sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q93088 with row-specific R16C substitution reconstructed during review and applied mutation signature R16C to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

substrate_name: L-homocysteine

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB reviewed accession O09171 (BHMT1_RAT), checked by direct UniProt FASTA/API lookup

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

substrate: L-homocysteine

source: brenda


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

organism: Dengue virus

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

proof_lines: pH 7.5, 20°C, Michaelis constants for S-adenosyl-methionine (AdoMet) in both reactions are about 10fold lower than for their respective RNA substrates, suggesting that the rate-limiting steps in methylase reactions are associated with RNA t

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


organism: Orthopoxvirus vaccinia

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

mutation_type: substitution

proof_lines: mutant enzyme F679N, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


substrate_name: S-adenosyl-L-methionine

proof_lines: wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C

substrate: S-adenosyl-L-methionine


proof_lines: mutant enzyme K607Q, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme E763A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme N570A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme R632Q, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


organism: Gallus sp.

substrate_name: tetrahydrofolic acid

proof_lines:
25 mM KCl
150 mM KCl

substrate: tetrahydrofolic acid


organism: Homo sapiens

proof_lines: dextran-rich phase, at pH 7.4, temperature not specified in the publication

proof_lines: 66 mM Tris, pH 7.4, 50 mM KCl, temperature not specified in the publication

proof_lines: PEG-rich phase, at pH 7.4, temperature not specified in the publication


organism: Lathyrus oleraceus


organism: Mus musculus

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Staphylococcus lugdunensis

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


enzyme_display_name: diacylglycerol O-acyltransferase

organism: Bos taurus

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

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

assay_conditions_summary: cofactor CoA

enzyme: diacylglycerol O-acyltransferase

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


organism: Brassica napus

substrate_name: 1,2-Diacyl-sn-glycerol; Acyl-CoA

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

substrate: 1,2-Diacyl-sn-glycerol; Acyl-CoA


organism: Glycine max

proof_lines:
with stearoyl-CoA
with oleoyl-CoA


organism: Helianthus annuus

substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


organism: Mycolicibacterium smegmatis


substrate_name: sn-1,2-Dioleoylglycerol; Oleoyl-CoA

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

substrate: sn-1,2-Dioleoylglycerol; Oleoyl-CoA


enzyme_display_name: protein O-GlcNAc transferase

substrate_name: UDP-GlcNAc

enzyme: protein O-GlcNAc transferase

substrate: UDP-GlcNAc


substrate_name: UDP-N-azidoacetylglucosamine

substrate: UDP-N-azidoacetylglucosamine


proof_lines: Y434A mutant, approximately double the Km value of wild type


proof_lines: pH and temperature not specified in the publication, mutant enzyme N186A


proof_lines: pH and temperature not specified in the publication, mutant enzyme N84A


proof_lines: pH and temperature not specified in the publication, mutant enzyme N458A


proof_lines: pH and temperature not specified in the publication, mutant enzyme N424A


proof_lines: pH and temperature not specified in the publication, mutant enzyme N155A


enzyme_display_name: deoxyhypusine synthase

organism: Saccharomyces cerevisiae

substrate_name: spermidine

assay_conditions_summary: cofactor NAD+

proof_lines:
yeast recombinant eIF-5Ab
yeast recombinant eIF-5Aa

enzyme: deoxyhypusine synthase

substrate: spermidine


enzyme_display_name: phosphoserine transaminase

organism: Arabidopsis thaliana

enzyme: phosphoserine transaminase


organism: Escherichia coli

proof_lines: MalE/PdxC(SerC) fusion protein, pH 8.2, 37°C


organism: Ovis aries


organism: Spinacia oleracea

substrate_name: L-glutamate

substrate: L-glutamate


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed accession P56558

proof_lines: calculated from the linear regions of the reciprocal plot from 0.05 mM to 4.8 mM UDP-GlcNAc, His-p110 trimer


enzyme_display_name: spermidine synthase

organism: Sus scrofa

enzyme: spermidine synthase


organism: Thermotoga maritima

sequence_source: UniProtKB reviewed accession Q9WZC2 via RCSB PDB 1INL/1JQ3 SIFTS mapping


organism: Homo sapiens

substrate_name: putrescine

proof_lines:
pH 9.5, 37°C
reaction with putrescine
pH 9.5

substrate: putrescine


proof_lines: pH and temperature not specified in the publication


substrate_name: NAD+

sequence_source: UniProtKB reviewed accession Q6AY53

substrate: NAD+


enzyme_display_name: aminodeoxychorismate synthase

enzyme: aminodeoxychorismate synthase


substrate_name: L-glutamine

proof_lines: mutant K213A/Q147K amidotransferase activity, pH 8.0, 25°C

substrate: L-glutamine


organism: Stenotrophomonas maltophilia

proof_lines: PabB, second half of the reaction, pH 8.0, 25°C

proof_lines: PabB, addition of Escherichia coli PabA enhances the reaction rate 20fold in the absence of glutamine, pH 8.0, 25°C


enzyme_display_name: cAMP-dependent protein kinase

enzyme: cAMP-dependent protein kinase


substrate_name: ATP; p65

verification_status: unverified

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: pH 7.0, 30°C, recombinant catalytic subunit Cgamma

proof_lines: pH 7.5, 30°C, recombinant catalytic subunit

substrate: ATP; p65

status: unverified


organism: Manduca sexta

substrate_name: Kemptide

assay_conditions_summary: pH 7; 295.15 K; cofactor ATP

proof_lines:
pH 7.0, 22°C, catalytic subunit
ATP in form of MgATP2-

substrate: Kemptide


organism: Mus musculus

substrate_name: RFARKGSLREKNV

proof_lines: pH 7.0, 30°C, recombinant catalytic subunit Calpha

substrate: RFARKGSLREKNV


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: pH 7.0, 37°C, recombinant mutant M120G catalytic subunit


substrate_name: Leu-Arg-Arg-Ala-Ser-Leu-Gly

assay_conditions_summary: pH 7; cofactor ATP

proof_lines: pH 7.0, temperature not specified in the publication, myristoylated enzyme mutant K7C

proof_lines: pH 7.0, temperature not specified in the publication, enzyme mutant K7C

substrate: Leu-Arg-Arg-Ala-Ser-Leu-Gly


proof_lines: pH 7.0, temperature not specified in the publication, myristoylated wild-type enzyme and enzyme mutant K7C

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

proof_lines: pH 7.0, 37°C, recombinant wild-type catalytic subunit


substrate_name: peptide RRYSV

substrate: peptide RRYSV


organism: Mytilus galloprovincialis

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: C-subunit isoform C4, in 50 mM Tris-HCl (pH 7.0), 1 mM dithiothreitol, 5 mM MgCl2, 0.2 mM ATP, at 25°C

proof_lines: C-subunit isoform C1, in 50 mM Tris-HCl (pH 7.0), 1 mM dithiothreitol, 5 mM MgCl2, 0.2 mM ATP, at 25°C

proof_lines: C-subunit isoform C3, in 50 mM Tris-HCl (pH 7.0), 1 mM dithiothreitol, 5 mM MgCl2, 0.2 mM ATP, at 25°C


enzyme_display_name: dephospho-CoA kinase

substrate_name: ATP; Dephospho-CoA

assay_conditions_summary: cofactor ATP

enzyme: dephospho-CoA kinase

substrate: ATP; Dephospho-CoA


substrate_name: ATP

proof_lines:
cytosolic enzyme
mitochondrial enzyme

substrate: ATP


enzyme_display_name: triokinase

substrate_name: D-Glyceraldehyde; ATP

enzyme: triokinase

substrate: D-Glyceraldehyde; ATP


substrate_name: ATP; D-Glyceraldehyde

assay_conditions_summary: pH 7.5; 297.15 K; cofactor ATP

proof_lines: pH 7.5, 23-24°C, cosubstrate 0.5 mM MgATP2-

substrate: ATP; D-Glyceraldehyde


enzyme_display_name: N-acetylglucosamine kinase

substrate_name: N-acetyl-D-galactosamine

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

enzyme: N-acetylglucosamine kinase

substrate: N-acetyl-D-galactosamine


organism: Candida albicans

substrate_name: N-acetyl-D-glucosamine

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: N-acetyl-D-glucosamine


organism: Tetradesmus obliquus

substrate_name: L-phosphoserine

substrate: L-phosphoserine


organism: Trichomonas vaginalis

substrate_name: O-phospho-L-serine

substrate: O-phospho-L-serine


proof_lines: glutamate production in the presence of chorismate, pH 8.0, 37°C

proof_lines: NH3-dependent p-aminobenzoate production in the absence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C

proof_lines: p-aminobenzoate or pyruvate production in the presence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C


substrate_name: chorismate

proof_lines: wild-type, cosubstrate L-glutamine, pH 8.5, 25°C

proof_lines: wild type amidotransferase activity, pH 8.0, 25°C

proof_lines: wild-type, cosubstrate NH4+, pH 8.5, 25°C

substrate: chorismate


proof_lines: mutant K274R, cosubstrate L-glutamine, pH 8.5, 25°C

proof_lines: mutant K274R, cosubstrate NH4+, pH 8.5, 25°C


proof_lines: mutant K274A, cosubstrate L-glutamine, pH 8.5, 25°C

proof_lines: mutant K274A, cosubstrate NH4+, pH 8.5, 25°C


organism: Clostridium acetobutylicum


assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP


substrate_name: Unknown

proof_lines: recombinant mutant S338A catalytic subunit, pH 7.5

substrate: Unknown


proof_lines: recombinant wild-type catalytic subunit, pH 7.5


proof_lines: pH and temperature not specified in the publication


organism: Zea mays

substrate_name: RRASVA

substrate: RRASVA


organism: Columba sp.

