sequence_variant_note: Resolved canonical sequence from uniprot:Q16774 and applied mutation signature R96G to reconstruct the assayed variant sequence.


enzyme_display_name: serine C-palmitoyltransferase

organism: Sphingomonas paucimobilis

substrate_name: L-serine

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 UniProtKB:Q93UV0 plus direct V246M reconstruction and applied mutation signature V246M to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

data_origin: experimental

enzyme: serine C-palmitoyltransferase

substrate: L-serine

status: corrected

source: oed


source_db: brenda

kcat_over_km_display: Not reported

sequence_source: UniProtKB:Q93UV0 plus direct V246M reconstruction

source: brenda


substrate_name: palmitoyl-CoA

verification_status: unverified

kcat_over_km_origin: calculated

substrate: palmitoyl-CoA

status: unverified


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93UV0 plus direct G385F reconstruction and applied mutation signature G385F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q93UV0 plus direct G385F reconstruction


substrate_name: myristoyl-CoA

mutation_signature: Unknown

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

assay_conditions_summary: pH 7.5; 298.15 K; buffer reaction; cofactor CoA

substrate: myristoyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93UV0 plus direct R378K reconstruction and applied mutation signature R378K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R378K, with palmitoyl-CoA as cosubstrate, at pH 7.5 and 25°C

proof_lines: mutant enzyme R378K, with myristoyl-CoA as cosubstrate, at pH 7.5 and 25°C


substrate_name: caproyl-CoA

substrate: caproyl-CoA


organism: Bacteriovorax stolpii

sequence_source: UniProtKB reviewed accession A7BFV8 fetched 2026-06-07

assay_conditions_summary: cofactor CoA


organism: Homo sapiens

substrate_name: L-Serine; Palmitoyl-CoA

kcat_display: Not reported

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

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

proof_lines: SABIO-RK modifier species: serine C-palmitoyltransferase(Enzyme) mutant hLCB1-C133W/hLCB2a/ssSPTa

substrate: L-Serine; Palmitoyl-CoA


substrate_name: Palmitoyl-CoA; L-Serine

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

substrate: Palmitoyl-CoA; L-Serine


sequence_source: UniProtKB reviewed accession O15269 fetched 2026-06-07

assay_conditions_summary: pH 8

proof_lines: at pH 8.0, temperature not specified in the publication


organism: Sphingobacterium multivorum

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

sequence_source: UniProtKB reviewed accession A7BFV6 fetched 2026-06-07

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

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

source_databases_merged: brenda skid


organism: Sphingobacterium spiritivorum

sequence_source: UniProtKB reviewed accession A7BFV7 fetched 2026-06-07


mutation_signature: Δ2

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

mutation_type: deletion


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession Q93UV0 fetched 2026-06-07 by applying R378A to the canonical sequence and applied mutation signature R378A to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutant R378A
pH 7.5, 37°C, recombinant mutant R378A


enzyme_display_name: guanylate kinase

substrate_name: GMP

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q16774 canonical sequence reconstructed with source mutation R96G after confirming Q16774 residue 96 is R. and applied mutation signature R96G to reconstruct the assayed variant sequence.

enzyme: guanylate kinase

substrate: GMP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q16774 and applied mutation signature S186Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer triplicate with 10 nM hGMPK in a; cofactor NADH

column_label: Table 2 (Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK), hGMPK row S186Y; column kcat (s^-1) = 96.5 +/- 0.7; column Km (uM) = 36.8 +/- 0.7; column kcat/Km (s^-1 uM^-1) = 2.6 +/- 0.1; column s20,w (S) = 2.14 +/- 0.03; column Tm (oC) = 44.6 +/- 0.2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 96.5 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the value stays 96.5. Km: printed Table 2 cell 36.8 uM; 36.8 / 1000 = 0.0368 mM. kcat/Km: printed Table 2 cell 2.6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.6 x 1000 = 2600.0 s^-1 mM^-1.

row_label: Table 2, hGMPK row S186Y

table_label: Table 2: Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK (J. Biol. Chem. 2019, 294(31):11920-11933)


sequence_source: UniProtKB REST Q16774 canonical sequence.


substrate_name: dGMP; ATP

assay_conditions_summary: cofactor ATP

substrate: dGMP; ATP


organism: Mus musculus

sequence_source: UniProtKB REST Q64520 canonical sequence.


organism: Oryza sativa Japonica Group

sequence_source: UniProtKB REST Q10M74 canonical sequence.

proof_lines: recombinant chloroplast isozyme, pH 7.5, 30°C


sequence_source: UniProtKB REST Q2QPW1 canonical sequence.

proof_lines: recombinant cytosolic isozyme, pH 7.5, 30°C


enzyme_display_name: lignin peroxidase

organism: Phanerochaete sordida

substrate_name: veratryl alcohol

sequence_source: UniProtKB:B6ZKF4 REST FASTA, fetched 2026-06-07

enzyme: lignin peroxidase

substrate: veratryl alcohol


organism: Rhodococcus jostii

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0SE24 REST FASTA with N246A reconstruction, fetched 2026-06-07 and applied mutation signature N246A to reconstruct the assayed variant sequence.


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0SE24 and applied mutation signature N246A to reconstruct the assayed variant sequence.

smiles: OO

assay_conditions_summary: pH 5; 298.15 K; buffer 50 mM sodium malonate

column_label: Table 2 (Kinetic parameters of recombinant Rh_DypB peroxidase on H2O2), row 'Addition of 2 mM Mn2+'; column kcat (s^-1) = 34.0 ± 1.2; column Km (mM) = 0.04 ± 0.01; column kcat/Km (head prints no unit; decoded unit s^-1 mM^-1 from the kcat and Km column heads) = 850 ± 91; column Ki (mM) = 2.8 ± 0.3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 34.0 s^-1; already in s^-1, no unit conversion applies; the exported value is 34.0 s^(-1). Km: printed Table 2 cell 0.04 mM; already in mM, no unit conversion applies; the exported value is 0.04 mM. kcat/Km: printed Table 2 cell 850 in the kcat/Km column, whose unit is s^-1 mM^-1 because kcat is printed in s^-1 and Km in mM (34.0 / 0.04 = 850 confirms it); already in s^-1 mM^-1, no unit conversion applies; the exported value is 850.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'Addition of 2 mM Mn2+': kcat = 34.0 ± 1.2 s^-1; Km = 0.04 ± 0.01 mM; printed kcat/Km = 850 ± 91 in the kcat/Km column, whose head prints no unit and whose unit is s^-1 mM^-1 (the kcat column unit s^-1 over the Km column unit mM); Ki = 2.8 ± 0.3 mM.

row_label: Table 2, H2O2 row 'Addition of 2 mM Mn2+' (recombinant Rh_DypB, the N246A variant of R. jostii RHA1 DypB)

table_label: Table 2: Kinetic parameters of recombinant Rh_DypB peroxidase on H2O2 (Appl Microbiol Biotechnol 2018, 102:10579-10588)

status: verified


column_label: Table 1 (Kinetic parameters of recombinant Rh_DypB peroxidase on Mn2+, ABTS, and 2,6-DMP), row (B) In presence of 0.3 mM H2O2, ABTS column group; column kcat (s^-1) = 15.4 ± 0.73; column Km (mM) = 15.6 ± 1.3; column kcat/Km (head prints no unit; decoded unit s^-1 mM^-1 from the kcat and Km column heads) = 0.98 ± 0.1.

normalized_value_unit_evidence: kcat: printed Table 1 row (B) ABTS cell 15.4 s^-1; already in s^-1, no unit conversion applies; the exported value is 15.4 s^(-1). Km: printed Table 1 row (B) ABTS cell 15.6 mM; already in mM, no unit conversion applies; the exported value is 15.6 mM. kcat/Km: printed Table 1 row (B) ABTS cell 0.98 in the kcat/Km column, whose unit is s^-1 mM^-1 because kcat is printed in s^-1 and Km in mM; already in s^-1 mM^-1, no unit conversion applies, so the paper value is 0.98 s^(-1)*mM^(-1); the exported value is 0.9871794871794872 s^(-1)*mM^(-1), which is the full-precision quotient 15.4 / 15.6.

raw_value_unit_evidence: Table 1, row (B) In presence of 0.3 mM H2O2, ABTS column group: kcat = 15.4 ± 0.73 s^-1; Km = 15.6 ± 1.3 mM; printed kcat/Km = 0.98 ± 0.1 in the kcat/Km column, whose head prints no unit and whose unit is s^-1 mM^-1 (the kcat column unit s^-1 over the Km column unit mM).

