sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WPA3 canonical sequence with D32E reconstructed during review and applied mutation signature D32E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C


enzyme_display_name: dephospho-CoA kinase

organism: Mycobacterium tuberculosis

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature R140K to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, DCoA span, enzyme row R140K: Km(uM) = 181; Kcat (min^-1) = 0.453; Kcat/Km (uM^-1 min^-1) = 0.00250.

normalized_value_unit_evidence: Km: printed Table 2 DCoA-span cell 181 uM; 181 / 1000 = 0.181 mM. kcat: printed Table 2 DCoA-span cell 0.453 min^-1; 0.453 / 60 = 0.00755 s^(-1). kcat/Km: printed Table 2 DCoA-span cell 0.00250 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.00250 x 1000 / 60 = 0.04166666666666667 s^(-1)*mM^(-1). The exported values of this row are kcat 0.0076, kcat_over_km 0.041988950276243095, km 0.181; the metrics this record corrects are kcat, kcat_over_km.

raw_value_unit_evidence: Table 2, DCoA span, enzyme row R140K: Km = 181 uM; Kcat = 0.453 min^-1; printed Kcat/Km = 0.00250 uM^-1 min^-1.

row_label: Table 2, DCoA block, enzyme row R140K

table_label: Table 2: Kinetic parameters of the wild type and mutant mycobacterial dephosphocoenzyme A kinases (nr- no reaction; nd-not determined) (PLoS One 2011)

data_origin: experimental

enzyme: dephospho-CoA kinase

status: corrected

source: oed


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature D32A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, ATP span, enzyme row D32A: Km(uM) = 57.5; Kcat (min^-1) = 0.84; Kcat/Km (uM^-1 min^-1) = 0.0146.

normalized_value_unit_evidence: Km: printed Table 2 ATP-span cell 57.5 uM; 57.5 / 1000 = 0.0575 mM. kcat: printed Table 2 ATP-span cell 0.84 min^-1; 0.84 / 60 = 0.013999999999999999 s^(-1). kcat/Km: printed Table 2 ATP-span cell 0.0146 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0146 x 1000 / 60 = 0.24333333333333335 s^(-1)*mM^(-1). The exported values of this row are kcat 0.014, kcat_over_km 0.2434782608695652, km 0.0575; the metrics this record corrects are kcat_over_km.

raw_value_unit_evidence: Table 2, ATP span, enzyme row D32A: Km = 57.5 uM; Kcat = 0.84 min^-1; printed Kcat/Km = 0.0146 uM^-1 min^-1.

row_label: Table 2, ATP block, enzyme row D32A

substrate: ATP


enzyme_display_name: beta-D-fucosidase

organism: Bifidobacterium breve

substrate_name: p-Nitrophenyl-beta-D-fucoside

mutation_signature: Unknown

sequence_source: UniProtKB:P94248 canonical sequence

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

enzyme: beta-D-fucosidase

substrate: p-Nitrophenyl-beta-D-fucoside


substrate_name: H2O; p-Nitrophenyl-beta-D-fucoside

kcat_over_km_display: Not reported

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

substrate: H2O; p-Nitrophenyl-beta-D-fucoside


organism: Haloferax volcanii

substrate_name: 2-nitrophenyl beta-D-galactoside

source_db: brenda

verification_status: unverified

kcat_display: Not reported

sequence_source: UniProtKB:P94804 checked but not accepted because of EC and organism contradiction

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

proof_lines: pH 7.2, 22°C, the enzyme also shows beta-fucosidase activity

substrate: 2-nitrophenyl beta-D-galactoside

status: unverified

source: brenda


organism: Putranjiva roxburghii

substrate_name: cellobiose

sequence_source: UniProtKB:A0A023MIF8 canonical sequence

proof_lines:
pH 4.6, 37°C, recombinant enzyme
pH 4.6, 37°C, native enzyme

substrate: cellobiose


enzyme_display_name: brevianamide F prenyltransferase (deoxybrevianamide E-forming)

organism: Aspergillus versicolor

substrate_name: cyclo-L-Trp-L-Phe

kcat_over_km_origin: calculated

sequence_source: UniProtKB REST direct accession lookup: I4AY86 / NOTF_ASPVE, reviewed entry, retrieved 2026-06-11.