substrate_name: dephospho-CoA

assay_conditions_summary: pH 8.2; 310.15 K; cofactor CoA

substrate: dephospho-CoA


organism: Corynebacterium ammoniagenes

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP


enzyme_display_name: carbamate kinase

organism: Enterococcus faecalis

substrate_name: ATP; NH3; CO2

assay_conditions_summary: pH 7.5; 308.15 K; cofactor ATP

proof_lines:
pH 7.5, 35°C
dATP in form of MgATP2-
ATP in form of MgATP2-

enzyme: carbamate kinase

substrate: ATP; NH3; CO2


substrate_name: ATP; CO2; NH3

proof_lines: SABIO-RK modifier species: carbamate kinase(Enzyme) mutant strain SW25

substrate: ATP; CO2; NH3


organism: Lentilactobacillus buchneri

substrate_name: Carbamoyl phosphate

assay_conditions_summary: pH 5; 303.15 K; cofactor ADP

proof_lines:
cosubstrate MgADP-, 30°C, pH 5.0
30°C, pH 5.0
ADP in form of MgADP-

substrate: Carbamoyl phosphate


organism: Mycoplasma arthritidis

substrate_name: Carbamoyl phosphate; ADP

substrate: Carbamoyl phosphate; ADP


organism: Neurospora crassa

substrate_name: bicarbonate

substrate: bicarbonate


enzyme_display_name: RNA uridylyltransferase

substrate_name: UTP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

enzyme: RNA uridylyltransferase

substrate: UTP


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed accession P81799 (NAGK_RAT); direct EC+organism lookup, catalytic EC 2.7.1.59 evidence PMID 9523722.

proof_lines: enzyme from kidney with N-acetyl-D-glucosamine as substrate, 32°C, pH 7.5


organism: Streptococcus pyogenes

substrate_name: ATP; N-Acetyl-D-glucosamine

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: for reaction with N-acetyl-D-glucosamine, 30°C, pH 7.4

substrate: ATP; N-Acetyl-D-glucosamine


organism: Sus scrofa

substrate_name: ATP

assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

substrate: ATP


organism: Yarrowia lipolytica

substrate_name: D-mannose

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: D-mannose


enzyme_display_name: N-acylmannosamine kinase

substrate_name: N-acetyl-D-mannosamine

assay_conditions_summary: pH 8.1; 310.15 K; cofactor ATP

proof_lines:
pH 8.1, 37°C
pH 7.5, 37°C, hexamer
pH 7.5, 37°C, dimer

enzyme: N-acylmannosamine kinase

substrate: N-acetyl-D-mannosamine


organism: Salmonella enterica subsp. enterica serovar Typhimurium

sequence_source: UniProtKB reviewed accession Q8ZLQ8 (NANK_SALTY); protein-name fallback for Salmonella typhimurium, EC 2.7.1.60. Checked top Typhimurium strain accessions A0A0H3NSF7 and A0A0F6B7C6; their NanK sequences matched Q8ZLQ8.

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP


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

organism: Actinidia chinensis

substrate_name: Phosphate; GDP-L-galactose

substrate: Phosphate; GDP-L-galactose


organism: Arabidopsis thaliana

substrate_name: GDP-L-galactose; Phosphate

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

substrate: GDP-L-galactose; Phosphate


organism: Brassica rapa


organism: Pisum sativum


organism: Bacillus subtilis

substrate_name: undecaprenyl phosphate

substrate: undecaprenyl phosphate


organism: Escherichia coli

substrate_name: dodecaprenylphosphate

proof_lines:
pH 7.5, 30°C
pH 7.8, 37°C, solubilized enzyme
pH 7.8, 37°C

substrate: dodecaprenylphosphate


enzyme_display_name: tagatose-bisphosphate aldolase

substrate_name: D-Tagatose 1,6-bisphosphate

proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant Q59A

enzyme: tagatose-bisphosphate aldolase

substrate: D-Tagatose 1,6-bisphosphate


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant F67H


source_db: oed

source: oed


kcat_over_km_origin: calculated

sequence_source: UniProtKB reviewed accession P0AB74 direct lookup on 2026-06-11

data_origin: experimental


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant S61T/G64T/F67H


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant Q59A/S61T/D288A


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant Q59A/F67H


sequence_source: UniProtKB reviewed entry P0AB74 FASTA/JSON direct lookup


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant S61T


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant Q59A/G64T/F67H


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant D288A


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant G64T


sequence_source: UniProtKB reviewed entry P0C8J6 (GATY_ECOLI), direct REST lookup on 2026-06-11


enzyme_display_name: diaminopimelate decarboxylase

sequence_source: UniProtKB REST direct lookup: Q949X7

enzyme: diaminopimelate decarboxylase


sequence_source: UniProtKB REST direct lookup: Q94A94


organism: Bacillus anthracis

sequence_source: UniProtKB REST direct lookup: A0A6L7HN53


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 REST direct lookup: P00861

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

source_databases_merged: sabio_rk brenda skid


organism: Helicobacter pylori

sequence_source: UniProtKB REST direct lookup: P56129

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: P56129 and applied mutation signature I148L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: mutant enzyme I148L, in 100 mM Tris, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: P56129 and applied mutation signature I148G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I148G, in 100 mM Tris, pH 8.0


proof_lines: wild type enzyme, in 100 mM Tris, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: P56129 and applied mutation signature I148D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I148D, in 100 mM Tris, pH 8.0


substrate_name: D-Fructose 1,6-bisphosphate

substrate: D-Fructose 1,6-bisphosphate


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant 2-5C1(H26Y/D104G/V121A)


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant 3-23B5(H26Y/D104G/V121A/P256L))


sequence_variant_note: Resolved canonical sequence from UniProtKB:P56129 canonical FASTA fetched during review; I148A reconstructed from canonical residue I148. and applied mutation signature I148A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I148A, in 100 mM Tris, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:P56129 canonical FASTA fetched during review; I148F reconstructed from canonical residue I148. and applied mutation signature I148F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I148F, in 100 mM Tris, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:P56129 canonical FASTA fetched during review; I148K reconstructed from canonical residue I148. and applied mutation signature I148K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I148K, in 100 mM Tris, pH 8.0


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB:Q58497 reviewed FASTA fetched during exact accession lookup.


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WIU7 reviewed FASTA fetched during exact accession lookup.


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

proof_lines:
pH 7.8, 25°C
pH 8.0, 37°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=7.8

source_databases_merged: brenda skid


organism: Staphylococcus aureus

sequence_source: UniProtKB:Q5HG20 reviewed FASTA fetched during exact accession lookup.


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant 1-20H6(S106G)


organism: Lactococcus lactis subsp. cremoris


enzyme_display_name: DNA nucleotidylexotransferase

organism: Bos taurus

substrate_name: 2bA FAM oligo

sequence_source: UniProtKB reviewed canonical FASTA P06526, accessed 2026-06-11

proof_lines:
wild type enzyme, at pH 7.2 and 37Â°C
wild type enzyme, at pH 7.2 and 47Â°C

enzyme: DNA nucleotidylexotransferase

substrate: 2bA FAM oligo


proof_lines: mutant enzyme K177N/E178G/K271E/F280L/M283K/H405P, at pH 7.2 and 37Â°C

proof_lines: mutant enzyme K177N/E178G/K271E/F280L/M283K/H405P, at pH 7.2 and 47Â°C


organism: Homo sapiens

substrate_name: dATP

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed canonical FASTA P04053 with selected R336A substitution, accessed 2026-06-11 and applied mutation signature R336A to reconstruct the assayed variant sequence.

substrate: dATP


substrate_name: n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n DNA; dATP

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed canonical FASTA P04053 with selected D345E substitution, accessed 2026-06-11 and applied mutation signature D345E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA nucleotidylexotransferase(Enzyme) mutant D345E


substrate_name: dATP; n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n DNA

sequence_source: Reconstructed from UniProtKB reviewed canonical FASTA P04053 with selected R336A substitution, accessed 2026-06-11

proof_lines: SABIO-RK modifier species: DNA nucleotidylexotransferase(Enzyme) mutant R336A


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed canonical FASTA P04053 with selected D343E substitution, accessed 2026-06-11 and applied mutation signature D343E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA nucleotidylexotransferase(Enzyme) mutant D343E

substrate: dATP; n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n DNA


substrate: n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n n+1 n DNA; dATP


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed canonical FASTA P04053 with selected R336Q substitution, accessed 2026-06-11 and applied mutation signature R336Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA nucleotidylexotransferase(Enzyme) mutant R336Q


organism: Escherichia coli (strain K12)

substrate_name: meso-2,6-diaminoheptanedioate (at pH 6.8 and 37 degrees Celsius)

source_db: uniprot

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

source: uniprot


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

verification_status: corrected

status: corrected


substrate_name: tagatose-1,6-bisphosphate (when expressed alone)


organism: Vibrio vulnificus

sequence_source: UniProtKB REST lookup for A0A3Q0L347


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant 1-24H12(H26Y)


proof_lines: SABIO-RK modifier species: tagatose-bisphosphate aldolase(Enzyme) mutant 1-20F8(D104G)


sequence_source: UniProtKB REST direct lookup: P04053


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: P04053; D345E reconstructed locally and applied mutation signature D345E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: P04053; D343E reconstructed locally and applied mutation signature D343E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: P04053; R336Q reconstructed locally and applied mutation signature R336Q to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: Q9X1K5; E315T reconstructed locally and applied mutation signature E315T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct lookup: Q9X1K5

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


organism: Vibrio cholerae serotype O1

sequence_source: UniProtKB REST direct lookup: Q9KVL7

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


sequence_source: UniProtKB REST direct lookup: A0A3Q0L347


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

proof_lines:
pH 6.6, 37°C, primer oligo(dT)20
37°C, primer (dA)12-18
at 37°C


substrate_name: oligonucleotide primers

proof_lines: 37°C, pH 7.5, primer d(T)200, DNA polymerase lambda

proof_lines: 37°C, pH 7.5, primer d(N)36, DNA polymerase lambda

substrate: oligonucleotide primers


organism: Sus scrofa


organism: Trypanosoma brucei

substrate_name: RNAn containing a terminal U residue

proof_lines: RNA editing core complex RECC, pH 8.0, temperature not specified in the publication

proof_lines: recombinant enzyme, pH 8.0, temperature not specified in the publication

substrate: RNAn containing a terminal U residue


substrate_name: UTP

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

proof_lines: mutant V271R, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication

proof_lines: mutant V271R, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication

substrate: UTP


proof_lines: mutant K149A, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication


organism: Mus musculus

substrate_name: dATP (at 35 degrees Celsius)

substrate: dATP (at 35 degrees Celsius)


proof_lines: The catalytic efficiency measured with tagatose-1,6-bisphosphate as substrate is 340-fold higher than that with fructose-1,6-bisphosphate.


