyme: Flavonol 3-sulfotransferase

substrate: Rhamnetin; 3'-Phosphoadenylyl sulfate


substrate_name: quercetin

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P52836 canonical sequence by applying selected mutation_signature K59R after direct residue check on 2026-06-11 and applied mutation signature K59R to reconstruct the assayed variant sequence.

substrate: quercetin


substrate_name: Quercetin; 3'-Phosphoadenylyl sulfate

proof_lines: SABIO-RK modifier species: flavonol 3-sulfotransferase(Enzyme) mutant K284R

substrate: Quercetin; 3'-Phosphoadenylyl sulfate


substrate_name: 3'-Phosphoadenylyl sulfate

sequence_source: UniProtKB:P52836 direct REST lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:P52836 direct REST lookup and applied mutation signature G281A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: 3'-Phosphoadenylyl sulfate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P52836 direct REST lookup and applied mutation signature K284G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: flavonol 3-sulfotransferase(Enzyme) mutant K284G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P52836 direct REST lookup and applied mutation signature K277G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: flavonol 3-sulfotransferase(Enzyme) mutant K277G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P52836 direct REST lookup and applied mutation signature K59R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P52836 direct REST lookup and applied mutation signature K284R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O52063 canonical sequence with row-specific mutation reconstruction and applied mutation signature K65R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 301.00 K; buffer 200 mM sodium phosphate; cofactor ADP


sequence_source: UniProtKB O52063 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB O52063 canonical sequence with row-specific mutation reconstruction and applied mutation signature W309F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O52063 canonical sequence with row-specific mutation reconstruction and applied mutation signature D188A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O52063 canonical sequence with row-specific mutation reconstruction and applied mutation signature Q160R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 301.00 K; cofactor ADP


sequence_variant_note: Resolved canonical sequence from UniProtKB O52063 canonical sequence with row-specific mutation reconstruction and applied mutation signature N304D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O52063 canonical sequence with row-specific mutation reconstruction and applied mutation signature H219A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O52063 canonical sequence with row-specific mutation reconstruction and applied mutation signature W309A to reconstruct the assayed variant sequence.


enzyme_display_name: (d)CTP diphosphatase

substrate_name: H2O; CTP

sequence_source: UniProtKB:P77788 direct accession lookup on 2026-06-11

enzyme: (d)CTP diphosphatase

substrate: H2O; CTP


substrate_name: dCTP

substrate: dCTP


substrate_name: CTP

substrate: CTP


enzyme_display_name: XTP/dITP diphosphatase

organism: Arabidopsis thaliana

substrate_name: dITP

sequence_source: UniProtKB:Q8L968 direct accession lookup on 2026-06-11

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

enzyme: XTP/dITP diphosphatase

substrate: dITP


substrate_name: ITP

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9BY32 direct accession lookup plus R178S reconstruction on 2026-06-11 and applied mutation signature R178S to reconstruct the assayed variant sequence.

proof_lines: pH not specified in the publication, 37°C, recombinant mutant R178S

substrate: ITP


sequence_source: UniProtKB:Q9BY32 direct accession lookup on 2026-06-11

proof_lines: pH not specified in the publication, 37°C, recombinant wild-type enzyme


enzyme_display_name: diacylglycerol O-acyltransferase

organism: Acinetobacter baylyi ADP1

substrate_name: palmitoyl-CoA

sequence_source: UniProt REST direct accession lookup for Q8GGG1

assay_conditions_summary: pH 7.4; 308.15 K; cofactor CoA

proof_lines:
pH 7.4, 35°C
Raw SKiD Env: Temp=35°C, pH=7.4

enzyme: diacylglycerol O-acyltransferase

substrate: palmitoyl-CoA


organism: Acinetobacter calcoaceticus

substrate_name: 1,2-Dipalmitoyl glycerol; Palmitoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: 1,2-Dipalmitoyl glycerol; Palmitoyl-CoA


organism: Brassica napus

substrate_name: oleoyl-CoA

sequence_source: UniProt REST direct accession lookup for K9LL63

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

proof_lines: pH 7.4, 30°C, recombinant full-length wild-type enzyme

substrate: oleoyl-CoA


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

proof_lines: pH 7.4, 30°C, recombinant truncated enzyme mutant BnaDGAT181-501


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession lookup for Q9M4V2 and applied mutation signature I447F to reconstruct the assayed variant sequence.


sequence_source: UniProt REST direct accession lookup for Q9M4V2

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

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


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession lookup for Q9M4V2 and applied mutation signature F449C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession lookup for Q9M4V2 and applied mutation signature V125F to reconstruct the assayed variant sequence.


substrate_name: 3-Dehydro-L-gulonate 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature E112A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'E112A'; column 'kcat (s-1)' = 0.3; column 'KM (M)' = 3.4 x 10^-4; column 'kcat/KM (M-1 s-1)' = 8.8 x 10^2. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.3 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 0.3 s^(-1). Km: printed Table 1 cell 3.4 x 10^-4 M; 1 M is 1000 mM, so 3.4 x 10^-4 x 1000 = 0.34 mM. kcat/Km: printed Table 1 cell 8.8 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.8 x 10^2 / 1000 = 0.88 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'E112A': kcat = 0.3 s-1; KM = 3.4 x 10^-4 M; printed kcat/KM = 8.8 x 10^2 M-1 s-1.

row_label: Table 1, printed row 'E112A' (the mutant E112A entry of the single kinetic table in this article)

substrate: 3-Dehydro-L-gulonate 6-phosphate


substrate_name: 3-Dehydro-L-gulonate 6-phosphate; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 direct accession check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature R139V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-dehydro-L-gulonate-6-phosphate decarboxylase(Enzyme) mutant R139V

substrate: 3-Dehydro-L-gulonate 6-phosphate; H+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39304 and applied mutation signature K64A/E112A/H136A/R139V to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'K64A/E112A/H136A/R139V'; column 'kcat (s-1)' = 0.26; column 'KM (M)' = 1.4 x 10^-3; column 'kcat/KM (M-1 s-1)' = 1.9 x 10^2. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.26 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 0.26 s^(-1). Km: printed Table 1 cell 1.4 x 10^-3 M; 1 M is 1000 mM, so 1.4 x 10^-3 x 1000 = 1.4 mM. kcat/Km: printed Table 1 cell 1.9 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^2 / 1000 = 0.19 s^(-1)*mM^(-1).

row_label: Table 1, printed row 'K64A/E112A/H136A/R139V' (the mutant K64A/E112A/H136A/R139V entry of the single kinetic table in this article)