organism: Pyrococcus horikoshii

substrate_name: (R)-glycerate

assay_conditions_summary: pH 7; 318.15 K; cofactor ATP

proof_lines: the reaction mixture contains 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, 0.3 mM NADH, 1 mM phosphoenolpyruvate, 10 nM purified glycerate kinase, 3.5 units pyruvate kinase and 5 units lactate dehydrogenase in 50 mM potassium phosphate (pH 7.

substrate: (R)-glycerate


enzyme_display_name: glycerate 2-kinase

organism: Thermoplasma acidophilum

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8; 328.15 K; cofactor ATP

proof_lines: in 100 mM Tris-HCl (pH 8), 5 mM EGTA, 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, at 55°C

enzyme: glycerate 2-kinase

source: brenda


organism: Escherichia coli

substrate_name: D-mannitol[side 1]

assay_conditions_summary: pH 7; 310.15 K; buffer HEPES

proof_lines: in sodium phosphate buffer, at pH 7.0 and 37°C

substrate: D-mannitol[side 1]


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: 5'-deoxyadenosylcobinamide phosphate

substrate: 5'-deoxyadenosylcobinamide phosphate


enzyme_display_name: cardiolipin synthase (CMP-forming)

organism: Rattus norvegicus

substrate_name: egg yolk phosphatidylglycerol

proof_lines: pH 8.5, 37°C, at optimal concentration of phospholipid activators

proof_lines: at high Co2+ concentration, pH pH 9.0, 37°C

proof_lines: at low Co2+ concentration, pH pH 9.0, 37°C

enzyme: cardiolipin synthase (CMP-forming)

substrate: egg yolk phosphatidylglycerol


enzyme_display_name: thiosulfate--thiol sulfurtransferase

organism: Acinetobacter calcoaceticus

substrate_name: cyanide

enzyme: thiosulfate--thiol sulfurtransferase

substrate: cyanide


organism: Saccharomyces cerevisiae

substrate_name: glutathione

proof_lines: pH 8.1, 37°C, with benzenethiosulfonate as the other substrate

proof_lines: pH 8.1, 37°C, with thiosulfate as the other substrate

substrate: glutathione


organism: Homo sapiens


organism: squid

substrate_name: 3'-phosphoadenylyl sulfate

substrate: 3'-phosphoadenylyl sulfate


organism: Paenibacillus sp.


organism: Rhodococcus erythropolis

proof_lines:
pH 7.0, 28°C
pH 7.4, 35°C
pH 7.0, 28°C, recombinant enzyme


enzyme_display_name: retinoid isomerohydrolase

organism: Bos taurus

substrate_name: all-trans-retinyl palmitate

proof_lines: pH and temperature not specified in the publication

enzyme: retinoid isomerohydrolase

substrate: all-trans-retinyl palmitate


organism: Gallus gallus

assay_conditions_summary: pH 8; 310.15 K; buffer 10 mM BTP

proof_lines: purified enzyme, in 10 mM BTP buffer, pH 8.0, 100 mM NaCl, at 37°C


substrate_name: an all-trans-retinyl ester

substrate: an all-trans-retinyl ester


organism: Sus scrofa


organism: Aspergillus nidulans

substrate_name: mannitol 1-phosphate

proof_lines: at 2 mM mannitol 1-phosphate the maximal activity was underestimated, additional information

substrate: mannitol 1-phosphate


organism: Caloglossa continua

substrate_name: D-mannitol 1-phosphate

substrate: D-mannitol 1-phosphate


organism: Ectocarpus siliculosus


organism: Eimeria tenella


organism: Pyricularia oryzae


source_db: uniprot

protein_accession_database: UniProt

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

source: uniprot


organism: Escherichia coli (strain K12)

substrate_name: fructose-1-P (with magnesium ions as cofactor and at pH 9)

assay_conditions_summary: pH 9

proof_lines: kcat is 3.7 sec(-1) with fructose-1-P as substrate. kcat is 2.7 sec(-1) with ribose-5-P as substrate. kcat is 13 sec(-1) with glucose-6-P as substrate. kcat is 3.1 sec(-1) with fructose-6-P as substrate. kcat is 7.5 sec(-1) with beta-D-gluc


substrate_name: 2-deoxyglucose-6-P (with manganese ions as cofactor and at pH 9)

proof_lines: kcat is 33 sec(-1) with 2-deoxyglucose-6-P as substrate. kcat is 11 sec(-1) with mannose-6-P as substrate. kcat is 9.4 sec(-1) with 2-deoxyribose-5-P as substrate. kcat is 2.8 sec(-1) with ribose-5-P as substrate. kcat is 25 sec(-1) with gl


enzyme_display_name: pseudouridine 5'-phosphatase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: XMP

proof_lines: kcat is 1.9 sec(-1) with XMP as substrate.

enzyme: pseudouridine 5'-phosphatase

substrate: XMP


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 15.0 min(-1) with 2',3'-cAMP as substrate. kcat is 22.1 min(-1) with 2',3'-cGMP as substrate. kcat is 9.2 min(-1) with 3',5'-cAMP as substrate. kcat is 7.7 min(-1) with 3',5'-cGMP as substrate.


substrate_name: Unknown

km_display: Not reported

proof_lines: The 2',3'-cyclic phosphodiesterase activity is higher than that of the 5'-nucleotidase with the four major nucleotides used as substrates.

substrate: Unknown


organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

substrate_name: PEP (at pH 6.5)

proof_lines: kcat is 0.18 sec(-1) with PEP as substrate. kcat is 0.38 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.32 sec(-1) with 2',3'-cCMP as substrate. kcat is 0.42 sec(-1) with 2',3'-cGMP as substrate. kcat is 0.20 sec(-1) with pNPP as substrate

substrate: PEP (at pH 6.5)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 2.8 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.55 sec(-1) with pNPP as substrate. kcat is 12.4 sec(-1) with bis(pNPP) as substrate.


organism: Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)

proof_lines: kcat is 2.0 sec(-1) with beta-Ara2. kcat is 0.013 sec(-1) with Ara-Hyp. kcat is 6.3 sec(-1) with Ara(2)-Hyp.


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

substrate_name: cyclobis-(1-6)-alpha-nigerosyl (CNN)

proof_lines: kcat is 22.3 sec(-1) for cyclobis-(1-6)-alpha-nigerosyl (CNN) as substrate.

substrate: cyclobis-(1-6)-alpha-nigerosyl (CNN)


enzyme_display_name: exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)

organism: Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)

proof_lines: kcat is 54 sec(-1) with beta-1,2-glucotetrasaccharide as substrate. kcat is 29 sec(-1) with beta-1,2-glucopentasaccharide as substrate. kcat is 0.48 sec(-1) with beta-1,2-glucan (with an average DP of 77) as substrate.


enzyme_display_name: arylformamidase

organism: Bacillus anthracis

substrate_name: N-formyl-L-kynurenine

proof_lines: kcat is 50.56 sec(-1) for N-formyl-L-kynurenine as substrate.

enzyme: arylformamidase

substrate: N-formyl-L-kynurenine


organism: Streptococcus bovis

substrate_name: H2O; D-Mannitol 1-phosphate

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

substrate: H2O; D-Mannitol 1-phosphate


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

mutation_type: substitution


organism: Homo sapiens

substrate_name: pseudouridine 5'-phosphate

substrate: pseudouridine 5'-phosphate


organism: Bacillus sp. (in: firmicutes)

substrate_name: bis(p-nitrophenyl)phosphate

substrate: bis(p-nitrophenyl)phosphate


organism: Bacillus subtilis


organism: Escherichia coli


organism: Fusarium culmorum

substrate_name: cyclic 2',3'-GMP

substrate: cyclic 2',3'-GMP


organism: Haemophilus influenzae


organism: Mycobacterium tuberculosis

substrate_name: p-nitrophenyl phosphate

assay_conditions_summary: pH 8.5; buffer Tris-HCl

proof_lines: wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2

substrate: p-nitrophenyl phosphate


organism: Myxococcus xanthus

substrate_name: cyclic 2',3'-AMP

assay_conditions_summary: pH 8

substrate: cyclic 2',3'-AMP


organism: Proteus mirabilis


organism: Proteus vulgaris


organism: Shigella sonnei


organism: Vibrio alginolyticus

proof_lines:
with 200 mM NaCl
without NaCl


organism: Bacteroides thetaiotaomicron

ki_unit: mM


organism: Bifidobacterium longum


enzyme_display_name: C5a peptidase

organism: Streptococcus pyogenes

substrate_name: SQLRANISHKDMQLGR

proof_lines:
pH 7.4, 25°C
pH 7.4, 25°C, Km above 2 mM

enzyme: C5a peptidase

substrate: SQLRANISHKDMQLGR


enzyme_display_name: complement subcomponent C1r

substrate_name: N-acetyl-Arg methyl ester

enzyme: complement subcomponent C1r

substrate: N-acetyl-Arg methyl ester


organism: Elizabethkingia meningoseptica

substrate_name: Fetuin glycopeptide

substrate: Fetuin glycopeptide


organism: Mus musculus


organism: Prunus amygdalus var. dulcis

substrate_name: bromelain undecapeptide

proof_lines: stem bromelain undecapeptide, glycopeptidase group C

substrate: bromelain undecapeptide


organism: Saccharomyces cerevisiae

substrate_name: asialo fetuin glycopeptide I

substrate: asialo fetuin glycopeptide I


organism: Sus scrofa

substrate_name: Beta-aspartylglycosylamine

substrate: Beta-aspartylglycosylamine


organism: Bos taurus


organism: Drosophila melanogaster

proof_lines:
formamidase I
formamidase II


organism: Gallus gallus


organism: Neurospora crassa


organism: Ogataea henricii

proof_lines:
formamidase II
formamidase I


organism: Oncorhynchus mykiss

substrate_name: N-formyl-DL-kynurenine

substrate: N-formyl-DL-kynurenine


organism: Rattus sp.


organism: Streptomyces parvulus


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: N-substituted formamide deformylase

organism: Arthrobacter pascens

substrate_name: N-benzylformamide

proof_lines:
25°C, pH 7.5, recombinant enzyme
pH 7.0, 25°C
pH 7.5, 25°C

enzyme: N-substituted formamide deformylase

substrate: N-benzylformamide


enzyme_display_name: cyanoalanine nitrilase

organism: Brassica rapa

proof_lines: in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C

enzyme: cyanoalanine nitrilase


organism: Pseudomonas sp.


