substrate_name: paromamine

proof_lines: 37°C, pH not specified in the publication, cosubstrate: UDP-alpha-D-kanosamine

proof_lines: 37°C, pH not specified in the publication, cosubstrate: UDP-alpha-D-glucose

substrate: paromamine


enzyme_display_name: Trehalose-6-phosphate synthase

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

substrate_name: UDP-Glc (in the presence of polyanion)

source_db: uniprot

verification_status: unverified

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

data_origin: experimental

enzyme: Trehalose-6-phosphate synthase

substrate: UDP-Glc (in the presence of polyanion)

status: unverified

source: uniprot


enzyme_display_name: UniProt K7NBW3

organism: Siraitia grosvenorii

substrate_name: UDP-alpha-D-glucose

source_db: skid

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

sequence_source: multiple

source_databases_merged: skid uniprot

enzyme: UniProt K7NBW3

substrate: UDP-alpha-D-glucose

source: skid


enzyme_display_name: mogroside IE synthase

substrate_name: mogrol

source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T79Y/L48M/R28H/L109I to reconstruct the assayed variant sequence.

enzyme: mogroside IE synthase

substrate: mogrol

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T79Y/L48M/R28H/L109I/S15A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T79Y/L48M/R28H/L109I/S15A/M76L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T79Y/L48M/R28H/L109I/S15A/M76L/H47R to reconstruct the assayed variant sequence.


organism: Vitis amurensis

substrate_name: malvidin 3-O-beta-D-glucoside

source_db: brenda

assay_conditions_summary: pH 7

substrate: malvidin 3-O-beta-D-glucoside

source: brenda


enzyme_display_name: beta-1,2-mannobiose phosphorylase

organism: Listeria innocua

substrate_name: D-fructose

proof_lines: kcat is 31 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 3.9 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 12 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction). kca

source_databases_merged: brenda skid uniprot

enzyme: beta-1,2-mannobiose phosphorylase

substrate: D-fructose


substrate_name: D-mannopyranose

substrate: D-mannopyranose


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


substrate_name: phosphate

proof_lines: 30°C, pH 7, cosubstrate: beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose

proof_lines: 30°C, pH 7, cosubstrate: beta-D-mannopyranosyl-(1->2)-D-mannopyranose

source_databases_merged: brenda skid

substrate: phosphate


enzyme_display_name: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)

organism: Dianthus caryophyllus

verification_status: verified

assay_conditions_summary: pH 5; 303.15 K; buffer 0.1 M citrate

column_label: Results prose page 3380, native Dc AA5GT clause of the kinetic parameter sentence: 'kcat for VG = 0.01 s^-1' and 'Km for VG = 46.5 uM'; the same clause also prints kcat for Cy3G = 0.06 s^-1 and Km for Cy3G = 13.0 uM, which belong to the acceptor axis; no kcat/Km is printed for native Dc AA5GT with VG.

normalized_value_unit_evidence: kcat: printed value 0.01 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.01 s^(-1). Km: printed value 46.5 uM; 46.5 / 1000 = 0.0465 mM. kcat/Km: no printed value for this pair, so the paper value 0.21505376344086022 s^(-1)*mM^(-1) is the quotient 0.01 / 0.0465 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Results prose, page 3380, native Dc AA5GT clause: kcat for VG = 0.01 s^-1; Km for VG = 46.5 uM; the article text prints no kcat/Km for native Dc AA5GT with VG.

row_label: page-3380 kinetic parameter sentence, native Dc AA5GT clause, VG donor values

table_label: Results prose, page 3380, section 'Kinetic Properties and Substrate Preferences of Acceptor and Donor Molecules of Dc AA5GT and Dg AA7GT' (The Plant Cell 2010, 22:3374-3389); the article has no kinetic table, the sentence cites the online-only Supplemental Table 3

status: verified


substrate_name: cyanidin 3-O-beta-D-glucoside

assay_conditions_summary: pH 5

proof_lines:
pH 5.0, 30°C, native enzyme
pH 5.0, 30°C, recombinant enzyme

enzyme: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)

substrate: cyanidin 3-O-beta-D-glucoside


enzyme_display_name: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)

organism: Delphinium grandiflorum


enzyme: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)


enzyme_display_name: 1,2-beta-oligomannan phosphorylase

organism: Thermoanaerobacter sp.

substrate_name: alpha-D-mannose

assay_conditions_summary: pH 5; buffer pH 5

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / acceptor D-Mannose; columns kcat s^-1 1.9; Km mM 0.41; printed kcat/Km 4.6; export-normalized kcat/Km 4.63414634146341

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.41 normalized_unit=mM; kcat/Km normalized_value=4.63414634146341 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; Km raw_value=0.41 raw_unit=mM; printed kcat/Km=4.6 s^-1 mM^-1

row_label: Teth514_1788 / acceptor D-Mannose

source_databases_merged: brenda uniprot

enzyme: 1,2-beta-oligomannan phosphorylase

substrate: alpha-D-mannose


column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / acceptor D-Fructose; columns kcat s^-1 2; Km mM 0.2; printed kcat/Km 10; export-normalized kcat/Km 10

normalized_value_unit_evidence: kcat normalized_value=2 normalized_unit=s^-1; Km normalized_value=0.2 normalized_unit=mM; kcat/Km normalized_value=10 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=2.0 raw_unit=s^-1; Km raw_value=0.20 raw_unit=mM; printed kcat/Km=10 s^-1 mM^-1

row_label: Teth514_1788 / acceptor D-Fructose


column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / donor a-Man1P; columns kcat s^-1 22; Km mM 1.4; printed kcat/Km 16; export-normalized kcat/Km 15.7142857142857

normalized_value_unit_evidence: kcat normalized_value=22 normalized_unit=s^-1; Km normalized_value=1.4 normalized_unit=mM; kcat/Km normalized_value=15.7142857142857 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=22 raw_unit=s^-1; Km raw_value=1.4 raw_unit=mM; printed kcat/Km=16 s^-1 mM^-1

row_label: Teth514_1788 / donor a-Man1P


proof_lines: cosubstrate: [(1->2)-beta-D-mannosyl]4, pH 5.0, 30°C, phosphorolytic reaction

proof_lines: cosubstrate: [(1->2)-beta-D-mannosyl]3, pH 5.0, 30°C, phosphorolytic reaction

proof_lines: cosubstrate: [(1->2)-beta-D-mannosyl]2, pH 5.0, 30°C, phosphorolytic reaction


enzyme_display_name: phlorizin synthase

organism: Malus domestica

substrate_name: phloretin

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

enzyme: phlorizin synthase

substrate: phloretin


enzyme_display_name: glucosylglycerate phosphorylase

organism: Xylanimonas protaetiae

substrate_name: D-glycerate

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

mutation_type: substitution

proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme H344A

enzyme: glucosylglycerate phosphorylase

substrate: D-glycerate


proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342D


proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme Q345A


proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme P343A


proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, mutant enzyme L342A


substrate_name: L-Glycerate

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

proof_lines: pH 7.0, 30°C, with 30 mM alpha-D-glucose 1-phosphate as cosubstrate, wild-type enzyme

substrate: L-Glycerate


substrate_name: sucrose

substrate: sucrose


substrate_name: fructose

substrate: fructose


enzyme_display_name: acylphloroglucinol glucosyltransferase

organism: Fragaria x ananassa

proof_lines:
pH 7.0, 30°C, allelic protein UGT71K3b
pH 7.0, 30°C, allelic protein UGT71K3a

enzyme: acylphloroglucinol glucosyltransferase


proof_lines:
pH 7.0, 30°C, allelic protein UGT71K3b
pH 7.0, 30°C, allelic protein UGT71K3a
pH 7.0, 30°C, UGT71K3a


enzyme_display_name: Beta-1,2-mannobiose phosphorylase

organism: Thermoanaerobacter sp. (strain X514)

substrate_name: D-mannose (for the synthetic reaction)

assay_conditions_summary: pH 5.5; buffer pH 5

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1789 / acceptor D-Mannose; columns Km mM 0.46

raw_value_unit_evidence: Km raw_value=0.46 raw_unit=mM for acceptor D-Mannose; paper row also reports kcat 10 s^-1 and kcat/Km 22 but the export row is Km-only.

row_label: Teth514_1789 / acceptor D-Mannose

enzyme: Beta-1,2-mannobiose phosphorylase

substrate: D-mannose (for the synthetic reaction)


substrate_name: D-fructose (for the synthetic reaction)

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1789 / acceptor D-Fructose; columns Km mM 0.69

raw_value_unit_evidence: Km raw_value=0.69 raw_unit=mM for acceptor D-Fructose; paper row also reports kcat 11 s^-1 and kcat/Km 16 but the export row is Km-only.

