enzyme_display_name: N-acetylglucosamine kinase

organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: N-acetylglucosamine (GlcNAc)

enzyme: N-acetylglucosamine kinase

substrate: N-acetylglucosamine (GlcNAc)


organism: Escherichia coli (strain K12)

substrate_name: GlcNAc (at 37 degrees Celsius and pH 7.5)

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7.5; cofactor ATP

data_origin: experimental

source: uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: N-acetylglucosamine

assay_conditions_summary: cofactor ATP

substrate: N-acetylglucosamine


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

organism: Arabidopsis thaliana

substrate_name: GDP-L-galactose

substrate: GDP-L-galactose


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


organism: Aquifex aeolicus (strain VF5)

substrate_name: UDP-MurNAc-pentapeptide

substrate: UDP-MurNAc-pentapeptide


enzyme_display_name: flavonol 3-sulfotransferase

organism: Flaveria chlorifolia

substrate_name: rhamnetin

enzyme: flavonol 3-sulfotransferase

substrate: rhamnetin


enzyme_display_name: pectinesterase

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

enzyme: pectinesterase


enzyme_display_name: histidinol-phosphatase

organism: Escherichia coli O157:H7

substrate_name: histidinol phosphate (in the presence of Mg(2+))

enzyme: histidinol-phosphatase


enzyme_display_name: sphingomyelin phosphodiesterase

organism: Caenorhabditis elegans

substrate_name: sphingomyelin (at pH 5.0)

assay_conditions_summary: pH 5

enzyme: sphingomyelin phosphodiesterase

substrate: sphingomyelin (at pH 5.0)


substrate_name: sphingomyelin (N-acyl-sphing-4-enine-1-phosphocholine) (at pH 5.0)


organism: Homo sapiens

substrate_name: sphingomyelin (at pH 7.4 and 37 degrees Celsius in the presence of 0.05% Triton X-100)


substrate_name: Unknown

km_display: Not reported

substrate: Unknown


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

organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

substrate_name: NAD(+)

substrate: NAD(+)


organism: Staphylococcus aureus (strain MSSA476)

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


enzyme_display_name: beta-aspartyl-peptidase

substrate_name: L-asparagine (L-Asn)

enzyme: beta-aspartyl-peptidase

substrate: L-asparagine (L-Asn)


organism: Rattus norvegicus


enzyme_display_name: endopeptidase La

organism: Bacillus subtilis (strain 168)

substrate_name: ATP

enzyme: endopeptidase La

substrate: ATP


organism: Mus musculus

substrate_name: sphingomyelin (at pH 7.4 and 37 degrees Celsius)


enzyme_display_name: alpha-D-xyloside xylohydrolase

organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)

substrate_name: isoprimeverose

enzyme: alpha-D-xyloside xylohydrolase

substrate: isoprimeverose


organism: Lactiplantibacillus pentosus


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: maltose

substrate: maltose


enzyme_display_name: beta-D-fucosidase

organism: Bifidobacterium breve

substrate_name: pNP-beta-D-glucoside

enzyme: beta-D-fucosidase

substrate: pNP-beta-D-glucoside


substrate_name: ATP for ATPase activity

substrate: ATP for ATPase activity


enzyme_display_name: chitin deacetylase

substrate_name: GlcNAc(6) (at 50 degrees Celsius and pH 8)

assay_conditions_summary: pH 8

enzyme: chitin deacetylase


enzyme_display_name: (d)CTP diphosphatase

organism: Escherichia coli (strain K12)

enzyme: (d)CTP diphosphatase


enzyme_display_name: arogenate dehydratase

substrate_name: arogenate

enzyme: arogenate dehydratase

substrate: arogenate


verification_status: unverified

status: unverified


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

organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

proof_lines: The kinetic parameters are studied for the 3C-like proteinase domain.

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

substrate: peptide TSAVLQSGFRK-NH(2)


organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)


organism: Vaccinia virus (strain Western Reserve)

substrate_name: GpppA

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

proof_lines: A-570 and A-763 mutants have 3-fold and 10-fold higher Km values for GpppA.

substrate: GpppA


organism: Cryptococcus neoformans (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)

substrate_name: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate) (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 7.5 sec(-1) with AICAR formyltransferase activity with (6S)-10-formyltetrahydrofolate as substrate (PubMed:36063996). kcat is 7.7 sec(-1) for FAICAR cyclization activity (at pH 7.5 and 37 degrees Celsius) (PubMed:36063996).


substrate_name: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate)

proof_lines: kcat is 3.7 sec(-1) for AICAR formyltransferase activity with (6S)-10-formyltetrahydrofolate as substrate (PubMed:10985775). kcat is 4.1 sec(-1) for AICAR formyltransferase activity with 10-formyldihydrofolate as substrate (PubMed:10985775)


enzyme_display_name: diacylglycerol O-acyltransferase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

assay_conditions_summary: cofactor CoA

enzyme: diacylglycerol O-acyltransferase


enzyme_display_name: beta-carotene 15,15'-dioxygenase

substrate_name: all-trans-beta-carotene

proof_lines: kcat is 0.45 min(-1) with all-trans-beta-carotene as substrate.

enzyme: beta-carotene 15,15'-dioxygenase

substrate: all-trans-beta-carotene


organism: Uncultured marine bacterium 66A03

substrate_name: beta-carotene

proof_lines: The kcat is 4.5-fold higher with beta-carotene than with beta-cryptoxanthin as substrate.

substrate: beta-carotene


enzyme_display_name: NAD(P)H oxidase (H2O2-forming)

organism: Homo sapiens

substrate_name: F-actin (at saturating NADPH concentration)

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 0.28 sec(-1) for NADPH for the NADPH oxidase reaction.

enzyme: NAD(P)H oxidase (H2O2-forming)


substrate_name: NADPH

proof_lines: kcat is 11.84 min(-1) for the NADPH oxidase activity releasing hydrogen peroxide from O2.

substrate: NADPH


enzyme_display_name: type I protein arginine methyltransferase

substrate_name: S-adenosyl-L-methionine (at pH 8)

proof_lines: kcat is 0.1 min(-1) with RPS2 as substrate (at pH 8).

substrate: S-adenosyl-L-methionine (at pH 8)


organism: Dengue virus type 2 (strain Thailand/NGS-C/1944)

substrate_name: triphosphorylated RNA

proof_lines: Vmax with 0.65 nmol/s/ug enzyme for RTPase activity with triphosphorylated RNA as substrate.

substrate: triphosphorylated RNA


substrate_name: C26:0-CoA (with 1,2-dipalmitin as the acyl acceptor and at 37 degrees Celsius)


enzyme_display_name: phosphoserine transaminase

proof_lines: No activity could be observed with non-phosphorylated substrates.