row_label: Table 1, row (B) In presence of 0.3 mM H2O2, ABTS column group (recombinant Rh_DypB, the N246A variant of R. jostii RHA1 DypB)

table_label: Table 1: Kinetic parameters of recombinant Rh_DypB peroxidase on Mn2+, ABTS, and 2,6-DMP (Appl Microbiol Biotechnol 2018, 102:10579-10588)


substrate_name: Mn(II)

sequence_source: UniProtKB:Q0SE24 REST FASTA with N246A reconstruction, fetched 2026-06-07

substrate: Mn(II)


proof_lines: pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2

proof_lines: pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2 mM Mn2+

proof_lines: pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2


organism: Trametopsis cervina

sequence_source: UniProtKB:Q60FD2 REST FASTA, fetched 2026-06-07

assay_conditions_summary: pH 3; buffer 20 mM sodium succinate

proof_lines: recombinant enzyme without veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)

proof_lines: recombinant enzyme with veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)


organism: Rattus norvegicus

substrate_name: ATP; GMP

sequence_source: UniProtKB Q71RR7 REST lookup on 2026-06-07

substrate: ATP; GMP


organism: Rickettsia conorii

substrate_name: guanosine monophosphate

sequence_source: UniProtKB Q92GC9 REST lookup on 2026-06-07

substrate: guanosine monophosphate


enzyme_display_name: UDP-N-acetylglucosamine diphosphorylase

organism: Arabidopsis thaliana

substrate_name: N-Acetyl-D-glucosamine 1-phosphate; UTP

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

sequence_source: UniProtKB Q940S3 REST lookup on 2026-06-07

enzyme: UDP-N-acetylglucosamine diphosphorylase

substrate: N-Acetyl-D-glucosamine 1-phosphate; UTP


sequence_source: UniProtKB O64765 REST lookup on 2026-06-07


organism: Escherichia coli

sequence_source: UniProtKB P0ACC7 canonical sequence only; row-specific G14A His6-tagged sequence unresolved

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant G14A His6-tagged


substrate_name: UTP

sequence_source: UniProtKB P0ACC7 REST lookup on 2026-06-07

substrate: UTP


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ACC7 canonical sequence plus selected R18A mutation reconstructed on 2026-06-07 and applied mutation signature R18A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P0ACC7 canonical sequence only; row-specific truncated His6-tagged sequence unresolved

mutation_type: truncation

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant truncated His6-tagged


organism: Saccharomyces cerevisiae

substrate_name: N-Acetyl-D-glucosamine 1-phosphate

sequence_source: UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature.

substrate: N-Acetyl-D-glucosamine 1-phosphate


substrate_name: UTP; N-Acetyl-D-glucosamine 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature. and applied mutation signature R116A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant R116A

substrate: UTP; N-Acetyl-D-glucosamine 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature. and applied mutation signature G111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature. and applied mutation signature G114A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant G114A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature. and applied mutation signature G112A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant G112A


proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant G111A


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; row-specific G14A variant sequence not accepted.


sequence_source: UniProtKB reviewed P0ACC7 direct REST lookup.


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; K25A His6-tagged variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant K25A His6-tagged


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; row-specific K25A variant sequence not accepted.


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; R18A His6-tagged variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant R18A His6-tagged


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; deletion/truncation variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU-del78 N-terminal His6-tag

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU-del130 N-terminal His6-tag

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU-del227 N-terminal His6-tag


km_display: Not reported

sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; C307A His6-tagged variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU C307A N-terminal His6-tagged


sequence_source: UniProtKB reviewed P0ACC7 canonical sequence checked directly; C296A His6-tagged variant sequence not accepted.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU C296A N-terminal His6-tagged


sequence_source: UniProtKB:P0ACC7 REST FASTA plus PMID 9733680 His6-GlmU C385A construct context; accessed 2026-06-07

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU C385A N-terminal His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ACC7 REST FASTA plus PMID 9733680 His6-GlmU C324A construct context; accessed 2026-06-07 and applied mutation signature C324A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant GlmU C324A N-terminal His6-tagged


organism: Giardia duodenalis

sequence_source: UniProtKB:Q8MUP8 REST FASTA; accessed 2026-06-07

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

proof_lines: Mg-UTP, purified recombinant native enzyme, pH 7.5, 37°C


sequence_source: UniProtKB:Q16222 REST FASTA; accessed 2026-06-07


organism: Mycobacterium tuberculosis

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

sequence_source: UniProtKB:P9WMN3 REST FASTA; accessed 2026-06-07

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.5

source_databases_merged: sabio_rk brenda skid


sequence_source: UniProtKB:A5U161 REST FASTA; accessed 2026-06-07

assay_conditions_summary: pH 7.5; 303.15 K; buffer containing 10 mM MgCl2 throughout the purification process

column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'GlcNAc-1P', fixed-substrate column value 'UTP'; column 'K_m (uM)' = 30; column 'k_cat (s^-1)' = 100; column 'k_cat/K_m (M^-1 s^-1)' = 3.2 x 10^6; column 'K_d (uM)' = ND.

normalized_value_unit_evidence: Km: printed Table 1 cell 30 uM; 30 / 1000 = 0.03 mM. kcat: printed Table 1 cell 100 s^-1; already in s^-1, no unit conversion applies, so the paper value is 100 s^(-1). kcat/Km: printed Table 1 cell 3.2 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.2 x 10^6 / 1000 = 3200 s^-1 mM^-1. The printed efficiency cell is the paper's own fitted catalytic efficiency and is taken as the primary reported value for this metric.

raw_value_unit_evidence: Table 1, varied-substrate row 'GlcNAc-1P', fixed substrate 'UTP': Km = 30 uM; kcat = 100 s^-1; printed kcat/Km = 3.2 x 10^6 M^-1 s^-1.

row_label: Table 1, canonical-order row with varied substrate 'GlcNAc-1P' and fixed substrate 'UTP'

table_label: Table 1: Steady-State Kinetic Parameters for GlmU (Biochemistry 2018, 57, 3387-3401)


assay_conditions_summary: pH 7.5; 303.15 K; buffer containing 10 mM MgCl2

column_label: Table 1 (Steady-State Kinetic Parameters for GlmU), varied-substrate row 'UTP', fixed-substrate column value 'GlcNAc-1P'; column 'K_m (uM)' = 8; column 'k_cat (s^-1)' = 120; column 'k_cat/K_m (M^-1 s^-1)' = 1.5 x 10^7; column 'K_d (uM)' = ND.

normalized_value_unit_evidence: Km: printed Table 1 cell 8 uM; 8 / 1000 = 0.008 mM; the exported value is 0.008 mM. kcat: printed Table 1 cell 120 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 120.0 s^(-1). kcat/Km: printed Table 1 cell 1.5 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.5 x 10^7 / 1000 = 15000.0 s^-1 mM^-1; the exported value is 15000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, varied-substrate row 'UTP', fixed substrate 'GlcNAc-1P': Km = 8 uM; kcat = 120 s^-1; printed kcat/Km = 1.5 x 10^7 M^-1 s^-1.

row_label: Table 1, canonical-order row with varied substrate 'UTP' and fixed substrate 'GlcNAc-1P'

table_label: Table 1: Steady-State Kinetic Parameters for GlmU (Biochemistry 2018, 57(23):3387-3401)


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature L117A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature P122A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant P122A


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature R116A to reconstruct the assayed variant sequence.


sequence_source: uniprot:P43123 direct lookup


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature T115A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant T115A


sequence_source: uniprot:P43123 direct lookup; reconstructed from canonical sequence


substrate_name: N-acetyl-D-glucosamine 1-phosphate

substrate: N-acetyl-D-glucosamine 1-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot:P43123 direct lookup; reconstructed from canonical sequence and applied mutation signature K123A to reconstruct the assayed variant sequence.


organism: Sulfurisphaera tokodaii

sequence_source: UniProtKB reviewed accession Q975F9 direct REST lookup on 2026-06-07


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession Q975F9 direct REST lookup on 2026-06-07 with Y97N substitution and applied mutation signature Y97N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession Q975F9 direct REST lookup on 2026-06-07 with Y97V substitution and applied mutation signature Y97V to reconstruct the assayed variant sequence.


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

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


substrate_name: diphosphate

substrate: diphosphate


organism: Xanthomonas oryzae pv. oryzae

substrate_name: Unknown

ki_unit: mM

sequence_source: UniProtKB reviewed accession Q2P7P9 direct REST lookup on 2026-06-07

proof_lines: substrate N-acetyl-alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C

substrate: Unknown


enzyme_display_name: CCA tRNA nucleotidyltransferase

organism: Archaeoglobus fulgidus

substrate_name: CTP

sequence_source: UniProtKB reviewed accession O28126 direct REST lookup on 2026-06-07

assay_conditions_summary: pH 8.5; 323.15 K; cofactor ATP

proof_lines:
pH 8.5, 50°C
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=50°C, pH=8.5

enzyme: CCA tRNA nucleotidyltransferase

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 and applied mutation signature K123A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant K123A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 and applied mutation signature L117A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant L117A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q975F9 and applied mutation signature Y97M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q975F9 and applied mutation signature Y97V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q975F9 and applied mutation signature Y97N to reconstruct the assayed variant sequence.