row_label: Teth514_1789 / acceptor D-Fructose

substrate: D-fructose (for the synthetic reaction)


substrate_name: alpha-D-mannose 1-phosphate (for the synthetic reaction)

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1789 / donor a-Man1P; columns Km mM 2.1

raw_value_unit_evidence: Km raw_value=2.1 raw_unit=mM for donor a-Man1P; paper row also reports kcat 12 s^-1 and kcat/Km 5.7 but the export row is Km-only.

row_label: Teth514_1789 / donor a-Man1P


organism: Allomeiothermus silvanus

assay_conditions_summary: pH 6

proof_lines: kcat is 0.83 sec(-1) towards 2-O-(alpha-D-glucopyranosyl)-D-glycerate for the phosphorolytic direction (at pH 6.0 and 42 degrees Celsius). kcat is 0.98 sec(-1) towards phosphate for the phosphorolytic direction (at pH 6.0 and 42 degrees Cel


enzyme_display_name: oleanolate 3-O-glucosyltransferase

organism: Barbarea vulgaris

substrate_name: glycyrrhetinic acid

enzyme: oleanolate 3-O-glucosyltransferase

substrate: glycyrrhetinic acid


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


enzyme_display_name: alpha-maltose-1-phosphate synthase

organism: Mycobacterium tuberculosis

substrate_name: ADP-alpha-D-glucose

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

assay_conditions_summary: pH 7; cofactor ADP

proof_lines: with 4.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C

proof_lines: with 2.5 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C

proof_lines: with 0.25 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C

enzyme: alpha-maltose-1-phosphate synthase

substrate: ADP-alpha-D-glucose


proof_lines: with 0.1 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C

proof_lines: with 4.0 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C

proof_lines: with 0.5 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C


organism: Leishmania major

substrate_name: UDP-alpha-D-glucopyranose

km_display: Not reported

substrate: UDP-alpha-D-glucopyranose


substrate_name: UDP-alpha-D-galactopyranose

substrate: UDP-alpha-D-galactopyranose


substrate_name: UDP-alpha-D-galactofuranose

substrate: UDP-alpha-D-galactofuranose


substrate_name: GDP-alpha-D-mannopyranose

substrate: GDP-alpha-D-mannopyranose


substrate_name: GDP-alpha-D-glucopyranose

substrate: GDP-alpha-D-glucopyranose


organism: Bacteroides thetaiotaomicron


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


substrate_name: N,N'-diacetylchitobiose

substrate: N,N'-diacetylchitobiose


organism: Unknown

substrate_name: Unknown

assay_conditions_summary: pH 5.5; cofactor ADP

substrate: Unknown


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

proof_lines:
37°C, pH 5.5, cosubstrate: UDP-glucose
37°C, pH 5.5, cosubstrate: ADP-glucose
37°C, pH 5.5, cosubstrate: TDP-glucose


enzyme_display_name: L-demethylnoviosyl transferase

organism: Streptomyces niveus

substrate_name: novobiocic acid

proof_lines: kcat is 313 min(-1) with novobiocic acid as substrate.

enzyme: L-demethylnoviosyl transferase

substrate: novobiocic acid


enzyme_display_name: Glucosylglycerate phosphorylase

organism: Escherichia coli (strain K12)

substrate_name: 2-O-(alpha-D-glucopyranosyl)-D-glycerate (at pH 6.5 and 30 degrees Celsius)

column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjM / alpha-(1,2)-D-glucose-D-glycerate; fixed substrate phosphate (20 mM); columns Km column raw 0.069 +/- 0.002 normalized 0.069 mM; export values for required/current metrics match these normalized values.

raw_value_unit_evidence: Km raw_value=0.069 +/- 0.002 raw_unit=mM

enzyme: Glucosylglycerate phosphorylase


substrate_name: phosphate (at pH 6.5 and 30 degrees Celsius)

column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjM / phosphate; fixed substrate alpha-(1,2)-D-glucose-D-glycerate (1 mM); columns Km column raw 2.2 +/- 0.5 normalized 2.2 mM; export values for required/current metrics match these normalized values.

raw_value_unit_evidence: Km raw_value=2.2 +/- 0.5 raw_unit=mM


substrate_name: alpha-D-glucose 1-phosphate (at pH 6.5 and 30 degrees Celsius)

column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjM / alpha-D-glucose-1-P; fixed substrate D-glycerate (4 mM); columns Km column raw 9.4 +/- 1.4 normalized 9.4 mM; export values for required/current metrics match these normalized values.

raw_value_unit_evidence: Km raw_value=9.4 +/- 1.4 raw_unit=mM


sequence_variant_note: Mutation signature T71K could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
pH 7, 30°C, allelic protein UGT71K3b
pH 7, 30°C, allelic protein UGT71K3a


substrate_name: quercetin

proof_lines:
pH 7, 30°C, allelic protein UGT71K3a
pH 7, 30°C, allelic protein UGT71K3b

substrate: quercetin


substrate_name: pelargonidin

substrate: pelargonidin


substrate_name: kaempferol

substrate: kaempferol


substrate_name: acetylphloroglucinol

substrate: acetylphloroglucinol


organism: Escherichia coli

substrate_name: GDP-L-fucose

assay_conditions_summary: pH 8

proof_lines: kcat is 8.8 min(-1) with GDP-colitose as substrate. kcat is 12 min(-1) with GDP-L-fucose as substrate. kcat is 5.2 min(-1) with beta-Gal-(1->3)-GlcNAc as substrate.

substrate: GDP-L-fucose


enzyme_display_name: glucosylgalactose phosphorylase

organism: Paenibacillus polymyxa

enzyme: glucosylgalactose phosphorylase


substrate_name: phosphate

substrate: phosphate


substrate_name: D-galactopyranose

substrate: D-galactopyranose


substrate_name: alpha-D-glucopyranose 1-phosphate

substrate: alpha-D-glucopyranose 1-phosphate


substrate_name: L-arabinose

substrate: L-arabinose


enzyme_display_name: sterol 27-beta-glucosyltransferase

organism: Withania somnifera

enzyme: sterol 27-beta-glucosyltransferase


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: estradiol

substrate: estradiol


substrate_name: withanolide A

substrate: withanolide A


substrate_name: testosterone

substrate: testosterone


organism: Linum usitatissimum

substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


proof_lines: kcat is 1.9 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 2.0 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 25 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction).


enzyme_display_name: NDP-glycosyltransferase

organism: Bacillus subtilis

substrate_name: genistein

verification_status: corrected

column_label: Table 1; row Genistein (4); columns Km, kcat, and kcat/Km; raw cells 22.6 +/- 3.1 uM, 1.6 +/- 0.1 s^-1, and 7.2 x 10^4 s^-1 M^-1.

row_label: Genistein (4)

table_label: Table 1: Kinetic parameters of Bs-YjiC towards apigenin (3) and genistein (4)

enzyme: NDP-glycosyltransferase

substrate: genistein

status: corrected


substrate_name: apigenin

column_label: Table 1; row Apigenin (3); columns Km, kcat, and kcat/Km; raw cells 19.4 +/- 2.6 uM, 1.9 +/- 0.1 s^-1, and 9.8 x 10^4 s^-1 M^-1.

row_label: Apigenin (3)

substrate: apigenin


enzyme_display_name: solabiose phosphorylase

organism: Paenibacillus borealis

substrate_name: D-galactose

proof_lines: kcat is 9.14 sec(-1) for the phosphorolysis of solabiose. kcat is 14.5 sec(-1) for the synthesis of solabiose.

enzyme: solabiose phosphorylase

substrate: D-galactose


substrate_name: solabiose

column_label: Prose reports phosphorolysis kcat and KmB where B is solabiose

row_label: Phosphorolysis of solabiose; B = solabiose

table_label: PMID 34997180 PMC8741936 section Enzymatic characteristics of PBOR_28850

substrate: solabiose


substrate_name: alpha-D-glucose 1-phosphate

column_label: Prose reports synthesis kcat and KmA where A is alpha-Glc1P

row_label: Synthesis of solabiose; A = alpha-Glc1P

substrate: alpha-D-glucose 1-phosphate


column_label: Prose reports phosphorolysis KmA 1.53 +/- 0.05 mM where A is inorganic phosphate

normalized_value_unit_evidence: 1.53 mM phosphate Km

row_label: Phosphorolysis of solabiose; A = inorganic phosphate


organism: Vigna angularis

proof_lines: enzyme hyperactivated with 3 mM benzalkonium chloride, at pH 7.0 and 30°C


organism: Limosilactobacillus fermentum

substrate_name: amylose

substrate: amylose


enzyme_display_name: Galactofuranosyltransferase GlfT2

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: UDP-Galf

proof_lines: kcat is 430 min(-1) for galtactose transfer on beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl.