substrate: cyclo-L-Trp-L-Phe


substrate_name: cyclo-D-Trp-D-Pro

enzyme: brevianamide F prenyltransferase (deoxybrevianamide E-forming)

substrate: cyclo-D-Trp-D-Pro


substrate_name: cyclo-L-Trp-D-Pro

substrate: cyclo-L-Trp-D-Pro


substrate_name: cyclo-D-Trp-L-Pro

substrate: cyclo-D-Trp-L-Pro


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature G8A to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, ATP span, enzyme row G8A: Km(uM) = 59.8; Kcat (min^-1) = 2.563; Kcat/Km (uM^-1 min^-1) = 0.0428.

normalized_value_unit_evidence: Km: printed Table 2 ATP-span cell 59.8 uM; 59.8 / 1000 = 0.0598 mM. kcat: printed Table 2 ATP-span cell 2.563 min^-1; 2.563 / 60 = 0.04271666666666667 s^(-1). kcat/Km: printed Table 2 ATP-span cell 0.0428 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0428 x 1000 / 60 = 0.7133333333333334 s^(-1)*mM^(-1). The exported values of this row are kcat 0.043, kcat_over_km 0.7190635451505016, km 0.0598; the metrics this record corrects are kcat, kcat_over_km.

raw_value_unit_evidence: Table 2, ATP span, enzyme row G8A: Km = 59.8 uM; Kcat = 2.563 min^-1; printed Kcat/Km = 0.0428 uM^-1 min^-1.

row_label: Table 2, ATP block, enzyme row G8A


sequence_source: UniProtKB REST direct accession lookup: P9WPA3 / COAE_MYCTU, reviewed entry, retrieved 2026-06-11.

proof_lines: wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C


column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, DCoA span, enzyme row WT: Km(uM) = 34.9; Kcat (min^-1) = 1.758; Kcat/Km (uM^-1 min^-1) = 0.0503.

normalized_value_unit_evidence: Km: printed Table 2 DCoA-span cell 34.9 uM; 34.9 / 1000 = 0.0349 mM. kcat: printed Table 2 DCoA-span cell 1.758 min^-1; 1.758 / 60 = 0.0293 s^(-1). kcat/Km: printed Table 2 DCoA-span cell 0.0503 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0503 x 1000 / 60 = 0.8383333333333334 s^(-1)*mM^(-1). The exported values of this row are kcat 0.0293, kcat_over_km 0.839541547277937, km 0.0349; the metrics this record corrects are kcat_over_km.

raw_value_unit_evidence: Table 2, DCoA span, enzyme row WT: Km = 34.9 uM; Kcat = 1.758 min^-1; printed Kcat/Km = 0.0503 uM^-1 min^-1.

row_label: Table 2, DCoA block, enzyme row WT


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature D32E to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, ATP span, enzyme row D32E: Km(uM) = 34.5; Kcat (min^-1) = 3.996; Kcat/Km (uM^-1 min^-1) = 0.1158.

normalized_value_unit_evidence: Km: printed Table 2 ATP-span cell 34.5 uM; 34.5 / 1000 = 0.0345 mM. kcat: printed Table 2 ATP-span cell 3.996 min^-1; 3.996 / 60 = 0.06659999999999999 s^(-1). kcat/Km: printed Table 2 ATP-span cell 0.1158 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.1158 x 1000 / 60 = 1.9300000000000002 s^(-1)*mM^(-1). The exported values of this row are kcat 0.067, kcat_over_km 1.9420289855072463, km 0.0345; the metrics this record corrects are kcat, kcat_over_km.

raw_value_unit_evidence: Table 2, ATP span, enzyme row D32E: Km = 34.5 uM; Kcat = 3.996 min^-1; printed Kcat/Km = 0.1158 uM^-1 min^-1.