organism: Exiguobacterium sibiricum

substrate_name: ATP

sequence_source: UniProtKB B1YHR1 direct REST lookup on 2026-06-07

assay_conditions_summary: pH 7.6; 277.15 K; cofactor ATP

substrate: ATP


organism: Geobacillus stearothermophilus

sequence_source: UniProtKB Q7SIB1 direct REST lookup on 2026-06-07

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


organism: Homo sapiens

substrate_name: a tRNA precursor

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

proof_lines: mutant D139A, pH not specified in the publication, temperature not specified in the publication

substrate: a tRNA precursor


sequence_source: UniProtKB Q96Q11 direct REST lookup on 2026-06-07

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


substrate_name: armless tRNA(Arg) precursor

proof_lines:
addition of 2C, pH 7.6, 20°C
addition of 2C + A, pH 7.6, 20°C

substrate: armless tRNA(Arg) precursor


organism: Methanocaldococcus jannaschii

substrate_name: tRNA precursor; ATP; CTP

sequence_source: UniProtKB Q58511 direct REST lookup on 2026-06-07

substrate: tRNA precursor; ATP; CTP


organism: Planococcus halocryophilus

sequence_source: UniProtKB A0A1C7DQ98 direct REST lookup on 2026-06-07

proof_lines:
pH 7.6, 25°C
pH 7.6, 4°C
Raw SKiD Env: Temp=25°C, pH=7.6


sequence_source: UniProtKB:A0A1C7DQ98 direct accession lookup


organism: Saccharolobus shibatae

sequence_source: UniProtKB:P77978 direct accession lookup


assay_conditions_summary: pH 8.1; 343.15 K; cofactor ATP


proof_lines:
pH 8.1, 70°C, wild-type enzyme
pH 9.0, 70°C, wild-type enzyme


sequence_source: UniProtKB:P77978 direct accession lookup; variant sequence not reconstructed


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature K153A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature Y158A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature G166R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature H129A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature G169R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 canonical sequence with direct mutation-signature reconstruction and applied mutation signature Y90E/E92F to reconstruct the assayed variant sequence.


organism: Sulfolobus shibatae

sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature Y90E/E92F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant Y90E/E92F


substrate_name: CTP; ATP; tRNA precursor

sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature G169R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant G169R

substrate: CTP; ATP; tRNA precursor


substrate_name: CTP; tRNA precursor; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature H129A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant H129A

substrate: CTP; tRNA precursor; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature R125A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant R125A


sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature G166R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant G166R


sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature K153A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant K153A


sequence_source: UniProtKB P77978 direct FASTA

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


substrate_name: tRNA precursor; CTP; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB P77978 direct FASTA; variant sequence reconstructed from source mutation signature and applied mutation signature H93V/Y95V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant H93V/Y95V

substrate: tRNA precursor; CTP; ATP


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


sequence_source: UniProtKB:P77978 direct FASTA, checked 2026-06-07

assay_conditions_summary: pH 9; 343.15 K; cofactor ATP

proof_lines: pH 9.0, 70°C, in presence of 0.1 mM each of UTP, ATP and GTP


sequence_source: UniProtKB:P21269 direct FASTA, checked 2026-06-07

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


proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant E92F


proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant K149A


sequence_variant_note: Resolved canonical sequence from UniProtKB:O28126 direct REST lookup; P295T reconstructed from canonical sequence and applied mutation signature P295T to reconstruct the assayed variant sequence.

proof_lines: C74 addition, pH and temperature not specified in the publication, mutant enzyme P295T

proof_lines: A76 addition, pH and temperature not specified in the publication, mutant enzyme P295T

proof_lines: C75 addition, pH and temperature not specified in the publication, mutant enzyme P295T


sequence_variant_note: Resolved canonical sequence from UniProtKB:O28126 direct REST lookup; P295G reconstructed from canonical sequence and applied mutation signature P295G to reconstruct the assayed variant sequence.

proof_lines: A76 addition, pH and temperature not specified in the publication, mutant enzyme P295G

proof_lines: C74 addition, pH and temperature not specified in the publication, mutant enzyme P295G

proof_lines: C75 addition, pH and temperature not specified in the publication, mutant enzyme P295G


sequence_variant_note: Resolved canonical sequence from UniProtKB:O28126 direct REST lookup; P295A reconstructed from canonical sequence and applied mutation signature P295A to reconstruct the assayed variant sequence.

proof_lines: A76 addition, pH and temperature not specified in the publication, mutant enzyme P295A

proof_lines: C74 addition, pH and temperature not specified in the publication, mutant enzyme P295A

proof_lines: C75 addition, pH and temperature not specified in the publication, mutant enzyme P295A


sequence_source: UniProtKB:O28126 direct REST lookup for canonical context only

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

proof_lines: C74 addition, pH and temperature not specified in the publication, mutant enzyme P295SA

proof_lines: C75 addition, pH and temperature not specified in the publication, mutant enzyme P295SA

proof_lines: A76 addition, pH and temperature not specified in the publication, mutant enzyme P295SA


sequence_source: UniProtKB:O28126 direct REST lookup

proof_lines: A76 addition, pH and temperature not specified in the publication, wild-type enzyme

proof_lines: C74 addition, pH and temperature not specified in the publication, wild-type enzyme

proof_lines: C75 addition, pH and temperature not specified in the publication, wild-type enzyme


organism: Bacillus subtilis

sequence_source: UniProtKB:P42977 direct REST lookup


organism: Exiguobacterium artemiae

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


substrate_name: GMP

sequence_source: UniProtKB:P60546; PMID:24722991 maps EcGK to EMBL:M84400

proof_lines: recombinant cytosolic isozyme, pH 7.5, 30°C

substrate: GMP


enzyme_display_name: dextranase

organism: Streptococcus mutans

substrate_name: dextran T70

sequence_variant_note: Resolved canonical sequence from UniProtKB F5BA50 REST/FASTA direct check on 2026-06-07; D500T reconstructed from the checked canonical residue. and applied mutation signature D500T to reconstruct the assayed variant sequence.

enzyme: dextranase

substrate: dextran T70


substrate_name: Dextran

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB Q54443 REST/FASTA direct check on 2026-06-07.

substrate: Dextran

source: skid


organism: Pseudarthrobacter oxydans


organism: Pseudothermotoga lettingae

substrate_name: dextran T2000

sequence_source: UniProtKB:A8F6K5 direct FASTA lookup 2026-06-07

assay_conditions_summary: pH 4.3; 328.15 K; buffer 40 mM sodium acetate

proof_lines: in 40 mM sodium acetate buffer (pH4.3) at 55°C

substrate: dextran T2000


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature T563N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q54443 direct FASTA lookup 2026-06-07


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature T558H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature W279A/T563N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W279A/T563N, at pH 5.0 and 35°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature W279F/T563N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W279F/T563N, at pH 5.0 and 35°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q54443 direct FASTA lookup 2026-06-07 plus selected BRENDA mutation signature and applied mutation signature W279F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P77978 reconstructed Y158A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P77978 reconstructed Y158A and applied mutation signature Y158A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CCA  tRNA nucleotidyltransferase(Enzyme) mutant Y158A


organism: Paenibacillus sp.


proof_lines: mutant enzyme N102C/D500G, at pH 5.0 and 40°C


proof_lines: mutant enzyme N102P/D500T, at pH 5.0 and 40°C


proof_lines: mutant enzyme N102P/D500G, at pH 5.0 and 40°C


organism: Caulobacter vibrioides (strain NA1000 / CB15N)

substrate_name: hexadecanoyl-CoA

source_db: uniprot

substrate: hexadecanoyl-CoA

source: uniprot


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: GlcNAc-1-P (at pH 7.6)

assay_conditions_summary: pH 7.6; cofactor CoA

substrate: GlcNAc-1-P (at pH 7.6)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Escherichia coli (strain K12)

substrate_name: ATP (in the tRNA-NT activity assay)

substrate: ATP (in the tRNA-NT activity assay)


substrate_name: tRNA precursor

substrate: tRNA precursor


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)


substrate_name: L-serine

substrate: L-serine


organism: Arabidopsis thaliana

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


substrate_name: N-acetylglucosamine 1-phosphate

substrate: N-acetylglucosamine 1-phosphate


organism: Bacteriovorax stolpii

proof_lines: kcat is 0.03 sec(-1) (in the presence of 100 uM of palmitoyl-CoA).


organism: Sphingobacterium multivorum


organism: Sphingobacterium spiritivorum


organism: Sphingomonas paucimobilis

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

proof_lines: kcat is 140 min(-1) with palmitoyl-CoA as substrate (PubMed:11279212). kcat is 2.3 sec(-1) with palmitoyl-CoA as substrate (PubMed:17557831). kcat is 1.150 sec(-1) with palmitoyl-CoA as substrate (PubMed:19376777). kcat is 0.045 sec(-1) wit


organism: Homo sapiens

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

column_label: Table 2 (Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK), hGMPK row WT; column kcat (s^-1) = 58.5 +/- 0.3; column Km (uM) = 20.7 +/- 0.3; column kcat/Km (s^-1 uM^-1) = 2.8 +/- 0.1; column s20,w (S) = 2.04 +/- 0.03; column Tm (oC) = 47.4 +/- 0.4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 58.5 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the value stays 58.5. Km: printed Table 2 cell 20.7 uM; 20.7 / 1000 = 0.0207 mM. kcat/Km: printed Table 2 cell 2.8 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.8 x 1000 = 2800.0 s^-1 mM^-1.

row_label: Table 2, hGMPK row WT


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: dTMP (at pH 7.2 and 30 degrees Celsius)

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: kcat is 3.4 sec(-1) with dTMP as substrate (at pH 7.2 and 30 degrees Celsius) (PubMed:18477629). kcat is 3.2 sec(-1) with dTMP as substrate (at pH 7.2 and 30 degrees Celsius) (PubMed:19126267). kcat is 3.1 sec(-1) with dTMP as substrate (Pu

substrate: dTMP (at pH 7.2 and 30 degrees Celsius)