organism: Zea mays


enzyme_display_name: ADP-sugar diphosphatase

organism: Escherichia coli

substrate_name: ADP-ribose

assay_conditions_summary: pH 7.5; cofactor ADP

enzyme: ADP-sugar diphosphatase

substrate: ADP-ribose


organism: Rattus norvegicus

substrate_name: ADP-Rib

assay_conditions_summary: cofactor ADP

substrate: ADP-Rib


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: ADP-glucose

substrate: ADP-glucose


enzyme_display_name: adenylylsulfatase

substrate_name: Adenosine 5'-phosphosulfate; H2O

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

assay_conditions_summary: cofactor ATP

enzyme: adenylylsulfatase

substrate: Adenosine 5'-phosphosulfate; H2O


organism: Comamonas terrigena

substrate_name: adenosine 5'-phosphosulfate

substrate: adenosine 5'-phosphosulfate


enzyme_display_name: carboxynorspermidine decarboxylase

organism: Campylobacter jejuni

substrate_name: carboxyspermidine

proof_lines: pH and temperature not specified in the publication

enzyme: carboxynorspermidine decarboxylase

substrate: carboxyspermidine


organism: Eshraghiella crossota


organism: Vibrio alginolyticus

substrate_name: carboxynorspermidine

substrate: carboxynorspermidine


organism: Vibrio vulnificus


enzyme_display_name: porphobilinogen synthase

organism: Bos taurus

enzyme: porphobilinogen synthase


organism: Cereibacter sphaeroides


organism: Coturnix japonica

proof_lines:
liver enzyme
shell gland enzyme


organism: Drosophila melanogaster


assay_conditions_summary: pH 6

proof_lines:
at pH 6 and pH 8.5
at pH 6.8


organism: Homo sapiens


organism: Ictalurus punctatus


organism: Lathyrus oleraceus

proof_lines:
at pH 7.5
at pH 9


organism: Mus musculus

proof_lines:
pH 7.5
pH 6.4 and 37°C


organism: Mycolicibacterium phlei


organism: Neurospora crassa


organism: Plasmodium falciparum


organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 8.6; buffer Na-Hepes


organism: Pyrobaculum calidifontis

proof_lines: presence of zinc and 2-mercaptoethanol, pH 6.8, 70°C


organism: Rattus sp.

substrate_name: 5-aminolevulinic acid

proof_lines: expressed from expression vector pET28a+, His-tag removed

substrate: 5-aminolevulinic acid


organism: Rhodobacter capsulatus

proof_lines:
in absence of 2-mercaptoethanol
in presence of 2-mercaptoethanol


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P05373 reviewed HEM2_YEAST; PMID 2204246 names yeast structural gene HEM2; PubChem CID 137 for substrate SMILES

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

data_origin: experimental


organism: Tetradesmus obliquus


organism: Toxoplasma gondii


organism: Zea mays

proof_lines: in the presence of Hg2+, at pH 8.2 and 37°C

proof_lines: in the absence of Hg2+, at pH 8.2 and 37°C


organism: Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)

substrate_name: N-formyl-L-kynurenine

proof_lines: kcat is 43.94 sec(-1) for N-formyl-L-kynurenine as substrate.

substrate: N-formyl-L-kynurenine


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

proof_lines: kcat is 0.77 sec(-1) for N-formyl-L-kynurenine as substrate.


organism: Drosophila melanogaster

proof_lines: kcat is 1584 min(-1) with N-formyl-L-kynurenine as substrate.


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

proof_lines: kcat is 114.21 sec(-1) for N-formyl-L-kynurenine as substrate.


enzyme_display_name: UDP-2,3-diacylglucosamine diphosphatase

organism: Escherichia coli (strain K12)

enzyme: UDP-2,3-diacylglucosamine diphosphatase


enzyme_display_name: inosine/xanthosine triphosphatase

substrate_name: ITP

proof_lines: kcat is 573.3 sec(-1) with ITP as substrate. kcat is 2625 sec(-1) with XTP as substrate. kcat is 119 sec(-1) with GDP as substrate. kcat is 616.5 sec(-1) with dITP as substrate. kcat is 22.3 sec(-1) with GTP as substrate.

enzyme: inosine/xanthosine triphosphatase

substrate: ITP


enzyme_display_name: D-ornithine/D-lysine decarboxylase

organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

proof_lines: kcat is 1.8 sec(-1) with D-ornithine as substrate. kcat is 4.4 sec(-1) with D-lysine as substrate.

enzyme: D-ornithine/D-lysine decarboxylase


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

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

proof_lines: KM values are given with the protein sequence containing Glu instead of Lys at position 184, the effect of the variation on activity is unclear.


organism: Pisum sativum


organism: Lathyrus oleraceus

proof_lines:
pH 7.5, 30°C
isoform HMM2, 30°C
isoform HMM1, 30°C


organism: Glycyrrhiza echinata


organism: Medicago truncatula


organism: Methanosarcina barkeri

substrate_name: methyl-CoM

substrate: methyl-CoM


verification_status: unverified

status: unverified


sequence_source: UniProtKB reviewed entry Q48924, exact accession lookup on 2026-06-29


substrate_name: methylmercaptopropionate

sequence_source: UniProtKB reviewed Q48924 direct accession follow-up

proof_lines:
pH 7.0, 37°C
recombinant enzyme, pH 7.0, 37°C

substrate: methylmercaptopropionate


enzyme_display_name: 2-deoxystreptamine glucosyltransferase

organism: Streptomyces kanamyceticus

substrate_name: UDP-D-glucose

proof_lines: using UDP-D-glucose as donor, in 100 mM Tris-HCl (pH 7.6), 10 mM MgCl2, 6 mM 2-mercaptoethanol, and 1 mM phenylmethylsulfonyl fluoride, at 30°C

proof_lines: using UDP-N-acetyl-alpha-D-glucosamine as donor, in 100 mM Tris-HCl (pH 7.6), 10 mM MgCl2, 6 mM 2-mercaptoethanol, and 1 mM phenylmethylsulfonyl fluoride, at 30°C

enzyme: 2-deoxystreptamine glucosyltransferase

substrate: UDP-D-glucose


organism: Rhodothermus marinus

substrate_name: CTP

substrate: CTP


substrate_name: 2-Deoxystreptamine; UDP-D-glucose

sequence_source: UniProtKB reviewed accession Q65CC1 via exact accession lookup on 2026-06-29

substrate: 2-Deoxystreptamine; UDP-D-glucose


organism: Archaeoglobus fulgidus

substrate_name: 1L-myo-inositol 1-phosphate

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

sequence_source: UniProtKB reviewed accession O29976 via exact accession lookup on 2026-06-29

proof_lines: 90°C, pH 7.0, cytoplasmic CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34)

proof_lines: pH and temperature not specified in the publication

source_databases_merged: brenda skid

substrate: 1L-myo-inositol 1-phosphate


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

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

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


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

substrate_name: CTP (at pH 7 and 90 degrees Celsius)

substrate: CTP (at pH 7 and 90 degrees Celsius)


enzyme_display_name: type I site-specific deoxyribonuclease

organism: Escherichia coli

substrate_name: ATP

assay_conditions_summary: 310.15 K; cofactor ATP

enzyme: type I site-specific deoxyribonuclease

substrate: ATP


organism: Micrococcus luteus

substrate_name: DNA; ATP; H2O

assay_conditions_summary: pH 9.4; 303.15 K; cofactor ATP

substrate: DNA; ATP; H2O


organism: Pseudomonas sp. (strain ADP)

substrate_name: hydroxyatrazine

verification_status: corrected

assay_conditions_summary: pH 7; buffer 50 mM phosphate; cofactor ADP

substrate: hydroxyatrazine

status: corrected


organism: Pseudomonas sp.

substrate_name: Hydroxyatrazine

source_db: oed

verification_status: verified

sequence_source: UniProtKB reviewed accession P95442/ATZB_PSESD FASTA, checked 2026-06-29; entry cites PMID 17660279 for EC 3.5.4.43 and AtzB function.

assay_conditions_summary: pH 7; 296.15 K; cofactor ADP

column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column IEOT of the deamination block: row Km (uM) = 20; row kcat (s-1) = 3.2; row kcat/Km (mM-1 s-1) = 160. Captured primary segment: Table 2, substrate column IEOT (deamination block) | construct AtzB wild type | substrate IEOT, 2-(N-Ethylamino)-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine, hydroxyatrazine | condition pH 7.0 at 23 C | Km 20 uM | kcat 3.2 s-1 | kcat/Km 160 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 20 uM; 1 uM is 1/1000 mM, so 20 / 1000 = 0.02 mM. kcat: printed Table 2 cell 3.2 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 3.2 s^(-1). kcat/Km: printed Table 2 cell 160 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 160.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate column IEOT (deamination block), AtzB wild type: Km = 20 uM; kcat = 3.2 s-1; printed kcat/Km = 160 mM-1 s-1.

table_label: Table 2: Kinetic values for substrate hydrolysis by AtzB (Journal of Bacteriology 2007, 189(19):6989-6997)

substrate: Hydroxyatrazine

status: verified

source: oed


kcat_over_km_origin: calculated

column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column CIOT of the dechlorination block: row Km (uM) = 120; row kcat (s-1) = 1.9; row kcat/Km (mM-1 s-1) = 16. Captured primary segment: Table 2, substrate column CIOT (dechlorination block) | construct AtzB wild type | substrate CIOT, 2-Chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine | condition pH 7.0 at 23 C | Km 120 uM | kcat 1.9 s-1 | kcat/Km 16 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 120 uM; 1 uM is 1/1000 mM, so 120 / 1000 = 0.12 mM. kcat: printed Table 2 cell 1.9 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 1.9 s^(-1). kcat/Km: printed Table 2 cell 16 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the printed cell reads 16.0 s^(-1)*mM^(-1). Quotient disclosure for this column: 1.9 / 0.12 = 15.833333333333334 s^-1 mM^-1, against the printed catalytic-efficiency cell 16 mM-1 s-1, which is that same quantity written to the precision the table uses.

raw_value_unit_evidence: Table 2, substrate column CIOT (dechlorination block), AtzB wild type: Km = 120 uM; kcat = 1.9 s-1; printed kcat/Km = 16 mM-1 s-1.


column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column IIOT of the deamination block: row Km (uM) = 29; row kcat (s-1) = 0.8; row kcat/Km (mM-1 s-1) = 28. Captured primary segment: Table 2, substrate column IIOT (deamination block) | construct AtzB wild type | substrate IIOT, 2,4-Diisopropylamino-6-hydroxy-1,3,5-triazine | condition pH 7.0 at 23 C | Km 29 uM | kcat 0.8 s-1 | kcat/Km 28 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 29 uM; 1 uM is 1/1000 mM, so 29 / 1000 = 0.029 mM. kcat: printed Table 2 cell 0.8 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 0.8 s^(-1). kcat/Km: printed Table 2 cell 28 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the printed cell reads 28.0 s^(-1)*mM^(-1). Quotient disclosure for this column: 0.8 / 0.029 = 27.586206896551726 s^-1 mM^-1, against the printed catalytic-efficiency cell 28 mM-1 s-1, which is that same quantity written to the precision the table uses.

raw_value_unit_evidence: Table 2, substrate column IIOT (deamination block), AtzB wild type: Km = 29 uM; kcat = 0.8 s-1; printed kcat/Km = 28 mM-1 s-1.