enzyme: phosphoserine transaminase


proof_lines: kcat is 23.8 sec (-1) for the transaminase reaction with 3-phosphooxypyruvate and L-glutamate as substrates. kcat is 8.6 sec (-1) for the transaminase reaction with 2-oxoglutarate and O-phospho-L-serine as substrates.


enzyme_display_name: dephospho-CoA kinase

substrate_name: dephospho-CoA

enzyme: dephospho-CoA kinase

substrate: dephospho-CoA


enzyme_display_name: N-acetylglucosamine kinase

organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)

substrate_name: N-acetylmuramate

proof_lines: kcat is 65.0 sec(-1) with GlcNAc as substrate. kcat is 42.8 sec(-1) with MurNAc as substrate.

enzyme: N-acetylglucosamine kinase

substrate: N-acetylmuramate


organism: Shewanella sp. (strain ANA-3)

substrate_name: GalNAc

proof_lines: kcat is 40.3 sec(-1) for kinase activity with GalNAc as substrate. kcat is 7.1 sec(-1) for kinase activity with GlcNAc as substrate.

substrate: GalNAc


organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)

substrate_name: L-Asn

proof_lines: Enzyme is inactive on alpha-aspartyl dipeptides.

substrate: L-Asn


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


enzyme_display_name: bleomycin hydrolase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: N-terminal acetylation of lysine-4-methyl-7-coumarylamide (Ac-Lys-AMC) reduces the catalytic efficiency 50-fold towards this substrate.

enzyme: bleomycin hydrolase


organism: Bombyx mori

proof_lines: kcat is 7.62 min(-1) for GlcNAc(3) (PubMed:30755482). kcat is 5.59 min(-1) for GlcNAc(4) (PubMed:30755482). kcat is 7.52 min(-1) for GlcNAc(5) (PubMed:30755482). kcat is 9.07 min(-1) for GlcNAc(6) (PubMed:30755482). kcat is 0.097 min(-1) fo


organism: Colletotrichum lindemuthianum

substrate_name: GlcNAc(2) (at 45 degrees Celsius and pH 8.5)

proof_lines: kcat is: 8.52 sec(-1) with GlcNAc(2) as substrate (at 45 degrees Celsius and pH 8.5), 11 sec(-1) with GlcNAc(2) as substrate (at 30 degrees Celsius and pH 8.5), 5.94 sec(-1) with GlcNAc(3) as substrate (at 45 degrees Celsius and pH 8.5), 1.


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

substrate_name: GlcNAc(5) (at 37 degrees Celsius, pH 8 and in presence of Co(2+))

proof_lines: kcat is 7 sec(-1) with GlcNAc(5) as substrate.


enzyme_display_name: RNA uridylyltransferase

substrate_name: UTP (at 27 degrees Celsius and with 6(U) single-stranded RNA as substrate)

proof_lines: kcat is 0.5 min(-1) with UTP (PubMed:17189640). kcat is 0.3 min(-1) with 6(U) single-stranded RNA (PubMed:17189640).

enzyme: RNA uridylyltransferase


enzyme_display_name: sphingomyelin phosphodiesterase

substrate_name: sphingomyelin

enzyme: sphingomyelin phosphodiesterase

substrate: sphingomyelin


organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)

substrate_name: Xyl-alpha-PNP

proof_lines: kcat is 1.6 sec(-1) for Xyl-alpha-PNP. kcat is 0.071 sec(-1) for Glc-alpha-PNP. kcat is 32.6 sec(-1) for XXXG. kcat is 31.0 sec(-1) for XLLG. kcat is 1.78 sec(-1) for isoprimeverose.

substrate: Xyl-alpha-PNP


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

substrate_name: NAD(+)

proof_lines: kcat is 10.3 min(-1) with NAD(+) as substrate.

substrate: NAD(+)


enzyme_display_name: beta-aspartyl-peptidase

organism: Escherichia coli (strain K12)

substrate_name: beta-L-Asp-L-Leu

proof_lines: No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-amide, L-Gln, aspartylglucosamides alpha- or gamma-aspartyl dipeptides.

enzyme: beta-aspartyl-peptidase

substrate: beta-L-Asp-L-Leu


organism: Lupinus luteus

proof_lines: No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-amide, L-Gln or aspartylglucosamides.


organism: Pseudomonas sp. (strain ADP)

substrate_name: N-methylammelide

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 178 sec(-1) for N-methylammelide. kcat is 209 sec(-1) for N-ethylammelide. kcat is 80.6 sec(-1) for N-hydroxyethylammelide. kcat is 13.3 sec(-1) for N-isopropylammelide. kcat is 98.2 sec(-1) for N-cyclopropylammelide. kcat is 0.07 s

substrate: N-methylammelide


enzyme_display_name: XTP/dITP diphosphatase

substrate_name: XTP (at pH 10.0 and 37 degrees Celsius)

assay_conditions_summary: pH 10

proof_lines: Vmax values are similar for XTP, dITP and ITP. Activity toward dATP, dCTP and dTTP is less than 1% of the rate of XTP hydrolysis. dGTP and dUTP are hydrolyzed at 10-12% of the rate of XTP hydrolysis (PubMed:12297000). kcat is 5.7 sec(-1) wi

enzyme: XTP/dITP diphosphatase

substrate: XTP (at pH 10.0 and 37 degrees Celsius)


substrate_name: ITP

proof_lines: kcat is 580 sec(-1) with ITP as substrate (PubMed:11278832). kcat is 360 sec(-1) with dITP as substrate (PubMed:11278832). kcat is 640 sec(-1) with XTP as substrate (PubMed:11278832). kcat is 79.6 sec(-1) with dITP as substrate (PubMed:1709

substrate: ITP


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

substrate_name: XTP (at pH 7.6 and 80 degrees Celsius)

proof_lines: kcat is 1009 sec(-1) with XTP as substrate. kcat is 911.7 sec(-1) with ITP as substrate. kcat is 97.6 sec(-1) with GTP as substrate. kcat is 96.6 sec(-1) with dGTP as substrate (at pH 7.6 and 80 degrees Celsius) (PubMed:10404228). kcat is 1

substrate: XTP (at pH 7.6 and 80 degrees Celsius)


organism: Mus musculus

substrate_name: dITP

proof_lines: kcat is 84 sec(-1) with dITP as substrate (PubMed:17090528). kcat is 115 sec(-1) with dHAPTP as substrate (PubMed:17090528). kcat is 12.4 sec(-1) with dGTP as substrate (PubMed:17090528).