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 69.7 sec(-1) for GalN-1-P acetyltransferase activity. kcat is 123.2 sec(-1) for GlcN-1-P acetyltransferase activity.


organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12)

substrate_name: CTP

proof_lines: The KM for ATP is much higher than 30 uM.

substrate: CTP


organism: Bacillus licheniformis

substrate_name: Unknown

sequence: AYTVTLYLQG

wild_type_sequence: AYTVTLYLQG

proof_lines: Because of the indeterminate molecular weight of dextran, an approximate KM value of 0.3738 mg/ml was determined.

substrate: Unknown


organism: Agaricus bisporus

substrate_name: veratryl alcohol

substrate: veratryl alcohol


organism: Agaricus campestris


organism: Bjerkandera adusta

substrate_name: Veratryl alcohol; H2O2

proof_lines: lignin peroxidase activity, pH 3.5, 25°C

proof_lines: lignine peroxidas activity, pH 3.5, 25°C

substrate: Veratryl alcohol; H2O2


organism: Bjerkandera sp.

proof_lines:
Lip-2, depending on pH
Lip-5, depending on pH


organism: Brevibacillus laterosporus

substrate_name: n-Propanol

substrate: n-Propanol


organism: Comamonas sp.

substrate_name: Direct Blue GLL dye

substrate: Direct Blue GLL dye


substrate_name: dGMP

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5, 37ºC
pH 7.5, 30ºC
pH 7.5, isoenzyme 2

substrate: dGMP


organism: Gloeophyllum sepiarium

assay_conditions_summary: pH 2.5; 298.15 K; buffer 50 mM sodium tartrate

proof_lines: in 50 mM sodium tartrate buffer, at pH 2.5, 25°C


organism: Lentinus sajor-caju


organism: Lenzites betulinus


organism: Loweporus lividus

assay_conditions_summary: pH 2.5; 298.15 K; buffer sodium tartrate

proof_lines: 0.4 mM H2O2, 50 mM sodium tartrate buffer pH 2.5, 25°C

proof_lines: 2 mM veratryl alcohol, 50 mM sodium tartrate buffer pH 2.5, 25°C


organism: Phanerochaete chrysosporium

substrate_name: H2O2; 2,4-Dibromophenol

substrate: H2O2; 2,4-Dibromophenol


organism: Phanerodontia chrysosporium


proof_lines: pH 5.5, 30°C, purified enzyme from free Phanerochaete chrysosporium

proof_lines: pH 5.5, 30°C, purified enzyme from immobilized Phanerochaete chrysosporium


organism: Pleurotus ostreatus


organism: Pleurotus sapidus


organism: Polyporous velutinus


organism: Streptomyces griseosporeus


organism: Trametes hirsuta


organism: Trametes sanguinea


organism: Trametes versicolor

proof_lines: enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane, 25°C, pH 5.0


organism: Tropicoporus linteus


organism: Volvariella volvacea


organism: Cucurbita pepo


organism: Homo sapiens

substrate_name: myristoyl-CoA

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines:
pH 8.0, 37°C, recombinant SPTLC3
pH 8.0, 37°C, microsomes

substrate: myristoyl-CoA


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

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


substrate_name: L-alanine

proof_lines: C133W mutant protein, pH not specified in the publication, temperature not specified in the publication

proof_lines: C133W mutant protein, substrate serine, pH and temperature not specified in the publication

substrate: L-alanine


organism: Rattus norvegicus


organism: Rhizorhabdus wittichii

substrate_name: stearoyl-CoA

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

substrate: stearoyl-CoA


organism: Sphingomonas paucimobilis

substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 8.1; 310.15 K; cofactor CoA

proof_lines:
recombinant enzyme
native and recombinant enzyme
native enzyme

substrate: palmitoyl-CoA


organism: Bos taurus

substrate_name: GTP

proof_lines:
calculated as GDP produced
pH 7.5

substrate: GTP


organism: Helianthus tuberosus

substrate_name: GMP

substrate: GMP


assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor ATP

proof_lines: wild type enzyme, in 100 mM Tris–HCl buffer pH 7.5, 4 mM ATP, 10 mM MgCl2, 1 mM dithiothreitol, 100 mM KCl, at 30°C


proof_lines: mutant S35N/V168F, in 100 mM Tris–HCl buffer pH 7.5, 4 mM ATP, 10 mM MgCl2, 1 mM dithiothreitol, 100 mM KCl, at 30°C


organism: Mus musculus

assay_conditions_summary: pH 8; cofactor ATP

proof_lines:
pH 8.0, 37ºC
pH 8.0, 37ºC, dGMP kinase activity


organism: Plasmodium falciparum


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from direct_uniprot_ec_organism_lookup:P15454 and applied mutation signature S35P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_ec_organism_lookup:P15454 and applied mutation signature S35P/D101S to reconstruct the assayed variant sequence.


substrate_name: ATP

assay_conditions_summary: pH 7.7; cofactor ATP

proof_lines:
pH 7.7, 25ºC, reverse reaction
pH 7.5, 25ºC
pH 7.7, 25ºC, forward reaction

substrate: ATP


sequence_variant_note: Resolved canonical sequence from direct_uniprot_ec_organism_lookup:P15454 and applied mutation signature Y78F to reconstruct the assayed variant sequence.


organism: Sus scrofa

proof_lines: pH 7.5, 30ºC, higher affinity than 9-(6-phosphonohexyl)guanine for guanylate kinases al pH values below 7.5


organism: Escherichia coli

substrate_name: N-acetyl-D-glucosamine 1-phosphate

proof_lines:
purified del227 enzyme, pH 7.4
purified del233 enzyme, pH 7.4
purified Tr250 enzyme, pH 7.4

substrate: N-acetyl-D-glucosamine 1-phosphate


organism: Giardia duodenalis

substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


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


organism: Neurospora crassa


organism: Ovis aries


substrate_name: diphosphate

substrate: diphosphate


substrate_name: UTP; D-Glucose 1-phosphate

proof_lines: pH 7.5, 37°C, 10 mM N-acetyl-D-glucose 1-phosphate

substrate: UTP; D-Glucose 1-phosphate


organism: Yersinia pseudotuberculosis

proof_lines: pH 8.2, 37°C, recombinant His6-tagged enzyme


organism: Arabidopsis thaliana

substrate_name: a tRNA precursor

proof_lines: the mutant with alterations at the extreme C-terminus of the tail domain, pH 9.0, 37°C

substrate: a tRNA precursor


proof_lines: pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C74

proof_lines: pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-A76

proof_lines: pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C75


organism: Romanomermis culicivorax

substrate_name: armless tRNA(Ile) precursor

proof_lines:
addition of 2C + A, pH 7.6, 20°C
addition of 2C, pH 7.6, 20°C

substrate: armless tRNA(Ile) precursor


organism: Ascospirella lutea

substrate_name: Dextran T-2000

substrate: Dextran T-2000


organism: Aspergillus carneus

substrate_name: isomaltoheptaose

substrate: isomaltoheptaose


organism: Cellulosimicrobium sp. THN1

substrate_name: Dextran T10

substrate: Dextran T10


organism: Purpureocillium lilacinum

substrate_name: Dextran

proof_lines: isoform D-I, calculated as released reducing sugar, 40°C, pH 6.0

proof_lines: isoform D-II, calculated as released reducing sugar, 40°C, pH 5.0

proof_lines: isoform D-II, calculated as released reducing sugar, 40°C, pH 3.0

substrate: Dextran


organism: Sporothrix schenckii


organism: Streptococcus sobrinus

proof_lines:
175000-molecular-weight dextranase
160000-molecular-weight dextranase


organism: Streptomyces sp.

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


organism: Talaromyces aculeatus

proof_lines: based on the molecular weight of isomaltose


organism: Talaromyces funiculosus


organism: Talaromyces pinophilus

substrate_name: dextran T40

substrate: dextran T40


organism: Thermoanaerobacter pseudethanolicus

substrate_name: dextran T500

sequence_source: UniProtKB:B0KBZ7 (TrEMBL); RCSB PDB 5AXG accession anchor

substrate: dextran T500


organism: Chaetomium erraticum

proof_lines: ultrasound/microwave irradiation shock treatment, pH 5.4, 40°C


organism: Chaetomium globosum

substrate_name: dextran T2000

sequence_source: UniProtKB A0A346FYQ3 / GenBank AXN77607.1

substrate: dextran T2000


organism: Fusarium verticillioides


organism: Lipomyces starkeyi


organism: Penicillium cyclopium

substrate_name: dextran T5

proof_lines:
at pH 5.0 and 50°C
at pH 5.0 and 55°C

substrate: dextran T5


organism: Polystichum aculeatum

proof_lines:
substrate dextran 40 kDa, pH 5.0, 35°C
substrate dextran 70 kDa, pH 5.0, 35°C
substrate dextran 20 kDa, pH 5.0, 35°C


organism: Plasmodium falciparum

substrate_name: dGMP

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8I2M1 and RefSeq XP_001352159.1 after PMID 18374996 identified the enzyme as PlasmoDB PFI1420w; coordinate check confirmed canonical residue 76 is Y. and applied mutation signature Y76F to reconstruct the assayed variant sequence.