row_label: Table 2, ATP block, enzyme row D32E


enzyme_display_name: squalene monooxygenase

organism: Rattus norvegicus

substrate_name: H+; O2; Squalene; NADPH

mutation_signature: Δ1

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

mutation_type: deletion

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) wildtype delta1-99, C-terminal His-tag

enzyme: squalene monooxygenase

substrate: H+; O2; Squalene; NADPH


substrate_name: Squalene; O2; H+; NADPH

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F523A delta1-99, C-terminal His-tag

substrate: Squalene; O2; H+; NADPH


substrate_name: NADPH; Squalene; O2; H+

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y528A delta1-99, C-terminal His-tag

substrate: NADPH; Squalene; O2; H+


substrate_name: H+; O2; NADPH; Squalene

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y209A delta1-99, C-terminal His-tag

substrate: H+; O2; NADPH; Squalene


substrate_name: NADPH; O2; Squalene; H+

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F223A delta1-99, C-terminal His-tag

substrate: NADPH; O2; Squalene; H+


proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F476A delta1-99, C-terminal His-tag


proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F228A delta1-99, C-terminal His-tag


substrate_name: NADPH; O2; H+; Squalene

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F491A delta1-99, C-terminal His-tag

substrate: NADPH; O2; H+; Squalene


organism: Homo sapiens

mutation_type: truncation

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) wildtype (aa 118–574), N-terminally truncated and N-terminal His-tag


substrate_name: O2; H+; Squalene; NADPH

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y194A delta1-99, C-terminal His-tag

substrate: O2; H+; Squalene; NADPH


substrate_name: O2; NADPH; H+; Squalene

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y493A delta1-99, C-terminal His-tag

substrate: O2; NADPH; H+; Squalene


substrate_name: Squalene; O2; NADPH; H+

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y334A delta1-99, C-terminal His-tag

substrate: Squalene; O2; NADPH; H+


proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y473A delta1-99, C-terminal His-tag


substrate_name: H+; NADPH; O2; Squalene

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F522A delta1-99, C-terminal His-tag

substrate: H+; NADPH; O2; Squalene


substrate_name: H+; Squalene; NADPH; O2

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F305A delta1-99, C-terminal His-tag

substrate: H+; Squalene; NADPH; O2


substrate_name: NADPH; H+; Squalene; O2

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F287A delta1-99, C-terminal His-tag