column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column IMOT of the deamination block: row Km (uM) = 40; row kcat (s-1) = 1.4; row kcat/Km (mM-1 s-1) = 35. Captured primary segment: Table 2, substrate column IMOT (deamination block) | construct AtzB wild type | substrate IMOT, 6-Hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine | condition pH 7.0 at 23 C | Km 40 uM | kcat 1.4 s-1 | kcat/Km 35 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 40 uM; 1 uM is 1/1000 mM, so 40 / 1000 = 0.04 mM. kcat: printed Table 2 cell 1.4 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 1.4 s^(-1). kcat/Km: printed Table 2 cell 35 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 35.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate column IMOT (deamination block), AtzB wild type: Km = 40 uM; kcat = 1.4 s-1; printed kcat/Km = 35 mM-1 s-1.


column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column CEOT of the dechlorination block: row Km (uM) = 230; row kcat (s-1) = 1.6; row kcat/Km (mM-1 s-1) = 7. Captured primary segment: Table 2, substrate column CEOT (dechlorination block) | construct AtzB wild type | substrate CEOT, 2-Chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine | condition pH 7.0 at 23 C | Km 230 uM | kcat 1.6 s-1 | kcat/Km 7 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 230 uM; 1 uM is 1/1000 mM, so 230 / 1000 = 0.23 mM. kcat: printed Table 2 cell 1.6 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 1.6 s^(-1). kcat/Km: printed Table 2 cell 7 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the printed cell reads 7.0 s^(-1)*mM^(-1). Quotient disclosure for this column: 1.6 / 0.23 = 6.956521739130435 s^-1 mM^-1, against the printed catalytic-efficiency cell 7 mM-1 s-1, which is that same quantity written to the precision the table uses.

raw_value_unit_evidence: Table 2, substrate column CEOT (dechlorination block), AtzB wild type: Km = 230 uM; kcat = 1.6 s-1; printed kcat/Km = 7 mM-1 s-1.


substrate_name: H2O; Hydroxyatrazine

sequence_source: UniProtKB reviewed accession P95442/ATZB_PSESD FASTA, checked 2026-06-29; selected SABIO accession text '(P95442)*2' was interpreted only as identity context and not as a clean source tuple.

normalized_value_unit_evidence: Km: printed Table 2 cell 20 uM; 1 uM is 1/1000 mM, so 20 / 1000 = 0.02 mM. kcat: printed Table 2 cell 3.2 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 3.2 s^(-1). kcat/Km: printed Table 2 cell 160 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the printed cell reads 160.0 s^(-1)*mM^(-1). The live export row holds no kcat_over_km for this measurement and this pass adds none.

row_label: Table 2, substrate column IEOT (deamination block), AtzB wild type

substrate: H2O; Hydroxyatrazine


organism: Streptococcus pneumoniae

proof_lines: Km-value is determined using purified membranes from Escherichia coli expressing Streptococcus pneumoniae, pH 7.4, 37°C


enzyme_display_name: D-amino-acid N-acetyltransferase

organism: Saccharomyces cerevisiae

substrate_name: D-serine

sequence_source: UniProtKB reviewed accession P39979 (HPA3_YEAST), queried from the PMID 15375647 HPA3/Hpa3p paper anchor

assay_conditions_summary: 303.15 K; cofactor CoA

enzyme: D-amino-acid N-acetyltransferase

substrate: D-serine


organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

substrate_name: glycerol-3-phosphate (at 37 degrees Celsius and at pH 7.4)


substrate_name: Acetyl-CoA; D-Serine

sequence_source: UniProtKB reviewed accession P39979 (HPA3_YEAST), checked by direct UniProt REST/flat-file lookup on 2026-06-29

assay_conditions_summary: cofactor CoA

substrate: Acetyl-CoA; D-Serine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: D-Serine

substrate: D-Serine


organism: Homo sapiens

substrate_name: glucosylceramide

substrate: glucosylceramide


substrate_name: UDP-D-galactose; Glucosylceramide

sequence_source: UniProtKB reviewed accession Q9UBX8 (B4GT6_HUMAN), fetched 2026-06-29

substrate: UDP-D-galactose; Glucosylceramide


organism: Catharanthus roseus

substrate_name: UDP-alpha-D-glucose

sequence_source: UniProtKB reviewed accession U3U992 (UGT8_CATRO), fetched 2026-06-29

substrate: UDP-alpha-D-glucose


substrate_name: 7-deoxyloganetic acid

proof_lines: kcat is 0.130 sec(-1) for 7-deoxyloganetic acid. kcat is 0.325 sec(-1) for UPD-glucose.

substrate: 7-deoxyloganetic acid


proof_lines: kcat is 0.130 sec(-1) with 7-deoxyloganetic acid as substrate. kcat is 0.325 sec(-1) with UDP-glucose as substrate (PubMed:24104568). kcat is 1.25 sec(-1) with 7-deoxyloganetic acid as substrate (PubMed:24710322).


substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Rattus norvegicus


organism: Unknown

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Azospirillum brasilense

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


organism: Rhodospirillum rubrum

substrate_name: NAD

substrate: NAD


organism: Bacillus subtilis (strain 168)

substrate_name: Unknown

proof_lines: The Km value for methylglucuronoxylan from sweetgum is 1.63 mg/ml. The activity is directly correlated to the degree of substitution of the glucuronosyl moiety on the xylan chain.

substrate: Unknown


organism: Dickeya chrysanthemi


enzyme_display_name: Glucuronoxylanase XynC

organism: Bacillus subtilis

substrate_name: H2O; 4-O-Methyl-D-glucuronoxylan

sequence_source: UniProtKB reviewed accession Q45070 direct lookup

enzyme: Glucuronoxylanase XynC

substrate: H2O; 4-O-Methyl-D-glucuronoxylan


enzyme_display_name: albendazole monooxygenase

substrate_name: trimethylamine (at pH 8.5)

enzyme: albendazole monooxygenase

substrate: trimethylamine (at pH 8.5)


organism: Dicrocoelium dendriticum

substrate_name: albendazole S-oxide

proof_lines: mitochondrial fraction in vitro, pH 7.4, 37°C

proof_lines: microsomal fraction in vitro, pH 7.4, 37°C

substrate: albendazole S-oxide


organism: Ictalurus punctatus

substrate_name: H+; NADPH; O2; Albendazole

assay_conditions_summary: cofactor NADPH

substrate: H+; NADPH; O2; Albendazole


organism: Oncorhynchus mykiss


organism: Oreochromis sp.


organism: Escherichia coli

substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: UDPglucose

substrate: UDPglucose


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: lipopolysaccharide

proof_lines: in presence of optimal concentrations of phosphatidylethanolamine

substrate: lipopolysaccharide


organism: Salmonella typhimurium

substrate_name: UDPglucose; Lipopolysaccharide

sequence_source: UniProtKB:P19817 canonical FASTA, direct exact-accession lookup on 2026-06-29

substrate: UDPglucose; Lipopolysaccharide


substrate_name: beta-Alanine

sequence_source: UniProtKB:P50554 linked from PMID 10989446

proof_lines: competitive to beta-alanine, pH 8.8, 37°C

proof_lines: uncompetitive against 2-oxoglutarate, pH 8.8, 37°C

substrate: beta-Alanine


substrate_name: 2-Oxoglutarate; L-3-Amino-isobutanoate

sequence_source: UniProtKB:P50554 direct accession lookup

substrate: 2-Oxoglutarate; L-3-Amino-isobutanoate


proof_lines: pH 7.5, 30°C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP-


enzyme_display_name: [pyruvate, phosphate dikinase] kinase

organism: Arabidopsis thaliana

substrate_name: Pyruvate, phosphate dikinase; ADP

enzyme: [pyruvate, phosphate dikinase] kinase

substrate: Pyruvate, phosphate dikinase; ADP


enzyme_display_name: molybdenum cofactor sulfurtransferase

substrate_name: L-Cysteine; 1,4-Dithiothreitol

proof_lines: for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C

enzyme: molybdenum cofactor sulfurtransferase

substrate: L-Cysteine; 1,4-Dithiothreitol


organism: Homo sapiens

substrate_name: Benzamidoxime; NADH; H+

substrate: Benzamidoxime; NADH; H+


organism: Sus scrofa


enzyme_display_name: CoA:oxalate CoA-transferase

substrate_name: acetyl-CoA

assay_conditions_summary: pH 6.7; 298.15 K; cofactor CoA

enzyme: CoA:oxalate CoA-transferase

substrate: acetyl-CoA


substrate_name: oxalate

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

substrate: oxalate


substrate_name: NAD+

proof_lines: cosubstrate native ADP-D-ribosyl-[dinitrogen reductase], in the presence of MgADP-

proof_lines: cosubstrate ADP-D-ribosyl-[dinitrogen reductase] from Klebsiella pneumoniae, in the absence of MgADP-

proof_lines: cosubstrate ADP-D-ribosyl-[dinitrogen reductase] from Azotobacter vinelandii, in the absence of MgADP-

substrate: NAD+


organism: Zea mays

substrate_name: ADP

assay_conditions_summary: pH 8.3; 303.15 K; cofactor ADP

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

proof_lines: pyruvate,Pi dikinase phosphorylated at a His residue, pH 8.3, temperature not specified in the publication

substrate: ADP


enzyme_display_name: carbonic anhydrase

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

enzyme: carbonic anhydrase


substrate_name: ADP (at pH 6.8)

assay_conditions_summary: pH 6.8; cofactor ADP

substrate: ADP (at pH 6.8)


substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: benzamidoxime

substrate: benzamidoxime


organism: Acetobacter aceti

substrate_name: oxalate (at pH 6.7 and 25 degrees Celsius)

sequence_source: source_record; UniProtKB:A9X6P9

assay_conditions_summary: pH 6.7; cofactor CoA

proof_lines: kcat is 1.8 sec(-1) for the CoA-transferase activity with oxalate as substrate (at pH 6.7 and 25 degrees Celsius). kcat is 2 sec(-1) for the CoA-transferase activity with acetyl-CoA as substrate (at pH 6.7 and 25 degrees Celsius).


organism: Escherichia coli (strain K12)

substrate_name: acetyl-CoA (at pH 6.7 and 25 degrees Celsius)

sequence_source: source_record; UniProtKB:P76518

proof_lines: kcat is 11 sec(-1) for the CoA-transferase activity with acetyl-CoA as substrate (at pH 6.7 and 25 degrees Celsius). kcat is 15 sec(-1) for the CoA-transferase activity with oxalate as substrate (at pH 6.7 and 25 degrees Celsius).