substrate: dGMP


substrate_name: GMP

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8I2M1 and RefSeq XP_001352159.1 after PMID 18374996 identified the enzyme as PlasmoDB PFI1420w; coordinate check confirmed canonical residue 103 is N. and applied mutation signature N103D to reconstruct the assayed variant sequence.

substrate: GMP


substrate_name: Unknown

sequence_source: Canonical UniProtKB Q8I2M1 and RefSeq XP_001352159.1 sequence for the PMID 18374996 PFI1420w Plasmodium falciparum guanylate kinase family.

assay_conditions_summary: cofactor ATP

proof_lines:
versus ATP
versus GMP

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8I2M1 and RefSeq XP_001352159.1 after PMID 18374996 identified the enzyme as PlasmoDB PFI1420w; coordinate check confirmed canonical residue 74 is D. and applied mutation signature D74A to reconstruct the assayed variant sequence.


sequence_source: Canonical UniProtKB Q8I2M1 and RefSeq XP_001352159.1 sequence for PMID 18374996 PFI1420w Plasmodium falciparum guanylate kinase.


organism: Rattus norvegicus

substrate_name: ATP

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

substrate: ATP


enzyme_display_name: cytochrome-c peroxidase

organism: Nitrosomonas europaea

enzyme: cytochrome-c peroxidase


organism: Paracoccus denitrificans

substrate_name: ferrocytochrome c

substrate: ferrocytochrome c


organism: Paracoccus pantotrophus

substrate_name: horse heart ferrocytochrome c

assay_conditions_summary: pH 7

proof_lines: membrane solution, 50 mM NaCl, at pH 7.0

substrate: horse heart ferrocytochrome c


organism: Rhodobacter capsulatus

substrate_name: H2O2; Ferrocytochrome c2

proof_lines:
pH 7.0
horse

substrate: H2O2; Ferrocytochrome c2


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 6; 298.15 K; buffer 0.1 M potassium phosphate

proof_lines: pH 6, 20 mM potassium phosphate, wild-type enzyme

proof_lines: pH 6, 200 mM potassium phosphate, wild-type enzyme


assay_conditions_summary: pH 6

proof_lines: pH 6, 20 mM potassium phosphate, V197C/C128A mutant

proof_lines: pH 6, 200 mM potassium phosphate, V197C/C128A mutant


proof_lines: covalent complex of mutant E290C, pH 7.5, 25°C, 100 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex

proof_lines: covalent complex of mutant E290C, pH 7.5, 25°C, 10 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex


substrate_name: iso-1 ferrocytochrome c

assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.1 M potassium phosphate

proof_lines: Km above 0.1 mM, mutant enzyme D34K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C

substrate: iso-1 ferrocytochrome c


proof_lines: mutant enzyme E118K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


proof_lines: mutant enzyme E17K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


organism: Leishmania major

sequence_source: UniProtKB:Q4Q3K2 via RCSB 4GED

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


proof_lines: DELTA10 deltion mutant substrate, pH and temperature not specified in the publication


proof_lines: K98A substrate mutant, pH and temperature not specified in the publication


proof_lines: R24A substrate mutant, pH and temperature not specified in the publication


organism: Methylococcus capsulatus

substrate_name: ferrocytochrome c555

substrate: ferrocytochrome c555


organism: Geobacter sulfurreducens

sequence_source: UniProtKB Q749D0 direct accession lookup on 2026-06-07


sequence_source: UniProtKB P55929 direct accession lookup on 2026-06-07


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB P14532 direct accession lookup on 2026-06-07

proof_lines: pH 7, 25 microM H2O2, protein film voltammetry, the midpoint potentials of the turnover signals are used to calculate Michaelis-Menten kinetics


substrate_name: cytochrome c

sequence_source: UniProtKB P00431 canonical accession lookup on 2026-06-07; row-specific W191 replacement not specified

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

substrate: cytochrome c


substrate_name: guaiacol

sequence_source: Reconstructed from UniProtKB P00431 canonical sequence and UniProt mature-chain feature coordinates on 2026-06-07

sequence_variant_note: Mutation signature Y36A/W191F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: guaiacol


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P00431 canonical sequence and UniProt mature-chain feature coordinates on 2026-06-07 and applied mutation signature W191F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: mutant W191F, pH 6.0, 25°C, the W191F mutation dramatically reduces the activity toward cytochrome c, but in the other variants which do not contain the W191F mutation the activity toward cytochrome c is largely unaffected


sequence_variant_note: Mutation signature N184R/W191F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: ascorbate

sequence_variant_note: Mutation signature N184R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
mutant N184R, pH 6.0, 25°C
mutant FY36A/N184R, pH 6.0, 25°C

substrate: ascorbate


sequence_source: UniProtKB P00431 direct accession check; variant reconstructed from mature-chain mutation signature in selected source evidence

sequence_variant_note: Mutation signature Y36A/N184R/W191F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant Y36A/N184R/W191F, pH 6.0, 25°C, guaiacol oxidation is not significantly affected by any of the mutations, including W191F, which is consistent with the idea that aromatic substrates such as guaiacol bind at a separate location close


sequence_source: UniProtKB P00431 direct accession check

proof_lines: wild-type cytochrome c peroxidase, pH 6.0, 25°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


substrate_name: Ferrocytochrome c; H2O2

sequence_variant_note: Mutation signature H175Q/W191F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: cytochrome-c peroxidase(Enzyme) mutant His175Gln/Trp191Phe

substrate: Ferrocytochrome c; H2O2


substrate_name: H2O2; Ferrocytochrome c

sequence_variant_note: Resolved canonical sequence from UniProtKB P00431 direct accession check; variant reconstructed from mature-chain mutation signature in selected source evidence and applied mutation signature H175Q with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cytochrome-c peroxidase(Enzyme) mutant His175Gln

substrate: H2O2; Ferrocytochrome c


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

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


sequence_variant_note: Resolved canonical sequence from UniProtKB P00431 direct accession check; variant reconstructed from mature-chain mutation signature in selected source evidence and applied mutation signature H175C with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cytochrome-c peroxidase(Enzyme) mutant His175Cys


sequence_variant_note: Resolved canonical sequence from uniprot:P00431|reconstructed_variant_sequence:H175E_mature_chain_maps_to_precursor_H242E and applied mutation signature H175E with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cytochrome-c peroxidase(Enzyme) mutant His175Glu


organism: Shewanella oneidensis

sequence_variant_note: Resolved canonical sequence from uniprot:Q8EF24|reconstructed_variant_sequence:F102W and applied mutation signature F102W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature D18K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D18K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature E209K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E209K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature E291K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E291K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature E290K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E290K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature E98K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E98K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361; PMID 17580971 recombinant rCcP matches mature baker yeast CcP except intended mutation and applied mutation signature D33K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D33K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C


organism: Bacillus anthracis

substrate_name: nicotinate ribonucleotide

sequence_source: RCSB:2QTR entity 1 and UniProtKB:C3L5T6 direct lookups

substrate: nicotinate ribonucleotide


organism: Escherichia coli

sequence_source: UniProtKB:P0A752 direct REST lookup, release 2026_01


substrate_name: beta-nicotinate D-ribonucleotide

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P0A752 canonical sequence using PMID 28455340 variant label; submitted A0A140NE60 is inactive/deleted and applied mutation signature Y84V/Y118D to reconstruct the assayed variant sequence.

substrate: beta-nicotinate D-ribonucleotide


sequence_source: UniProtKB:P0A752 direct REST lookup; submitted A0A140NE60 is inactive/deleted


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P0A752 canonical sequence using PMID 28455340 variant label; submitted A0A140NE60 is inactive/deleted and applied mutation signature A86W/Y118N to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB:P0A752 canonical sequence using PMID 28455340 variant label; submitted A0A140NE60 is inactive/deleted


enzyme_display_name: tryptophan 2,3-dioxygenase

organism: Homo sapiens

substrate_name: L-tryptophan

sequence_source: UniProtKB REST P48775 FASTA checked 2026-06-07

proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme

enzyme: tryptophan 2,3-dioxygenase

substrate: L-tryptophan


substrate_name: L-Tryptophan

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P48775 FASTA checked 2026-06-07 and applied mutation signature Y42A to reconstruct the assayed variant sequence.

substrate: L-Tryptophan


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P48775 FASTA checked 2026-06-07 and applied mutation signature R144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P48775 FASTA checked 2026-06-07 and applied mutation signature Y45A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed P0A752 after UniProtKB A0A140NE60 direct lookup returned inactive/deleted with UniParc UPI00001120B4 mapping to P0A752. and applied mutation signature A86W/Y118N to reconstruct the assayed variant sequence.


substrate_name: reduced nicotinamide nucleotide

sequence_source: UniProtKB reviewed Q96T66 direct REST/FASTA check.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

column_label: Table 1: Kinetic Parameters of Human NMNAT Isozymes (Biochemistry 2007, volume 46, number 16, pages 4912-4922); printed substrate heads ATP, NMN, NaMN and NMNH, each with printed column heads Km (uM), kcat (s-1) and kcat/Km (s-1 M-1). Body row 'NMNAT3', substrate head 'NMNH'; column Km (uM) = 130; column kcat (s-1) = 7.2; column kcat/Km (s-1 M-1) = 0.55 x 10^5. captured primary segment: NMNAT3 | NMNH | Km 130 uM | kcat 7.2 s^-1 | kcat/Km 0.55 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 130 uM; 1 uM is 0.001 mM, so 130 / 1000 = 0.13 mM; the exported value is 0.13 mM. kcat: printed Table 1 cell 7.2 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 7.2 s^(-1); the exported value is 7.2 s^(-1). kcat/Km: printed Table 1 cell 0.55 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell is 55.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.2 / 0.13 = 55.38461538461539 s^-1 mM^-1, the exported value; in the units Table 1 prints, 7.2 s^-1 divided by 130 uM is 0.5538 x 10^5 M^-1 s^-1, which rounds to the printed catalytic-efficiency cell 0.55 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1, body row 'NMNAT3', substrate head 'NMNH': Km = 130 uM; kcat = 7.2 s^-1; printed kcat/Km = 0.55 x 10^5 M^-1 s^-1.