substrate: dITP


proof_lines: kcat is 33.5 sec(-1) with dITP as substrate (PubMed:17090528). kcat is 23.4 sec(-1) with dHAPTP as substrate (PubMed:17090528). kcat is 20.9 sec(-1) with dGTP as substrate (PubMed:17090528).


enzyme_display_name: N-acylmannosamine kinase

substrate_name: N-acyl-D-mannosamine (at 25 degrees Celsius and pH 7.6)

proof_lines: Catalytic efficiency with N-acyl-D-mannosamine as substrate is 136-fold higher than that with D-glucose.

enzyme: N-acylmannosamine kinase


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: UTP

proof_lines: Mutation of His-336 to Asn decreases the Km for ATP to 65 uM and increases the Km for UTP to 45 uM.

substrate: UTP


organism: Trypanosoma brucei brucei

substrate_name: UTP (with 6(U) single-stranded RNA as substrate)

proof_lines: KM is 18-28 mM for UTP (at 27 degrees Celsius and 12 (U) single-stranded RNA as substrate) (PubMed:15304317). kcat is 100 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.0012 min(-1) with UTP and dou


proof_lines: kcat is 0.18 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.04 min(-1) with UTP and double-stranded RNA as substrates (PubMed:19465686).

substrate: UTP (with 6(U) single-stranded RNA as substrate)


proof_lines: kcat is 0.0007 min(-1) with UTP and 6(U) single-stranded RNA as substrates (PubMed:19465686). kcat is 0.002 min(-1) with UTP and double-stranded RNA as substrates (PubMed:19465686). kcat is 0.02 min(-1) with UTP and with RNA with no U in 3'


substrate_name: Unknown

proof_lines: KM is 36-48 uM for UTP (at 27 degrees Celsius and with 12(U) single-stranded RNA as substrate).

substrate: Unknown


enzyme_display_name: protein O-GlcNAc transferase

organism: Arabidopsis thaliana

substrate_name: GDP-beta-L-fucose

enzyme: protein O-GlcNAc transferase

substrate: GDP-beta-L-fucose


organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6)

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


organism: Homo sapiens

substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


enzyme_display_name: tryprostatin B synthase

organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: brevianamide F

enzyme: tryprostatin B synthase

substrate: brevianamide F


enzyme_display_name: brevianamide F prenyltransferase (deoxybrevianamide E-forming)

organism: Aspergillus sp. (strain MF297-2)


enzyme_display_name: linoleate 8R-lipoxygenase

organism: Penicillium oxalicum

substrate_name: palmitoleic acid

source_db: brenda

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

enzyme: linoleate 8R-lipoxygenase

substrate: palmitoleic acid

source: brenda


enzyme_display_name: beta-carotene 15,15'-dioxygenase

organism: Galleria mellonella

substrate_name: alpha-carotene

substrate: alpha-carotene


organism: Gallus gallus

substrate_name: beta-carotene

substrate: beta-carotene


organism: Oryctolagus cuniculus

substrate_name: beta-apo-10'-carotenol + O2

substrate: beta-apo-10'-carotenol + O2


organism: Rattus norvegicus

substrate_name: all-trans-beta-carotene

sequence_source: UniProtKB reviewed accession Q91XT5 (BCDO1_RAT), exact EC 1.13.11.63 and organism Rattus norvegicus lookup

proof_lines:
pH 7.7, 37°C
intestinal enzyme

substrate: all-trans-beta-carotene


organism: Sus scrofa


enzyme_display_name: phenol 2-monooxygenase (NADPH)

organism: Acinetobacter radioresistens

substrate_name: NADH

assay_conditions_summary: cofactor NADH

enzyme: phenol 2-monooxygenase (NADPH)

substrate: NADH


organism: Auxenochlorella pyrenoidosa

substrate_name: phenol

substrate: phenol


organism: Candida albicans


organism: Candida tropicalis

substrate_name: resorcinol

proof_lines:
crude extract
at pH 7.6 and 30°C

substrate: resorcinol


organism: Cutaneotrichosporon cutaneum

proof_lines:
value depends on phenolic substrate
cosubstrate 3-fluorophenol
+ phenol or resorcinol


organism: Ectopseudomonas mendocina


organism: Pseudomonas fluorescens

proof_lines:
strain B PC18
strain F PC17
strain F PC20


organism: Pseudomonas putida

proof_lines:
strain EST1412
strain B PC30
strain B PC16


organism: Stutzerimonas stutzeri

substrate_name: Benzene

assay_conditions_summary: 298.15 K; cofactor NADPH

proof_lines:
25°C, recombinant enzyme
reconstituted enzyme complex
phenol hydrolxylase component P

substrate: Benzene


enzyme_display_name: squalene monooxygenase

organism: Homo sapiens

substrate_name: squalene

sequence_source: UniProtKB reviewed Q14534 (ERG1_HUMAN), cited to PMID 10666321

proof_lines: recombinant enzyme, Km for electron transfer partner NADPH-cytochrone P 450 reductase

enzyme: squalene monooxygenase

substrate: squalene


mutation_signature: recombinant truncated enzyme mutant

ki_unit: mM

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

mutation_type: truncation

proof_lines: recombinant truncated enzyme mutant, pH 7.4, 37°C


sequence_source: UniProtKB reviewed P52020 (ERG1_RAT), cited to PMID 17112472

proof_lines: pH 7.4, 37°C, recombinant His-tagged wild-type enzyme


substrate_name: Reduced acceptor; O2; Squalene

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor FAD

proof_lines: non-competitive, non-time dependent inhibition

substrate: Reduced acceptor; O2; Squalene


enzyme_display_name: vitamin D3 24-hydroxylase

substrate_name: 1alpha,25-dihydroxyvitamin D3

proof_lines: wild type enzyme, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication

enzyme: vitamin D3 24-hydroxylase

substrate: 1alpha,25-dihydroxyvitamin D3


mutation_type: substitution

proof_lines: mutant enzyme T416S, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme T416A, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme T416V, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme I500T, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme T416M, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme I500L, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme I500F, in 100 mM Tris-HCl, pH 7.4, temperature not specified in the publication


substrate_name: O2; H+; Calcidiol; NADPH

proof_lines: pH and temperature not specified in the publication

substrate: O2; H+; Calcidiol; NADPH


enzyme_display_name: NAD(P)H oxidase (H2O2-forming)

organism: Bos taurus

substrate_name: Unknown

substrate: Unknown


organism: Helicobacter pylori

substrate_name: NADPH

proof_lines: at 25°C, pH not specified in the publication

substrate: NADPH


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH

proof_lines: pH 7.4, 30°C, 1.5 mM Ca2+, patients with Graves disease

proof_lines: Ki above 0.03 mM, 0.1 M phosphate buffer, pH 7.4, 37°C


mutation_signature: N-terminal truncated recombinant enzyme N-terminal truncated recombinant enzyme


organism: Trichophyton rubrum


substrate_name: 25-hydroxyvitamin D3

proof_lines: in 0.1 mM Tris-HCl (pH 7.4), temperature not specified in the publication

substrate: 25-hydroxyvitamin D3


assay_conditions_summary: pH 7.3; 310.15 K; cofactor NADPH

proof_lines: subunit p40phox-depleted cytosol in the presence of recombinant wild-type p40phox, pH 7.3, 37°C

proof_lines: subunit p40phox-depleted cytosol in the absencee of recombinant wild-type p40phox, pH 7.3, 37°C