substrate: NADPH; H+; Squalene; O2


enzyme_display_name: linoleate 8R-lipoxygenase

organism: Colletotrichum gloeosporioides

substrate_name: palmitoleate

sequence_source: EBI Proteins API / UniProt accession A0A0S2SWE4

smiles: CCCCCC/C=C\CCCCCCCC(=O)O

enzyme: linoleate 8R-lipoxygenase

substrate: palmitoleate


substrate_name: oleate

smiles: CCCCCCCC/C=C\CCCCCCCC(=O)O

substrate: oleate


organism: Gaeumannomyces graminis

substrate_name: Linoleate; O2

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

sequence_source: EBI Proteins API / UniProt accession Q9UUS2

substrate: Linoleate; O2


organism: Candida albicans

substrate_name: H+; Squalene; NADH; O2

sequence_source: EBI Proteins API / UniProt accession Q92206

assay_conditions_summary: cofactor NADH

substrate: H+; Squalene; NADH; O2


substrate_name: Squalene

sequence_source: EBI Proteins API / UniProt accession Q14534

substrate: Squalene


assay_conditions_summary: cofactor NADPH


substrate_name: Protein

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

substrate: Protein


substrate_name: H+; Squalene; O2; NADPH

km_display: Not reported

sequence_source: EBI Proteins API UniProtKB accession P52020

substrate: H+; Squalene; O2; NADPH


substrate_name: O2; H+; NADPH; Squalene

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

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant delta-N-99 His-tagged

substrate: O2; H+; NADPH; Squalene


organism: Saccharomyces cerevisiae

substrate_name: H+; O2; Squalene; NADPH

sequence_source: EBI Proteins API UniProtKB accession P32476

substrate: H+; O2; Squalene; NADPH


organism: Candidatus Liberibacter asiaticus

proof_lines: pH 8.2, 37°C, AICAR TFase activity of CLasATIC


organism: Cryptococcus neoformans

sequence_source: EBI Proteins API UniProtKB accession J9VJP1


organism: Escherichia coli

sequence_source: EBI Proteins API UniProtKB accession P15639

proof_lines: pH 7.5, temperature not specified in the publication


organism: Gallus gallus

sequence_source: EBI Proteins API UniProtKB accession P31335


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: EBI Proteins API UniProtKB:P31939 (Swiss-Prot), checked 2026-06-11

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

source_databases_merged: sabio_rk brenda skid


organism: Staphylococcus lugdunensis

proof_lines: full length bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC), pH 7.4, temperature not specified in the publication


mutation_signature: AICAR transformylase activity of domain truncation pET- -AICARTF1

proof_lines: AICAR transformylase activity of domain truncation mutant pET-28c-AICARTF1, pH 7.4, temperature not specified in the publication


enzyme_display_name: deoxyhypusine synthase

organism: Cryptosporidium parvum

substrate_name: spermidine

sequence_source: EBI Proteins API UniProtKB:A3FQA5 (TrEMBL), checked 2026-06-11

enzyme: deoxyhypusine synthase

substrate: spermidine


substrate_name: Spermidine; [eIF5A-precursor]-lysine

sequence_source: EBI Proteins API UniProtKB:P49366 (Swiss-Prot), checked 2026-06-11

proof_lines: pH and temperature not specified in the publication

substrate: Spermidine; [eIF5A-precursor]-lysine


organism: Leishmania donovani

sequence_source: EBI Proteins API UniProtKB:B5APK2 (Swiss-Prot), checked 2026-06-11


substrate_name: [eIF5A-precursor]-lysine; Spermidine

substrate: [eIF5A-precursor]-lysine; Spermidine


organism: Senecio vernalis

sequence_source: EBI Proteins API UniProtKB:Q9SC14 (Swiss-Prot), checked 2026-06-11


substrate_name: Putrescine

sequence_source: EBI Proteins API UniProt-backed record Q9SC14 checked 2026-06-11

smiles: NCCCCN

substrate: Putrescine


substrate_name: Spermidine

smiles: NCCCCNCCCN

substrate: Spermidine


organism: Theileria parva


organism: Trichomonas vaginalis

sequence_source: EBI Proteins API UniProt-backed record F1AQF9 checked 2026-06-11


organism: Trypanosoma brucei brucei

sequence_source: EBI Proteins API UniProt-backed record Q38BX0 checked 2026-06-11


substrate_name: NAD+

sequence_source: EBI Proteins API UniProt-backed record Q38BX0 checked 2026-06-11; H266A coordinate check failed

assay_conditions_summary: cofactor NAD+

proof_lines: mutant H266A, pH not specified in the publication, temperature not specified in the publication

substrate: NAD+


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


sequence_variant_note: Resolved canonical sequence from EBI Proteins API UniProt-backed record Q38BX0 checked 2026-06-11; E166A reconstructed from direct 1-based residue check and applied mutation signature E166A to reconstruct the assayed variant sequence.

proof_lines: mutant E166A, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: phosphoserine transaminase

organism: Arabidopsis thaliana

substrate_name: 3-Phosphohydroxypyruvate; L-Glutamate

sequence_source: EBI Proteins API UniProt accession Q96255

proof_lines:
pH 8.2, 25°C
Raw SKiD Env: Temp=25°C, pH=8.2

enzyme: phosphoserine transaminase

substrate: 3-Phosphohydroxypyruvate; L-Glutamate


substrate_name: L-Glutamate; 3-Phosphohydroxypyruvate

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

substrate: L-Glutamate; 3-Phosphohydroxypyruvate


organism: Bombyx mori

sequence_source: EBI Proteins API UniProt accession Q2F5M8

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


organism: Bos taurus

sequence_source: EBI Proteins API UniProt accession A0A3S5ZPF7


organism: Entamoeba histolytica

sequence_source: EBI Proteins API UniProt accession Q60I38

proof_lines:
pH 8.5, 25°C
Raw SKiD Env: Temp=25°C, pH=8.5
Raw SKiD Env: Temp=-----, pH=8.5