row_label: Table 1, body row NMNAT3, substrate head NMNH

substrate: reduced nicotinamide nucleotide


substrate_name: Nicotinate D-ribonucleotide

substrate: Nicotinate D-ribonucleotide


sequence_source: UniProtKB reviewed Q9BZQ4 direct REST/FASTA check.


substrate_name: ATP

substrate: ATP


sequence_source: UniProtKB reviewed Q9HAN9 direct REST/FASTA check.


column_label: Table 1: Kinetic Parameters of Human NMNAT Isozymes (Biochemistry 2007, volume 46, number 16, pages 4912-4922); printed substrate heads ATP, NMN, NaMN and NMNH, each with printed column heads Km (uM), kcat (s-1) and kcat/Km (s-1 M-1). Body row 'NMNAT1', substrate head 'NMNH'; column Km (uM) = 294; column kcat (s-1) = 18.6; column kcat/Km (s-1 M-1) = 0.63 x 10^5. captured primary segment: NMNAT1 | NMNH | Km 294 uM | kcat 18.6 s^-1 | kcat/Km 0.63 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 294 uM; 1 uM is 0.001 mM, so 294 / 1000 = 0.294 mM; the exported value is 0.294 mM. kcat: printed Table 1 cell 18.6 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 18.6 s^(-1); the exported value is 18.6 s^(-1). kcat/Km: printed Table 1 cell 0.63 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell is 63.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 18.6 / 0.294 = 63.26530612244899 s^-1 mM^-1, the exported value; in the units Table 1 prints, 18.6 s^-1 divided by 294 uM is 0.6327 x 10^5 M^-1 s^-1, which rounds to the printed catalytic-efficiency cell 0.63 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1, body row 'NMNAT1', substrate head 'NMNH': Km = 294 uM; kcat = 18.6 s^-1; printed kcat/Km = 0.63 x 10^5 M^-1 s^-1.

row_label: Table 1, body row NMNAT1, substrate head NMNH


substrate_name: ATP; Nicotinate D-ribonucleotide

substrate: ATP; Nicotinate D-ribonucleotide


mutation_signature: recombinant truncated enzyme mutant

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

proof_lines: pH 8.0, 25°C, recombinant truncated enzyme mutant


substrate_name: O2; L-Tryptophan

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant Y42A (aa 19-388)

substrate: O2; L-Tryptophan


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

proof_lines: pH and temperature not specified in the publication


substrate_name: L-Tryptophan; O2

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant TDO2 (M108I), aa 40-390, His-tagged

substrate: L-Tryptophan; O2


sequence_source: UniProtKB REST P48775 canonical sequence

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


sequence_source: UniProtKB reviewed accession Q9HAN9 direct FASTA/API lookup


sequence_source: UniProtKB reviewed accession Q96T66 direct FASTA/API lookup


sequence_source: UniProtKB reviewed accession Q9BZQ4 direct FASTA/API lookup


column_label: Table 1: Kinetic Parameters of Human NMNAT Isozymes (Biochemistry 2007, volume 46, number 16, pages 4912-4922); printed substrate heads ATP, NMN, NaMN and NMNH, each with printed column heads Km (uM), kcat (s-1) and kcat/Km (s-1 M-1). Body row 'NMNAT2', substrate head 'NMNH'; column Km (uM) = 304; column kcat (s-1) = 3.3; column kcat/Km (s-1 M-1) = 0.11 x 10^5. captured primary segment: NMNAT2 | NMNH | Km 304 uM | kcat 3.3 s^-1 | kcat/Km 0.11 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 304 uM; 1 uM is 0.001 mM, so 304 / 1000 = 0.304 mM; the exported value is 0.304 mM. kcat: printed Table 1 cell 3.3 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 3.3 s^(-1); the exported value is 3.3 s^(-1). kcat/Km: printed Table 1 cell 0.11 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell is 11.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.3 / 0.304 = 10.855263157894736 s^-1 mM^-1, the exported value; in the units Table 1 prints, 3.3 s^-1 divided by 304 uM is 0.1086 x 10^5 M^-1 s^-1, which rounds to the printed catalytic-efficiency cell 0.11 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1, body row 'NMNAT2', substrate head 'NMNH': Km = 304 uM; kcat = 3.3 s^-1; printed kcat/Km = 0.11 x 10^5 M^-1 s^-1.

row_label: Table 1, body row NMNAT2, substrate head NMNH


organism: Mycobacterium tuberculosis

substrate_name: nicotinate beta-D-ribonucleotide

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJJ5 plus PMID 25631047/PDB 4RPI numbering context and applied mutation signature L164A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: nicotinate beta-D-ribonucleotide


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJJ5 plus PMID 25631047/PDB 4RPI numbering context and applied mutation signature W117F with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJJ5 plus RCSB PDB 4RPI W117A construct and applied mutation signature W117A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


organism: Xanthomonas campestris

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_Q8PDA8_and_PMID_18783250 and applied mutation signature H55A to reconstruct the assayed variant sequence.


substrate_name: O2; 5-Fluorotryptophan

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant H55A C-terminal His6-tagged

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant TDO H55A, C-terminal His6-tag

substrate: O2; 5-Fluorotryptophan


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_Q8PDA8_and_PMID_18783250 and applied mutation signature H55S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q8PDA8 direct REST/FASTA check


proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant H55S C-terminal His6-tagged

proof_lines: SABIO-RK modifier species: tryptophan 2,3-dioxygenase(Enzyme) mutant TDO H55S, C-terminal His6-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8PDA8 canonical sequence plus UniProt/RCSB-supported H55 variant reconstruction and applied mutation signature H55A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8PDA8 canonical sequence plus UniProt/RCSB-supported H55 variant reconstruction and applied mutation signature H55S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q8PDA8 canonical sequence plus UniProt/RCSB-supported H55 variant reconstruction


smiles: O=O


organism: Monosiga brevicollis

sequence_source: UniProtKB REST direct lookup A9V766; TrEMBL; Tryptophan 2,3-dioxygenase; organism Monosiga brevicollis; EC 1.13.11.11; canonical sequence length 546.


organism: Mus musculus

sequence_source: UniProtKB REST direct lookup P48776; Swiss-Prot; Tryptophan 2,3-dioxygenase; organism Mus musculus; EC 1.13.11.11; canonical sequence length 406.


substrate_name: O2; D-Tryptophan

substrate: O2; D-Tryptophan


organism: Rattus norvegicus

sequence_source: UniProtKB REST direct lookup P21643; Swiss-Prot; Tryptophan 2,3-dioxygenase; organism Rattus norvegicus; EC 1.13.11.11; canonical sequence length 406.


sequence_source: UniProtKB REST direct lookup Q8PDA8; Swiss-Prot; Tryptophan 2,3-dioxygenase; organism Xanthomonas campestris pv. campestris strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25; EC 1.13.11.11; canonical sequence length 298.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8PDA8; direct REST FASTA/JSON check on 2026-06-07 and applied mutation signature H55S to reconstruct the assayed variant sequence.


substrate_name: 6-Methyltryptophan; O2

sequence_source: UniProtKB reviewed accession Q8PDA8; direct REST FASTA/JSON check on 2026-06-07

substrate: 6-Methyltryptophan; O2


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8PDA8; direct REST FASTA/JSON check on 2026-06-07 and applied mutation signature H55A to reconstruct the assayed variant sequence.


substrate_name: Phosphoenolpyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08839; direct REST FASTA/JSON check on 2026-06-07 and applied mutation signature C502A to reconstruct the assayed variant sequence.

substrate: Phosphoenolpyruvate


sequence_source: UniProtKB reviewed accession P08839; direct REST FASTA/JSON check on 2026-06-07


organism: Cupriavidus metallidurans

sequence_source: UniProtKB:Q1LK00 official UniProt REST lookup 2026-06-07


sequence_source: UniProtKB:P48775 official UniProt REST lookup 2026-06-07


sequence_variant_note: Resolved canonical sequence from UniProtKB:P48775 official UniProt REST lookup 2026-06-07 plus selected H76S mutation signature and applied mutation signature H76S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P48775 official UniProt REST lookup 2026-06-07 plus selected S151A mutation signature and applied mutation signature S151A to reconstruct the assayed variant sequence.