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 5.5; 338.15 K; cofactor NADH


assay_conditions_summary: pH 7.2; 303.15 K; cofactor NADPH


enzyme_display_name: thiosulfate dehydrogenase

organism: Acidiphilium acidophilum

substrate_name: thiosulfate

assay_conditions_summary: pH 7

proof_lines:
at pH 7
at least, at pH 3

enzyme: thiosulfate dehydrogenase

substrate: thiosulfate


organism: Acidithiobacillus ferrooxidans


organism: Allochromatium vinosum

substrate_name: ferricyanide

sequence_source: UniProtKB reviewed accession D3RVD4; EC 1.8.2.2 catalytic activity cites PMID 16995898.

substrate: ferricyanide


enzyme_display_name: 4-hydroxy-2-oxoheptanedioate aldolase

organism: Escherichia coli

proof_lines: The catalytic efficiency measured with 3-deoxy-D-manno-oct-2-ulosonate (KDO) is 37800-fold lower than that with 4-hydroxy-2-ketohexanoate.

enzyme: 4-hydroxy-2-oxoheptanedioate aldolase


enzyme_display_name: arogenate dehydratase

organism: Petunia hybrida

substrate_name: L-arogenate

proof_lines: kcat is 0.194 sec(-1) with L-arogenate as substrate (PubMed:20215586). kcat is 0.012 sec(-1) with prephenate as substrate (PubMed:20215586).

enzyme: arogenate dehydratase

substrate: L-arogenate


proof_lines: kcat is 0.267 sec(-1) with L-arogenate as substrate.


proof_lines: kcat is 1.231 sec(-1) with L-arogenate as substrate (PubMed:20215586). kcat is 0.060 sec(-1) with prephenate as substrate (PubMed:20215586).


organism: Campylobacter jejuni


organism: Pseudomonas aeruginosa


organism: Rhodopila globiformis


organism: Rhodotorula sp.

proof_lines: with native cytochrome c as electron acceptor


organism: Thermithiobacillus tepidarius

proof_lines:
with cytochrome c as electron acceptor
with ferricyanide as electron acceptor


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

organism: Orthopoxvirus vaccinia

substrate_name: S-adenosyl-L-methionine

proof_lines: mutant enzyme K607A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C

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

substrate: S-adenosyl-L-methionine


proof_lines: mutant enzyme F679I, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme K607R, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme F679V, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme F679L, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: mutant enzyme N570D, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


organism: Thiobacillus sp.

proof_lines: sulfite resembles the sulfonate part of thiosulfate and might, therefore, block the active site of the enzyme

proof_lines: it is possible that selenite blocks access to the thiosulfate dehydrogenase or has an inhibiting effect on the respiratory chain itself


organism: Thiobacillus thioparus

proof_lines:
ferricyanide as electron acceptor
cytochrome c as electron acceptor


organism: Aphanothece halophytica

substrate_name: L-homocysteine; glycinebetaine

substrate: L-homocysteine; glycinebetaine


organism: Homo sapiens

substrate_name: S-methyl-L-methionine; betaine; L-homocysteine; DL-homocysteine; L-Asp

proof_lines: IC50 for betaine-homocysteine S-methyltransferase about 0.077 mM, pH 7.5, 37°C


substrate_name: betaine; L-homocysteine

sequence_variant_note: Resolved canonical sequence from UniProt Q93088 reviewed BHMT1 sequence fetched via UniProt REST; R239Q reconstructed after confirming residue 239 is R. and applied mutation signature R239Q to reconstruct the assayed variant sequence.

substrate: betaine; L-homocysteine


substrate_name: L-homocysteine; betaine

sequence_variant_note: Resolved canonical sequence from UniProt Q93088 reviewed BHMT1 sequence fetched via UniProt REST; G199S reconstructed after confirming residue 199 is G. and applied mutation signature G199S to reconstruct the assayed variant sequence.

substrate: L-homocysteine; betaine


proof_lines: mutant enzyme F679H, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C


proof_lines: intact mRNA capping enzyme and isolated methyltransferase domain


organism: Gallus sp.


substrate_name: L-homocysteine

sequence_source: UniProtKB reviewed accession Q93088 (BHMT1_HUMAN), checked by direct UniProt FASTA/API lookup

substrate: L-homocysteine


substrate_name: betaine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q93088 with row-specific P197S substitution reconstructed during review and applied mutation signature P197S to reconstruct the assayed variant sequence.