enzyme_display_name: mannosyl-3-phosphoglycerate phosphatase

organism: Pyrococcus horikoshii

sequence_source: UniProtKB REST canonical sequence for O58690 (MPGP_PYRHO), queried 2026-06-29; MD5=7F432BF84DD27642FF31B20A7399BDAD

enzyme: mannosyl-3-phosphoglycerate phosphatase


organism: Thermus thermophilus

sequence_source: UniProtKB REST canonical sequence for Q84B23 (Q84B23_THETH), queried 2026-06-29; MD5=4A54F9943D4012189CAC75E5918BA5E4


organism: Bacteroides thetaiotaomicron

sequence_source: UniProtKB REST canonical sequence for Q8AAI7 (GMHBA_BACTN), queried 2026-06-29; MD5=B66102C560A5B5E75D6F57A4B1790364


enzyme_display_name: N(1)-aminopropylagmatine ureohydrolase

organism: Thermococcus kodakarensis

sequence_source: UniProtKB REST canonical sequence for Q5JI38 (APAUH_THEKO), queried 2026-06-29; MD5=35228BD9D101E7D36A16160659A45C80

smiles: N=C(N)NCCCCNCCCN

enzyme: N(1)-aminopropylagmatine ureohydrolase


substrate_name: agmatine

smiles: N=C(N)NCCCCN

substrate: agmatine


enzyme_display_name: prephenate decarboxylase

organism: Bacillus subtilis

substrate_name: prephenate

sequence_source: UniProtKB REST canonical sequence for P39638 (BACA_BACSU), queried 2026-06-29; MD5=33BE7A58F2127EF6C2CF88A017EC4144

enzyme: prephenate decarboxylase

substrate: prephenate


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

substrate_name: GPG (at 30 degrees Celsius)

substrate: GPG (at 30 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: glucosyl-3-phosphoglycerate (at 37 degrees Celsius)


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

substrate_name: GPG (at 70 degrees Celsius)

substrate: GPG (at 70 degrees Celsius)


sequence_source: UniProtKB reviewed accession O58690 (MPGP_PYRHO)


enzyme_display_name: coccolysin

organism: Enterococcus faecalis

substrate_name: Substance P

proof_lines:
scissile bond Gln6-Phe7
scissile bond Phe7-Phe8
scissile bond Gly9-Leu10

enzyme: coccolysin

substrate: Substance P


organism: Enterococcus faecalis subsp. liquefaciens

substrate_name: Insulin B chain; H2O

substrate: Insulin B chain; H2O


organism: Planktothrix agardhii

sequence_source: UniProtKB reviewed accession A0A073CEA3 (AERD_PLAA1)

proof_lines: pH and temperature not specified in the publication


organism: Salinispora tropica


organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

substrate_name: alpha-HBP (at pH 7.5 and 25 degrees Celsius)

proof_lines: kcat is 29 sec(-1) and 13 sec(-1) with alpha-HBP and beta-HBP as substrate, respectively. Thus, the enzyme displays 6-fold more efficiency towards the alpha- than the beta-anomer (PubMed:20050615).


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate (at pH 7.4)

proof_lines: kcat is 0.12 sec(-1) for D-glycero-alpha-D-manno-heptose 1,7-bisphosphate.


organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)

substrate_name: APA

proof_lines: kcat is 70.8 sec(-1) with APA as substrate.

substrate: APA


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

substrate_name: N(1)-aminopropylagmatine (at pH 7.5 and 70 degrees Celsius)

proof_lines: kcat is 1.86 sec(-1) for ureohydrolase activity with agmatine as substrate (at pH 7.5 and 70 degrees Celsius). kcat is 1.01 sec(-1) for ureohydrolase activity with N(1)-aminopropylagmatine as substrate (at pH 7.5 and 70 degrees Celsius).


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 190 min(-1) for decarboxylase activity with prephenate as substrate.


organism: Planktothrix agardhii (strain NIVA-CYA 126/8)

proof_lines: kcat is 245 min(-1) for decarboxylase activity with prephenate as substrate.


enzyme_display_name: xylonate dehydratase

organism: Pseudomonas sp.

substrate_name: D-gluconate

enzyme: xylonate dehydratase

substrate: D-gluconate


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

substrate_name: xylonate

substrate: xylonate


organism: Escherichia coli

substrate_name: D-xylonate

sequence_source: UniProtKB:P39358 REST lookup on 2026-06-29

substrate: D-xylonate


organism: Haloferax volcanii

substrate_name: D-Gluconate; D-Xylonate

sequence_source: UniProtKB:D4GP40 REST lookup on 2026-06-29

substrate: D-Gluconate; D-Xylonate


substrate_name: D-xylonate; D-gluconate

assay_conditions_summary: pH 7.5; 315.15 K; buffer 0.1 M Tris-HCl

proof_lines: at 42°C, in 0.1 M Tris-HCl buffer, pH 7.5, 2.5 M KCl, 50 mM MgCl2

substrate: D-xylonate; D-gluconate


organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)

proof_lines: kcat is 1406 min(-1) with D-xylonate as substrate. kcat is 2626 min(-1) with D-gluconate as substrate. kcat is 46 min(-1) with L-arabinonate as substrate. kcat is 218 min(-1) with D-galactonate as substrate. kcat is 196 min(-1) with D-fucon


organism: Escherichia coli (strain K12)


enzyme_display_name: 3-methyl-L-tyrosine peroxygenase

organism: Streptomyces lavendulae

proof_lines: kcat is 17.8 min(-1) with 3-methyl-L-tyrosine as substrate. kcat is 12.3 min(-1) with L-tyrosine as substrate.

enzyme: 3-methyl-L-tyrosine peroxygenase


substrate_name: L-tyrosine

sequence_source: UniProtKB B0CN28 direct FASTA/JSON lookup

substrate: L-tyrosine


enzyme_display_name: 9beta-pimara-7,15-diene oxidase

organism: Oryza sativa subsp. japonica

substrate_name: syn-pimaradiene

proof_lines: kcat is 46 sec(-1) with syn-pimaradiene as substrate and 49 sec(-1) with syn-stemodene as substrate.

enzyme: 9beta-pimara-7,15-diene oxidase

substrate: syn-pimaradiene


organism: Oryza sativa

substrate_name: 9beta-Pimara-7,15-diene; NADPH; O2

sequence_source: UniProtKB reviewed accession Q0JF01 (C99A3_ORYSJ)

substrate: 9beta-Pimara-7,15-diene; NADPH; O2


organism: Arabidopsis thaliana

sequence_source: UniProtKB Q42569 canonical sequence from direct REST lookup


proof_lines: kcat is 0.74 min(-1) for (22S)-22-hydroxycampesterol (PubMed:22822057). kcat is 0.11 min(-1) for (22R,23R)-22,23-dihydroxycampesterol (PubMed:22822057).


enzyme_display_name: gibberellin A9 O-methyltransferase

substrate_name: gibberellin a4

sequence_source: UniProtKB:F4JUY5 (GAMT1_ARATH, UniProtKB reviewed (Swiss-Prot))

enzyme: gibberellin A9 O-methyltransferase

substrate: gibberellin a4


substrate_name: gibberellin a9

substrate: gibberellin a9


enzyme_display_name: gibberellin A4 carboxyl methyltransferase

sequence_source: UniProtKB:Q5XF78 (GAMT2_ARATH, UniProtKB reviewed (Swiss-Prot))


enzyme: gibberellin A4 carboxyl methyltransferase


proof_lines: kcat is 0.01 sec(-1) for GA4. kcat is 0.026 sec(-1) for GA9.


proof_lines: kcat is 0.0015 sec(-1) for GA4. kcat is 0.0018 sec(-1) for GA9.


enzyme_display_name: 10-deoxymethynolide syntase

organism: Streptomyces venezuelae

enzyme: 10-deoxymethynolide syntase


proof_lines: pH 7.2, 30°C, kcat for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of 10-deoxymethynolide

proof_lines: pH 7.2, 30°C, KM-value for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of 10-deoxymethynolide

proof_lines: pH 7.2, 30°C, kcat/Km-value for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of 10-deoxymethynolide


enzyme_display_name: narbonolide synthase

enzyme: narbonolide synthase


proof_lines: pH 7.2, 30°C, kcat for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of narbonolide

proof_lines: pH 7.2, 30°C, Km-valkue for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of narbonolide

proof_lines: pH 7.2, 30°C, kcat/Km-value for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of narbonolide


sequence_source: source_record; UniProt Q9ZGI2 FASTA match checked 2026-06-30

proof_lines: kcat is 56 min(-1) for thioesterase activity with 2-methyl-3-ketopentanoyl-SNAC as substrate. kcat is 7.9 min(-1) for thioesterase activity with (2S,3R)-2-methyl-3-hydroxyacyl-SNAC as substrate. kcat is 4.3 min(-1) for thioesterase activity


enzyme_display_name: baicalein 7-O-glucuronosyltransferase

organism: Scutellaria baicalensis

substrate_name: baicalein

enzyme: baicalein 7-O-glucuronosyltransferase

substrate: baicalein


substrate_name: UDP-D-glucuronate; Baicalein

sequence_source: UniProtKB reviewed Swiss-Prot Q76MR7 direct accession lookup; canonical sequence for UBGAT_SCUBA.

substrate: UDP-D-glucuronate; Baicalein


substrate_name: scutellarein

substrate: scutellarein


enzyme_display_name: soyasapogenol B glucuronide galactosyltransferase

organism: Glycine max

substrate_name: UDP-D-galactose; Soyasapogenol B monoglucuronide

sequence_source: UniProtKB reviewed accession D4Q9Z4


substrate_name: soyasapogenol B 3-O-beta-D-glucuronide

enzyme: soyasapogenol B glucuronide galactosyltransferase

substrate: soyasapogenol B 3-O-beta-D-glucuronide


enzyme_display_name: [amino group carrier protein]-gamma-(L-lysyl)-L-glutamate

organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

proof_lines: kcat is 1.0 sec(-1) with N(2)-acetyl-L-ornithine as substrate. kcat is 0.8 sec(-1) with N(2)-acetyl-L-lysine as substrate.