enzyme: Galactofuranosyltransferase GlfT2

substrate: UDP-Galf


organism: Allomeiothermus silvanus (strain ATCC 700542 / DSM 9946 / NBRC 106475 / NCIMB 13440 / VI-R2)

substrate_name: alpha-D-glucose 1-phosphate (at pH 6.5 and 42 degrees Celsius)


substrate_name: D-glycerate (at pH 6.5 and 30 degrees Celsius)

proof_lines: kcat is 2.2 sec(-1) for phosphorolysis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate, kcat is 325 sec(-1) for glyceration of alpha-D-glucose 1-phosphate.


enzyme_display_name: Alpha-maltose-1-phosphate synthase

substrate_name: ADP-glucose (with 4 mM of G1P)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature G1P with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 97.9 sec(-1) for G1P as substrate (with 0.5 mM of ADP-glucose). kcat is 80.6 sec(-1) for G1P as substrate (with 4 mM of ADP-glucose). kcat is 39 sec(-1) for G1P as substrate (with 0.1 mM of ADP-glucose). kcat is 29.2 sec(-1) for ADP

enzyme: Alpha-maltose-1-phosphate synthase

substrate: ADP-glucose (with 4 mM of G1P)


substrate_name: G1P (with 4 mM of ADP-glucose)

substrate: G1P (with 4 mM of ADP-glucose)


enzyme_display_name: Galactofuranosyltransferase GlfT1

substrate_name: O-decenyl beta-D-Galf(1->6)-beta-D-Galf (at 37 degrees Celsius)

enzyme: Galactofuranosyltransferase GlfT1


organism: Perilla frutescens

substrate_name: UDPglucose; Cyanidin 3-O-glucoside

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

substrate: UDPglucose; Cyanidin 3-O-glucoside


organism: Streptomyces kanamyceticus

substrate_name: Paromamine; UDP-kanosamine

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

substrate: Paromamine; UDP-kanosamine


organism: Acholeplasma laidlawii

substrate_name: UDP-D-glucose; sn-1,2-Dioleoylglycerol

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

substrate: UDP-D-glucose; sn-1,2-Dioleoylglycerol


organism: Bifidobacterium adolescentis


substrate_name: Phosphate; Glucosylglycerate

substrate: Phosphate; Glucosylglycerate


enzyme_display_name: UniProt Q92DF6

organism: Listeria innocua

proof_lines: kcat is 31 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 3.9 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 12 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction). kca

enzyme: UniProt Q92DF6


organism: Thermoanaerobacter sp. (strain X514)

substrate_name: beta-1,2-Man2 (for the synthetic reaction)

proof_lines: kcat is 10 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 11 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 7.0 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction). kca


enzyme_display_name: 1,2-beta-oligomannan phosphorylase

organism: Thermoanaerobacter sp.

proof_lines: kcat is 1.9 sec(-1) with D-mannose as substrate (for the synthetic reaction). kcat is 2.0 sec(-1) with D-fructose as substrate (for the synthetic reaction). kcat is 25 sec(-1) with beta-1,2-Man2 as substrate (for the synthetic reaction). kc

enzyme: 1,2-beta-oligomannan phosphorylase


organism: Escherichia coli

substrate_name: GDP-colitose

substrate: GDP-colitose


substrate_name: alpha-glucan

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature G1P with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

substrate: alpha-glucan


enzyme_display_name: Protein O-glucosyltransferase 1

organism: Homo sapiens

substrate_name: Unknown

enzyme: Protein O-glucosyltransferase 1

substrate: Unknown


enzyme_display_name: NDP-glycosyltransferase YjiC

organism: Bacillus subtilis (strain 168)

substrate_name: 2-chloro-4-nitrophenyl glycoside

proof_lines: kcat is 1.9 sec(-1) with apigenin as substrate. kcat is 1.6 sec(-1) with genistein as substrate (PubMed:28315700). kcat is 164 min(-1) with 2-chloro-4-nitrophenyl glycoside as substrate (PubMed:33152360).

enzyme: NDP-glycosyltransferase YjiC

substrate: 2-chloro-4-nitrophenyl glycoside


enzyme_display_name: glucosylglycerate phosphorylase

organism: Meiothermus silvanus

substrate_name: Glucosylglycerate; Phosphate

enzyme: glucosylglycerate phosphorylase

substrate: Glucosylglycerate; Phosphate


organism: Spirochaeta thermophila


organism: Streptococcus mutans


organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)

substrate_name: poly(RboP)

substrate: poly(RboP)


enzyme_display_name: UDP-glycosyltransferase 71K3

organism: Fragaria ananassa

enzyme: UDP-glycosyltransferase 71K3


organism: Mycobacterium tuberculosis


organism: Gentiana triflora


enzyme_display_name: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)

organism: Dianthus caryophyllus

proof_lines: kcat is 0.06 sec(-1) with cyanidin 3-glucopyranoside (with native enzyme at pH 5.0 and 30 degrees Celsius). kcat is 0.01 sec(-1) with 1-O-beta-D-vanillyl-glucose (with native enzyme at pH 5.0 and 30 degrees Celsius). kcat is 0.07 sec(-1) wi


enzyme_display_name: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)

organism: Delphinium grandiflorum

proof_lines: kcat is 0.17 sec(-1) with cyanidin 3-glucopyranoside (at pH 5.0 and 30 degrees Celsius). kcat is 0.10 sec(-1) with 1-O-beta-D-vanillyl-glucose (at pH 5.0 and 30 degrees Celsius).


enzyme_display_name: L-noviosyl transferase

organism: Streptomyces niveus

substrate_name: Novobiocic acid; dTDP-L-noviose

enzyme: L-noviosyl transferase

substrate: Novobiocic acid; dTDP-L-noviose


organism: Acholeplasma laidlawii


enzyme: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)


substrate_name: Cyanidin 3,7-di-O-beta-D-glucoside

substrate: Cyanidin 3,7-di-O-beta-D-glucoside


substrate_name: Cyanidin 3-O-beta-D-glucoside

assay_conditions_summary: pH 6; 303.15 K; buffer 0.1 M citrate

column_label: Results prose page 3380, Dg AA7GT clause of the kinetic parameter sentence: 'kcat for Cy3G = 0.17 s^-1' and 'Km for Cy3G = 22.9 uM'; Results prose page 3381, recombinant AA7GT sentence: '7-O-glucosyltransferase activity for Cy3G (kcat/Km = 7.3 x 10^3)', in the s^-1 M^-1 unit the article states for kcat/Km on page 3380.

normalized_value_unit_evidence: kcat: printed value 0.17 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.17 s^(-1). Km: printed value 22.9 uM; 22.9 / 1000 = 0.0229 mM. kcat/Km: printed value 7.3 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7300 / 1000 = 7.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Results prose, page 3380, Dg AA7GT clause: kcat for Cy3G = 0.17 s^-1; Km for Cy3G = 22.9 uM. Results prose, page 3381, recombinant AA7GT sentence: printed kcat/Km for Cy3G = 7.3 x 10^3 s^-1 M^-1.

row_label: page-3380 kinetic parameter sentence, Dg AA7GT clause, Cy3G acceptor values; page-3381 recombinant AA7GT efficiency sentence, Cy3G value

table_label: Results prose, pages 3380 and 3381, section 'Kinetic Properties and Substrate Preferences of Acceptor and Donor Molecules of Dc AA5GT and Dg AA7GT' (The Plant Cell 2010, 22:3374-3389); the article has no kinetic table, the sentences cite the online-only Supplemental Table 3

substrate: Cyanidin 3-O-beta-D-glucoside


substrate_name: Cyanin

substrate: Cyanin


enzyme_display_name: beta-1,2-mannobiose phosphorylase

organism: Listeria innocua

column_label: Table 2; beta-1,2-Man2 row; kcat, KmA, kcat/KmA columns.

normalized_value_unit_evidence: Already in export units: kcat 35 s^-1; KmA 0.44 mM; kcat/KmA 79 s^-1 mM^-1. Export kcat/Km is 79.54545454545455, so not exact.

row_label: Table 2 beta-1,2-Man2 row

table_label: Tsuda et al. 2015, FEBS Letters, Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua; kinetic table evidence

enzyme: beta-1,2-mannobiose phosphorylase


column_label: Table 2; beta-1,2-Man3 row; kcat, KmA, kcat/KmA columns.

normalized_value_unit_evidence: Already in export units: kcat 12 s^-1; KmA 4.1 mM; kcat/KmA 3.0 s^-1 mM^-1. Export kcat/Km is 2.9268292682926833, so not exact.

row_label: Table 2 beta-1,2-Man3 row


substrate_name: alpha-D-mannose 1-phosphate

column_label: Table 1; alpha-Man1P donor row; kcat, Km, kcat/Km columns.

normalized_value_unit_evidence: Already in export units: kcat 33 s^-1; Km 3.1 mM; kcat/Km 11 s^-1 mM^-1. Export kcat/Km is 10.64516129032258, so not exact.