substrate: betaine


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


organism: Rattus norvegicus

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


organism: Dengue virus

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


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


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


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


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


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


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


substrate_name: tetrahydrofolic acid

proof_lines:
25 mM KCl
150 mM KCl

substrate: tetrahydrofolic acid


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

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

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


organism: Lathyrus oleraceus


organism: Mus musculus


organism: Staphylococcus lugdunensis

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


enzyme_display_name: diacylglycerol O-acyltransferase

organism: Bos taurus

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

enzyme: diacylglycerol O-acyltransferase

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


organism: Brassica napus

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

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

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


organism: Glycine max

proof_lines:
with stearoyl-CoA
with oleoyl-CoA


organism: Helianthus annuus

substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


substrate_name: Unknown


organism: Mycolicibacterium smegmatis


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

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

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


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


substrate_name: UDP-N-azidoacetylglucosamine

substrate: UDP-N-azidoacetylglucosamine


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


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


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


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


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


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


enzyme_display_name: deoxyhypusine synthase

organism: Saccharomyces cerevisiae

substrate_name: spermidine

assay_conditions_summary: cofactor NAD+

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

enzyme: deoxyhypusine synthase

substrate: spermidine


enzyme_display_name: phosphoserine transaminase

organism: Arabidopsis thaliana

enzyme: phosphoserine transaminase


organism: Escherichia coli

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


organism: Ovis aries


organism: Spinacia oleracea

substrate_name: L-glutamate

substrate: L-glutamate


sequence_source: UniProtKB reviewed accession P56558

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


enzyme_display_name: spermidine synthase

organism: Sus scrofa

enzyme: spermidine synthase

substrate: Unknown


organism: Thermotoga maritima

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


organism: Homo sapiens

substrate_name: putrescine

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

substrate: putrescine


proof_lines: pH and temperature not specified in the publication


organism: Rattus norvegicus

substrate_name: NAD+

sequence_source: UniProtKB reviewed accession Q6AY53

substrate: NAD+


enzyme_display_name: aminodeoxychorismate synthase

enzyme: aminodeoxychorismate synthase


substrate_name: L-glutamine

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

substrate: L-glutamine


organism: Stenotrophomonas maltophilia

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

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


enzyme_display_name: cAMP-dependent protein kinase

enzyme: cAMP-dependent protein kinase


substrate_name: ATP; p65

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

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

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

substrate: ATP; p65


organism: Manduca sexta

substrate_name: Kemptide

assay_conditions_summary: pH 7; 295.15 K; cofactor ATP

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

substrate: Kemptide


organism: Mus musculus

substrate_name: RFARKGSLREKNV

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

substrate: RFARKGSLREKNV


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

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


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

assay_conditions_summary: pH 7; cofactor ATP

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

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

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


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

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

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


substrate_name: peptide RRYSV

substrate: peptide RRYSV


organism: Mytilus galloprovincialis

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

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

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

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


enzyme_display_name: dephospho-CoA kinase

substrate_name: ATP; Dephospho-CoA

assay_conditions_summary: cofactor ATP

enzyme: dephospho-CoA kinase

substrate: ATP; Dephospho-CoA


substrate_name: ATP

proof_lines:
cytosolic enzyme
mitochondrial enzyme

substrate: ATP


enzyme_display_name: triokinase

substrate_name: D-Glyceraldehyde; ATP

enzyme: triokinase

substrate: D-Glyceraldehyde; ATP


substrate_name: ATP; D-Glyceraldehyde

assay_conditions_summary: pH 7.5; 297.15 K; cofactor ATP

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

substrate: ATP; D-Glyceraldehyde


enzyme_display_name: N-acetylglucosamine kinase

substrate_name: N-acetyl-D-galactosamine

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

enzyme: N-acetylglucosamine kinase

substrate: N-acetyl-D-galactosamine


organism: Candida albicans

substrate_name: N-acetyl-D-glucosamine

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: N-acetyl-D-glucosamine


organism: Tetradesmus obliquus

substrate_name: L-phosphoserine

substrate: L-phosphoserine


organism: Trichomonas vaginalis

substrate_name: O-phospho-L-serine

substrate: O-phospho-L-serine


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

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

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


substrate_name: chorismate

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

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

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

substrate: chorismate


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

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


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

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


organism: Clostridium acetobutylicum


assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP


substrate_name: Unknown

proof_lines: recombinant mutant S338A catalytic subunit, pH 7.5

substrate: Unknown


proof_lines: recombinant wild-type catalytic subunit, pH 7.5


proof_lines: pH and temperature not specified in the publication


organism: Zea mays

substrate_name: RRASVA

substrate: RRASVA


organism: Columba sp.