organism: Thermus thermophilus

sequence_source: UniProtKB reviewed accession Q93R93

enzyme: [amino group carrier protein]-gamma-(L-lysyl)-L-glutamate


enzyme_display_name: taurine--pyruvate aminotransferase

organism: Bilophila wadsworthia

substrate_name: taurine

enzyme: taurine--pyruvate aminotransferase

substrate: taurine


sequence_source: UniProtKB FASTA Q9APM5


substrate_name: Pyruvate; Taurine

substrate: Pyruvate; Taurine


organism: Geobacillus thermodenitrificans subsp. thermodenitrificans

sequence_source: UniProtKB FASTA A0A0S2VC96


substrate_name: glycyrrhetinic acid-3-O-monoglucoside

sequence_source: UniProtKB reviewed accession D4Q9Z4 direct REST lookup on 2026-06-30

substrate: glycyrrhetinic acid-3-O-monoglucoside


organism: Campylobacter jejuni subsp. jejuni serotype O:2

sequence_source: UniProtKB reviewed accession Q0P8J8 direct REST lookup on 2026-06-30


substrate_name: CTP

substrate: CTP


organism: Pseudomonas denitrificans

sequence_source: UniProtKB reviewed accession P29936 direct REST lookup on 2026-06-30; sequence kept as context only because of taxonomy caveat


organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: adenosylcobinamide-GDP

substrate: adenosylcobinamide-GDP


organism: Sinorhizobium sp

substrate_name: alpha-ribazole 5'-phosphate

substrate: alpha-ribazole 5'-phosphate


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: L-glutamine phosphate

proof_lines: kcat is 57 min(-1) with L-glutamine phosphate as substrate (in the presence of MgCTP) (PubMed:29023101). kcat is 0.35 min(-1) with L-glutamine phosphate as substrate (in the presence of MnCTP). kcat is 0.6 min(-1) with phosphoramidate as su

substrate: L-glutamine phosphate


organism: Salmonella enterica

substrate_name: alpha-ribazole

substrate: alpha-ribazole


enzyme_display_name: phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase

organism: Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B)

proof_lines: kcat is 2.0 sec(-1) for 5-phospho-alpha-D-ribose 1,2-cyclic phosphate. kcat is 7.4 sec(-1) for D-ribofuranose 2,5-bisphosphate.


enzyme_display_name: Phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase

enzyme_name_source: UniProtKB C8WJZ5

organism: Eggerthella lenta

sequence_source: UniProtKB C8WJZ5 FASTA


substrate_name: D-ribofuranose 2,5-bisphosphate

enzyme: Phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase

substrate: D-ribofuranose 2,5-bisphosphate


enzyme_display_name: linear primary-alkylsulfatase

organism: Pseudomonas aeruginosa

substrate_name: SDS

sequence_source: UniProtKB direct accession lookup: Q9I5I9

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

enzyme: linear primary-alkylsulfatase

substrate: SDS


organism: Pseudomonas sp. S9

sequence_source: UniProtKB direct accession lookup: F2WP51

proof_lines:
at pH 7.1 and 25°C
at pH 9.0 and 70°C
Raw SKiD Env: Temp=25°C, pH=7.1


enzyme_display_name: chorismatase

organism: Actinoplanes sp. N902-109

substrate_name: chorismate

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

enzyme: chorismatase

substrate: chorismate


organism: Streptomyces hygroscopicus subsp. ascomyceticus

sequence_source: UniProtKB direct accession lookup: Q9KID9

proof_lines: wild type enzyme, in 100 mM Tris-HCl (pH 7.0), at 25°C


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


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

proof_lines: kcat is 337 min(-1) with 1-octyl sulfate as substrate. kcat is 5.4 min(-1) with (R)-2-octyl sulfate as substrate.


organism: Pseudomonas sp

proof_lines: kcat is 4.88 sec(-1) with SDS as substrate.


organism: Streptomyces hygroscopicus

proof_lines: kcat is 17.6 sec(-1) for chorismatase activity with chorismate as substrate.


assay_conditions_summary: pH 7; 293.15 K; buffer deuterated potassium phosphate

proof_lines: in deuterated potassium phosphate buffer (20 mM, pH 7.0), at 20°C


enzyme_display_name: [amino group carrier protein]-lysine hydrolase

organism: Thermus thermophilus

sequence_source: UniProtKB reviewed accession Q5SHH3; direct REST check on 2026-06-30


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8VUS5; direct REST check on 2026-06-30 and applied mutation signature R282E to reconstruct the assayed variant sequence.

enzyme: [amino group carrier protein]-lysine hydrolase


sequence_source: UniProtKB reviewed accession Q8VUS5; direct REST check on 2026-06-30


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8VUS5; direct REST check on 2026-06-30 and applied mutation signature R286E to reconstruct the assayed variant sequence.


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

proof_lines: kcat is 51.8 sec(-1) with N(2)-acetyl-L-lysine. kcat is 28.1 sec(-1) with N(2)-acetyl-L-ornithine.


enzyme_display_name: barbiturase

organism: Nocardioides sp.

substrate_name: H2O; Barbituric acid

sequence_source: UniProtKB A1SPN2 reviewed entry fetched 2026-06-30

enzyme: barbiturase

substrate: H2O; Barbituric acid


sequence_source: UniProtKB A1SGT4 reviewed entry fetched 2026-06-30


organism: Rhodococcus erythropolis

substrate_name: Barbiturate

sequence_source: UniProtKB Q8RSQ2 reviewed entry fetched 2026-06-30

substrate: Barbiturate


organism: Mycobacterium sp.


substrate_name: barbituric acid

proof_lines: kcat is 115 sec(-1) with barbituric acid as substrate.

substrate: barbituric acid


enzyme_display_name: spore photoproduct lyase

organism: Bacillus subtilis (strain 168)

substrate_name: SPTpT

proof_lines: SPTpT is the spore photoproduct of the TpT dinucleoside.

enzyme: spore photoproduct lyase

substrate: SPTpT


organism: Bacillus subtilis

sequence_source: UniProtKB reviewed entry P37956


organism: Geobacillus thermodenitrificans

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


proof_lines: mutant C140A, pH and temperature not specified in the publication


proof_lines: mutant Y98F, pH and temperature not specified in the publication


enzyme_display_name: 3-cyanoalanine hydratase

organism: Lupinus angustifolius

substrate_name: Beta-cyano-L-alanine

enzyme: 3-cyanoalanine hydratase

substrate: Beta-cyano-L-alanine


organism: Pseudomonas sp.


substrate_name: H2O; 3-Cyano-L-alanine

sequence_source: UniProtKB reviewed exact accession Q3LRV4

substrate: H2O; 3-Cyano-L-alanine


sequence_source: UniProtKB reviewed exact accession Q5QGZ8


organism: Arabidopsis thaliana

substrate_name: Ala(CN) (for the nitrilase activity)

substrate: Ala(CN) (for the nitrilase activity)


substrate_name: Ala(CN)

substrate: Ala(CN)


enzyme_display_name: (S)-scoulerine 9-O-methyltransferase

organism: Berberis wilsoniae

substrate_name: S-adenosyl-L-methionine

enzyme: (S)-scoulerine 9-O-methyltransferase

substrate: S-adenosyl-L-methionine


organism: Papaver somniferum

substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


organism: Eschscholzia californica subsp. californica

substrate_name: (S)-reticuline

sequence_source: UniProtKB A0A224ALZ8 FASTA/JSON, direct exact-accession lookup

proof_lines: cosubstrate (S)-reticuline, product norlaudanine, pH 8.4, 35°C

proof_lines: cosubstrate (S)-scoulerine, product (S)-tetrahydrocolumbamine, pH 8.4, 35°C

substrate: (S)-reticuline


substrate_name: (S)-norreticuline

substrate: (S)-norreticuline


sequence_source: UniProtKB I3PLQ7 FASTA/JSON, direct exact-accession lookup

proof_lines: pH 7.5, 37°C, recombinant detagged enzyme


organism: Stephania intermedia

sequence_source: UniProtKB A0A5P9PAM0 FASTA/JSON, direct exact-accession lookup; UniProt entry is flagged as Fragment


enzyme_display_name: aspartate racemase

organism: Acropora millepora

substrate_name: D-Aspartate

proof_lines: recombinant His-tagged mutant P150S, pH 8.0, 30°C

enzyme: aspartate racemase

substrate: D-Aspartate


substrate_name: L-aspartate

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

substrate: L-aspartate


organism: Anadara broughtonii

assay_conditions_summary: pH 5.53; 303.15 K; cofactor ATP

proof_lines:
pH 5.53, 1 mM ATP
pH 5.53, 2 mM ATP
pH 8.0, 30°C


organism: Anneissia japonica


organism: Aplysia californica


organism: Bifidobacterium bifidum

substrate_name: D-Asp

substrate: D-Asp


organism: Enterococcus faecalis

substrate_name: L-Asp

substrate: L-Asp


organism: Macrostomum lignano


organism: Manihot esculenta

substrate_name: D-glutamic acid

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

substrate: D-glutamic acid


organism: Mus musculus


organism: Saccoglossus kowalevskii

substrate_name: D-glutamate

proof_lines: wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme

proof_lines: pH 8.0, temperature not specified in the publication, wild-type enzyme, Asp/GluR enzyme

proof_lines: pH 8.0, temperature not specified in the publication, wild-type enzyme, AspR enzyme

substrate: D-glutamate


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme S156A, AspR enzyme


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme AS56A, AspR enzyme


proof_lines: mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme


organism: Sphagnum girgensohnii


organism: Spirogyra pratensis


organism: Streptococcus thermophilus

proof_lines: recombinant enzyme, pH 8.3, 37°C, coupling method assay


organism: Magallana gigas


proof_lines: recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C


organism: Microcystis aeruginosa

sequence_source: UniProtKB REST exact accession Q9RNB4


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession Q9RNB4 plus C195S reconstruction and applied mutation signature C195S to reconstruct the assayed variant sequence.


organism: Penaeus monodon


organism: Picrophilus oshimae


organism: Pyrococcus horikoshii

sequence_source: UniProtKB REST exact accession O58403


organism: Solanum lycopersicum

substrate_name: D-serine

sequence_source: UniProtKB REST exact accession A0A3Q7FTJ5

substrate: D-serine


organism: Thermococcus litoralis

sequence_source: UniProtKB REST exact accession H3ZNI2


enzyme_display_name: isocitrate dehydrogenase (NADP(+))

organism: Aeropyrum pernix

substrate_name: NADP+

sequence_source: UniProtKB exact accession Q9YE81 via rest.uniprot.org/uniprotkb/Q9YE81

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+

enzyme: isocitrate dehydrogenase (NADP(+))

substrate: NADP+


organism: Archaeoglobus fulgidus

substrate_name: NAD+

sequence_source: UniProtKB exact accession O29610 via rest.uniprot.org/uniprotkb/O29610

assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=60°C, pH=8

substrate: NAD+


organism: Bos taurus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


organism: Desulfotalea psychrophila

sequence_source: UniProtKB exact accession Q6AQ66 via rest.uniprot.org/uniprotkb/Q6AQ66

assay_conditions_summary: 278.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=5°C, pH=-----
Raw SKiD Env: Temp=25°C, pH=-----


organism: Escherichia coli

substrate_name: isocitrate

sequence_source: UniProtKB exact accession P08200 via rest.uniprot.org/uniprotkb/P08200

substrate: isocitrate


organism: Homo sapiens

sequence_source: UniProtKB exact accession O75874 via rest.uniprot.org/uniprotkb/O75874

assay_conditions_summary: pH 6.8; 310.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6.8
Raw SKiD Env: Temp=21°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.2


sequence_source: UniProtKB exact accession P48735 via rest.uniprot.org/uniprotkb/P48735