enzyme_display_name: metallocarboxypeptidase D

organism: Unknown

substrate_name: Dansyl-Pro-Ala-Arg

enzyme: metallocarboxypeptidase D

substrate: Dansyl-Pro-Ala-Arg


sequence_variant_note: Resolved canonical sequence from Direct UniProt REST EC+organism/RET2 lookup, accession Q86MV5 and applied mutation signature V271R/C83F to reconstruct the assayed variant sequence.

proof_lines: mutant V271R/C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication

proof_lines: mutant V271R/C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication


sequence_source: Direct UniProt REST EC+organism/RET2 lookup, accession Q86MV5

proof_lines: wild-type, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication

proof_lines: wild-type, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Direct UniProt REST EC+organism/RET2 lookup, accession Q86MV5 and applied mutation signature C83F to reconstruct the assayed variant sequence.

proof_lines: mutant C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication

proof_lines: mutant C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication


organism: Priestia megaterium

substrate_name: UDP-MurNAc-pentapeptide

substrate: UDP-MurNAc-pentapeptide


substrate_name: UDP-MurNAc-Ala-D-Glu-Lys-Gly-D-Ala

proof_lines:
pH 7.8, 37°C, exchange reaction
pH 7.8, 37°C, transfer reaction
pH 7.8, 37°C

substrate: UDP-MurNAc-Ala-D-Glu-Lys-Gly-D-Ala


enzyme_display_name: flavonol 3-sulfotransferase

organism: Flaveria bidentis

substrate_name: quercetin

proof_lines: cosubstrate quercetin, recombinant enzyme

enzyme: flavonol 3-sulfotransferase

substrate: quercetin


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

substrate_name: NAD

assay_conditions_summary: cofactor ADP

proof_lines: For ADP-ribosyltransferase activity of the catalytic fragment 399-605.

substrate: NAD


organism: Vibrio cholerae

proof_lines: For ADP-ribosyltransferase activity of a catalytic fragment of residues 459-666.


enzyme_display_name: pectinesterase

organism: Solanum betaceum

substrate_name: Pectin

enzyme: pectinesterase

substrate: Pectin


organism: Solanum lycopersicum

substrate_name: n n n n n n H2O; Pectin

substrate: n n n n n n H2O; Pectin


enzyme_display_name: histidinol-phosphatase

organism: Corynebacterium glutamicum

substrate_name: L-histidinol phosphate

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

enzyme: histidinol-phosphatase

substrate: L-histidinol phosphate


organism: Escherichia coli

sequence_source: UniProtKB:Q9S5G5; PubMed-linked PDB entries 2FPR, 2FPS, 2FPU, 2FPW, 2FPX

proof_lines: in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Co2+

proof_lines: in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mn2+

proof_lines: in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Zn2+


organism: Neurospora crassa


organism: Saccharomyces cerevisiae


organism: Anas platyrhynchos

substrate_name: H2O; Dansyl-Phe-Ala-Arg

sequence_source: UniProtKB reviewed accession Q90240/CBPD_ANAPL FASTA and JSON, fetched 2026-06-11; sequence version 1; length 1389 aa.

substrate: H2O; Dansyl-Phe-Ala-Arg


substrate_name: Dansyl-Phe-Ala-Arg

substrate: Dansyl-Phe-Ala-Arg


substrate_name: Dansyl-Phe-Ala-Arg; H2O

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

proof_lines: SABIO-RK modifier species: metallocarboxypeptidase D(Enzyme) mutant gp120 (first and second carboxypeptidase-like domain)

proof_lines: SABIO-RK modifier species: metallocarboxypeptidase D(Enzyme) mutant gp75 (first carboxypeptidase-like domain)

proof_lines: SABIO-RK modifier species: metallocarboxypeptidase D(Enzyme) mutant gp60-120 (second carboxypeptidase-like domain)

substrate: Dansyl-Phe-Ala-Arg; H2O


organism: Homo sapiens

substrate_name: dansyl-Phe-Ala-Arg

sequence_source: UniProtKB reviewed accession O75976/CBPD_HUMAN FASTA and JSON, fetched 2026-06-11; sequence version 2; length 1380 aa.

substrate: dansyl-Phe-Ala-Arg


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O75976/CBPD_HUMAN FASTA and JSON, fetched 2026-06-11; sequence version 2; length 1380 aa. Variant reconstructed locally from selected mutation signature E350Q. and applied mutation signature E350Q to reconstruct the assayed variant sequence.

proof_lines:
mutant E350Q, pH 6.5, 37°C
pH 6.5, 37°C, mutant enzyme E350Q


proof_lines:
pH 6.5, 37°C, wild-type enzyme
wild-type, pH 6.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O75976/CBPD_HUMAN FASTA and JSON, fetched 2026-06-11; sequence version 2; length 1380 aa. Variant reconstructed locally from selected mutation signature E762Q. and applied mutation signature E762Q to reconstruct the assayed variant sequence.

proof_lines:
mutant E762Q, pH 6.5, 37°C
pH 6.5, 37°C, mutant enzyme E762Q


sequence_source: UniProtKB reviewed accession O75976/CBPD_HUMAN FASTA and JSON, fetched 2026-06-11; sequence version 2; length 1380 aa. Variant reconstructed locally from selected mutation signature E350Q.


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Thermococcus onnurineus

substrate_name: L-phosphoserine

proof_lines: in the presence of 1 mM Co2+, at 80°C and pH 6.5

proof_lines: in the presence of 1 mM Ni2+, at 80°C and pH 6.5

proof_lines: in the presence of 1 mM Mn2+, at 80°C and pH 6.5

substrate: L-phosphoserine


organism: Thermus thermophilus


enzyme_display_name: sphingomyelin phosphodiesterase

organism: Bacillus cereus

substrate_name: sphingomyelin

proof_lines: in presence of Mg2+ and sodium deoxycholate

enzyme: sphingomyelin phosphodiesterase

substrate: sphingomyelin


organism: Bos taurus

proof_lines:
37°C, pH 7.4
in 100 mM Tris-HCl (pH 7.5), at 37°C


proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas aeruginosa

substrate_name: elongation factor 2

assay_conditions_summary: cofactor NAD+

substrate: elongation factor 2


organism: Vibrio cholerae serotype O1

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

proof_lines: 37°C, pH 7, 1400fold more potent than NAD+ and 400fold more potent than diethylamino(benzylidine-amino)guanidine


organism: Flaveria chlorifolia

proof_lines:
cosubstrate rhamnetin
cosubstrate quercetin, pH 7.5, 30°C
pH 6.0


organism: Dickeya chrysanthemi


substrate_name: Unknown

substrate: Unknown


organism: Kionochaeta sp.


organism: Mus musculus


organism: Plasmodium falciparum


organism: Rasamsonia emersonii


organism: Rattus norvegicus

substrate_name: Sphingomyelin; H2O

proof_lines:
lysosomes, at 0.5 mM sphingomyelin
microsomes
37°C, pH 7.4

substrate: Sphingomyelin; H2O


enzyme_display_name: alpha-D-xyloside xylohydrolase

organism: Aspergillus niger

proof_lines: pH 4.8, temperature not specified in the publication

enzyme: alpha-D-xyloside xylohydrolase


substrate_name: NAD+

sequence_source: UniProtKB P11439 direct REST/FASTA lookup on 2026-06-11

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NAD+; Peptide diphthamide

substrate: NAD+; Peptide diphthamide


organism: Anas platyrhynchos

substrate_name: Dansyl-Phe-Phe-Arg

sequence_source: UniProtKB Q90240 direct REST/FASTA lookup on 2026-06-11

substrate: Dansyl-Phe-Phe-Arg


substrate_name: Dansyl-Pro-Ala-Arg

substrate: Dansyl-Pro-Ala-Arg


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProtKB O75976 direct REST/FASTA lookup on 2026-06-11 and applied mutation signature E762Q to reconstruct the assayed variant sequence.


substrate_name: Dansyl-Ala-Arg

sequence_source: UniProtKB Q9JHW1 direct REST/FASTA lookup on 2026-06-11

substrate: Dansyl-Ala-Arg


organism: Aspergillus oryzae

substrate_name: 4-nitrophenyl alpha-D-xylopyranoside

proof_lines:
at pH 4.5 and 55°C
at pH 7.0 and 30°C

substrate: 4-nitrophenyl alpha-D-xylopyranoside


enzyme_display_name: beta-D-fucosidase

organism: Asclepias curassavica

substrate_name: p-nitrophenyl-beta-D-fucoside

enzyme: beta-D-fucosidase

substrate: p-nitrophenyl-beta-D-fucoside


organism: Aspergillus phoenicis


organism: Bifidobacterium breve clb

substrate_name: p-nitrophenyl-beta-D-glucoside

substrate: p-nitrophenyl-beta-D-glucoside


organism: Bos taurus


organism: Dalbergia cochinchinensis


enzyme_display_name: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

substrate_name: NADP+

assay_conditions_summary: pH 7; 301.15 K; cofactor NADP+

substrate: NADP+


organism: Oryctolagus cuniculus

substrate_name: NAD+; H2O

assay_conditions_summary: cofactor NADP+

enzyme: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

substrate: NAD+; H2O


organism: Pseudomonas putida KB1

substrate_name: thio-NAD+

substrate: thio-NAD+


organism: Saccharomyces cerevisiae


organism: Streptomyces griseus


enzyme_display_name: dipeptidyl-peptidase I

substrate_name: sarcosyl-Phe-ethyl ester

assay_conditions_summary: pH 5

enzyme: dipeptidyl-peptidase I

substrate: sarcosyl-Phe-ethyl ester


organism: Escherichia coli

proof_lines: 25°C, recombinant mutant H540V/N604T of beta-galactosidase, EC 3.2.1.22


organism: Lactuca sativa


organism: Littorina littorea


organism: Ovis aries aries


organism: Patella vulgata


organism: Turbo cornutus

substrate_name: p-nitrophenyl-beta-D-galactoside

substrate: p-nitrophenyl-beta-D-galactoside


organism: Capra hircus


organism: Homo sapiens

assay_conditions_summary: pH 5.5; 294.15 K; buffer acetate

proof_lines:
tetrameric enzyme, at pH 5.5 and °C
monomeric enzyme, at pH 5.5 and °C
in H2O, pH 5.6, at 21°C