substrate_name: dephospho-CoA

assay_conditions_summary: pH 8.2; 310.15 K; cofactor CoA

substrate: dephospho-CoA


organism: Corynebacterium ammoniagenes

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP


enzyme_display_name: carbamate kinase

organism: Enterococcus faecalis

substrate_name: ATP; NH3; CO2

assay_conditions_summary: pH 7.5; 308.15 K; cofactor ATP

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

enzyme: carbamate kinase

substrate: ATP; NH3; CO2


substrate_name: ATP; CO2; NH3

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

substrate: ATP; CO2; NH3


organism: Lentilactobacillus buchneri

substrate_name: Carbamoyl phosphate

assay_conditions_summary: pH 5; 303.15 K; cofactor ADP

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

substrate: Carbamoyl phosphate


organism: Mycoplasma arthritidis

substrate_name: Carbamoyl phosphate; ADP

substrate: Carbamoyl phosphate; ADP


organism: Neurospora crassa

substrate_name: bicarbonate

substrate: bicarbonate


enzyme_display_name: RNA uridylyltransferase

organism: Homo sapiens

substrate_name: UTP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

enzyme: RNA uridylyltransferase

substrate: UTP


organism: Rattus norvegicus

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

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


organism: Streptococcus pyogenes

substrate_name: ATP; N-Acetyl-D-glucosamine

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

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

substrate: ATP; N-Acetyl-D-glucosamine


organism: Sus scrofa

substrate_name: ATP

assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

substrate: ATP


organism: Yarrowia lipolytica

substrate_name: D-mannose

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: D-mannose


enzyme_display_name: N-acylmannosamine kinase

substrate_name: N-acetyl-D-mannosamine

assay_conditions_summary: pH 8.1; 310.15 K; cofactor ATP

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

enzyme: N-acylmannosamine kinase

substrate: N-acetyl-D-mannosamine


organism: Salmonella enterica subsp. enterica serovar Typhimurium

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

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP


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

organism: Actinidia chinensis

substrate_name: Phosphate; GDP-L-galactose

substrate: Phosphate; GDP-L-galactose


organism: Arabidopsis thaliana

substrate_name: GDP-L-galactose; Phosphate

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

substrate: GDP-L-galactose; Phosphate


organism: Brassica rapa


organism: Pisum sativum


organism: Bacillus subtilis

substrate_name: undecaprenyl phosphate

substrate: undecaprenyl phosphate


organism: Escherichia coli

substrate_name: dodecaprenylphosphate

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

substrate: dodecaprenylphosphate


enzyme_display_name: tagatose-bisphosphate aldolase

substrate_name: D-Tagatose 1,6-bisphosphate

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

enzyme: tagatose-bisphosphate aldolase

substrate: D-Tagatose 1,6-bisphosphate


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


source_db: oed

source: oed


kcat_over_km_origin: calculated

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


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


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


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


sequence_source: UniProtKB reviewed entry P0AB74 FASTA/JSON direct lookup


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


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


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


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


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


enzyme_display_name: diaminopimelate decarboxylase

sequence_source: UniProtKB REST direct lookup: Q949X7

enzyme: diaminopimelate decarboxylase


sequence_source: UniProtKB REST direct lookup: Q94A94


organism: Bacillus anthracis

sequence_source: UniProtKB REST direct lookup: A0A6L7HN53


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

sequence_source: UniProtKB REST direct lookup: P00861

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

source_databases_merged: sabio_rk brenda skid


organism: Helicobacter pylori

sequence_source: UniProtKB REST direct lookup: P56129

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

assay_conditions_summary: pH 8

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


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

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


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


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

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


substrate_name: D-Fructose 1,6-bisphosphate

substrate: D-Fructose 1,6-bisphosphate


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


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


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

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


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

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


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

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


organism: Methanocaldococcus jannaschii

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


organism: Mycobacterium tuberculosis

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


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

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

source_databases_merged: brenda skid


organism: Staphylococcus aureus

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


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


organism: Lactococcus lactis subsp. cremoris


enzyme_display_name: DNA nucleotidylexotransferase

organism: Bos taurus

substrate_name: 2bA FAM oligo

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

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

enzyme: DNA nucleotidylexotransferase

substrate: 2bA FAM oligo


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

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


organism: Homo sapiens

substrate_name: dATP

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

substrate: dATP


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

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

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


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

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

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


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

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

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


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


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

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


organism: Escherichia coli (strain K12)

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

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


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

verification_status: corrected

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

status: corrected


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


organism: Vibrio vulnificus

sequence_source: UniProtKB REST lookup for A0A3Q0L347


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

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


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


sequence_source: UniProtKB REST direct lookup: P04053


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


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


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


organism: Thermotoga maritima

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


sequence_source: UniProtKB REST direct lookup: Q9X1K5


organism: Vibrio cholerae serotype O1

sequence_source: UniProtKB REST direct lookup: Q9KVL7

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


sequence_source: UniProtKB REST direct lookup: A0A3Q0L347


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

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


substrate_name: oligonucleotide primers

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

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

substrate: oligonucleotide primers


organism: Sus scrofa


organism: Trypanosoma brucei

substrate_name: RNAn containing a terminal U residue

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

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

substrate: RNAn containing a terminal U residue


substrate_name: UTP

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

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

substrate: UTP


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


organism: Mus musculus

substrate_name: dATP (at 35 degrees Celsius)

substrate: dATP (at 35 degrees Celsius)


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


enzyme_display_name: metallocarboxypeptidase D

organism: Unknown

substrate_name: Dansyl-Pro-Ala-Arg

enzyme: metallocarboxypeptidase D

substrate: Dansyl-Pro-Ala-Arg


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

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

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


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

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

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


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

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

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


organism: Priestia megaterium

substrate_name: UDP-MurNAc-pentapeptide

substrate: UDP-MurNAc-pentapeptide


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

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

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


enzyme_display_name: flavonol 3-sulfotransferase

organism: Flaveria bidentis

substrate_name: quercetin

proof_lines: cosubstrate quercetin, recombinant enzyme

enzyme: flavonol 3-sulfotransferase

substrate: quercetin


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

substrate_name: NAD

assay_conditions_summary: cofactor ADP

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

substrate: NAD


organism: Vibrio cholerae

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


enzyme_display_name: pectinesterase

organism: Solanum betaceum

substrate_name: Pectin

enzyme: pectinesterase

substrate: Pectin


organism: Solanum lycopersicum

substrate_name: n n n n n n H2O; Pectin

substrate: n n n n n n H2O; Pectin


enzyme_display_name: histidinol-phosphatase

organism: Corynebacterium glutamicum

substrate_name: L-histidinol phosphate

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

enzyme: histidinol-phosphatase

substrate: L-histidinol phosphate


organism: Escherichia coli

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

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

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

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


organism: Neurospora crassa


organism: Saccharomyces cerevisiae


organism: Anas platyrhynchos

substrate_name: H2O; Dansyl-Phe-Ala-Arg

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

substrate: H2O; Dansyl-Phe-Ala-Arg


substrate_name: Dansyl-Phe-Ala-Arg

substrate: Dansyl-Phe-Ala-Arg


substrate_name: Dansyl-Phe-Ala-Arg; H2O

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

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

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

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

substrate: Dansyl-Phe-Ala-Arg; H2O


organism: Homo sapiens

substrate_name: dansyl-Phe-Ala-Arg

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

substrate: dansyl-Phe-Ala-Arg


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

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


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


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

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


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


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Thermococcus onnurineus

substrate_name: L-phosphoserine

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

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

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

substrate: L-phosphoserine


organism: Thermus thermophilus


enzyme_display_name: sphingomyelin phosphodiesterase

organism: Bacillus cereus

substrate_name: sphingomyelin

proof_lines: in presence of Mg2+ and sodium deoxycholate

enzyme: sphingomyelin phosphodiesterase

substrate: sphingomyelin


organism: Bos taurus

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


proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas aeruginosa

substrate_name: elongation factor 2

assay_conditions_summary: cofactor NAD+

substrate: elongation factor 2


organism: Vibrio cholerae serotype O1

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

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


organism: Flaveria chlorifolia

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


organism: Dickeya chrysanthemi


substrate_name: Unknown

substrate: Unknown


organism: Kionochaeta sp.