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

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


organism: Mus musculus

sequence_source: UniProtKB exact accession P54071 via rest.uniprot.org/uniprotkb/P54071

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.5


sequence_source: UniProtKB exact accession O88844 via rest.uniprot.org/uniprotkb/O88844


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB exact accession P9WKL1 via rest.uniprot.org/uniprotkb/P9WKL1

assay_conditions_summary: pH 7.5; cofactor NADP+


organism: Saccharomyces cerevisiae

substrate_name: NADPH

sequence_source: UniProtKB exact accession P21954 via rest.uniprot.org/uniprotkb/P21954

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

substrate: NADPH


organism: Sus scrofa

sequence_source: UniProtKB exact accession P33198 via rest.uniprot.org/uniprotkb/P33198

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


organism: Trypanosoma cruzi

sequence_source: UniProtKB exact accession Q4E4L7 via rest.uniprot.org/uniprotkb/Q4E4L7

assay_conditions_summary: cofactor NADP+


enzyme_display_name: pyranose dehydrogenase (acceptor)

organism: Leucoagaricus meleagris

substrate_name: ferricenium ion

sequence_source: UniProtKB Q3L245 reviewed Swiss-Prot entry PDH1_MACME

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8.5
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=2

enzyme: pyranose dehydrogenase (acceptor)

substrate: ferricenium ion


enzyme_display_name: carboxylesterase

organism: Actinidia eriantha

substrate_name: 4-methylumbelliferyl heptanoate

enzyme: carboxylesterase

substrate: 4-methylumbelliferyl heptanoate


substrate_name: 4-nitrophenyl dodecanoate

proof_lines:
Raw SKiD Env: Temp=60°C, pH=8
Raw SKiD Env: Temp=70°C, pH=7

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl propionate

substrate: 4-nitrophenyl propionate


substrate_name: 4-nitrophenyl palmitate

substrate: 4-nitrophenyl palmitate


organism: Bacillus subtilis

substrate_name: p-nitrophenyl acetate

substrate: p-nitrophenyl acetate


substrate_name: 4-nitrophenyl laurate

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

substrate: 4-nitrophenyl laurate


organism: Ferroplasma acidiphilum

substrate_name: 4-nitrophenyl butyrate

proof_lines:
Raw SKiD Env: Temp=50°C, pH=2
Raw SKiD Env: Temp=35°C, pH=6

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl acetate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=-----

substrate: 4-nitrophenyl acetate


organism: Oryctolagus cuniculus

substrate_name: irinotecan

substrate: irinotecan


organism: Pyrobaculum calidifontis

substrate_name: 4-nitrophenyl pentanoate

substrate: 4-nitrophenyl pentanoate


organism: Pyrococcus furiosus


organism: Saccharolobus shibatae


organism: Saccharolobus solfataricus

substrate_name: 4-nitrophenyl caprylate

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

substrate: 4-nitrophenyl caprylate


organism: Sulfolobus islandicus


organism: Sulfurisphaera tokodaii

substrate_name: 4-nitrophenyl hexanoate

proof_lines:
Raw SKiD Env: Temp=70°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

substrate: 4-nitrophenyl hexanoate


organism: Vulcanisaeta moutnovskia


enzyme_display_name: dimethylnonatriene synthase

organism: Arabidopsis thaliana

substrate_name: (E,E)-geranyllinalool

enzyme: dimethylnonatriene synthase

substrate: (E,E)-geranyllinalool


substrate_name: (3S)-(E)-Nerolidol; O2; NADPH; H+

sequence_source: UniProtKB:Q9LSF8 canonical sequence, reviewed entry C82G1_ARATH

assay_conditions_summary: cofactor NADPH

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

substrate: (3S)-(E)-Nerolidol; O2; NADPH; H+


organism: Zea mays

substrate_name: NADPH; O2; (3S)-(E)-Nerolidol; H+

sequence_source: UniProtKB:A0A1D6HSP4 canonical sequence, reviewed entry C92C5_MAIZE

substrate: NADPH; O2; (3S)-(E)-Nerolidol; H+


sequence_source: UniProtKB:A0A1D6HSP4 canonical sequence; current UniProt B6ST66 lookup redirects to A0A1D6HSP4


enzyme_display_name: C-19 steroid 1alpha-hydroxylase

organism: Sorangium cellulosum (strain So ce56)

substrate_name: nootkatone (in the presence of FdR_B and Fdx2)

proof_lines: kcat is 0.70 sec(-1) with nootkatone as substrate (in the presence of FdR_B and Fdx2). kcat is 0.96 sec(-1) with nootkatone as substrate (in the presence of FdR_B and Fdx8).

enzyme: C-19 steroid 1alpha-hydroxylase


organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


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


organism: Sorangium cellulosum

substrate_name: testosterone

proof_lines: pH and temperature not specified in the publication

substrate: testosterone


substrate_name: progesterone

sequence_source: UniProtKB:A9FDB7 plus selected source mutation note

sequence_variant_note: Mutation signature S276I matches the mutant residue at offset -4 and the reference residue at offset -10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH and temperature not specified in the publication, single-mutant enzyme S276I with a truncation of the first 50 amino acid residues at the N terminus

substrate: progesterone


sequence_variant_note: Mutation signature S276N matches the mutant residue at offset +5 and the reference residue at offset -10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH and temperature not specified in the publication, single mutant enzyme S276N with a truncation of the first 50 amino acid residues at the N terminus


sequence_source: UniProtKB:A9FDB7 plus selected source truncation note

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

mutation_type: truncation

proof_lines: pH and temperature not specified in the publication, mutant enzyme with a truncation of the first 50 amino acid residues at the N terminus


organism: Mycobacterium smegmatis


organism: Mycolicibacterium smegmatis

substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


organism: Corynebacterium glutamicum

sequence_source: UniProtKB reviewed Q8NTA6; PMID 18390549; RCSB/PDBe 3C4V maps entity 1 to Q8NTA6.


enzyme_display_name: N,N'-diacetylchitobiose phosphorylase

organism: Vibrio furnissii

substrate_name: N-acetyl-D-glucosamine

sequence_source: UniProtKB reviewed accession Q9F8X1, direct REST lookup on 2026-06-30

proof_lines: pH 7.0, 30°C, reverse phosphorolysis reaction

enzyme: N,N'-diacetylchitobiose phosphorylase

substrate: N-acetyl-D-glucosamine


organism: Vibrio proteolyticus

substrate_name: N,N'-diacetylchitobiose

sequence_source: UniProtKB reviewed accession Q76IQ9, direct REST lookup on 2026-06-30

proof_lines:
pH 7.0, 30°C
Raw SKiD Env: Temp=30°C, pH=7

substrate: N,N'-diacetylchitobiose


enzyme_display_name: lycopaoctaene synthase

organism: Botryococcus braunii

substrate_name: geranylgeranyl diphosphate

enzyme: lycopaoctaene synthase

substrate: geranylgeranyl diphosphate


enzyme_display_name: pyridoxamine-phosphate transaminase

organism: Clostridium butyricum

substrate_name: pyridoxamine 5'-phosphate

proof_lines: cosubstrate pyridoxamine 5-phosphate, pH 8.0, 37°C

enzyme: pyridoxamine-phosphate transaminase

substrate: pyridoxamine 5'-phosphate


organism: Treponema denticola

substrate_name: L-Alanine; Pyridoxal phosphate

sequence_source: UniProtKB Q56257 canonical sequence, checked 2026-06-30; context only because the accession EC conflicts with the selected EC.

substrate: L-Alanine; Pyridoxal phosphate


substrate_name: L-Alanine

substrate: L-Alanine


substrate_name: D-Alanine

substrate: D-Alanine


enzyme_display_name: ribonuclease M5

organism: Bacillus subtilis

substrate_name: 5S-rRNA precursor; H2O

sequence_source: UniProtKB:P37547 direct REST lookup

enzyme: ribonuclease M5

substrate: 5S-rRNA precursor; H2O


substrate_name: artificial 5S rRNA precursor substrate in complex with BL16 subunit


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed accession O88488 (PTPRQ_RAT), direct REST check on 2026-06-30; CRC64 F0FA703022EB25D5; length 2302.


organism: Ciona intestinalis

substrate_name: phosphatidylinositol 3,4-bisphosphate

proof_lines: pH not specified in the publication, 23°C, Vmax: 0.121 nmol/min/microgram

substrate: phosphatidylinositol 3,4-bisphosphate


organism: Homo sapiens

substrate_name: Inositol 1,3,4,5-tetrakisphosphate

substrate: Inositol 1,3,4,5-tetrakisphosphate


organism: Arabidopsis thaliana

substrate_name: p-NPP

substrate: p-NPP


substrate_name: PtdIns(3,4,5)P3; 1D-myo-inositol 1,3,4-trisphosphate; 1D-myo-inositol 1,3,4,5-tetrakisphosphate; 1D-myo-inositol 1,3,4,5,6-pentakisphosphate


organism: Brassica oleracea

assay_conditions_summary: pH 5; 310.15 K; buffer ammonium acetate

proof_lines: in ammonium acetate buffer, pH 5.0, at 37°C


organism: Lilium longiflorum


sequence_source: UniProtKB reviewed accession Q5H7P5 direct REST lookup on 2026-06-30; UniProtKB reviewed (Swiss-Prot); Lilium longiflorum; Mannosylglycoprotein endo-beta-mannosidase; EC 3.2.1.152.


enzyme_display_name: 1,2-dihydroxynaphthalene dioxygenase

organism: Pseudomonas putida

sequence_source: UniProtKB:P11861 reviewed Swiss-Prot entry NAHC1_PSEPU, cross-checked against PMID 7204331 and strain NCIMB 9816/DSM 8368/PG evidence.

enzyme: 1,2-dihydroxynaphthalene dioxygenase


organism: Sphingobium xenophagum

substrate_name: O2; Naphthalene-1,2-diol

sequence_source: UniProtKB reviewed entry P74836

substrate: O2; Naphthalene-1,2-diol


assay_conditions_summary: pH 5.5; buffer acetic acid-NaOH

proof_lines: Under alkaline conditions (pH 11), the cleavage of 1,2-DHN yield cis-2'-hydroxybenzalpyruvate.