organism: Mus musculus


organism: Rattus norvegicus

substrate_name: glucagon

proof_lines:
removal of His-Ser
removal of the first dipeptide

substrate: glucagon


organism: Vigna radiata


enzyme_display_name: carboxypeptidase M

proof_lines: wild-type enzyme lacking the C-terminal hydrophobic membrane anchor signal

enzyme: carboxypeptidase M


enzyme_display_name: beta-aspartyl-peptidase

organism: Cavia porcellus

substrate_name: beta-Asp-Phe

enzyme: beta-aspartyl-peptidase

substrate: beta-Asp-Phe


substrate_name: beta-aspartyl-L-leucine

substrate: beta-aspartyl-L-leucine


enzyme_display_name: endopeptidase La

substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines:
mutant S679W
mutant S679W with S3 peptide

enzyme: endopeptidase La

substrate: ATP


substrate_name: human titin

proof_lines: unfolded, bearing a sul20C peptide variant with an N-terminal PABA fluorophoreand a nitrotyrosine quencher at the penultimate C-terminal position followed by alanine at the C-terminus of the I27 domain, pH 8.0, 37°C

substrate: human titin


substrate_name: bacteriophage lambda N-protein

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines:
37°C
pH 7.2, 37°C
protein hydrolysis

substrate: bacteriophage lambda N-protein


organism: Dickeya chrysanthemi

substrate_name: Pectin

sequence_variant_note: Resolved canonical sequence from UniProt P0C1A9 plus RCSB 2NSP/SIFTS and PMID 17717531 mutagenesis context and applied mutation signature Q153A to reconstruct the assayed variant sequence.

substrate: Pectin


sequence_variant_note: Resolved canonical sequence from UniProt P0C1A9 plus RCSB 2NSP/SIFTS and PMID 17717531 mutagenesis context and applied mutation signature V198A to reconstruct the assayed variant sequence.


verification_status: verified

sequence_source: UniProt P0C1A9 plus RCSB 2NSP/SIFTS and PMID 17717531 paper context

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

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

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

row_label: Table III, enzyme row PME3937 wild-type

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

status: verified


sequence_variant_note: Resolved canonical sequence from UniProt P0C1A9 plus RCSB 2NSP/SIFTS and PMID 17717531 mutagenesis context and applied mutation signature Q177A to reconstruct the assayed variant sequence.


organism: Penicillium oxalicum

substrate_name: citrus pectin

substrate: citrus pectin


organism: Prunus armeniaca

proof_lines: immobilized enzyme, Vmax: 14.6 micromol/min/mg, no difference between free and immobilized enzyme in Km but in Vmax (8.4fold higher value)


organism: Saccharomyces cerevisiae


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines: Y(3-NO2)-RGIT2-aminobuytric acid-SGRQ-K(anthranilamide) stimulated ATP hydrolysis

proof_lines: Y(3-NO2)-RGITCSGRQ-K(anthranilamide) stimulated ATP hydrolysis


enzyme_display_name: bleomycin hydrolase

organism: Bos taurus

substrate_name: bleomycin A2

enzyme: bleomycin hydrolase

substrate: bleomycin A2


organism: Lactococcus lactis

substrate_name: Met-Ala-Ser

substrate: Met-Ala-Ser


organism: Oryctolagus cuniculus


enzyme_display_name: chymosin

proof_lines:
hydrolysis by calf chymosin
hydrolysis by transgenic chymosin
hydrolysis by recombinant chymosin

enzyme: chymosin


organism: Escherichia coli

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

proof_lines: pH 7.8, 37°C, mutant D676N, 0.3 mg/ml casein


proof_lines: pH 7.8, 37°C, wild-type, 0.3 mg/ml casein


proof_lines: pH 7.8, 37°C, mutant H667Y, 0.3 mg/ml casein


proof_lines: pH 7.8, 37°C, mutant H665Y, 0.3 mg/ml casein


proof_lines: pH 7.8, 37°C, mutant S679A, 0.3 mg/ml casein


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines:
second KI-value, pH 8.0, 37°C
first KI-value, pH 8.0, 37°C


substrate_name: kappa-casein

substrate: kappa-casein


organism: Bubalus bubalis


organism: Callithrix jacchus

proof_lines: hydrolysis of the Glu148 variant by D289M/Q298L mutant chymosin

proof_lines: hydrolysis of the parent peptide by D289M/Q298L mutant chymosin

proof_lines: hydrolysis of the Phe148 variant (cleavage L147-F148) by D289M/Q298L mutant chymosin


proof_lines: hydrolysis of the Phe148 variant (cleavage L147-F148) by wild type chymosin

proof_lines: hydrolysis of the Glu171 variant by wild type chymosin

proof_lines: hydrolysis of the parent peptide by wild type chymosin


proof_lines: hydrolysis of the Glu148 variant by Gln298Leu mutant chymosin

proof_lines: hydrolysis of the parent peptide by Gln298Leu mutant chymosin

proof_lines: hydrolysis of the Phe148 variant (cleavage L147-F148) by Gln298Leu mutant chymosin


proof_lines: hydrolysis of the Phe148 variant (cleavage F147-R148) by Asp289Met mutant chymosin

proof_lines: hydrolysis of the Phe148 variant (cleavage L147-F148) by Asp289Met mutant chymosin

proof_lines: hydrolysis of the Glu171 variant by Asp289Met mutant chymosin


organism: Camelus dromedarius

substrate_name: undecapeptide analogue to chymosin sensitive region of bovine kappa-casein


organism: Homo sapiens


enzyme_display_name: omega-amidase

organism: Bacillus subtilis

substrate_name: succinamate

enzyme: omega-amidase

substrate: succinamate


proof_lines: Km (open chain form), 37°C, pH 8.5, vmax: 5.9 micromol/mg*min

proof_lines: apparent Km, 37°C, pH 8.5, vmax: 5.9 micromol/mg*min


enzyme_display_name: chitin deacetylase

organism: Aspergillus nidulans

substrate_name: glycol chitin

enzyme: chitin deacetylase

substrate: glycol chitin


organism: Colletotrichum lindemuthianum

sequence_source: UniProtKB Q6DWK3 reviewed entry; PMID 12775215 and related Colletotrichum lindemuthianum chitin deacetylase evidence


organism: Mortierella sp.

substrate_name: hexa-N-acetylchitohexaose

substrate: hexa-N-acetylchitohexaose


sequence_source: UniProtKB Q06703 reviewed Cda2p entry; PMID 11812231 evidence


organism: Leucobacter triazinivorans

substrate_name: N-isopropylammelide

substrate: N-isopropylammelide


organism: Pseudomonas sp.

substrate_name: N-cyclopropylammelide

sequence_source: UniProtKB O52063 reviewed AtzC entry; PMID 12218024 evidence

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ADP

substrate: N-cyclopropylammelide


substrate_name: Dansyl-Ala-Arg

substrate: Dansyl-Ala-Arg


organism: Anas platyrhynchos

substrate_name: dansyl-Phe-Phe-Arg

proof_lines:
enzyme form gp180
enzyme form gp170
dansyl-Phe-Ala-Arg, enzyme form gp180

substrate: dansyl-Phe-Phe-Arg


organism: Anas sp.


substrate_name: Dansyl-Leu-Ala-Arg

proof_lines: dansyl-Phe-Leu-Arg, membrane- bound enzyme

substrate: Dansyl-Leu-Ala-Arg


enzyme_display_name: (d)CTP diphosphatase

sequence_variant_note: Resolved canonical sequence from UniProtKB:P77788 canonical sequence with directly checked E33A reconstruction and applied mutation signature E33A to reconstruct the assayed variant sequence.

proof_lines: mutant E33A, pH not specified in the publication, temperature not specified in the publication

enzyme: (d)CTP diphosphatase


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77788 canonical sequence with directly checked D118A reconstruction and applied mutation signature D118A to reconstruct the assayed variant sequence.

proof_lines: mutant D118A, pH not specified in the publication, temperature not specified in the publication


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77788 canonical sequence with directly checked E33A/D118E reconstruction and applied mutation signature E33A/D118E to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant E33A/D118E


organism: Synechococcus phage S-PM2

substrate_name: GTP

proof_lines: pH and temperature not specified in the publication

substrate: GTP


enzyme_display_name: signal-recognition-particle GTPase

organism: Acidianus ambivalens

enzyme: signal-recognition-particle GTPase


enzyme_display_name: nucleoside diphosphate phosphatase

organism: Caenorhabditis elegans

substrate_name: UDP

enzyme: nucleoside diphosphate phosphatase

substrate: UDP


organism: Glycine max

substrate_name: ATP

substrate: ATP


organism: Rattus norvegicus

substrate_name: IDP

proof_lines:
in presence of Mn2+
native enzyme in presence of ATP
native enzyme in absesence of ATP

substrate: IDP


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB:P77788 FASTA; mutation from selected BRENDA note and PMID 15823026 Orf135 mutagenesis context and applied mutation signature R72A to reconstruct the assayed variant sequence.

proof_lines: mutant R72A, pH not specified in the publication, temperature not specified in the publication


substrate_name: dCTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P77788 FASTA; mutation from selected BRENDA note and PMID 15823026 Orf135 mutagenesis context and applied mutation signature D118E to reconstruct the assayed variant sequence.

proof_lines: mutant D118E, pH not specified in the publication, temperature not specified in the publication

substrate: dCTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77788 FASTA; mutation from selected BRENDA note and PMID 15823026 Orf135 mutagenesis context and applied mutation signature D118N to reconstruct the assayed variant sequence.

proof_lines: mutant D118N, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: diaminopimelate decarboxylase

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

enzyme: diaminopimelate decarboxylase


organism: Landoltia punctata


organism: Lysinibacillus sphaericus

substrate_name: Unknown

substrate: Unknown


organism: Methanocaldococcus jannaschii


organism: Mycobacterium tuberculosis

proof_lines: in 100 mM TEA-HCl pH 7.8, temperature not specified in the publication


organism: Mus musculus


substrate_name: 2-Oxoglutaramate; H2O

proof_lines: pH 8.5, only 0.3% of alpha-ketoglutaramate exists in open-chain structure

proof_lines: with substrate, acyl donor: p-methylphenyl glutarate, Km for total methylamine, for free-base form of methylamine, Km is about 102 times smaller

substrate: 2-Oxoglutaramate; H2O


organism: Solanum lycopersicum


organism: Thermus aquaticus

substrate_name: hydroxylamine

substrate: hydroxylamine


organism: Absidia orchidis vel coerulea


organism: Amylomyces rouxii

sequence_source: UniProtKB reviewed accession P50325, fetched by direct EC+organism lookup and FASTA retrieval on 2026-06-11