organism: Macaca fascicularis

sequence_source: UniProtKB:G7P6G7 official UniProt REST lookup 2026-06-07


sequence_source: UniProtKB:A9V766 official UniProt REST lookup 2026-06-07


sequence_source: UniProtKB P9WJJ5 live FASTA direct check on 2026-06-07


organism: Plasmodium falciparum

sequence_source: UniProtKB Q8IE38 live FASTA direct check on 2026-06-07

proof_lines: recombinant His6-tagged enzyme, pH 7.5, 37°C


proof_lines: mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant C43A, pH not specified in the publication, temperature not specified in the publication


substrate_name: nicotinic acid ribonucleotide

sequence_source: UniProtKB REST direct accession lookup: Q8IE38

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

substrate: nicotinic acid ribonucleotide


proof_lines: mutant C41A, pH not specified in the publication, temperature not specified in the publication


organism: Saccharomyces cerevisiae

substrate_name: diphosphate

sequence_source: UniProtKB REST direct accession lookup: P53204

substrate: diphosphate


organism: Streptococcus pyogenes

substrate_name: Unknown

sequence_source: UniProtKB REST direct accession lookup: Q5XDT7

substrate: Unknown


enzyme_display_name: adenine deaminase

organism: Aspergillus nidulans

substrate_name: H2O; Adenine

sequence_source: UniProtKB REST direct accession lookup: Q8X1T6

enzyme: adenine deaminase

substrate: H2O; Adenine


organism: Blastobotrys adeninivorans

sequence_source: UniProtKB REST direct accession lookup: L8BT48


organism: Helicobacter pylori

substrate_name: Adenine; H2O

substrate: Adenine; H2O


sequence_source: UniProtKB reviewed P9WJJ5 canonical wild-type sequence, fetched 2026-06-07

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


substrate_name: adenine

substrate: adenine


sequence_source: UniProtKB:P53909 canonical sequence; direct UniProt lookup on 2026-06-07


organism: Schizosaccharomyces pombe

sequence_source: UniProtKB:Q9P6I7 canonical sequence; direct UniProt lookup on 2026-06-07


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Homo sapiens

substrate_name: L-tryptophan

proof_lines: kcat is 0.54 sec(-1) with L-tryptophan as substrate.

substrate: L-tryptophan


organism: Escherichia coli (strain K12)

substrate_name: mannitol phosphate

proof_lines: Enzyme I-Ntr activity requires high ionic strength.

substrate: mannitol phosphate


substrate_name: ZFPEP

proof_lines: kcat is 3830 min(-1) with PEP as substrate. kcat is 370 min(-1) with ZFPEP as substrate. kcat is 285 min(-1) with ZMePEP as substrate. kcat is 15.8 min(-1) with ZClPEP as substrate. kcat is 2.8 min(-1) with EClPEP as substrate.

substrate: ZFPEP


organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)

substrate_name: nicotinamide mononucleotide

proof_lines: kcat is 4.9 sec(-1) with nicotinamide mononucleotide as substrate. kcat is 3.0 sec(-1) with nicotinate mononucleotide as substrate.

substrate: nicotinamide mononucleotide


substrate_name: NMN

proof_lines: KM is >100 uM for triazofurin monophosphate.

substrate: NMN


organism: Mus musculus

substrate_name: nicotinamide mononucleotide (NMN)

proof_lines: kcat is 4.5 sec(-1) with ATP as substrate (PubMed:19403820). kcat is 5.5 sec(-1) with nicotinamide mononucleotide (NMN) as substrate (PubMed:19403820).

substrate: nicotinamide mononucleotide (NMN)


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


substrate_name: pyrogallol

proof_lines: pH 6, 20 mM potassium phosphate, covalent complex

proof_lines: pH 6, 200 mM potassium phosphate, covalent complex

substrate: pyrogallol


organism: Saccharomyces pastorianus

substrate_name: ferrocytochrome c

proof_lines: yeast, with electron acceptor ethyl peroxide

proof_lines: horse heart, with electron acceptor H2O2

substrate: ferrocytochrome c


organism: Shewanella oneidensis

proof_lines: pH 7.5, temperature not specified in the publication


enzyme_display_name: cytochrome c peroxidase

substrate_name: iso-1 ferrocytochrome c

sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature E201K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.100 M ionic strength potassium phosphate

proof_lines: mutant enzyme E201K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C

enzyme: cytochrome c peroxidase

substrate: iso-1 ferrocytochrome c


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature D210K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D210K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature E32K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E32K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature R31E to reconstruct the assayed variant sequence.

proof_lines: Km above 0.1 mM, mutant enzyme R31E, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature D37K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D37K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


sequence_variant_note: Resolved canonical sequence from UniProt P00431 mature chain 68-361 plus PMID 17580971 mutation reconstruction and applied mutation signature E35K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E35K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25 C


organism: Canis lupus

substrate_name: L-Tryptophan; O2

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

substrate: L-Tryptophan; O2


organism: Bacillus subtilis

substrate_name: deamido-NAD+

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

substrate: deamido-NAD+


organism: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)

substrate_name: tryptophan

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

substrate: tryptophan


organism: Staphylococcus carnosus (strain TM300)

substrate_name: PEP

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

substrate: PEP


substrate_name: beta-nicotinamide D-ribonucleotide

substrate: beta-nicotinamide D-ribonucleotide


substrate_name: ATP

substrate: ATP


organism: Escherichia coli

substrate_name: nicotinate ribonucleotide

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

substrate: nicotinate ribonucleotide


organism: Nicotiana tabacum


organism: Saccharomyces cerevisiae

proof_lines: 37°C, pH 7.5, + nicotinate ribonucleotide


organism: Alteromonas macleodii

proof_lines: pH and temperature not specified in the publication


substrate_name: adenine

sequence_source: UniProtKB reviewed accession P39761 (ADEC_BACSU), checked during EC-organism lookup

substrate: adenine


organism: Burkholderia sp.


organism: Crithidia fasciculata


sequence_source: UniProtKB:P31441; NCBI RefSeq NP_418121.1 direct lookup


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P31441 / NCBI RefSeq NP_418121.1 using PMID 21247091 D474N mutant label and applied mutation signature D474N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P31441 / NCBI RefSeq NP_418121.1 using PMID 21247091 H92Q mutant label and applied mutation signature H92Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P31441 / NCBI RefSeq NP_418121.1 using PMID 21247091 H92D mutant label and applied mutation signature H92D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P31441 / NCBI RefSeq NP_418121.1 using PMID 21247091 D285A mutant label and applied mutation signature D285A to reconstruct the assayed variant sequence.


organism: Leishmania mexicana


organism: Leishmania tarentolae


organism: Methanocaldococcus jannaschii

sequence_source: UniProt Q58854 (ADEC_METJA), reviewed EC 3.5.4.2 adenine deaminase

proof_lines: wild-type, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt Q58854 canonical sequence with C127A reconstructed after confirming residue 127 is C and applied mutation signature C127A to reconstruct the assayed variant sequence.

proof_lines: mutant C127A, pH 7.0, temperature not specified in the publication


organism: Paenarthrobacter aurescens

sequence_source: UniProt A1R3U3 (paper-linked AAur1117 / Paenarthrobacter aurescens strain TC1), unreviewed EC 3.5.4.2 entry


organism: Pseudomonas aeruginosa

sequence_source: UniProt Q9I6Y4 (ADE_PSEAE / Pseudomonas aeruginosa PAO1 Pa0148), reviewed EC 3.5.4.2 adenine deaminase


organism: Mycobacterium tuberculosis

substrate_name: nicotinate beta-D-ribonucleotide

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; W45A applied with residue-numbering offset -5 and applied mutation signature W45A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

substrate: nicotinate beta-D-ribonucleotide


sequence_source: UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; T86A applied with residue-numbering offset -5 and applied mutation signature T86A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; W45A applied with residue-numbering offset -5


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; P44A applied with residue-numbering offset -5 and applied mutation signature P44A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJJ5 reviewed canonical FASTA retrieved 2026-06-07; K47A applied with residue-numbering offset -5 and applied mutation signature K47A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature H235Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 20 mM HEPES


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature H214N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature E236Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature D118N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature H120N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_paper_cloned_refseq_uniprot and applied mutation signature H90N to reconstruct the assayed variant sequence.


organism: Pseudomonas synxantha

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


sequence_source: UniProtKB:P53909 reviewed entry ADE_YEAST; REST record retrieved from rest.uniprot.org.

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

assay_conditions_summary: pH 7; 306.15 K; buffer 0.2 M phosphate

proof_lines: 0.067 mM adenine in 0.2 M phosphate buffer, 33°C, pH 7.0


organism: Schizosaccharomyces pombe

sequence_source: UniProtKB:Q9P6I7 reviewed entry ADE_SCHPO; REST record retrieved from rest.uniprot.org.