organism: Mus musculus


organism: Plasmodium falciparum


organism: Rasamsonia emersonii


organism: Rattus norvegicus

substrate_name: Sphingomyelin; H2O

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

substrate: Sphingomyelin; H2O


enzyme_display_name: alpha-D-xyloside xylohydrolase

organism: Aspergillus niger

proof_lines: pH 4.8, temperature not specified in the publication

enzyme: alpha-D-xyloside xylohydrolase


substrate_name: NAD+

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

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NAD+; Peptide diphthamide

substrate: NAD+; Peptide diphthamide


organism: Anas platyrhynchos

substrate_name: Dansyl-Phe-Phe-Arg

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

substrate: Dansyl-Phe-Phe-Arg


substrate_name: Dansyl-Pro-Ala-Arg

substrate: Dansyl-Pro-Ala-Arg


organism: Homo sapiens

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


substrate_name: Dansyl-Ala-Arg

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

substrate: Dansyl-Ala-Arg


organism: Aspergillus oryzae

substrate_name: 4-nitrophenyl alpha-D-xylopyranoside

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

substrate: 4-nitrophenyl alpha-D-xylopyranoside


enzyme_display_name: beta-D-fucosidase

organism: Asclepias curassavica

substrate_name: p-nitrophenyl-beta-D-fucoside

enzyme: beta-D-fucosidase

substrate: p-nitrophenyl-beta-D-fucoside


organism: Aspergillus phoenicis


organism: Bifidobacterium breve clb

substrate_name: p-nitrophenyl-beta-D-glucoside

substrate: p-nitrophenyl-beta-D-glucoside


organism: Bos taurus


organism: Dalbergia cochinchinensis


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

substrate_name: NADP+

assay_conditions_summary: pH 7; 301.15 K; cofactor NADP+

substrate: NADP+


organism: Oryctolagus cuniculus

substrate_name: NAD+; H2O

assay_conditions_summary: cofactor NADP+

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

substrate: NAD+; H2O


organism: Pseudomonas putida KB1

substrate_name: thio-NAD+

substrate: thio-NAD+


organism: Saccharomyces cerevisiae


organism: Streptomyces griseus


enzyme_display_name: dipeptidyl-peptidase I

substrate_name: sarcosyl-Phe-ethyl ester

assay_conditions_summary: pH 5

enzyme: dipeptidyl-peptidase I

substrate: sarcosyl-Phe-ethyl ester


organism: Escherichia coli

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


organism: Lactuca sativa


organism: Littorina littorea


organism: Ovis aries aries


organism: Patella vulgata


organism: Turbo cornutus

substrate_name: p-nitrophenyl-beta-D-galactoside

substrate: p-nitrophenyl-beta-D-galactoside


organism: Capra hircus


organism: Homo sapiens

assay_conditions_summary: pH 5.5; 294.15 K; buffer acetate

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


organism: Mus musculus


organism: Rattus norvegicus

substrate_name: glucagon

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

substrate: glucagon


organism: Vigna radiata


enzyme_display_name: carboxypeptidase M

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

enzyme: carboxypeptidase M


enzyme_display_name: beta-aspartyl-peptidase

organism: Cavia porcellus

substrate_name: beta-Asp-Phe

enzyme: beta-aspartyl-peptidase

substrate: beta-Asp-Phe


substrate_name: beta-aspartyl-L-leucine

substrate: beta-aspartyl-L-leucine


enzyme_display_name: endopeptidase La

substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines:
mutant S679W
mutant S679W with S3 peptide

enzyme: endopeptidase La

substrate: ATP


substrate_name: human titin

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

substrate: human titin


substrate_name: bacteriophage lambda N-protein

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

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

substrate: bacteriophage lambda N-protein


organism: Dickeya chrysanthemi

substrate_name: Pectin

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

substrate: Pectin


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


verification_status: verified

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

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

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

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

row_label: Table III, enzyme row PME3937 wild-type

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

status: verified


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


organism: Penicillium oxalicum

substrate_name: citrus pectin

substrate: citrus pectin


organism: Prunus armeniaca

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


organism: Saccharomyces cerevisiae


organism: Salmonella enterica subsp. enterica serovar Typhimurium

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

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


enzyme_display_name: bleomycin hydrolase

organism: Bos taurus

substrate_name: bleomycin A2

enzyme: bleomycin hydrolase

substrate: bleomycin A2


organism: Lactococcus lactis

substrate_name: Met-Ala-Ser

substrate: Met-Ala-Ser


organism: Oryctolagus cuniculus


enzyme_display_name: chymosin

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

enzyme: chymosin


organism: Escherichia coli

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

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


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


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


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


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


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

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


substrate_name: kappa-casein

substrate: kappa-casein


organism: Bubalus bubalis


organism: Callithrix jacchus

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

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

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


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

proof_lines: hydrolysis of the Glu171 variant by wild type chymosin

proof_lines: hydrolysis of the parent peptide by wild type chymosin


proof_lines: hydrolysis of the Glu148 variant by Gln298Leu mutant chymosin

proof_lines: hydrolysis of the parent peptide by Gln298Leu mutant chymosin

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


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

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

proof_lines: hydrolysis of the Glu171 variant by Asp289Met mutant chymosin


organism: Camelus dromedarius

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


organism: Homo sapiens


enzyme_display_name: omega-amidase

organism: Bacillus subtilis

substrate_name: succinamate

enzyme: omega-amidase

substrate: succinamate


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

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


enzyme_display_name: chitin deacetylase

organism: Aspergillus nidulans

substrate_name: glycol chitin

enzyme: chitin deacetylase

substrate: glycol chitin


organism: Colletotrichum lindemuthianum

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


organism: Mortierella sp.

substrate_name: hexa-N-acetylchitohexaose

substrate: hexa-N-acetylchitohexaose


sequence_source: UniProtKB Q06703 reviewed Cda2p entry; PMID 11812231 evidence


organism: Leucobacter triazinivorans

substrate_name: N-isopropylammelide

substrate: N-isopropylammelide


organism: Pseudomonas sp.

substrate_name: N-cyclopropylammelide

sequence_source: UniProtKB O52063 reviewed AtzC entry; PMID 12218024 evidence

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ADP

substrate: N-cyclopropylammelide


substrate_name: Dansyl-Ala-Arg

substrate: Dansyl-Ala-Arg


organism: Anas platyrhynchos

substrate_name: dansyl-Phe-Phe-Arg

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

substrate: dansyl-Phe-Phe-Arg


organism: Anas sp.