enzyme_display_name: kievitone hydratase

organism: Fusarium solani

substrate_name: xanthohumol

enzyme: kievitone hydratase

substrate: xanthohumol


sequence_source: UniProtKB C7ZKN4 context only


organism: Nectria haematococca

substrate_name: H2O; Xanthohumol

sequence_source: UniProtKB C7ZKN4 context from SABIO-RK token (C7ZKN4)*2

substrate: H2O; Xanthohumol


sequence_source: UniProtKB C7ZKN4


organism: Fusarium phaseoli

substrate_name: Kievitone

substrate: Kievitone


enzyme_display_name: 7-methylxanthosine synthase

organism: Coffea arabica

substrate_name: xanthosine

enzyme: 7-methylxanthosine synthase

substrate: xanthosine


substrate_name: S-Adenosyl-L-methionine; Xanthosine

sequence_source: UniProtKB reviewed entry Q9AVK0 checked 2026-06-30

substrate: S-Adenosyl-L-methionine; Xanthosine


enzyme_display_name: chalcone synthase

organism: Medicago sativa

substrate_name: Hexanoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P30074 and applied mutation signature F215S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Hexanoyl-CoA', F215S column group; column 'kcat (min^-1)' = 0.07; column 'Km (uM)' = 4.5; column 'kcat/Km (M^-1 s^-1)' = 272.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row Hexanoyl-CoA: kcat = 0.07 min^-1; Km = 4.5 uM; printed kcat/Km = 272 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'Hexanoyl-CoA'

table_label: Table 2. Steady-state kinetic parameters (Proc. Natl. Acad. Sci. U.S.A. 2002, 99(8): 5319-5324, journal page 5321)

enzyme: chalcone synthase

substrate: Hexanoyl-CoA


substrate_name: N-Methylanthraniloyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'N-methylanthraniloyl-CoA', F215S column group; column 'kcat (min^-1)' = 0.09; column 'Km (uM)' = 3.0; column 'kcat/Km (M^-1 s^-1)' = 500.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row N-methylanthraniloyl-CoA: kcat = 0.09 min^-1; Km = 3.0 uM; printed kcat/Km = 500 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'N-methylanthraniloyl-CoA'

substrate: N-Methylanthraniloyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P30074 and applied mutation signature F265V to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'o-Coumaroyl-CoA', F265V column group; column 'kcat (min^-1)' = 0.47; column 'Km (uM)' = 4.0; column 'kcat/Km (M^-1 s^-1)' = 1,958.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row o-Coumaroyl-CoA: kcat = 0.47 min^-1; Km = 4.0 uM; printed kcat/Km = 1,958 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'o-Coumaroyl-CoA'


substrate_name: butanoyl-CoA

sequence_source: UniProtKB REST accession P30074 canonical sequence

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Butyryl-CoA; literal cells kcat 0.91 min^-1, Km 4.2 uM, kcat/Km 3,611 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 0.91 min^-1 normalizes to 0.015166666666666667 s^-1 and is stored at current precision as 0.015; printed Km 4.2 uM normalizes to 0.004200000000000001 mM and is stored as 0.004; current stored quotient is 3.75 s^-1*mM^-1; the independently printed ratio normalizes to 3.611 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Butyryl-CoA: kcat 0.91 min^-1; Km 4.2 uM; kcat/Km 3,611 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Butyryl-CoA

substrate: butanoyl-CoA


substrate_name: heptanoyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Heptanoyl-CoA; literal cells kcat 3.03 min^-1, Km 4.0 uM, kcat/Km 12,625 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 3.03 min^-1 normalizes to 0.050499999999999996 s^-1 and is stored at current precision as 0.051; printed Km 4.0 uM normalizes to 0.004 mM and is stored as 0.004; current stored quotient is 12.749999999999998 s^-1*mM^-1; the independently printed ratio normalizes to 12.625 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Heptanoyl-CoA: kcat 3.03 min^-1; Km 4.0 uM; kcat/Km 12,625 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Heptanoyl-CoA

substrate: heptanoyl-CoA


column_label: Table 2. Steady-state kinetic parameters; CHS column group; row m-Coumaroyl-CoA; literal cells kcat 3.50 min^-1, Km 4.5 uM, kcat/Km 12,963 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 3.50 min^-1 normalizes to 0.058333333333333334 s^-1 and is stored at current precision as 0.058; printed Km 4.5 uM normalizes to 0.0045 mM and is stored as 0.005; current stored quotient is 11.6 s^-1*mM^-1; the independently printed ratio normalizes to 12.963 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row m-Coumaroyl-CoA: kcat 3.50 min^-1; Km 4.5 uM; kcat/Km 12,963 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | m-Coumaroyl-CoA


substrate_name: Benzoyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Benzoyl-CoA; literal cells kcat 1.73 min^-1, Km 2.2 uM, kcat/Km 13,106 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 1.73 min^-1 normalizes to 0.028833333333333332 s^-1 and is stored at current precision as 0.029; printed Km 2.2 uM normalizes to 0.0022 mM and is stored as 0.002; current stored quotient is 14.5 s^-1*mM^-1; the independently printed ratio normalizes to 13.106 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Benzoyl-CoA: kcat 1.73 min^-1; Km 2.2 uM; kcat/Km 13,106 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Benzoyl-CoA

substrate: Benzoyl-CoA


organism: Physcomitrium patens

substrate_name: p-Coumaroyl-CoA

sequence_source: UniProtKB REST accession Q2VAZ3 canonical sequence

assay_conditions_summary: pH 7.2; 310.15 K; cofactor CoA

proof_lines:
37°C, pH 7.2
Raw SKiD Env: Temp=37°C, pH=7.2

substrate: p-Coumaroyl-CoA


organism: Polygonum cuspidatum

substrate_name: malonyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession H9DV62 canonical sequence with R105Q substitution(s) applied and applied mutation signature R105Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: mutant enzyme R105Q, at pH 8.0, temperature not specified in the publication

substrate: malonyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession H9DV62 canonical sequence with Q82P substitution(s) applied and applied mutation signature Q82P to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q82P, at pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession H9DV62 canonical sequence with Q82P/C198F substitution(s) applied and applied mutation signature Q82P/C198F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q82P/C198F, at pH 8.0, temperature not specified in the publication


organism: Sorbus aucuparia

substrate_name: Malonyl-CoA; 4-Coumaroyl-CoA

sequence_source: UniProtKB REST accession Q27Z06 canonical sequence

assay_conditions_summary: cofactor CoA

substrate: Malonyl-CoA; 4-Coumaroyl-CoA


enzyme_display_name: Chalcone synthase 1

organism: Glycine max

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P24826 (CHS1_SOYBN); fetched by UniProt REST direct accession lookup on 2026-06-30 and applied mutation signature R58A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R58A, pH and temperature not specified in the publication

enzyme: Chalcone synthase 1


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P24826 (CHS1_SOYBN); fetched by UniProt REST direct accession lookup on 2026-06-30 and applied mutation signature K55A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K55A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P24826 (CHS1_SOYBN); fetched by UniProt REST direct accession lookup on 2026-06-30 and applied mutation signature K268A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K268A, pH and temperature not specified in the publication


sequence_source: UniProtKB reviewed accession P24826 (CHS1_SOYBN); fetched by UniProt REST direct accession lookup on 2026-06-30

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

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


organism: Humulus lupulus

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


enzyme_display_name: Chalcone synthase H1

sequence_source: UniProtKB reviewed accession Q9FEY5 (CHSH1_HUMLU); fetched by UniProt REST direct accession lookup on 2026-06-30

enzyme: Chalcone synthase H1


enzyme_display_name: Chalcone synthase 2

sequence_source: UniProtKB reviewed accession P30074 (CHS2_MEDSA); fetched by UniProt REST direct accession lookup on 2026-06-30

enzyme: Chalcone synthase 2


substrate_name: Octanoyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Octanoyl-CoA', F215S column group; column 'kcat (min^-1)' = 0.04; column 'Km (uM)' = 4.8; column 'kcat/Km (M^-1 s^-1)' = 150.

raw_value_unit_evidence: Journal page 5321, Table 2, F215S column group, substrate row Octanoyl-CoA: kcat = 0.04 min^-1; Km = 4.8 uM; printed kcat/Km = 150 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F215S column group, substrate row 'Octanoyl-CoA'

substrate: Octanoyl-CoA


substrate_name: phenylpropionyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row '3-Phenylpropionyl-CoA', F265V column group; column 'kcat (min^-1)' = 4.40; column 'Km (uM)' = 13.8; column 'kcat/Km (M^-1 s^-1)' = 5,314.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row 3-Phenylpropionyl-CoA: kcat = 4.40 min^-1; Km = 13.8 uM; printed kcat/Km = 5,314 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row '3-Phenylpropionyl-CoA'

substrate: phenylpropionyl-CoA


column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Hexanoyl-CoA; literal cells kcat 2.52 min^-1, Km 4.1 uM, kcat/Km 10,243 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 2.52 min^-1 normalizes to 0.042 s^-1 and is stored at current precision as 0.042; printed Km 4.1 uM normalizes to 0.0040999999999999995 mM and is stored as 0.004; current stored quotient is 10.5 s^-1*mM^-1; the independently printed ratio normalizes to 10.243 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Hexanoyl-CoA: kcat 2.52 min^-1; Km 4.1 uM; kcat/Km 10,243 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Hexanoyl-CoA


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Hexanoyl-CoA', F265V column group; column 'kcat (min^-1)' = 3.56; column 'Km (uM)' = 5.0; column 'kcat/Km (M^-1 s^-1)' = 11,866.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Hexanoyl-CoA: kcat = 3.56 min^-1; Km = 5.0 uM; printed kcat/Km = 11,866 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Hexanoyl-CoA'


substrate_name: Phenylacetyl-CoA

column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Phenylacetyl-CoA', F265V column group; column 'kcat (min^-1)' = 4.37; column 'Km (uM)' = 5.7; column 'kcat/Km (M^-1 s^-1)' = 12,778.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Phenylacetyl-CoA: kcat = 4.37 min^-1; Km = 5.7 uM; printed kcat/Km = 12,778 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Phenylacetyl-CoA'

substrate: Phenylacetyl-CoA


substrate_name: Feruloyl-CoA

column_label: Table 2. Steady-state kinetic parameters; CHS column group; row Feruloyl-CoA; literal cells kcat 1.04 min^-1, Km 5.2 uM, kcat/Km 3,333 M^-1 s^-1. All cells are from one wild-type CHS2 row and not from F265V, F215S, or ACS.

normalized_value_unit_evidence: Printed kcat 1.04 min^-1 normalizes to 0.017333333333333333 s^-1 and is stored at current precision as 0.017; printed Km 5.2 uM normalizes to 0.0052 mM and is stored as 0.005; current stored quotient is 3.4000000000000004 s^-1*mM^-1; the independently printed ratio normalizes to 3.333 s^-1*mM^-1.

raw_value_unit_evidence: Table 2, CHS column group, row Feruloyl-CoA: kcat 1.04 min^-1; Km 5.2 uM; kcat/Km 3,333 M^-1 s^-1. The Table 2 footnote fixes units as min^-1, uM, and M^-1 s^-1.

row_label: CHS column group | Feruloyl-CoA

substrate: Feruloyl-CoA


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Feruloyl-CoA', F265V column group; column 'kcat (min^-1)' = 2.43; column 'Km (uM)' = 9.0; column 'kcat/Km (M^-1 s^-1)' = 4,500.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Feruloyl-CoA: kcat = 2.43 min^-1; Km = 9.0 uM; printed kcat/Km = 4,500 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Feruloyl-CoA'