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


organism: Vicia faba


organism: Zea mays


organism: Escherichia coli K-12

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

proof_lines:
SgaH, pH 7.5, 25°C
SgbH, pH 7.5, 25°C

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


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

proof_lines: pH 7.5, 25°C, recombinant mutant E112A/H136A


proof_lines: pH 7.5, 25°C, recombinant mutant E112Q/H136A


proof_lines: pH 7.5, 25°C, recombinant mutant K64A/H136A


organism: Streptomyces coelicolor

sequence_variant_note: Resolved canonical sequence from UniProt Q9ZBP9; NCBI Protein CAA22423.1; PMID 16820862 mutation label K228G and applied mutation signature K228G with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O69874; NCBI Protein CAA19378.1; PMID 16820862 mutation label K147G and applied mutation signature K147G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9ZBP9; NCBI Protein CAA22423.1; PMID 16820862 mutation label G222V and applied mutation signature G222V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9ZBP9; NCBI Protein CAA22423.1; PMID 16820862 mutation label T226S and applied mutation signature T226S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O69874; NCBI Protein CAA19378.1; PMID 16820862 mutation label A145S and applied mutation signature A145S to reconstruct the assayed variant sequence.


proof_lines:
NG-Ffh, wild-type
NG-FtsY, wild-type


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P39304/ULAD_ECOLI; NCBI PubMed-protein links for PMID 15157077; RCSB 1Q6L SIFTS alignment to P39304 and applied mutation signature H136A/R139V/K64A/E112A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutants H136A/R139V and K64A/E112A/H136A/R139V


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P39304/ULAD_ECOLI; NCBI PubMed-protein links for PMID 15157077; RCSB 1Q6L SIFTS alignment to P39304 and applied mutation signature H136A/R139V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutant H136A/R139V


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P39304/ULAD_ECOLI; NCBI PubMed-protein links for PMID 15157077; RCSB 1Q6L SIFTS alignment to P39304 and applied mutation signature K64A/E112Q/H136A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutant K64A/E112Q/H136A


sequence_source: UniProtKB reviewed P39304/ULAD_ECOLI; NCBI PubMed-protein links for PMID 15157077; RCSB 1Q6L SIFTS alignment to P39304

column_label: Table 1: Kinetic Parameters of KGPDC (Biochemistry 2004, 43, 6427-6437, page 6431); printed row label 'wild type'; column 'kcat (s-1)' = 51; column 'KM (M)' = 6.7 x 10^-4; column 'kcat/KM (M-1 s-1)' = 7.7 x 10^4. The table prints no other kinetic column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 51 s-1; the printed unit is already the canonical unit, so no unit conversion applies and the canonical value is 51 s^(-1). Km: printed Table 1 cell 6.7 x 10^-4 M; 1 M is 1000 mM, so 6.7 x 10^-4 x 1000 = 0.67 mM. kcat/Km: printed Table 1 cell 7.7 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.7 x 10^4 / 1000 = 77 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed row 'wild type': kcat = 51 s-1; KM = 6.7 x 10^-4 M; printed kcat/KM = 7.7 x 10^4 M-1 s-1.

row_label: Table 1, printed row 'wild type' (the wild-type entry of the single kinetic table in this article)


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P39304/ULAD_ECOLI; NCBI PubMed-protein links for PMID 15157077; RCSB 1Q6L SIFTS alignment to P39304 and applied mutation signature K64R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P39304/ULAD_ECOLI; NCBI PubMed-protein links for PMID 15157077; RCSB 1Q6L SIFTS alignment to P39304 and applied mutation signature K64A/R139V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutant K64A/R139V


proof_lines: pH 7.5, 25°C, recombinant mutant K64A/E112A/H136A/R139V


proof_lines: pH 7.5, 25°C, recombinant mutant D67A/H136A

proof_lines: pH 7.5, 25°C, recombinant mutants D67A and H136A


proof_lines: pH 7.5, 25°C, recombinant mutant E112A/H136A/R139V


proof_lines: pH 7.5, 25°C, recombinant mutants K64R and D67N/H136A


proof_lines: pH 7.5, 25°C, recombinant mutant E112Q/H136A/R139V


proof_lines: pH 7.5, 25°C, recombinant mutant D67N/H136A


proof_lines: pH 7.5, 25°C, recombinant mutant E112D/R139V/T169A


organism: Methylomonas aminofaciens


organism: Canis lupus familiaris


proof_lines: maximal rate constant for the GTPase activity of the SRP-FtsY complex, GUAA mutant

proof_lines: maximal rate constant for the GTPase activity of the SRP-FtsY complex, UUUU mutant

proof_lines: maximal rate constant for the GTPase activity of the SRP-FtsY complex, UUCG mutant


proof_lines: maximal rate constant for the GTPase activity of the SRP-FtsY complex, no RNA

proof_lines: pH 7.5, 25°C, in the absence of 4.5S RNA

proof_lines: pH 7.5, 25°C, in the presence of 4.5S RNA


proof_lines: maximal rate constant for the GTPase activity of the SRP-FtsY complex, wild-type RNA


proof_lines:
NG-FtsY, mutant GTK-VSG
NG-Ffh, mutant GAK-VSG


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence; RCSB 1KW1/1Q6L SIFTS maps KGPDC chain to P39304; mutation from selected BRENDA note. and applied mutation signature H136A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence; RCSB 1KW1/1Q6L SIFTS maps KGPDC chain to P39304; mutation from selected BRENDA note. and applied mutation signature K64R/H136A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutant K64R/H136A


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence; RCSB 1KW1/1Q6L SIFTS maps KGPDC chain to P39304; mutation from selected BRENDA note. and applied mutation signature H136N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence; RCSB 1KW1/1Q6L SIFTS maps KGPDC chain to P39304; mutation from selected BRENDA note. and applied mutation signature K64A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence; RCSB 1KW1/1Q6L SIFTS maps KGPDC chain to P39304; mutation from selected BRENDA note. and applied mutation signature R139V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P39304 canonical sequence; RCSB 1KW1/1Q6L SIFTS maps KGPDC chain to P39304; mutation from selected BRENDA note. and applied mutation signature D67N to reconstruct the assayed variant sequence.


enzyme_display_name: tagatose-bisphosphate aldolase

organism: Klebsiella pneumoniae

substrate_name: D-tagatose 1,6-diphosphate

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

enzyme: tagatose-bisphosphate aldolase

substrate: D-tagatose 1,6-diphosphate


organism: Lactococcus cremoris

substrate_name: tagatose 1,6-diphosphate

substrate: tagatose 1,6-diphosphate


organism: Lactococcus lactis subsp. lactis

substrate_name: D-Tagatose 1,6-bisphosphate

substrate: D-Tagatose 1,6-bisphosphate


organism: Staphylococcus aureus


organism: Streptococcus pyogenes

proof_lines: isoform LacD.1, pH 7.5, temperature not specified in the publication

proof_lines: isoform LacD.2, pH 7.5, temperature not specified in the publication


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

proof_lines: mutant isoform LacD.1, C-terminal half replaced with 162 amino acid residues from the C-terminus of LacD.2, pH 7.5, temperature not specified in the publication


enzyme_display_name: 4-hydroxy-2-oxoheptanedioate aldolase

organism: Escherichia coli

substrate_name: DL-glyceraldehyde

proof_lines: Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C

proof_lines: Kcat(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C

proof_lines: steady-state kinetic parameter, with acetaldehyde as aldehyde donor, pH 8.0 and 25°C

enzyme: 4-hydroxy-2-oxoheptanedioate aldolase

substrate: DL-glyceraldehyde


organism: Saccharolobus solfataricus


enzyme_display_name: arogenate dehydratase

organism: Brevundimonas diminuta

substrate_name: L-arogenate

enzyme: arogenate dehydratase

substrate: L-arogenate


organism: Nicotiana sylvestris

substrate_name: L-Arogenate

substrate: L-Arogenate


organism: Pantoea agglomerans

substrate_name: Prephenate

proof_lines:
pH 7.2, 37°C
pH 7.2, 37°C, 0.01 mM tyrosine

substrate: Prephenate


organism: Pseudomonas aeruginosa


organism: Sorghum bicolor

proof_lines:
pH 8.0, 22°C, 0.01 mM tyrosine
pH 8.0, 22°C


organism: Spinacia oleracea


enzyme_display_name: cellobiose phosphorylase

organism: Cellulomonas uda

substrate_name: cellobiose

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB Q7WTR6 direct REST lookup retrieved 2026-06-12

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

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6.6
Raw SKiD Env: Temp=30°C, pH=6.6

enzyme: cellobiose phosphorylase

substrate: cellobiose

source: skid


enzyme_display_name: hexokinase

organism: Homo sapiens

substrate_name: D-glucose

sequence_source: UniProtKB:P19367 direct REST lookup

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=30°C, pH=7.5

enzyme: hexokinase

substrate: D-glucose


sequence_source: UniProtKB:P35557 direct REST lookup

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.1


organism: Kluyveromyces lactis

sequence_source: UniProtKB:P33284 direct REST lookup

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P04806 direct REST lookup


organism: Sulfurisphaera tokodaii

sequence_source: UniProtKB:Q96Y14 direct REST lookup

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ATP


enzyme_display_name: hydroperoxide dehydratase

organism: Solanum lycopersicum

proof_lines: kcat is 820 sec(-1) with 9-HPOD as substrate. kcat is 236 sec(-1) with 9-HPOT as substrate. kcat is 99 sec(-1) with 13-HPOD as substrate. kcat is 21 sec(-1) with 13-HPOT as substrate.

enzyme: hydroperoxide dehydratase


organism: Oryza sativa

substrate_name: (9S)-hydroperoxyoctadecatrienoic acid

sequence_source: UniProtKB reviewed accession Q7Y0C8 (C74A1_ORYSJ), matched to the PMID 23527858 OsAOS1/CYP74A1 context.