row_label: Table 1 alpha-Man1P donor row

substrate: alpha-D-mannose 1-phosphate


substrate_name: D-fructose

column_label: Table 1; d-Fructose acceptor row; kcat, Km, kcat/Km columns.

normalized_value_unit_evidence: Already in export units: kcat 3.9 s^-1; Km 1.5 mM; kcat/Km 2.7 s^-1 mM^-1. Export kcat/Km is 2.6, so not exact.

row_label: Table 1 d-Fructose acceptor row

substrate: D-fructose


substrate_name: D-mannopyranose

column_label: Table 1; d-Mannose acceptor row; kcat, Km, kcat/Km columns.

normalized_value_unit_evidence: Already in export units: kcat 31 s^-1; Km 2.1 mM; kcat/Km 15 s^-1 mM^-1. Export kcat/Km is 14.761904761904761, so not exact.

row_label: Table 1 d-Mannose acceptor row

substrate: D-mannopyranose


enzyme_display_name: phlorizin synthase

organism: Malus domestica

substrate_name: kaempferol

column_label: Table 4; row UDPG/Kaempferol - acceptor Kaempferol; Acceptors column Km (uM) raw value 2.09; Acceptors column kcat (s^-1) raw value 5.65; Acceptors column kcat/Km (s^-1*uM^-1) raw value 2.7

normalized_value_unit_evidence: kcat normalized_value=5.65 normalized_unit=s^-1; Km normalized_value=0.00209 normalized_unit=mM; kcat/Km normalized_value=2700 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=5.65 raw_unit=s^-1; Km raw_value=2.09 raw_unit=uM; kcat/Km raw_value=2.7 raw_unit=s^-1*uM^-1

row_label: UDPG/Kaempferol - acceptor Kaempferol

table_label: Table 4. Kinetic parameters of Md P2GT for accepted donor and acceptor combinations

enzyme: phlorizin synthase

substrate: kaempferol


substrate_name: luteolin

column_label: Table 4; row UDPG/Luteolin - acceptor Luteolin; Acceptors column Km (uM) raw value 2.89; Acceptors column kcat (s^-1) raw value 3.24; Acceptors column kcat/Km (s^-1*uM^-1) raw value 1.12

normalized_value_unit_evidence: kcat normalized_value=3.24 normalized_unit=s^-1; Km normalized_value=0.00289 normalized_unit=mM; kcat/Km normalized_value=1120 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=3.24 raw_unit=s^-1; Km raw_value=2.89 raw_unit=uM; kcat/Km raw_value=1.12 raw_unit=s^-1*uM^-1

row_label: UDPG/Luteolin - acceptor Luteolin

substrate: luteolin


substrate_name: isoliquiritigenin

column_label: Table 4; row UDPG/Isoliquiritigenin - acceptor Isoliquiritigenin; Acceptors column Km (uM) raw value 2.4; Acceptors column kcat (s^-1) raw value 4.35; Acceptors column kcat/Km (s^-1*uM^-1) raw value 1.81

normalized_value_unit_evidence: kcat normalized_value=4.35 normalized_unit=s^-1; Km normalized_value=0.0024 normalized_unit=mM; kcat/Km normalized_value=1810 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.35 raw_unit=s^-1; Km raw_value=2.4 raw_unit=uM; kcat/Km raw_value=1.81 raw_unit=s^-1*uM^-1

substrate: isoliquiritigenin


substrate_name: ADP-alpha-D-glucose

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

column_label: Table 4; row ADPG/Phloretin - donor ADPG; Donors column Km (uM) raw value 58.67; Donors column kcat (s^-1) raw value 4.65; Donors column kcat/Km (s^-1*uM^-1) raw value 0.08

normalized_value_unit_evidence: kcat normalized_value=4.65 normalized_unit=s^-1; Km normalized_value=0.05867 normalized_unit=mM; kcat/Km normalized_value=80 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.65 raw_unit=s^-1; Km raw_value=58.67 raw_unit=uM; kcat/Km raw_value=0.08 raw_unit=s^-1*uM^-1

row_label: ADPG/Phloretin - donor ADPG

substrate: ADP-alpha-D-glucose


substrate_name: phloretin

substrate: phloretin


substrate_name: quercetin

substrate: quercetin


substrate_name: UDP-alpha-D-galactose

column_label: Table 4; row UDP-Gal/Quercetin - donor UDP-Gal; Donors column Km (uM) raw value 26.19; Donors column kcat (s^-1) raw value 13.18; Donors column kcat/Km (s^-1*uM^-1) raw value 0.5

normalized_value_unit_evidence: kcat normalized_value=13.18 normalized_unit=s^-1; Km normalized_value=0.02619 normalized_unit=mM; kcat/Km normalized_value=500 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=13.18 raw_unit=s^-1; Km raw_value=26.19 raw_unit=uM; kcat/Km raw_value=0.5 raw_unit=s^-1*uM^-1

row_label: UDP-Gal/Quercetin - donor UDP-Gal

substrate: UDP-alpha-D-galactose


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Thermoanaerobacter sp.

column_label: PDF Table 2. The kinetic parameters for the phosphorolytic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / b-1,2-Man2; columns kcat s^-1 1.9; Km mM 0.52; printed kcat/Km 3.7; export-normalized kcat/Km 3.65384615384615

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.52 normalized_unit=mM; kcat/Km normalized_value=3.65384615384615 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; KmA raw_value=0.52 raw_unit=mM; printed kcat/KmA=3.7 s^-1 mM^-1


column_label: PDF Table 2. The kinetic parameters for the phosphorolytic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / b-1,2-Man3; columns kcat s^-1 20; Km mM 0.92; printed kcat/Km 22; export-normalized kcat/Km 21.7391304347826

normalized_value_unit_evidence: kcat normalized_value=20 normalized_unit=s^-1; Km normalized_value=0.92 normalized_unit=mM; kcat/Km normalized_value=21.7391304347826 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=20 raw_unit=s^-1; KmA raw_value=0.92 raw_unit=mM; printed kcat/KmA=22 s^-1 mM^-1


substrate_name: alpha-D-mannose

assay_conditions_summary: pH 5; 303.15 K; buffer pH 5

column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / acceptor D-Mannose; columns kcat s^-1 1.9; Km mM 0.41; printed kcat/Km 4.6; export-normalized kcat/Km 4.63414634146341

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.41 normalized_unit=mM; kcat/Km normalized_value=4.63414634146341 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; Km raw_value=0.41 raw_unit=mM; printed kcat/Km=4.6 s^-1 mM^-1

row_label: Teth514_1788 / acceptor D-Mannose

substrate: alpha-D-mannose


column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / donor a-Man1P; columns kcat s^-1 22; Km mM 1.4; printed kcat/Km 16; export-normalized kcat/Km 15.7142857142857

row_label: Teth514_1788 / donor a-Man1P


column_label: PDF Table 1. The kinetic parameters for the synthetic reactions catalyzed by Teth514_1788 and Teth514_1789; row Teth514_1788 / acceptor D-Fructose; columns kcat s^-1 2; Km mM 0.2; printed kcat/Km 10; export-normalized kcat/Km 10

normalized_value_unit_evidence: kcat normalized_value=2 normalized_unit=s^-1; Km normalized_value=0.2 normalized_unit=mM; kcat/Km normalized_value=10 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=2.0 raw_unit=s^-1; Km raw_value=0.20 raw_unit=mM; printed kcat/Km=10 s^-1 mM^-1

row_label: Teth514_1788 / acceptor D-Fructose


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


column_label: Table 1 row Phosphorolysis / Glucosylglycerate; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

row_label: Phosphorolysis / Glucosylglycerate

table_label: Table 1. Apparent kinetic parameters of M. silvanus glucosylglycerate phosphorylase


substrate_name: alpha-D-glucopyranose 1-phosphate

column_label: Table 1 row Synthesis / alpha-D-Glucose 1-phosphate; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

row_label: Synthesis / alpha-D-Glucose 1-phosphate

substrate: alpha-D-glucopyranose 1-phosphate


substrate_name: phosphate

smiles: O=P(O)(O)O

column_label: Table 1 row Phosphorolysis / Phosphate; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: Km = 2.5 mM; kcat = 0.98 s^-1; paper kcat/Km = 0.40 s^-1*mM^-1; exported kcat_over_km = 0.392 s^-1*mM^-1

row_label: Phosphorolysis / Phosphate

substrate: phosphate


substrate_name: D-Glycerate

column_label: Table 1 row Synthesis / D-Glycerate; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