substrate_name: O-phospho-L-serine

proof_lines: pH 8.5, temperature not specified in the publication, recombinant mutant EhPSAT_DELTA15

substrate: O-phospho-L-serine


proof_lines: pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme


mutation_signature: Δ4

proof_lines: pH 8.5, temperature not specified in the publication, recombinant mutant EhPSAT_DELTA4


organism: Aspergillus nidulans

substrate_name: linoleate

sequence_source: EBI Proteins API UniProt accession Q6RET3

smiles: CCCCC/C=C\C/C=C\CCCCCCCC(=O)O

substrate: linoleate


substrate_name: palmitoleate

substrate: palmitoleate


substrate_name: (11Z)-icos-11-enoic acid

smiles: CCCCCCCC/C=C\CCCCCCCCCC(=O)O

substrate: (11Z)-icos-11-enoic acid


substrate_name: oleate

substrate: oleate


organism: Colletotrichum gloeosporioides

sequence_source: EBI Proteins API UniProt accession A0A0S2SWE4


substrate_name: eicosenoic acid

sequence_source: EBI Proteins API UniProt accession A0A0S2SWE4 canonical context only

proof_lines: N-terminal 8-dioxygenase domain, pH 6.5, 40°C

proof_lines: recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C

proof_lines: recombinant enzyme, whole enzyme activity, pH 6.5, 40°C

substrate: eicosenoic acid


substrate_name: alpha-linolenate

smiles: CC/C=C\C/C=C\C/C=C\CCCCCCCC(=O)O

substrate: alpha-linolenate


enzyme_display_name: triokinase

organism: Homo sapiens

substrate_name: dihydroxyacetone

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

smiles: O=C(CO)CO

assay_conditions_summary: pH 7.5; 310.15 K; cofactor FMN

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 'T112A'; line 'kcat (s^-1)' = 0.51; line '10^6 Km (M)' = 6.63; line '10^-4 kcat/Km (M^-1 s^-1)' = 7.6.

normalized_value_unit_evidence: kcat: the printed cell 0.51 is already in s^-1, so no unit conversion applies and the canonical value is 0.51 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 6.63 is 6.63 x 10^-6 M = 6.63 uM, and 6.63 / 1000 gives 0.00663 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 7.6 is 7.6 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 76.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, DHA kinase (DHA) activity block, column 'T112A': printed 'kcat (s^-1)' cell 0.51; printed '10^6 Km (M)' cell 6.63; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 7.6.

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

enzyme: triokinase

substrate: dihydroxyacetone


substrate_name: D-glyceraldehyde

sequence_source: UniProtKB Q3LXA3 direct REST/FASTA check on 2026-06-11

substrate: D-glyceraldehyde


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q3LXA3 direct REST/FASTA check on 2026-06-11 and applied mutation signature C404A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C404A, with D-glyceraldehyde as cosubstrate,at pH 7.5 and 37°C

proof_lines: mutant enzyme C404A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3LXA3 and applied mutation signature C404A 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 'C404A'; line 'kcat (s^-1)' = 2.27; line '10^6 Km (M)' = 16.2; line '10^-4 kcat/Km (M^-1 s^-1)' = 14.0.

normalized_value_unit_evidence: kcat: the printed cell 2.27 is already in s^-1, so no unit conversion applies and the canonical value is 2.27 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 16.2 is 16.2 x 10^-6 M = 16.2 uM, and 16.2 / 1000 gives 0.0162 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 14.0 is 14.0 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 140.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GA kinase (GA) activity block, column 'C404A': printed 'kcat (s^-1)' cell 2.27; printed '10^6 Km (M)' cell 16.2; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 14.0.