substrate: (9S)-hydroperoxyoctadecatrienoic acid


organism: Solanum melongena

substrate_name: linoleate hydroperoxide

substrate: linoleate hydroperoxide


organism: Arabidopsis thaliana

sequence_source: UniProtKB Q96242 FASTA direct check


smiles: CCCCCC=CC=CC(CCCCCCCC(=O)O)OO


organism: Capsicum annuum

proof_lines: pH 5.5, 20°C, recombinant His6-tagged enzyme


organism: Cucumis sativus

proof_lines: pH 7.0, 23°C, recombinant mutant L98F/A287G enzyme


proof_lines: pH 7.0, 23°C, recombinant wild-type enzyme


proof_lines: pH 7.0, 23°C, recombinant mutant L93F/G283A enzyme


organism: Glycine max

sequence_source: UniProtKB REST direct accession check for M4WFN0


organism: Medicago truncatula

sequence_source: UniProtKB REST direct accession check for Q7X9B3


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 7.0, 23°C, recombinant mutant L97F/TCFNSF enzyme


organism: Olea europaea

mutation_signature: recombinant truncated enzyme

mutation_type: truncation

proof_lines: pH 7.5, 25°C, recombinant truncated enzyme


sequence_source: UniProtKB REST direct accession check for G8XQN2

proof_lines: pH 7.5, 25°C, recombinant full-length enzyme, with 2.5% glycine w/v

proof_lines: pH 7.5, 25°C, recombinant full-length enzyme, with 0.5 M NaCl


mutation_signature: recombinant truncated enzyme / recombinant truncated enzyme

proof_lines: pH 7.5, 25°C, recombinant truncated enzyme, with 0.5 M NaCl

proof_lines: pH 7.5, 25°C, recombinant truncated enzyme, with 2.5% glycine w/v


organism: Physcomitrium patens

sequence_source: UniProtKB REST direct accession lookup for A9SNA2; sequenceVersion=1; retrieved during this review.

assay_conditions_summary: pH 6; buffer containing 50 mM sodium phosphate, pH 6

proof_lines: with 0.0001 mg purified AOS1, in 1 mL of buffer containing 50 mM sodium phosphate, pH 6.0


organism: Solanum tuberosum

sequence_source: UniProtKB REST direct accession lookup for C7ENW3; sequenceVersion=1; retrieved during this review.


enzyme_display_name: carbonic anhydrase

organism: Stylophora pistillata

sequence_source: UniProtKB:B5SU02 direct REST lookup

assay_conditions_summary: pH 7.5; 293.15 K; buffer HEPES

proof_lines: at 20°C and pH 7.5 in 10 mM HEPES buffer

enzyme: carbonic anhydrase


assay_conditions_summary: pH 6.28; buffer context

proof_lines: pH 6.28, MES buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 7.23, 1-methylimidazolebuffer, carbonic anhydrase I mutant V62N,H67N,H200T


organism: Methanosarcina thermophila

sequence_source: UniProt P40881 precursor sequence with mature E62A reconstructed at precursor position 96 after the annotated 34 aa signal peptide.

sequence_variant_note: Mutation signature E62A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

smiles: O=C=O

assay_conditions_summary: pH 7.5; 298.15 K; buffer contexts (IMID

proof_lines: pH 7.5, 25°C, variant E62A, 50 mM IMID buffer

proof_lines: pH 7.5, 25°C, variant E62A, 50 mM MOPS-Ac buffer

proof_lines: pH 7.5, 25°C, variant E62A, 50 mM MOPS buffer


sequence_source: UniProt P40881 precursor sequence with mature E62T reconstructed at precursor position 96 after the annotated 34 aa signal peptide.

sequence_variant_note: Mutation signature E62T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 7.5; 298.15 K; buffer source context

proof_lines: pH 7.5, 25°C, variant E62T, 50 mM MOPS buffer


organism: Methanothermobacter thermautotrophicus

assay_conditions_summary: pH 8.5; 298.15 K; buffer imidazole/MOPS and unspecified

proof_lines: pH 8.5, 25°C, wild-type, imidazole buffer


assay_conditions_summary: pH 8.5; 298.15 K; buffer mapping

proof_lines: pH 8.5, 25°C, mutant D34A, imidazole buffer


enzyme_display_name: glucosyl-3-phosphoglycerate synthase

organism: Mycobacterium tuberculosis

substrate_name: UDP-glucose

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P9WMW9 FASTA direct lookup on 2026-06-13 and selected-row mutation signature T187A and applied mutation signature T187A to reconstruct the assayed variant sequence.

enzyme: glucosyl-3-phosphoglycerate synthase

substrate: UDP-glucose


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P9WMW9 FASTA direct lookup on 2026-06-13 and selected-row mutation signature R261A and applied mutation signature R261A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P9WMW9 FASTA direct lookup on 2026-06-13 and selected-row mutation signature E232A and applied mutation signature E232A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST direct accession lookup for P9WMW9 on 2026-06-13


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession lookup for P9WMW9 on 2026-06-13 and applied mutation signature H258A to reconstruct the assayed variant sequence.


organism: Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)

substrate_name: 3-PGA (at 30 degrees Celsius)

substrate: 3-PGA (at 30 degrees Celsius)


organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)

substrate_name: 3-PGA (at 37 degrees Celsius)

assay_conditions_summary: cofactor ADP

substrate: 3-PGA (at 37 degrees Celsius)


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)


organism: Persephonella marina (strain DSM 14350 / EX-H1)

substrate_name: 3-PGA (at 70 degrees Celsius)

substrate: 3-PGA (at 70 degrees Celsius)


organism: Petrotoga mobilis (strain DSM 10674 / SJ95)

substrate_name: 3-PGA (at 60 degrees Celsius)

substrate: 3-PGA (at 60 degrees Celsius)


organism: Mycobacterium tuberculosis variant bovis

sequence_source: UniProtKB reviewed Q7U0E1 (GPGS_MYCBO), direct EC+organism lookup; EC and protein-name evidence cite PMID:18221489.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP


organism: Persephonella marina

sequence_source: UniProtKB:A9QXB4 REST accession check on 2026-06-13


organism: Petrotoga mobilis

sequence_source: UniProtKB:A9BHI9 REST accession check on 2026-06-13


organism: Prochlorococcus marinus

substrate_name: ADP-glucose

sequence_source: UniProtKB:Q7VCL3 REST accession check on 2026-06-13

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

substrate: ADP-glucose


organism: Rhodopirellula baltica

sequence_source: UniProtKB:Q7UXY8 REST accession check on 2026-06-13

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP


organism: Synechococcus sp.


organism: Methanococcoides burtonii

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WMW9 and applied mutation signature E232A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WMW9 and applied mutation signature H258A to reconstruct the assayed variant sequence.


proof_lines: substrate 3-phospho-D-glycerate, pH 7.8, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WMW9 and applied mutation signature T187A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WMW9 and applied mutation signature R261A to reconstruct the assayed variant sequence.


organism: Mycolicibacterium smegmatis


enzyme_display_name: 2-pyrone-4,6-dicarboxylate lactonase

organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

substrate_name: a mixture of (4E)-oxalomesaconate/4-carboxy-2-hydroxymuconate (at pH 8.25)

proof_lines: kcat is 342 sec(-1) for the hydrolysis of 2-pyrone-4,6-dicarboxylate (at pH 8.25). kcat is 116 sec(-1) for the synthesis of 2-pyrone-4,6-dicarboxylat from OMA/CHM (at pH 8.25).

enzyme: 2-pyrone-4,6-dicarboxylate lactonase


organism: Phytopseudomonas straminea


organism: Comamonas testosteroni


organism: Sphingomonas paucimobilis

sequence_variant_note: Resolved canonical sequence from uniprot_accession:O87170; PMID 22475079; RCSB 4D8L and applied mutation signature Y49F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:O87170; PMID 22475079; RCSB 4D8L and applied mutation signature H33N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_source: uniprot_accession:O87170; PMID 22475079; RCSB 4D8L


sequence_variant_note: Resolved canonical sequence from uniprot_accession:O87170; PMID 22475079; RCSB 4D8L and applied mutation signature D248A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:O87170; PMID 22475079; RCSB 4D8L and applied mutation signature R124M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


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

proof_lines:
pH 8.25, 30°C
Raw SKiD Env: Temp=30°C, pH=8.25


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession:O87170; PMID 22475079; RCSB 4D8L and applied mutation signature Y156F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H180C with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y156F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R130M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature D248N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature H180C with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature H180A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature R217M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature R183M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature H33N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature R130M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


enzyme_display_name: 2-pyrone-4,6-dicarboxylate hydrolase

enzyme_name_source: UniProtKB:O87170 direct lookup

sequence_source: UniProtKB:O87170 direct lookup

assay_conditions_summary: pH 8.25; 303.15 K; buffer 50 mM BICINE

enzyme: 2-pyrone-4,6-dicarboxylate hydrolase


sequence_variant_note: Resolved canonical sequence from UniProtKB:O87170 direct lookup and applied mutation signature D248A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O87170 direct lookup and applied mutation signature D248N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O87170 direct lookup and applied mutation signature Y49F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O87170 direct lookup and applied mutation signature R217M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O87170 direct lookup and applied mutation signature H180A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O87170 direct lookup and applied mutation signature R183M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O87170 direct lookup and applied mutation signature R124M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


enzyme_display_name: Nitroalkane oxidase

organism: Fusarium oxysporum

substrate_name: nitroethane

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X1D8 canonical sequence fetched by direct UniProt REST lookup; row-specific variant reconstructed from selected mutation_signature D402E after residue-coordinate check. and applied mutation signature D402E to reconstruct the assayed variant sequence.

enzyme: Nitroalkane oxidase

substrate: nitroethane


organism: Podospora anserina

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B2AM55 and applied mutation signature D399N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor FAD

column_label: Table 1 (Steady-state kinetic parameters for wild-type and mutant PODANSg2158 with nitroethane as substrate), D399N column: parameter row 'kcat (s-1)' = 0.037; parameter row 'KNE (mM)' = 10; parameter row 'kcat/KNE (mM-1s-1)' = 0.004.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.037 s^-1; the cell is already in s^-1, so no unit conversion applies and the normalized value is 0.037 s^(-1). Km: printed Table 1 cell 10 mM; the cell is already in mM, so no unit conversion applies and the normalized value is 10.0 mM. kcat/Km: printed Table 1 cell 0.004 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell converts to 0.004 s^(-1)*mM^(-1) with no numeric change.