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'Octanoyl-CoA', F265V column group; column 'kcat (min^-1)' = 9.82; column 'Km (uM)' = 5.6; column 'kcat/Km (M^-1 s^-1)' = 29,226.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row Octanoyl-CoA: kcat = 9.82 min^-1; Km = 5.6 uM; printed kcat/Km = 29,226 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'Octanoyl-CoA'


column_label: Table 2 (Steady-state kinetic parameters), substrate row 'p-Coumaroyl-CoA', F265V column group; column 'kcat (min^-1)' = 2.01; column 'Km (uM)' = 5.0; column 'kcat/Km (M^-1 s^-1)' = 6,700.

raw_value_unit_evidence: Journal page 5321, Table 2, F265V column group, substrate row p-Coumaroyl-CoA: kcat = 2.01 min^-1; Km = 5.0 uM; printed kcat/Km = 6,700 M^-1 s^-1. The printed unit footnote of Table 2 fixes those three units for every cell of the table.

row_label: Table 2, F265V column group, substrate row 'p-Coumaroyl-CoA'


enzyme_display_name: pyruvate kinase

organism: Ricinus communis

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ADP

proof_lines: 2 isozymes with different kinetic mechanisms

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Unknown

assay_conditions_summary: cofactor ADP


enzyme_display_name: beta-lactamase

substrate_name: H2O; Cefoxitin

enzyme: beta-lactamase

substrate: H2O; Cefoxitin


organism: Bacillus cereus

substrate_name: 6-Aminopenicillanate; H2O

sequence_source: UniProtKB:P00809 FASTA direct lookup on 2026-06-30

substrate: 6-Aminopenicillanate; H2O


organism: Klebsiella pneumoniae

substrate_name: H2O; Cephalothin

substrate: H2O; Cephalothin


organism: Amycolatopsis methanolica


organism: Arabidopsis thaliana


organism: Bos taurus


organism: Chlamydia trachomatis


organism: Corynebacterium glutamicum


organism: Escherichia coli


organism: Homo sapiens

assay_conditions_summary: pH 8; 305.15 K; cofactor ADP

proof_lines: pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate

proof_lines: Zn2+ bound to the ADP-binding site of the free enzyme, pH 7.4, 37°C


organism: Rattus norvegicus


organism: Toxoplasma gondii

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ADP

proof_lines: PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C


substrate_name: Furopenem; H2O

assay_conditions_summary: pH 6.8; 313.15 K; buffer 50 mM HEPES

proof_lines: pH 7.0, temperature not specified in the publication

substrate: Furopenem; H2O


enzyme_display_name: bacterial sulfide:quinone reductase

substrate_name: Decylubiquinone; Sulfide

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

enzyme: bacterial sulfide:quinone reductase

substrate: Decylubiquinone; Sulfide


organism: Acidithiobacillus ferrooxidans

substrate_name: decylubiquinone

proof_lines: in 50 mM 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (pH 6.5), temperature not specified in the publication

substrate: decylubiquinone


substrate_name: Sulfide

sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature C128S to reconstruct the assayed variant sequence.

substrate: Sulfide


organism: Caldivirga maquilingensis

proof_lines: pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K

proof_lines: pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K


enzyme_display_name: phenylalanine 4-monooxygenase

substrate_name: L-phenylalanine

enzyme: phenylalanine 4-monooxygenase

substrate: L-phenylalanine


organism: Dictyostelium discoideum

sequence_source: UniProtKB REST Q54XS1 canonical sequence

assay_conditions_summary: pH 4


source_db: sabio_rk, brenda, skid

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 P00439 canonical sequence

proof_lines: pH 7.0, 25°C, recombinant enzyme, versus (6R)-tetrahydrobiopterin

source_databases_merged: sabio_rk brenda skid

source: sabio_rk, brenda, skid


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with R408W substitution applied during review and applied mutation signature R408W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 298.15 K; buffer 100 mM Na-HEPES

proof_lines: mutant enzyme R408W, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with L348V substitution applied during review and applied mutation signature L348V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L348V, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with P416Q substitution applied during review and applied mutation signature P416Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme P416Q, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


proof_lines: wild type enzyme, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37°C

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with R155H substitution applied during review and applied mutation signature R155H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R155H, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with D143G substitution applied during review and applied mutation signature D143G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D143G, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with R68S substitution applied during review and applied mutation signature R68S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 310.15 K; buffer 50 mM potassium phosphate

proof_lines: mutant enzyme R68S, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme R68S, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme R68S, using S-carboxymethyl-L-cysteine as cosubstrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with V388M substitution applied during review and applied mutation signature V388M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V388M, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme V388M, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme V388M, using S-carboxymethyl-L-cysteine as cosubstrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with I65T substitution applied during review and applied mutation signature I65T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I65T, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme I65T, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme I65T, using S-carboxymethyl-L-cysteine as cosubstrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with R261Q substitution applied during review and applied mutation signature R261Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R261Q, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme R261Q, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme R261Q, using S-carboxymethyl-L-cysteine as cosubstrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with Y414C substitution applied during review and applied mutation signature Y414C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y414C, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme Y414C, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme Y414C, using S-carboxymethyl-L-cysteine as cosubstrate


substrate_name: tetrahydrobiopterin

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with Y138E substitution applied during review and applied mutation signature Y138E to reconstruct the assayed variant sequence.

substrate: tetrahydrobiopterin


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P00439 canonical sequence with Y138F substitution applied during review and applied mutation signature Y138F to reconstruct the assayed variant sequence.


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


substrate_name: L-Tryptophan

substrate: L-Tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P04176 and applied mutation signature A47G 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P04176 and applied mutation signature H64N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P04176 and applied mutation signature L48V to reconstruct the assayed variant sequence.


organism: Physcomitrium patens

substrate_name: L-phenylalanine with (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin as cosubstrate

sequence_source: source_record; direct UniProt accession check for E5KBU4 matched organism Physcomitrium patens, EC 1.14.16.1, PMID 20959559, and 394 aa sequence length

proof_lines: kcat is 1.16 sec(-1) with L-phenylalanine as substrate and (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin as cosubstrate (PubMed:20959559). kcat is 6.89 sec(-1) with L-phenylalanine as substrate and 10-formyltetrahydrofolate as cosubstrate (Pub


organism: Pinus taeda

sequence_source: source_record; direct UniProt accession check for E5KBU3 matched organism Pinus taeda, EC 1.14.16.1, PMID 20959559, and 354 aa sequence length

proof_lines: kcat is 0.132 sec(-1) with L-phenylalanine as substrate and (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin as cosubstrate (PubMed:20959559). kcat is 2.30 sec(-1) with L-phenylalanine as substrate and 10-formyltetrahydrofolate as cosubstrate (Pu

substrate: L-phenylalanine with (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin as cosubstrate


sequence_variant_note: Resolved canonical sequence from direct_uniprot_exact_accession_reconstructed_variant and applied mutation signature Y138K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_exact_accession_reconstructed_variant and applied mutation signature Y138A to reconstruct the assayed variant sequence.


organism: Pseudomonas fluorescens

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q PheH'; column 'Vmax for phenylalanine hydroxylation (min-1)' = 840; column 'Kphe (µM)' = 569; column 'V/Kphe (µM-1 min-1)' = 1.48. The remaining three cells of the same printed row belong to the tyrosine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q PheH': Kphe = 569 uM; Vmax for phenylalanine hydroxylation = 840 min^-1; V/Kphe = 1.48 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q PheH', the three phenylalanine hydroxylation cells (Vmax for phenylalanine hydroxylation, Kphe, V/Kphe)


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q/Y277H/V379D to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q/Y277H/V379D PheH'; column 'Vmax for phenylalanine hydroxylation (min-1)' = 125; column 'Kphe (µM)' = 218; column 'V/Kphe (µM-1 min-1)' = 0.57. The remaining three cells of the same printed row belong to the tyrosine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q/Y277H/V379D PheH': Kphe = 218 uM; Vmax for phenylalanine hydroxylation = 125 min^-1; V/Kphe = 0.57 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q/Y277H/V379D PheH', the three phenylalanine hydroxylation cells (Vmax for phenylalanine hydroxylation, Kphe, V/Kphe)


sequence_variant_note: Resolved canonical sequence from direct_uniprot_exact_accession_reconstructed_variant and applied mutation signature V379D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q/V379D to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q/V379D PheH'; column 'Vmax for phenylalanine hydroxylation (min-1)' = 281; column 'Kphe (µM)' = 1080; column 'V/Kphe (µM-1 min-1)' = 0.26. The remaining three cells of the same printed row belong to the tyrosine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q/V379D PheH': Kphe = 1080 uM; Vmax for phenylalanine hydroxylation = 281 min^-1; V/Kphe = 0.26 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q/V379D PheH', the three phenylalanine hydroxylation cells (Vmax for phenylalanine hydroxylation, Kphe, V/Kphe)


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature Y277H to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'Y277H PheH'; column 'Vmax for phenylalanine hydroxylation (min-1)' = 604; column 'Kphe (µM)' = 574; column 'V/Kphe (µM-1 min-1)' = 1.05. The remaining three cells of the same printed row belong to the tyrosine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'Y277H PheH': Kphe = 574 uM; Vmax for phenylalanine hydroxylation = 604 min^-1; V/Kphe = 1.05 uM^-1 min^-1.

row_label: Table 3, enzyme row 'Y277H PheH', the three phenylalanine hydroxylation cells (Vmax for phenylalanine hydroxylation, Kphe, V/Kphe)


organism: Chromobacterium violaceum

sequence_source: UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30)

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

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature L101Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM HEPES-NaOH

proof_lines: mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature L101Y/W180F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature W180F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature T254A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature F258A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F258A, in 0.1 M Na-HEPES (pH 7.4) at 30°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: mutant enzyme S230P, in 0.1 M Na-HEPES (pH 7.4) at 30°C


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

assay_conditions_summary: pH 7.4; 303.15 K; buffer 50 mM HEPES-NaOH

proof_lines: wild type enzyme, in 0.1 M Na-HEPES (pH 7.4) at 30°C

proof_lines: wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)


proof_lines: mutant enzyme T254A, in 0.1 M Na-HEPES (pH 7.4) at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature Y155A to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme Y155A, in 0.1 M Na-HEPES (pH 7.4) at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P30967 -> primary P30967 (checked 2026-06-30) and applied mutation signature D139N to reconstruct the assayed variant sequence.


organism: Caenorhabditis elegans


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


proof_lines: mutant enzyme I234D, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol


proof_lines: wild type enzyme, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol


organism: Colwellia psychrerythraea 34H

proof_lines:
pH 7.0, 10°C, recombinant enzyme
pH 7.0, 25°C, recombinant enzyme


proof_lines: wild type enzyme, without preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C

proof_lines: wild type enzyme, 5 min preincubation with L-phenylalanine, 100 mM Tris-HCl (pH 7.5), at 37°C