row_label: Synthesis / D-Glycerate

substrate: D-Glycerate


substrate_name: phloroglucinol

substrate: phloroglucinol


substrate_name: pelargonidin

substrate: pelargonidin


enzyme_display_name: cyanidin 3-O-galactosyltransferase

organism: Camellia sinensis var. sinensis

substrate_name: cyanidin

column_label: Table 1 reports Cyanidin Km 32.64 +/- 3.48 uM, Vmax 3.29 +/- 0.21 uM min^-1, kcat 18.61 +/- 1.21 min^-1, kcat/Km 0.57 +/- 0.04 min^-1 uM^-1; Km matches, but converted kcat and kcat/Km differ slightly from current export

normalized_value_unit_evidence: Km normalized_value=0.03264 normalized_unit=mM; kcat normalized_value=0.3101666667 normalized_unit=s^-1; kcat_over_km normalized_value=9.5 normalized_unit=s^-1*mM^-1; current_export_kcat=0.31 s^-1; current_export_kcat_over_km=9.497549019607842 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=32.64 +/- 3.48 raw_unit=uM; kcat raw_value=18.61 +/- 1.21 raw_unit=min^-1; kcat_over_km raw_value=0.57 +/- 0.04 raw_unit=min^-1*uM^-1 for cyanidin

row_label: Table 1 Cyanidin row; Km, Vmax, kcat, and kcat/Km columns

table_label: PMID 34217130 ScienceDirect Table 1

enzyme: cyanidin 3-O-galactosyltransferase

substrate: cyanidin


substrate_name: myricetin

substrate: myricetin


substrate_name: delphinidin

column_label: Table 1 reports Delphinidin Km 45.59 +/- 3.12 uM, Vmax 6.63 +/- 0.1 uM min^-1, kcat 37.45 +/- 0.56 min^-1, kcat/Km 0.82 +/- 0.01 min^-1 uM^-1; Km matches, but converted kcat and kcat/Km differ slightly from current export

normalized_value_unit_evidence: Km normalized_value=0.04559 normalized_unit=mM; kcat normalized_value=0.6241666667 normalized_unit=s^-1; kcat_over_km normalized_value=13.6666666667 normalized_unit=s^-1*mM^-1; current_export_kcat=0.624 s^-1; current_export_kcat_over_km=13.687212107918404 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=45.59 +/- 3.12 raw_unit=uM; kcat raw_value=37.45 +/- 0.56 raw_unit=min^-1; kcat_over_km raw_value=0.82 +/- 0.01 raw_unit=min^-1*uM^-1 for delphinidin

row_label: Table 1 Delphinidin row; Km, Vmax, kcat, and kcat/Km columns

substrate: delphinidin


enzyme_display_name: UniProt P00491

organism: Homo sapiens

substrate_name: Methylthioinosine

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P00491

substrate: Methylthioinosine


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


enzyme_display_name: UniProt P0ABP8

organism: Escherichia coli

enzyme: UniProt P0ABP8


enzyme_display_name: UniProt P55859

organism: Bos taurus

substrate_name: Inosine

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

enzyme: UniProt P55859

substrate: Inosine


enzyme_display_name: UniProt Q2HXR2

organism: Toxoplasma gondii

substrate_name: guanosine

enzyme: UniProt Q2HXR2

substrate: guanosine


substrate_name: deoxyinosine

substrate: deoxyinosine


enzyme_display_name: UniProt Q6CSZ6

organism: Kluyveromyces lactis

substrate_name: Xanthosine

enzyme: UniProt Q6CSZ6

substrate: Xanthosine


substrate_name: adenosine

substrate: adenosine


substrate_name: nicotinamide riboside

substrate: nicotinamide riboside


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=-----, pH=5.7


substrate_name: deoxyguanosine

substrate: deoxyguanosine


proof_lines:
Raw SKiD Env: Temp=-----, pH=5.7
Raw SKiD Env: Temp=-----, pH=6.5


substrate_name: xanthine

proof_lines:
Raw SKiD Env: Temp=-----, pH=6
Raw SKiD Env: Temp=-----, pH=7.5

substrate: xanthine


substrate_name: guanine

substrate: guanine


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: UniProt P56463

organism: Helicobacter pylori

enzyme: UniProt P56463


enzyme_display_name: UniProt P45563

enzyme: UniProt P45563


substrate_name: cyanidin 3-O-beta-D-glucoside

column_label: Primary prose labels cyanidin 3-glucoside Km 20.9 uM.

raw_value_unit_evidence: cyanidin 3-glucoside Km 20.9 uM

row_label: cyanidin 3-glucoside

table_label: Recombinant Gt5GT7 substrate-specificity prose

substrate: cyanidin 3-O-beta-D-glucoside


substrate_name: delphinidin 3-O-beta-D-glucoside

column_label: Primary prose labels delphinidin 3-glucoside Km 29.5 uM.

raw_value_unit_evidence: delphinidin 3-glucoside Km 29.5 uM

row_label: delphinidin 3-glucoside

substrate: delphinidin 3-O-beta-D-glucoside


substrate_name: pelargonidin 3-glucoside

column_label: Primary prose labels pelargonidin 3-glucoside Km 12.2 mM.

normalized_value_unit_evidence: Km 12.2 mM

raw_value_unit_evidence: pelargonidin 3-glucoside Km 12.2 mM

row_label: pelargonidin 3-glucoside

substrate: pelargonidin 3-glucoside


substrate_name: malvidin 3-glucoside

column_label: Primary prose labels malvidin 3-glucoside Km 3.4 mM.

normalized_value_unit_evidence: Km 3.4 mM

raw_value_unit_evidence: malvidin 3-glucoside Km 3.4 mM

row_label: malvidin 3-glucoside

substrate: malvidin 3-glucoside


column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjM / alpha-(1,2)-D-glucose-D-glycerate; fixed substrate phosphate (20 mM); columns kcat column raw 2.1 +/- 0.2 normalized 2.1 s^-1; Km column raw 0.069 +/- 0.002 normalized 0.069 mM; kcat/Km column raw (3.1 +/- 0.1) x 10^4 M^-1 s^-1 normalized from same-row kcat and Km as 30.434782608695652 s^-1*mM^-1; export values for required/current metrics match these normalized values.

normalized_value_unit_evidence: kcat normalized_value=2.1 normalized_unit=s^-1; Km normalized_value=0.069 normalized_unit=mM; kcat/Km normalized_value=30.434782608695652 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=(3.1 +/- 0.1) x 10^4 M^-1 s^-1


enzyme_display_name: Phloretin 2'-O-glucosyltransferase

substrate_name: phloretin

enzyme: Phloretin 2'-O-glucosyltransferase

substrate: phloretin


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: GDP-beta-L-colitose

substrate: GDP-beta-L-colitose


enzyme: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)


substrate_name: Cyanidin 3,7-di-O-beta-D-glucoside

substrate: Cyanidin 3,7-di-O-beta-D-glucoside


substrate_name: Cyanidin 3-O-beta-D-glucoside

column_label: Publisher PDF page 7 kinetic prose for kcat and Km; page 8 prose for explicit kcat/Km; page 9 Table 2 confirms Cyanidin 3-glucoside is the active acceptor.

normalized_value_unit_evidence: kcat=0.07 s^-1; Km=0.0065 mM; explicit efficiency=10.0 s^-1 mM^-1.

raw_value_unit_evidence: kcat(Cy3G)=0.07 s^-1; Km(Cy3G)=6.5 microM; later main prose gives kcat/Km(Cy3G)=1.0 x 10^4 s^-1 M^-1.

row_label: Recombinant Dc AA5GT with Cy3G

table_label: Main-text kinetic prose citing Supplemental Table 3; explicit main-text efficiency comparison

substrate: Cyanidin 3-O-beta-D-glucoside


substrate_name: Cyanin

substrate: Cyanin


enzyme_display_name: NDP-glycosyltransferase

organism: Bacillus subtilis

substrate_name: apigenin

column_label: Table 1; row Apigenin (3); columns Km, kcat, and kcat/Km; raw cells 19.4 +/- 2.6 uM, 1.9 +/- 0.1 s^-1, and 9.8 x 10^4 s^-1 M^-1.

row_label: Apigenin (3)

enzyme: NDP-glycosyltransferase

substrate: apigenin


substrate_name: genistein

column_label: Table 1; row Genistein (4); columns Km, kcat, and kcat/Km; raw cells 22.6 +/- 3.1 uM, 1.6 +/- 0.1 s^-1, and 7.2 x 10^4 s^-1 M^-1.