raw_value_unit_evidence: Table 1, D399N column, nitroethane parameter rows: kcat (s-1) = 0.037; KNE (mM) = 10; kcat/KNE (mM-1s-1) = 0.004.

table_label: Table 1: Steady-state kinetic parameters for wild-type and mutant PODANSg2158 with nitroethane as substrate (Biochemistry 2010, 49(24):5035-5041)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B2AM55 and applied mutation signature R406K to reconstruct the assayed variant sequence.

column_label: Table 1 (Steady-state kinetic parameters for wild-type and mutant PODANSg2158 with nitroethane as substrate), R406K column: parameter row 'kcat (s-1)' = 9.0; parameter row 'KNE (mM)' = 25; parameter row 'kcat/KNE (mM-1s-1)' = 0.37.

normalized_value_unit_evidence: kcat: printed Table 1 cell 9.0 s^-1; the cell is already in s^-1, so no unit conversion applies and the normalized value is 9.0 s^(-1). Km: printed Table 1 cell 25 mM; the cell is already in mM, so no unit conversion applies and the normalized value is 25.0 mM. kcat/Km: printed Table 1 cell 0.37 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell converts to 0.37 s^(-1)*mM^(-1) with no numeric change.

raw_value_unit_evidence: Table 1, R406K column, nitroethane parameter rows: kcat (s-1) = 9.0; KNE (mM) = 25; kcat/KNE (mM-1s-1) = 0.37.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B2AM55 and applied mutation signature S273A to reconstruct the assayed variant sequence.

column_label: Table 1 (Steady-state kinetic parameters for wild-type and mutant PODANSg2158 with nitroethane as substrate), S273A column: parameter row 'kcat (s-1)' = 5.0; parameter row 'KNE (mM)' = 24; parameter row 'kcat/KNE (mM-1s-1)' = 0.21.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.0 s^-1; the cell is already in s^-1, so no unit conversion applies and the normalized value is 5.0 s^(-1). Km: printed Table 1 cell 24 mM; the cell is already in mM, so no unit conversion applies and the normalized value is 24.0 mM. kcat/Km: printed Table 1 cell 0.21 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell converts to 0.21 s^(-1)*mM^(-1) with no numeric change.

raw_value_unit_evidence: Table 1, S273A column, nitroethane parameter rows: kcat (s-1) = 5.0; KNE (mM) = 24; kcat/KNE (mM-1s-1) = 0.21.


sequence_variant_note: Resolved canonical sequence from UniProtKB B2AM55 canonical sequence fetched by direct UniProt REST lookup; row-specific variant reconstructed from selected mutation_signature S273A after residue-coordinate check. and applied mutation signature S273A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S273A, in 50 mM HEPES, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB B2AM55 canonical sequence fetched by direct UniProt REST lookup; row-specific variant reconstructed from selected mutation_signature D399N after residue-coordinate check. and applied mutation signature D399N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D399N, in 50 mM HEPES, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB B2AM55 canonical sequence fetched by direct UniProt REST lookup; row-specific variant reconstructed from selected mutation_signature R406K after residue-coordinate check. and applied mutation signature R406K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R406K, in 50 mM HEPES, pH 8.0, 30°C


substrate_name: nitroethane; O2

sequence_source: UniProtKB B2AM55 canonical wild-type sequence fetched by direct UniProt REST lookup.

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

proof_lines: wild type enzyme, in 50 mM HEPES, pH 8.0, 30°C

substrate: nitroethane; O2


enzyme_display_name: nitroalkane oxidase

organism: Pseudomonas aeruginosa

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9HWH9 PA4202/nmoA canonical sequence; H183C reconstructed after direct residue check showed H at canonical position 183. and applied mutation signature H183C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H183C, at 30°C, pH not specified in the publication

enzyme: nitroalkane oxidase


sequence_source: UniProtKB:B2AM55 direct REST lookup on 2026-06-13

smiles: O=O

column_label: Table 1 (Steady-state kinetic parameters for wild-type and mutant PODANSg2158 with nitroethane as substrate), Wild-Type column: parameter row 'kcat (s-1)' = 15; parameter row 'KO2 (mM)' = 0.39; parameter row 'kcat/KO2 (mM-1s-1)' = 38.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15 s^-1; the cell is already in s^-1, so no unit conversion applies and the normalized value is 15.0 s^(-1). Km: printed Table 1 cell 0.39 mM; the cell is already in mM, so no unit conversion applies and the normalized value is 0.39 mM. kcat/Km: printed Table 1 cell 38 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell converts to 38.0 s^(-1)*mM^(-1) with no numeric change.

raw_value_unit_evidence: Table 1, Wild-Type column, oxygen parameter rows: kcat (s-1) = 15; KO2 (mM) = 0.39; kcat/KO2 (mM-1s-1) = 38.


sequence_source: UniProtKB Q8X1D8 direct EC+organism lookup

assay_conditions_summary: pH 8


sequence_source: Canonical context from UniProtKB Q8X1D8; variant sequence not reconstructed because selected mutation label conflicts

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


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8X1D8 plus selected/PMC-supported mutation R409K and applied mutation signature R409K to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, mutant enzyme R409K, substrate inhibition constant


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8X1D8 plus selected/PMC-supported mutation D402E and applied mutation signature D402E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8X1D8 plus selected/PMC-supported mutation C397S and applied mutation signature C397S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q8X1D8 plus selected/PMC-supported mutation S171A and applied mutation signature S171A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


substrate_name: H2O; Nitroethane; O2 / 1-Nitrobutane; H2O; O2 / nitroethane

sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA lookup for Q8X1D8 on 2026-06-13 plus D402E reconstruction from the selected mutation label and applied mutation signature D402E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: nitroalkane oxidase(Enzyme) mutant D402E


sequence_source: UniProtKB REST/FASTA lookup for Q8X1D8 on 2026-06-13


sequence_source: UniProtKB REST/FASTA lookup for Q8X1D8 on 2026-06-13 plus D402E reconstruction from the selected mutation label


substrate_name: H2O2; Acetaldehyde; Nitrite / Nitroalkane reaction bundles

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

proof_lines:
cosubstrate D2O, 30°C, pH 8.5
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=°C, pH=8


substrate_name: 1-nitrohexane / 1-nitrooctane / nitroethane

sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA lookup for Q8X1D8 on 2026-06-13 plus S276A reconstruction from the selected mutation label and applied mutation signature S276A to reconstruct the assayed variant sequence.

proof_lines:
mutant S276A, pH 8.0, 30°C
mutant enzyme S276A, at pH 8.0 and 30°C


column_label: Table 2, substrate block 'nitroethane', enzyme-form column 'wild-type NAO'; column 'kcat(nitroethane) (s-1)' = 15; column 'K(nitroethane) (mM)' = 2.3; column 'kcat/K(nitroethane) (mM-1 s-1)' = 6.3

normalized_value_unit_evidence: kcat: printed Table 2 cell 15 s^-1; already in s^-1, so no unit conversion applies; the exported value is 15.0 s^(-1). Km: printed Table 2 cell 2.3 mM; already in mM, so no unit conversion applies; the exported value is 2.3 mM. kcat/Km: printed Table 2 cell 6.3 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell normalizes to 6.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, nitroethane block, wild-type NAO column: kcat = 15 s^-1; Km = 2.3 mM; printed kcat/Km = 6.3 mM^-1 s^-1.

table_label: Table 2: Kinetic parameters for wild-type nitroalkane oxidase, wild-type NAO column (Biochemistry 2009, 48(15):3407-3416)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature S276A to reconstruct the assayed variant sequence.

column_label: Table 2, substrate block 'nitroethane', enzyme-form column 'S276A NAO'; column 'kcat(nitroethane) (s-1)' = 1.0; column 'K(nitroethane) (mM)' = 3.3; column 'kcat/K(nitroethane) (mM-1 s-1)' = 0.30

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.0 s^-1; already in s^-1, so no unit conversion applies; the exported value is 1.0 s^(-1). Km: printed Table 2 cell 3.3 mM; already in mM, so no unit conversion applies; the exported value is 3.3 mM. kcat/Km: printed Table 2 cell 0.30 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell normalizes to 0.3 s^(-1)*mM^(-1). The exact quotient of the same two printed cells is 1.0 / 3.3 = 0.30303030303030304 s^-1 mM^-1, which the paper prints rounded to its own two-decimal precision as 0.30; the exported ratio keeps the exact quotient and is corroborated by that printed cell.

raw_value_unit_evidence: Table 2, nitroethane block, S276A NAO column: kcat = 1.0 s^-1; Km = 3.3 mM; printed kcat/Km = 0.30 mM^-1 s^-1.

table_label: Table 2: Kinetic parameters for S276A nitroalkane oxidase, S276A NAO column (Biochemistry 2009, 48(15):3407-3416)


substrate_name: nitroethane / 1-nitrohexane / 1-nitrooctane

proof_lines:
wild-type, pH 8.0, 30°C
wild type enzyme, at pH 8.0 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature R409K to reconstruct the assayed variant sequence.

column_label: Table 1 prints one enzyme-label column followed by four kinetic columns whose heads are kcat, s^-1 | kred, s^-1 | Km, mM | kcat/Km, mM^-1 s^-1. The cited cell set is Table 1, enzyme row R409K: kcat, s^-1 = 2.6; kred, s^-1 = 2.6; Km, mM = 26.3; kcat/Km, mM^-1 s^-1 = 0.098.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.6 under the column head kcat, s^-1; that column is already per second, so no unit conversion applies and the paper value is 2.6 s^(-1). Km: printed Table 1 cell 26.3 under the column head Km, mM; that column is already in millimolar, so no unit conversion applies and the paper value is 26.3 mM. kcat/Km: printed Table 1 cell 0.098 under the column head kcat/Km, mM^-1 s^-1; that head is already reciprocal millimolar per second, so no unit conversion applies and the paper value is 0.098 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R409K: kcat = 2.6 s^-1; kred = 2.6 s^-1; Km = 26.3 mM; printed kcat/Km = 0.098 mM^-1 s^-1.