substrate_name: Dansyl-Leu-Ala-Arg

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

substrate: Dansyl-Leu-Ala-Arg


enzyme_display_name: (d)CTP diphosphatase

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

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

enzyme: (d)CTP diphosphatase


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

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


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

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


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

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


organism: Synechococcus phage S-PM2

substrate_name: GTP

proof_lines: pH and temperature not specified in the publication

substrate: GTP


enzyme_display_name: signal-recognition-particle GTPase

organism: Acidianus ambivalens

enzyme: signal-recognition-particle GTPase


enzyme_display_name: nucleoside diphosphate phosphatase

organism: Caenorhabditis elegans

substrate_name: UDP

enzyme: nucleoside diphosphate phosphatase

substrate: UDP


organism: Glycine max

substrate_name: ATP

substrate: ATP


organism: Rattus norvegicus

substrate_name: IDP

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

substrate: IDP


organism: Escherichia coli

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

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


substrate_name: dCTP

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

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

substrate: dCTP


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

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


enzyme_display_name: diaminopimelate decarboxylase

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

enzyme: diaminopimelate decarboxylase


organism: Landoltia punctata


organism: Lysinibacillus sphaericus

substrate_name: Unknown

substrate: Unknown


organism: Methanocaldococcus jannaschii


organism: Mycobacterium tuberculosis

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


organism: Mus musculus


substrate_name: 2-Oxoglutaramate; H2O

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

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

substrate: 2-Oxoglutaramate; H2O


organism: Solanum lycopersicum


organism: Thermus aquaticus

substrate_name: hydroxylamine

substrate: hydroxylamine


organism: Absidia orchidis vel coerulea


organism: Amylomyces rouxii

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


organism: Vicia faba


organism: Zea mays


organism: Escherichia coli K-12

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

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

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


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

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


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


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


organism: Streptomyces coelicolor

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


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


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


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


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


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


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

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


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

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


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

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


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

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

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

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

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


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


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

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


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


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

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


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


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


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


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


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


organism: Methylomonas aminofaciens


organism: Canis lupus familiaris


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

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

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


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

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

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


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


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


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


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

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


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


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


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


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


enzyme_display_name: tagatose-bisphosphate aldolase

organism: Klebsiella pneumoniae

substrate_name: D-tagatose 1,6-diphosphate

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

enzyme: tagatose-bisphosphate aldolase

substrate: D-tagatose 1,6-diphosphate


organism: Lactococcus cremoris

substrate_name: tagatose 1,6-diphosphate

substrate: tagatose 1,6-diphosphate


organism: Lactococcus lactis subsp. lactis

substrate_name: D-Tagatose 1,6-bisphosphate

substrate: D-Tagatose 1,6-bisphosphate


organism: Staphylococcus aureus


organism: Streptococcus pyogenes

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

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


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

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


enzyme_display_name: 4-hydroxy-2-oxoheptanedioate aldolase

organism: Escherichia coli

substrate_name: DL-glyceraldehyde

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

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

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

enzyme: 4-hydroxy-2-oxoheptanedioate aldolase

substrate: DL-glyceraldehyde


organism: Saccharolobus solfataricus


enzyme_display_name: arogenate dehydratase

organism: Brevundimonas diminuta

substrate_name: L-arogenate

enzyme: arogenate dehydratase

substrate: L-arogenate


organism: Nicotiana sylvestris

substrate_name: L-Arogenate

substrate: L-Arogenate


organism: Pantoea agglomerans

substrate_name: Prephenate

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

substrate: Prephenate


organism: Pseudomonas aeruginosa


organism: Sorghum bicolor

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


organism: Spinacia oleracea


enzyme_display_name: cellobiose phosphorylase

organism: Cellulomonas uda

substrate_name: cellobiose

source_db: skid

source_license: CC BY-NC-ND 4.0

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

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

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

enzyme: cellobiose phosphorylase

substrate: cellobiose

source: skid


enzyme_display_name: hexokinase

organism: Homo sapiens

substrate_name: D-glucose

sequence_source: UniProtKB:P19367 direct REST lookup

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

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

enzyme: hexokinase

substrate: D-glucose


sequence_source: UniProtKB:P35557 direct REST lookup

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

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


organism: Kluyveromyces lactis

sequence_source: UniProtKB:P33284 direct REST lookup

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P04806 direct REST lookup


organism: Sulfurisphaera tokodaii

sequence_source: UniProtKB:Q96Y14 direct REST lookup

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ATP


enzyme_display_name: hydroperoxide dehydratase

organism: Solanum lycopersicum

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

enzyme: hydroperoxide dehydratase


organism: Oryza sativa

substrate_name: (9S)-hydroperoxyoctadecatrienoic acid

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

substrate: (9S)-hydroperoxyoctadecatrienoic acid


organism: Solanum melongena

substrate_name: linoleate hydroperoxide

substrate: linoleate hydroperoxide


organism: Arabidopsis thaliana

sequence_source: UniProtKB Q96242 FASTA direct check


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


organism: Capsicum annuum

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


organism: Cucumis sativus

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


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


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


organism: Glycine max

sequence_source: UniProtKB REST direct accession check for M4WFN0


organism: Medicago truncatula

sequence_source: UniProtKB REST direct accession check for Q7X9B3


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

proof_lines: pH 7.0, 23°C, recombinant mutant L97F/TCFNSF enzyme


organism: Olea europaea

mutation_signature: recombinant truncated enzyme

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


sequence_source: UniProtKB REST direct accession check for G8XQN2

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

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


mutation_signature: recombinant truncated enzyme / recombinant truncated enzyme

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

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


organism: Physcomitrium patens

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

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

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


organism: Solanum tuberosum

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


enzyme_display_name: carbonic anhydrase

organism: Stylophora pistillata

sequence_source: UniProtKB:B5SU02 direct REST lookup

assay_conditions_summary: pH 7.5; 293.15 K; buffer HEPES

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

enzyme: carbonic anhydrase


assay_conditions_summary: pH 6.28; buffer context

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

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

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


organism: Methanosarcina thermophila

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

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

smiles: O=C=O

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

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

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

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


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

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

assay_conditions_summary: pH 7.5; 298.15 K; buffer source context

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


organism: Methanothermobacter thermautotrophicus

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

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


assay_conditions_summary: pH 8.5; 298.15 K; buffer mapping

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


enzyme_display_name: glucosyl-3-phosphoglycerate synthase

organism: Mycobacterium tuberculosis

substrate_name: UDP-glucose

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

enzyme: glucosyl-3-phosphoglycerate synthase

substrate: UDP-glucose


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


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


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


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


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

substrate_name: 3-PGA (at 30 degrees Celsius)

substrate: 3-PGA (at 30 degrees Celsius)


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

substrate_name: 3-PGA (at 37 degrees Celsius)

assay_conditions_summary: cofactor ADP

substrate: 3-PGA (at 37 degrees Celsius)


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


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

substrate_name: 3-PGA (at 70 degrees Celsius)

substrate: 3-PGA (at 70 degrees Celsius)


organism: Petrotoga mobilis (strain DSM 10674 / SJ95)

substrate_name: 3-PGA (at 60 degrees Celsius)

substrate: 3-PGA (at 60 degrees Celsius)


organism: Mycobacterium tuberculosis variant bovis

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP


organism: Persephonella marina

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


organism: Petrotoga mobilis

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


organism: Prochlorococcus marinus

substrate_name: ADP-glucose

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

substrate: ADP-glucose


organism: Rhodopirellula baltica

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP


organism: Synechococcus sp.


organism: Methanococcoides burtonii

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


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


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


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


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


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


organism: Mycolicibacterium smegmatis


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

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

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

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

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


organism: Phytopseudomonas straminea


organism: Comamonas testosteroni


organism: Sphingomonas paucimobilis

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


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


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


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


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


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

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


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


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


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


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


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


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


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


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


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


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


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


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


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

enzyme_name_source: UniProtKB:O87170 direct lookup

sequence_source: UniProtKB:O87170 direct lookup

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

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


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


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


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


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


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


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


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


enzyme_display_name: Nitroalkane oxidase

organism: Fusarium oxysporum

substrate_name: nitroethane

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

enzyme: Nitroalkane oxidase

substrate: nitroethane


organism: Podospora anserina

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

assay_conditions_summary: pH 8; 303.15 K; cofactor FAD

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

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

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

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


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

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

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

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