row_label: Genistein (4)

substrate: genistein


enzyme_display_name: glucosylglycerate phosphorylase

organism: Winmispira thermophila

substrate_name: D-glycerate

enzyme: glucosylglycerate phosphorylase

substrate: D-glycerate


substrate_name: alpha-D-glucopyranose 1-phosphate

substrate: alpha-D-glucopyranose 1-phosphate


substrate_name: UDP-Glc

substrate: UDP-Glc


enzyme_display_name: Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase 1

organism: Perilla frutescens


organism: Vitis amurensis

substrate_name: malvidin 3-O-beta-D-glucoside

substrate: malvidin 3-O-beta-D-glucoside


substrate_name: UDP-Glc (in the presence of DOPG at 31%)


enzyme_display_name: L-demethylnoviosyl transferase

organism: Streptomyces niveus

substrate_name: novobiocic acid

enzyme: L-demethylnoviosyl transferase

substrate: novobiocic acid


enzyme_display_name: Protein O-glucosyltransferase 1

enzyme: Protein O-glucosyltransferase 1


organism: Campylobacter jejuni

proof_lines: recombinant mutant K75A/R72A/K68A, pH 7.5, 25°C


proof_lines: recombinant mutant K75A/R72A, pH 7.5, 25°C


proof_lines: recombinant mutant R72A/K68A, pH 7.5, 25°C


proof_lines: recombinant wild-type enzyme, pH 7.5, 25°C


substrate_name: phosphate

substrate: phosphate


organism: Mycobacterium tuberculosis

substrate_name: UDP-alpha-D-galactofuranose

proof_lines: mutant enzyme H413S, in 50 mM MOPS, pH 7.6, 50 mM KCl, 20 mM MgCl2, at 37°C

substrate: UDP-alpha-D-galactofuranose


proof_lines: mutant enzyme E300S, in 50 mM MOPS, pH 7.6, 50 mM KCl, 20 mM MgCl2, at 37°C


proof_lines: mutant enzyme W399S, in 50 mM MOPS, pH 7.6, 50 mM KCl, 20 mM MgCl2, at 37°C


proof_lines: wild type enzyme, in 50 mM MOPS, pH 7.6, 50 mM KCl, 20 mM MgCl2, at 37°C


enzyme_display_name: UniProt A0A0H3JPC6

organism: Staphylococcus aureus

substrate_name: UDP-N-acetyl-D-glucosamine

enzyme: UniProt A0A0H3JPC6

substrate: UDP-N-acetyl-D-glucosamine


organism: Drosophila melanogaster

substrate_name: UDP-GalNAc

substrate: UDP-GalNAc


substrate_name: EA2 peptide

substrate: EA2 peptide


substrate_name: lacto-N-fucopentaose I

substrate: lacto-N-fucopentaose I


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

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


enzyme_display_name: N-acetyllactosamine synthase

substrate_name: asialo-agalacto-transferrin

enzyme: N-acetyllactosamine synthase

substrate: asialo-agalacto-transferrin


substrate_name: lacto-N-triose II

substrate: lacto-N-triose II


organism: Allomeiothermus silvanus


substrate_name: UDPgalactose

proof_lines: reaction with glucose, wild-type enzyme and N-deglycosylated recombinant enzyme

substrate: UDPgalactose


substrate_name: D-glucose

proof_lines:
recombinant enzyme
recombinant N-deglycosylated enzyme

substrate: D-glucose


enzyme_display_name: type 1 galactoside alpha-(1,2)-fucosyltransferase

substrate_name: phenyl beta-D-galactoside

substrate: phenyl beta-D-galactoside


substrate_name: di-N-acetylchitobiose

enzyme: type 1 galactoside alpha-(1,2)-fucosyltransferase

substrate: di-N-acetylchitobiose


proof_lines: using beta-Galf-(1->5)-beta-Galf-(1->6)-beta-Galf-octyl as cosubstrate, in 50 mM MOPS pH 7.6 with 20 mM MgCl2, 5 mM 2-mercaptoethanol, at 37°C

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


proof_lines: using beta-Galf-(1->6)-beta-Galf-(1->5)-beta-Galf-octyl as cosubstrate, in 50 mM MOPS pH 7.6 with 20 mM MgCl2, 5 mM 2-mercaptoethanol, at 37°C

proof_lines: spectrophotometric assay, in 50 mM MOPS, pH 7.9, 50 mM KCl, 20 mM MgCl2, at 37°C


proof_lines:
GalNAc-T2
+/-0.002 mM, pH7.4
pH 7.4, 37°C, enzyme form pp-GalNAc-T15


substrate_name: UDP-Gal

substrate: UDP-Gal


organism: Mus musculus


substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Rattus norvegicus

substrate_name: UDP-N-acetyl-D-galactosamine

substrate: UDP-N-acetyl-D-galactosamine


substrate_name: GTTPSPVPTTS-(O-GalNAc)T-SAP

proof_lines:
pH 7.0, 37°C
enzyme form ppGaNTase-1
enzyme form ppGaNTase-T5

substrate: GTTPSPVPTTS-(O-GalNAc)T-SAP


organism: Streptomyces sp.

substrate_name: novobiocic acid

proof_lines: pH 6.0, temperature not specified in the publication

substrate: novobiocic acid


organism: Oryctolagus cuniculus


substrate_name: GTTPSPVPTTSTTSAP

substrate: GTTPSPVPTTSTTSAP


substrate_name: cyanidin 3-O-beta-D-glucoside

substrate: cyanidin 3-O-beta-D-glucoside


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


substrate_name: PPDAATAAPL

proof_lines: +/-0.05 mM, truncated wild-type P-T1/delta42

proof_lines: +/-0.3 mM, truncated wild-type P-T1/delta42

proof_lines: +/-0.7 mM, mutant W316Y, 38.5 times higher than wild-type

substrate: PPDAATAAPL


substrate_name: UDP-GalNAc

proof_lines: +/-0.8 mM, truncated wild-type P-T1/delta42

proof_lines: +/-0.6 mM, mutant F325L, 1.2 times higher than wild-type

proof_lines: +/-0.1 mM, mutant W316Y, 1.8 times higher than wild-type

substrate: UDP-GalNAc


enzyme_display_name: citrate (Si)-synthase

organism: Sus scrofa

substrate_name: oxaloacetate

enzyme: citrate (Si)-synthase

substrate: oxaloacetate


substrate_name: acetyl-CoA

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA


organism: Toxoplasma gondii


enzyme_display_name: UniProt Q5XA29

organism: Streptococcus pyogenes

substrate_name: uridine

enzyme: UniProt Q5XA29

substrate: uridine


enzyme_display_name: UniProt A0A410UCT3

organism: Phytophthora capsici

enzyme: UniProt A0A410UCT3


enzyme_display_name: UniProt G4VGH9

organism: Schistosoma mansoni

substrate_name: thymidine

enzyme: UniProt G4VGH9

substrate: thymidine


enzyme_display_name: UniProt Q16831

organism: Homo sapiens

enzyme: UniProt Q16831


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: UniProt P07650

organism: Escherichia coli

enzyme: UniProt P07650


enzyme_display_name: UniProt P19971

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=37°C, pH=8

enzyme: UniProt P19971


substrate_name: 2-deoxy-alpha-D-ribose 1-phosphate

substrate: 2-deoxy-alpha-D-ribose 1-phosphate


substrate_name: thymine

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.6

substrate: thymine


enzyme_display_name: UniProt Q57VC7

organism: Trypanosoma brucei brucei

enzyme: UniProt Q57VC7


substrate_name: adenine

substrate: adenine


enzyme_display_name: nucleoside deoxyribosyltransferase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V11A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

enzyme: nucleoside deoxyribosyltransferase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V11S with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt Q967M2

organism: Giardia intestinalis

enzyme: UniProt Q967M2


substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


substrate_name: diphosphate

substrate: diphosphate


substrate_name: AMP

substrate: AMP


enzyme_display_name: UniProt Q97W95

organism: Saccharolobus solfataricus

enzyme: UniProt Q97W95


proof_lines:
Raw SKiD Env: Temp=60°C, pH=4.1
Raw SKiD Env: Temp=36°C, pH=7.9


enzyme_display_name: hypoxanthine phosphoribosyltransferase

organism: Streptomyces cyanogenus

substrate_name: hypoxanthine

enzyme: hypoxanthine phosphoribosyltransferase

substrate: hypoxanthine


substrate_name: guanine

substrate: guanine


enzyme_display_name: UniProt P20035

organism: Plasmodium falciparum

substrate_name: IMP

enzyme: UniProt P20035

substrate: IMP


enzyme_display_name: UniProt Q07010

enzyme: UniProt Q07010


enzyme_display_name: UniProt Q5SLS3

organism: Thermus thermophilus

enzyme: UniProt Q5SLS3


enzyme_display_name: UniProt P00492

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.4

enzyme: UniProt P00492


substrate_name: xanthine

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=23°C, pH=7.4

substrate: xanthine


proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=28°C, pH=7.4
Raw SKiD Env: Temp=23°C, pH=7.4


proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=28°C, pH=7.4


enzyme_display_name: UniProt Q5ZVC1

organism: Legionella pneumophila

enzyme: UniProt Q5ZVC1


enzyme_display_name: UniProt Q9NJI5

organism: Leishmania tarentolae

substrate_name: 5-phosphoribosyl 1-diphosphate

enzyme: UniProt Q9NJI5

substrate: 5-phosphoribosyl 1-diphosphate


organism: Mycobacterium tuberculosis


organism: Trypanosoma cruzi

substrate_name: myristoyl-CoA

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

substrate: myristoyl-CoA


enzyme_display_name: fatty-acid synthase system

organism: Anas platyrhynchos

substrate_name: Unknown

ki_unit: mM

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

proof_lines:
pH 7.0, 37°C, substrate acetyl-CoA
pH 7.0, 37°C, substrate NADPH
pH 7.0, 37°C, substrate malonyl-CoA

enzyme: fatty-acid synthase system

substrate: Unknown


substrate_name: CAP5.5 peptide

proof_lines:
source Trypanosoma cruzi, pH 7.4, 30°C
source Trypanosoma brucei, pH 7.4, 30°C
pH 7.4, 30°C

substrate: CAP5.5 peptide


enzyme_display_name: UniProt P9WHK9

substrate_name: Orotate

enzyme: UniProt P9WHK9

substrate: Orotate


substrate_name: orotidine 5'-phosphate

substrate: orotidine 5'-phosphate


enzyme_display_name: UniProt P13298

organism: Saccharomyces cerevisiae

enzyme: UniProt P13298


enzyme_display_name: UniProt Q8T6J6

organism: Vigna mungo

enzyme: UniProt Q8T6J6


enzyme_display_name: UniProt P43490

substrate_name: phosphate

enzyme: UniProt P43490

substrate: phosphate


substrate_name: ATP

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

substrate: ATP


substrate_name: ADP

substrate: ADP


enzyme_display_name: UniProt Q9STG9

organism: Arabidopsis thaliana

enzyme: UniProt Q9STG9


enzyme_display_name: UniProt G7JFL4

organism: Medicago truncatula

enzyme: UniProt G7JFL4


enzyme_display_name: UniProt Q5HSJ4

organism: Campylobacter jejuni

enzyme: UniProt Q5HSJ4


enzyme_display_name: sterol 3beta-glucosyltransferase

organism: Zea mays

substrate_name: UDP-glucose

proof_lines: slightly lowered by phosphatidylcholine and phosphatidylglycerol

enzyme: sterol 3beta-glucosyltransferase

substrate: UDP-glucose


substrate_name: sitosterol

proof_lines: strongly lowered by phosphatidylcholine and phosphatidylglycerol

substrate: sitosterol


organism: Sus scrofa

substrate_name: asialo-mucin of Cowper's gland

proof_lines: calculated on the basis of terminal N-galactosaminyl residues

substrate: asialo-mucin of Cowper's gland


substrate_name: UDP-galactose

substrate: UDP-galactose


enzyme_display_name: trihydroxystilbene synthase

organism: Arachis hypogaea

substrate_name: malonyl-CoA

enzyme: trihydroxystilbene synthase

substrate: malonyl-CoA


assay_conditions_summary: pH 4; 303.15 K; cofactor CoA

proof_lines: pH 4.0, 30°C, recombinant STS, uncompetitive inhibition

proof_lines: pH 4.0, 30°C, recombinant STS, competitive inhibition


enzyme_display_name: UniProt P9WJJ7

substrate_name: quinolinic acid

enzyme: UniProt P9WJJ7

substrate: quinolinic acid


substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


enzyme_display_name: UniProt Q15274

organism: Homo sapiens

enzyme: UniProt Q15274


enzyme_display_name: UniProt Q05603

organism: Salmonella enterica

substrate_name: beta-nicotinate D-ribonucleotide

enzyme: UniProt Q05603

substrate: beta-nicotinate D-ribonucleotide


enzyme_display_name: UniProt P42085

organism: Bacillus subtilis

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

enzyme: UniProt P42085


substrate_name: Arabidopsis thaliana protein CDPK6-derived peptide


organism: Bos taurus

substrate_name: AQPTPPP

proof_lines: derived from the bovine myelin basic protein sequence

proof_lines: derived from the major acceptor sequence in myelin basic protein

substrate: AQPTPPP


enzyme_display_name: malate synthase

substrate_name: acetyl-CoA

enzyme: malate synthase

substrate: acetyl-CoA


substrate_name: glyoxylate

substrate: glyoxylate


enzyme_display_name: UniProt I0B503

organism: Schistosoma mansoni

enzyme: UniProt I0B503


substrate_name: adenosine

substrate: adenosine


enzyme_display_name: UniProt Q7XA67

enzyme: UniProt Q7XA67


enzyme_display_name: UniProt Q8YBL1

organism: Brucella melitensis

enzyme: UniProt Q8YBL1


enzyme_display_name: UniProt Q9T0I8

enzyme: UniProt Q9T0I8


enzyme_display_name: UniProt P50389

organism: Saccharolobus solfataricus

enzyme: UniProt P50389


substrate_name: S-adenosylhomocysteine

substrate: S-adenosylhomocysteine


enzyme_display_name: UniProt C9Z6T8

organism: Streptomyces scabiei

substrate_name: NAD+

enzyme: UniProt C9Z6T8

substrate: NAD+


enzyme_display_name: UniProt Q8N5Y8

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

enzyme: UniProt Q8N5Y8


enzyme_display_name: N-acetyllactosamine synthase

substrate_name: D-glucose

enzyme: N-acetyllactosamine synthase

substrate: D-glucose


enzyme_display_name: UniProt Q9HZK1

organism: Pseudomonas aeruginosa

substrate_name: adenine

enzyme: UniProt Q9HZK1

substrate: adenine


enzyme_display_name: alpha-tubulin N-acetyltransferase

enzyme: alpha-tubulin N-acetyltransferase


organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)

substrate_name: pABA (at 70 degrees Celsius)

substrate: pABA (at 70 degrees Celsius)


organism: Triticum aestivum

substrate_name: Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg

substrate: Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


enzyme_display_name: UniProt Q9BXR0

substrate_name: queuine

enzyme: UniProt Q9BXR0

substrate: queuine


substrate_name: UDP-GalNAc

substrate: UDP-GalNAc


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

organism: Enterococcus faecalis

substrate_name: Unknown

assay_conditions_summary: pH 8; 291.15 K; cofactor CoA

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: Unknown


organism: Escherichia coli

proof_lines: pH 7.5, 30°C, noncompetitive inhibition against (R)-3-hydroxymyristoyl-[acyl-carrier protein]


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

substrate_name: gentamicin C1a

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: gentamicin C1a


enzyme_display_name: UniProt P13721

organism: Rattus norvegicus

substrate_name: CMP-N-acetylneuraminate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P13721

substrate: CMP-N-acetylneuraminate


enzyme_display_name: UniProt P15907

substrate_name: CMP-N-acetyl-beta-neuraminate

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

enzyme: UniProt P15907

substrate: CMP-N-acetyl-beta-neuraminate


enzyme_display_name: UniProt A8QYL1

organism: Photobacterium sp.

substrate_name: lactose

enzyme: UniProt A8QYL1

substrate: lactose


substrate_name: methyl-beta-D-galactopyranoside

substrate: methyl-beta-D-galactopyranoside


enzyme_display_name: UniProt Q02745

organism: Sus scrofa

enzyme: UniProt Q02745


enzyme_display_name: UniProt Q15KI8

organism: Pasteurella multocida

enzyme: UniProt Q15KI8


enzyme_display_name: UniProt A5LHX0

organism: Photobacterium phosphoreum

enzyme: UniProt A5LHX0


proof_lines: pH 8.0, 25°C, recombinant His6-tagged LpxD


organism: Gallus gallus

substrate_name: acetyl-CoA

proof_lines:
acetyl-CoA hydrolysis
0.005 mM acetoacetyl-CoA
reombinant enzyme

substrate: acetyl-CoA


enzyme_display_name: 2-methylcitrate synthase

substrate_name: propionyl-CoA

enzyme: 2-methylcitrate synthase

substrate: propionyl-CoA


substrate_name: S-(3-Oxobutyl)-CoA; Acetyl-CoA; H2O

substrate: S-(3-Oxobutyl)-CoA; Acetyl-CoA; H2O


enzyme_display_name: sterol 3beta-glucosyltransferase

organism: Gossypium hirsutum

substrate_name: UDP-glucose

enzyme: sterol 3beta-glucosyltransferase

substrate: UDP-glucose


organism: Homo sapiens

substrate_name: UDP-Gal

substrate: UDP-Gal


substrate_name: acetoacetyl-CoA

proof_lines:
cytoplasmic isozymes I-IV
recombinant enzyme, hydrolase reaction

substrate: acetoacetyl-CoA


enzyme_display_name: UniProt P24173

substrate_name: ADP-L-glycero-beta-D-manno-heptose

enzyme: UniProt P24173

substrate: ADP-L-glycero-beta-D-manno-heptose


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


enzyme_display_name: type 1 galactoside alpha-(1,2)-fucosyltransferase

substrate_name: GDP-L-fucose

proof_lines:
H-gene encoded enzyme
enzyme from plasma
reaction with GM1, recombinant enzyme