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


proof_lines: wild-type, pH 7.5, 30°C, + Fe sequestered with a metal chelator, growth medium supplemented with Mn2+ prior to induction


organism: Kluyveromyces lactis


organism: Leishmania braziliensis


organism: Leishmania donovani


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31441 and applied mutation signature H90C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

column_label: Table 3 (Catalytic constants and metal binding properties of E. coli ADE mutants), mutant row 'H90C'; column 'Km (mM)' = 0.51; column 'kcat (s^-1)' = 0.053; column 'kcat/Km (M^-1 s^-1)' = 103; column 'Metal content (Mn)' = 0.032 +/- 0.003.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.51 under the column head Km (mM); the printed millimolar column needs no conversion, so the canonical value is 0.51 mM; the exported value is 0.51 mM. kcat: printed Table 3 cell 0.053 under the column head kcat (s^-1); the printed per-second column needs no conversion, so the canonical value is 0.053 s^-1; the exported value is 0.053 s^(-1). kcat/Km: printed Table 3 cell 103 under the column head kcat/Km (M^-1 s^-1); one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 103 / 1000 = 0.103 s^-1 mM^-1; the exported value 0.10392156862745097 s^(-1)*mM^(-1) is the quotient of this row's own two printed component cells, and the printed primary cell supersedes it.

raw_value_unit_evidence: Table 3, mutant row H90C: Km = 0.51 mM (printed with its tolerance 0.51 +/- 0.05); kcat = 0.053 s^-1 (printed with its tolerance 0.053 +/- 0.008); kcat/Km = 103 M^-1 s^-1 (printed with its tolerance 103 +/- 9). The printed column heads are Km (mM), kcat (s^-1) and kcat/Km (M^-1 s^-1).

row_label: Table 3, mutant row H90C

table_label: Table 3: Catalytic constants and metal binding properties of E. coli ADE mutants (Biochemistry 2011, 50(11):1917-1927)


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature D284A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature H90Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature E185Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature H473N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID:21247091 cloned E. coli K-12 ADE gi|16131535; NCBI NP_418121.1; UniProtKB reviewed P31441/ADEC_ECOLI; row-specific substitution reconstructed from the selected mutation signature. and applied mutation signature H92N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H235D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H214Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H92C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H235N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature E121Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31441 canonical sequence with PMID:21247091 Table 3 row-specific substitution and applied mutation signature H90D to reconstruct the assayed variant sequence.


organism: Unknown

substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Streptococcus salivarius

substrate_name: histidine-containing protein

substrate: histidine-containing protein


substrate_name: Protein histidine; Phosphoenolpyruvate

proof_lines:
between 0.2 and 0.4
inhibits the phosphorylated enzyme

substrate: Protein histidine; Phosphoenolpyruvate


substrate_name: Phosphoenolpyruvate; Protein histidine

sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature C502A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate---protein phosphotransferase(Enzyme) mutant C502A

substrate: Phosphoenolpyruvate; Protein histidine


organism: Salmonella typhimurium


organism: Staphylococcus carnosus


substrate_name: protein histidine

proof_lines:
at pH 7,0
at pH 6,1
at pH 7,9

substrate: protein histidine


organism: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)

substrate_name: (Phosphate)(32) (at pH 8.6)

sequence_source: source_record; UniProtKB A5U654 primary-source check

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: kcat is 199 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 7.5. kcat is 208 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 8.6. kcat is 108 sec(-1) with ATP as substrate at pH 7.5. kcat is 116 sec(-1) with ATP

substrate: (Phosphate)(32) (at pH 8.6)


enzyme_display_name: steroid 17alpha-monooxygenase

organism: Homo sapiens

substrate_name: progesterone (17-alpha hydroxylation)

proof_lines: kcat is 1.01 min(-1) with progesterone as substrate. kcat is 0.39 min(-1) with pregnenolone as substrate. kcat is 0.24 min(-1) with 17alpha-hydroxypregnenolone as substrate.

enzyme: steroid 17alpha-monooxygenase

substrate: progesterone (17-alpha hydroxylation)


organism: Thermobifida fusca

substrate_name: D-glucose

proof_lines: recombinant free cellulose-binding module fusion enzyme, pH 9.0, 50°C

proof_lines: recombinant free cellulose-binding module fusion enzyme, pH 7.5, 30°C

proof_lines: recombinant immobilized cellulose-binding module fusion enzyme, pH 9.0, 50°C

substrate: D-glucose


organism: Acidipropionibacterium acidipropionici


organism: Arthrobacter sp.

substrate_name: glucose

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

substrate: glucose


organism: Microlunatus phosphovorus


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8.6; cofactor ATP

proof_lines:
pH 8.6
pH 7.5
pH 7.5, reaction with ATP


organism: Mycolicibacterium phlei

proof_lines:
pH 8.5, 30°C, immobilized enzyme
pH 8.5, 37°C
pH 8.5, 30°C, soluble enzyme


organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: UTP

substrate: UTP


organism: Bos taurus

substrate_name: progesterone

substrate: progesterone


organism: Cavia porcellus


proof_lines:
pH 7.4
competitive substrate with progesterone
more than 0.003100


organism: Rattus norvegicus

proof_lines: C17,20 lyase activity in female duodenum


organism: Sus scrofa


substrate_name: (Phosphate)n; D-Glucose

sequence_source: UniProtKB reviewed accession A5U654

substrate: (Phosphate)n; D-Glucose


substrate_name: (Phosphate)n

substrate: (Phosphate)n


substrate_name: D-Glucose

substrate: D-Glucose


organism: Nostoc sp.

substrate_name: D-mannose

substrate: D-mannose


organism: Streptomyces coelicolor

sequence_source: UniProtKB unreviewed accession Q9ADE8

proof_lines:
at pH 7.7 and 28°C
pH 7.7, 28°C


organism: Danio rerio

proof_lines:
isoform P450 17A2, at pH 7.4 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.4


proof_lines:
isoform P450 17A1, at pH 7.4 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.4


substrate_name: pregnenolone

substrate: pregnenolone


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB:P05093 plus reconstructed R358Q and applied mutation signature R358Q to reconstruct the assayed variant sequence.

proof_lines: R358Q-mutant, inhibiton of 17alpha-hydrolase activity

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05093 plus reconstructed R347H and applied mutation signature R347H to reconstruct the assayed variant sequence.

proof_lines: R347H-mutant, inhibiton of 17alpha-hydrolase activity


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05093 plus reconstructed K89N and applied mutation signature K89N to reconstruct the assayed variant sequence.

proof_lines: K89N mutant expressed in Saccharomyces cerevisiae

proof_lines: K89N-mutant, inhibiton of 17alpha-hydrolase activity


substrate_name: NADPH; 17alpha-Hydroxyprogesterone

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

proof_lines: 17alpha-hydroxylation, pH 7.4, 37°C, presence of cytochrome b5

substrate: NADPH; 17alpha-Hydroxyprogesterone


sequence_source: UniProtKB:P05093 direct accession FASTA lookup


proof_lines: wild type, inhibiton of 17alpha-hydrolase activity


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05093 direct accession FASTA lookup with A105L substitution applied and applied mutation signature A105L to reconstruct the assayed variant sequence.


organism: Ovis aries

sequence_source: UniProtKB:Q29497 direct accession FASTA lookup

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

proof_lines: isozyme 1, pH 7.4, temperature not specified in the publication

proof_lines: isozyme 2, pH 7.4, temperature not specified in the publication


organism: Xenopus laevis

sequence_source: UniProtKB:Q9DDJ5 direct accession FASTA lookup


substrate_name: Pregnenolone

sequence_source: UniProtKB:Q9DDJ5 direct accession lookup

substrate: Pregnenolone


substrate_name: Progesterone

substrate: Progesterone


substrate_name: Progesterone; O2; NADPH

assay_conditions_summary: cofactor NADP+

substrate: Progesterone; O2; NADPH


organism: Anabaena sp.

substrate_name: mannose

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

substrate: mannose


organism: Corynebacterium glutamicum

substrate_name: ITP

assay_conditions_summary: pH 7; cofactor ATP

proof_lines: pH 7.0, temperature not specified in the publication

substrate: ITP


organism: Methylomonas methanica

sequence_source: UniProtKB:A0A3G4RHV5 direct accession lookup

assay_conditions_summary: pH 8.5; 301.15 K; cofactor ATP

column_label: Retained PMC HTML Table 2, PolyP-Glk column, Glucose rows: kcat substrate 0.395 1/min; Km app 0.45 +/- 0.12 mM; kcat/Km 0.87 1/min mM.

raw_value_unit_evidence: Table 2 PolyP-Glk/Glucose cells: kcat substrate 0.395 1/min; Km app 0.45 +/- 0.12 mM; independently printed kcat/Km 0.87 1/min mM.

row_label: PolyP-Glk / Glucose

table_label: Table 2. Kinetic parameters of ATP- and polyphosphate-dependent glucokinases from Methylomonas sp. 12.


enzyme_display_name: enoyl-CoA hydratase

organism: Amycolatopsis orientalis

substrate_name: crotonyl-CoA

sequence_source: source_record; confirmed against live UniProt REST accession G4V4T7 on 2026-06-08

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.7 min(-1) for enoyl-CoA-hydratase activity.

enzyme: enoyl-CoA hydratase

substrate: crotonyl-CoA


organism: Arabidopsis thaliana


organism: Escherichia coli (strain K12)

substrate_name: crotonyl-CoA (for enoyl-CoA hydratase activity)

assay_conditions_summary: cofactor NADH


organism: Homo sapiens


substrate_name: crotonyl-CoA ((2E)-butenoyl-CoA)

substrate: crotonyl-CoA ((2E)-butenoyl-CoA)


sequence_source: UniProt REST exact accession lookup

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23965 canonical sequence with row-specific K242T reconstruction and applied mutation signature K242T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23965 canonical sequence with row-specific K242C reconstruction and applied mutation signature K242C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23965 canonical sequence with row-specific K242D reconstruction and applied mutation signature K242D to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis

substrate_name: crotonoyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup: P9WNP3 and applied mutation signature D40N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: crotonoyl-CoA