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


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

proof_lines: wild type enzyme, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C


column_label: Table 1, Wild type column, DHA kinase (DHA) activity / Wild type: kcat 5.00 s^-1; Km 1.55 uM; kcat/Km 321 x 10^4 M^-1*s^-1.

raw_value_unit_evidence: Table 1; measurement Wild type; construct wild-type hTKFC; substrate dihydroxyacetone (DHA); condition pH 7.5; 37 °C; DHA kinase (DHA) activity; kcat raw_value=5.00 raw_unit=s^-1; Km raw_value=1.55 raw_unit=uM; kcat/Km raw_value=321 x 10^4 raw_unit=M^-1*s^-1.

row_label: DHA kinase (DHA) activity / Wild type

table_label: Table 1. Kinetic parameters of hTKFC and mutants


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 'DHA kinase (DHA) activity'; column 'K204A'; line 'kcat (s^-1)' = 2.79; line '10^6 Km (M)' = 2.52; line '10^-4 kcat/Km (M^-1 s^-1)' = 115.

normalized_value_unit_evidence: kcat: the printed cell 2.79 is already in s^-1, so no unit conversion applies and the canonical value is 2.79 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 2.52 is 2.52 x 10^-6 M = 2.52 uM, and 2.52 / 1000 gives 0.00252 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 115 is 115 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 1150.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, DHA kinase (DHA) activity block, column 'K204A': printed 'kcat (s^-1)' cell 2.79; printed '10^6 Km (M)' cell 2.52; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 115.

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


sequence_source: UniProtKB:P23721 direct lookup on 2026-06-11

proof_lines:
pH 8.2, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=8.2
Raw SKiD Env: Temp=30°C, pH=8.2


substrate_name: L-homoserine

proof_lines: pH 8.2, 30°C, recombinant wild-type enzyme

substrate: L-homoserine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23721 direct lookup plus R42W/R77W reconstruction on 2026-06-11 and applied mutation signature R42W/R77W to reconstruct the assayed variant sequence.

proof_lines: pH 8.2, 30°C, recombinant mutant R42W/R77W


organism: Glycine max

sequence_source: UniProtKB:I1JCA9 direct lookup on 2026-06-11


substrate_name: 2-Oxoglutarate; O-Phospho-L-serine

sequence_source: UniProtKB:Q9Y617 direct lookup on 2026-06-11

substrate: 2-Oxoglutarate; O-Phospho-L-serine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Y617 direct lookup plus D100A reconstruction on 2026-06-11 and applied mutation signature D100A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoserine transaminase(Enzyme) mutant D100A N-terminal His-tag


organism: Niallia circulans

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

sequence_source: UniProtKB:Q59196 direct lookup on 2026-06-11

assay_conditions_summary: pH 7

proof_lines:
pH 7.0
pH 9.0
Raw SKiD Env: Temp=-----, pH=7

source_databases_merged: brenda skid


substrate_name: L-glutamate

proof_lines: pH 9.5, 25°C, recombinant enzyme mutant K2G

proof_lines: pH 8.2, 25°C, recombinant enzyme mutant K2G

substrate: L-glutamate


enzyme_display_name: N-acylmannosamine kinase

organism: Escherichia coli

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

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

enzyme: N-acylmannosamine kinase


substrate_name: D-Glucose

substrate: D-Glucose


substrate_name: ATP; D-Glucose

assay_conditions_summary: cofactor ATP

substrate: ATP; D-Glucose


substrate_name: N-Acetyl-D-mannosamine

substrate: N-Acetyl-D-mannosamine


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)


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.


substrate_name: D-Mannose

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

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

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

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


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

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

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).


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.


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)


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.


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)


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)


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)


organism: Ovis aries

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


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.

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

substrate: L-Glutamate; 3-Phosphohydroxypyruvate


organism: Synechocystis sp.

sequence_source: UniProtKB P74281 canonical sequence, direct accession lookup


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.


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.


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

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


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, 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.


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.


sequence_source: UniProtKB Q9Y223 direct accession check

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


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

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

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

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


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

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

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+