row_label: Table 1, enzyme row R409K

table_label: Table 1: Kinetic Parameters for Active Site Variants of F. oxysporum NAO with Nitroethane (Arch Biochem Biophys 2017, 632:41-46)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature S171A to reconstruct the assayed variant sequence.

column_label: Table 1 prints one enzyme-label column followed by four kinetic columns whose heads are kcat, s^-1 | kred, s^-1 | Km, mM | kcat/Km, mM^-1 s^-1. The cited cell set is Table 1, enzyme row S171A: kcat, s^-1 = 5.4; kred, s^-1 = 49; Km, mM = 2.1; kcat/Km, mM^-1 s^-1 = 2.6.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.4 under the column head kcat, s^-1; that column is already per second, so no unit conversion applies and the paper value is 5.4 s^(-1). Km: printed Table 1 cell 2.1 under the column head Km, mM; that column is already in millimolar, so no unit conversion applies and the paper value is 2.1 mM. kcat/Km: printed Table 1 cell 2.6 under the column head kcat/Km, mM^-1 s^-1; that head is already reciprocal millimolar per second, so no unit conversion applies and the paper value is 2.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row S171A: kcat = 5.4 s^-1; kred = 49 s^-1; Km = 2.1 mM; printed kcat/Km = 2.6 mM^-1 s^-1.

row_label: Table 1, enzyme row S171A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature C397S to reconstruct the assayed variant sequence.

column_label: Table 1 prints one enzyme-label column followed by four kinetic columns whose heads are kcat, s^-1 | kred, s^-1 | Km, mM | kcat/Km, mM^-1 s^-1. The cited cell set is Table 1, enzyme row C397S: kcat, s^-1 = 5.4; kred, s^-1 = 42; Km, mM = 2.1; kcat/Km, mM^-1 s^-1 = 2.6.

raw_value_unit_evidence: Table 1, enzyme row C397S: kcat = 5.4 s^-1; kred = 42 s^-1; Km = 2.1 mM; printed kcat/Km = 2.6 mM^-1 s^-1.

row_label: Table 1, enzyme row C397S


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8X1D8 and applied mutation signature Y398F to reconstruct the assayed variant sequence.

column_label: Table 1 prints one enzyme-label column followed by four kinetic columns whose heads are kcat, s^-1 | kred, s^-1 | Km, mM | kcat/Km, mM^-1 s^-1. The cited cell set is Table 1, enzyme row Y398F: kcat, s^-1 = 11; kred, s^-1 = 96; Km, mM = 4.8; kcat/Km, mM^-1 s^-1 = 2.2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 11 under the column head kcat, s^-1; that column is already per second, so no unit conversion applies and the paper value is 11.0 s^(-1). Km: printed Table 1 cell 4.8 under the column head Km, mM; that column is already in millimolar, so no unit conversion applies and the paper value is 4.8 mM. kcat/Km: printed Table 1 cell 2.2 under the column head kcat/Km, mM^-1 s^-1; that head is already reciprocal millimolar per second, so no unit conversion applies and the paper value is 2.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Y398F: kcat = 11 s^-1; kred = 96 s^-1; Km = 4.8 mM; printed kcat/Km = 2.2 mM^-1 s^-1.

row_label: Table 1, enzyme row Y398F


sequence_variant_note: Resolved canonical sequence from UniProt Q8X1D8 canonical sequence; S171V reconstructed after confirming residue 171 is Ser in the canonical sequence. and applied mutation signature S171V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


sequence_source: UniProt Q8X1D8 reviewed F. oxysporum nitroalkane oxidase canonical sequence.

proof_lines: wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C

proof_lines: recombinant wild-type enzyme, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from UniProt Q8X1D8 canonical sequence; Y398F reconstructed after confirming residue 398 is Tyr in the canonical sequence. and applied mutation signature Y398F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


sequence_variant_note: Resolved canonical sequence from UniProt Q8X1D8 canonical sequence; S171T reconstructed after confirming residue 171 is Ser in the canonical sequence. and applied mutation signature S171T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C


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

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


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

proof_lines: mutant enzyme H183S, at 30°C, pH not specified in the publication


enzyme_display_name: glyoxylate reductase (NADP(+))

organism: Thermus thermophilus HB27

substrate_name: NADPH

assay_conditions_summary: pH 6.7; 318.15 K; cofactor NADPH

proof_lines: with glyoxylate as substrate, pH 6.7, 45°C

enzyme: glyoxylate reductase (NADP(+))

substrate: NADPH


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession F4I907; direct REST lookup on 2026-06-13

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

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH

proof_lines: with succinic semialdehyde as substrate, pH 7.6, 30°C

proof_lines: recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C

proof_lines: isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C


substrate_name: glyoxylate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature K170E to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E

substrate: glyoxylate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature F231A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; cofactor NADPH

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature T95A to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature S121A to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature N174A to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature D239A to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9LSV0; direct REST lookup on 2026-06-13 and applied mutation signature K170R to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R


organism: Acetobacter aceti

substrate_name: glycolate

assay_conditions_summary: pH 9; 318.15 K; cofactor NADP+

proof_lines: with NADP+ as cosubstrate, at pH 9.0 and 45°C

proof_lines: with NAD+ as cosubstrate, at pH 9.0 and 45°C

proof_lines: with NADPH as cosubstrate, at pH 4.0 and 45°C

substrate: glycolate


organism: Chlamydomonas reinhardtii


organism: Euglena gracilis

assay_conditions_summary: cofactor NADPH


organism: Homo sapiens

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines: pH 7.5, 37°C, recombinant enzyme, with NADPH


organism: Neurospora crassa


organism: Oryza sativa

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25°C

proof_lines: isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25°C


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 7.8, temperature not specified in the publication, recombinant truncated enzyme


sequence_source: UniProtKB REST JSON primaryAccession Q9LSV0, accessed 2026-06-13

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme

proof_lines: pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer

proof_lines: pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a microplate reader


assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C

proof_lines: isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.8 and 25°C


organism: Malus domestica

sequence_source: UniProtKB REST JSON primaryAccession A0A1C8M582, accessed 2026-06-13

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.5 and 25°C

proof_lines: isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.5 and 25°C


sequence_source: UniProtKB REST JSON primaryAccession A0A1C8M593, accessed 2026-06-13

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25°C

proof_lines: isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.3 and 25°C


organism: Paecilomyces sp. 'thermophila'

sequence_source: UniProtKB REST JSON primaryAccession A0A0H3U0Y7, accessed 2026-06-13

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NADPH

proof_lines: pH 7.5, 50°C, recombinant enzyme, with NADPH


organism: Oryza sativa Japonica Group

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH

proof_lines: isoform GR2, with NADPH as cosubstrate, at pH 7.4 and 30°C


organism: Populus gelrica


organism: Pyrococcus horikoshii OT3

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: with hydroxypyruvate as substrate, pH 7.5


organism: Sinorhizobium meliloti

substrate_name: pyruvate

substrate: pyruvate


organism: Spinacia oleracea

substrate_name: NADH

proof_lines:
cofactor NADPH
cofactor NADH

substrate: NADH


organism: Thermus thermophilus

proof_lines: pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme

proof_lines: pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme

proof_lines: pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme


organism: Saccharomyces cerevisiae


organism: Branchiostoma floridae

substrate_name: all-trans-retinal

assay_conditions_summary: pH 6; 310.15 K; cofactor NADH

proof_lines:
isoform 2, pH 6.0, 37°C
isoform 1, pH 6.0, 37°C

substrate: all-trans-retinal


substrate_name: NAD+

assay_conditions_summary: pH 7.3; 310.15 K; cofactor NAD+

proof_lines: pH and temperature not specified in the publication

substrate: NAD+


organism: Kangiella koreensis


organism: Rattus norvegicus

substrate_name: retinol

substrate: retinol


substrate_name: all-trans-retinol

sequence_source: UniProtKB REST direct lookup for O75452 on 2026-06-13

column_label: Table 1: Kinetic constants of purified AKR, MDR and SDR enzymes with retinoids (Biochem. J. 2006, 399:101-109); substrate block 'All-trans-Retinol'; enzyme column head 'RoDH-4'; parameter rows 'K m (uM)' = 1.1, 'k cat (min^-1)' = 1.20 and 'k cat /K m (mM^-1 min^-1)' = 1100. The six enzyme column heads read, left to right, AKR1B1, AKR1B10, ADH4, ADH1B2, RDH11* and RoDH-4.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.1 uM; 1.1 / 1000 = 0.0011 mM. kcat: printed Table 1 cell 1.20 min^-1; 1.20 / 60 = 0.02 s^-1. kcat/Km: printed Table 1 cell 1100 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 of 1 s^-1 mM^-1, so 1100 / 60 = 18.333333333333332 s^-1 mM^-1. Each of these converted quantities reproduces the exported value for this row: kcat 0.02 s^(-1), km 0.0011 mM.

raw_value_unit_evidence: Table 1, substrate block 'All-trans-Retinol', enzyme column 'RoDH-4': K m (uM) = 1.1; k cat (min^-1) = 1.20; printed k cat /K m (mM^-1 min^-1) = 1100.

substrate: all-trans-retinol


sequence_source: UniProtKB REST direct lookup for Q8IZV5 on 2026-06-13

assay_conditions_summary: pH 7.4; cofactor NADP+

proof_lines: wild type enzyme, in 100 mM sodium phosphate, pH 7.4


substrate_name: all-trans retinal

assay_conditions_summary: cofactor NADH

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

substrate: all-trans retinal


organism: Mus musculus

sequence_source: UniProtKB REST direct lookup for Q8VIJ7 on 2026-06-13


sequence_source: UniProtKB REST direct lookup for Q05A13 on 2026-06-13

assay_conditions_summary: cofactor NAD+

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


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WPR5 REST lookup on 2026-06-13


organism: Nostoc sp. PCC 7120 = FACHB-418


organism: Synechocystis sp. PCC 6803

sequence_source: UniProtKB reviewed accession P74334 REST lookup on 2026-06-13

proof_lines: recombinant enzyme, pH 7.0, 28°C, in presence of 0.1 CMC C8E6