substrate: GDP-L-fucose


proof_lines:
recombinant enzyme
enzyme from gastric mucosa
H-gene encoded enzyme

enzyme: type 1 galactoside alpha-(1,2)-fucosyltransferase


substrate_name: N-acetylglucosamine

smiles: CC(=O)NC(C=O)C(C(C(CO)O)O)O

proof_lines:
recombinant enzyme
recombinant N-deglycosylated enzyme

substrate: N-acetylglucosamine


substrate_name: lactosylceramide

substrate: lactosylceramide


substrate_name: N-acetyl-D-galactosamine

substrate: N-acetyl-D-galactosamine


enzyme_display_name: Geranylgeranyl pyrophosphate synthase BTS1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


substrate_name: isopentenyl diphosphate

smiles: CC(=C)CCOP(=O)(O)OP(=O)(O)O

enzyme: Geranylgeranyl pyrophosphate synthase BTS1

substrate: isopentenyl diphosphate


enzyme_display_name: UniProt P45741

organism: Paenibacillus thiaminolyticus

enzyme: UniProt P45741


enzyme_display_name: Thiamine-phosphate synthase

organism: Escherichia coli (strain K12)

substrate_name: HMP-PP

enzyme: Thiamine-phosphate synthase

substrate: HMP-PP


substrate_name: THZ-P

substrate: THZ-P


enzyme_display_name: UniProt P31153

substrate_name: L-methionine

smiles: CSCCC(C(=O)O)N

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

enzyme: UniProt P31153

substrate: L-methionine


enzyme_display_name: UniProt Q980S9

organism: Saccharolobus solfataricus

substrate_name: L-ethionine

smiles: CCSCCC(C(=O)O)N

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=65°C, pH=8

enzyme: UniProt Q980S9

substrate: L-ethionine


substrate_name: ATP

proof_lines:
Raw SKiD Env: Temp=65°C, pH=8
Raw SKiD Env: Temp=37°C, pH=8

substrate: ATP


enzyme_display_name: UniProt P13444

enzyme: UniProt P13444


enzyme_display_name: UniProt Q72I53

organism: Thermus thermophilus

enzyme: UniProt Q72I53


substrate_name: methionine

substrate: methionine


enzyme_display_name: UniProt P0A749

substrate_name: phosphoenolpyruvate

enzyme: UniProt P0A749

substrate: phosphoenolpyruvate


enzyme_display_name: UniProt P33038

organism: Enterobacter cloacae

substrate_name: UDP-N-acetyl-D-glucosamine

enzyme: UniProt P33038

substrate: UDP-N-acetyl-D-glucosamine


enzyme_display_name: N-acetyllactosamine synthase

organism: Mus musculus

substrate_name: asialo-agalacto-transferrin

enzyme: N-acetyllactosamine synthase

substrate: asialo-agalacto-transferrin


proof_lines: pH 7.2, temperature not specified in the publication


substrate_name: UDP-alpha-D-galactose

proof_lines:
at pH 6.3 and 37°C
recombinant enzyme
recombinant N-deglycosylated enzyme

substrate: UDP-alpha-D-galactose


organism: Methanosarcina barkeri

substrate_name: N-Furfurylformamide

substrate: N-Furfurylformamide


substrate_name: L-histidine

substrate: L-histidine


substrate_name: N-acetylglucosamine

substrate: N-acetylglucosamine


substrate_name: Gly-Ser-Ser-Lys-Pro-Lys-Asp-Lys-Asp-Pro

substrate: Gly-Ser-Ser-Lys-Pro-Lys-Asp-Lys-Asp-Pro


organism: Mycobacterium tuberculosis

smiles: CCCCCCCCCCC(C)O


organism: Plasmodium falciparum

substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: phloroglucinol synthase

organism: Pseudomonas fluorescens

substrate_name: malonyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: pH and temperature not specified in the publication

enzyme: phloroglucinol synthase

substrate: malonyl-CoA


enzyme_display_name: ATP citrate synthase

organism: Rattus norvegicus

substrate_name: citrate

enzyme: ATP citrate synthase

substrate: citrate


substrate_name: UDPgalactose

substrate: UDPgalactose


proof_lines:
enzyme from liver microsomal membrane
enzyme from serum
enzyme from liver


substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


enzyme_display_name: UniProt Q25704

enzyme: UniProt Q25704


enzyme_display_name: UniProt Q81VW8

organism: Bacillus anthracis

substrate_name: sulfanilamide

enzyme: UniProt Q81VW8

substrate: sulfanilamide


substrate_name: sulfisoxazole

substrate: sulfisoxazole


substrate_name: sulfamethoxazole

substrate: sulfamethoxazole


substrate_name: sulfamethizole

substrate: sulfamethizole


substrate_name: Sulfadiazine

substrate: Sulfadiazine


substrate_name: sulfathiazole

substrate: sulfathiazole


substrate_name: dapson

substrate: dapson


enzyme_display_name: UniProt P0AC13

organism: Escherichia coli MC4100

enzyme: UniProt P0AC13


enzyme_display_name: UniProt P53848

organism: Saccharomyces cerevisiae

enzyme: UniProt P53848


substrate_name: p-Aminobenzoic acid

substrate: p-Aminobenzoic acid


enzyme_display_name: UniProt P9WND1

enzyme: UniProt P9WND1


enzyme_display_name: UniProt P09158

organism: Escherichia coli

substrate_name: S-adenosylmethioninamine

enzyme: UniProt P09158

substrate: S-adenosylmethioninamine


enzyme_display_name: UniProt Q31QK9

organism: Synechococcus elongatus

substrate_name: putrescine

smiles: C(CCN)CN

enzyme: UniProt Q31QK9

substrate: putrescine


substrate_name: p60src-derived peptide

substrate: p60src-derived peptide


enzyme_display_name: cytochrome-b5 reductase

substrate_name: testosterone

enzyme: cytochrome-b5 reductase

substrate: testosterone


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

substrate_name: acetyl-CoA

proof_lines: absence of acetoacetyl-CoA, hydrolysis reaction

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: acetyl-CoA


enzyme_display_name: type 1 galactoside alpha-(1,2)-fucosyltransferase

substrate_name: GDP-L-fucose

proof_lines: reaction with porcine submaxillary mucin or intestinal glycoprotein

substrate: GDP-L-fucose


substrate_name: CoA

substrate: CoA


enzyme_display_name: ribonucleoside-diphosphate reductase

substrate_name: CDP

enzyme: ribonucleoside-diphosphate reductase

substrate: CDP


substrate_name: N-acetylglucosamine

substrate: N-acetylglucosamine


substrate_name: aquacobalamin

assay_conditions_summary: cofactor NADH

substrate: aquacobalamin


enzyme_display_name: catechol 1,2-dioxygenase

organism: Rhizobium leguminosarum

substrate_name: catechol

enzyme: catechol 1,2-dioxygenase

substrate: catechol


enzyme_display_name: protocatechuate 3,4-dioxygenase

substrate_name: protocatechuate

enzyme: protocatechuate 3,4-dioxygenase

substrate: protocatechuate


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

organism: Pseudomonas aeruginosa

substrate_name: gentamicin C1

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: gentamicin C1


enzyme_display_name: trimethylamine monooxygenase

organism: Ruegeria pomeroyi

substrate_name: N,N,N-trimethylamine

smiles: CN(C)C

assay_conditions_summary: pH 7.6; 295.15 K; buffer 80 mM PIPES

proof_lines: recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C

enzyme: trimethylamine monooxygenase

substrate: N,N,N-trimethylamine


enzyme_display_name: trans-aconitate 3-methyltransferase

substrate_name: Itaconate

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

enzyme: trans-aconitate 3-methyltransferase

substrate: Itaconate


enzyme_display_name: cysteine dioxygenase

substrate_name: Unknown

enzyme: cysteine dioxygenase

substrate: Unknown


enzyme_display_name: benzoate 1,2-dioxygenase

organism: Rhodococcus opacus

enzyme: benzoate 1,2-dioxygenase


enzyme_display_name: ferroxidase

substrate_name: Fe(II)

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication

enzyme: ferroxidase

substrate: Fe(II)


substrate_name: myristoyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
pH 8.0, 30°C, continuous assay
chemical transformation step
with Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg

substrate: myristoyl-CoA


enzyme_display_name: alcohol O-acetyltransferase

substrate_name: isoamyl alcohol

smiles: CC(C)CCO

proof_lines: Yeast alcohol acetyltransferase review context only; no row-specific accession anchor preserved.

enzyme: alcohol O-acetyltransferase

substrate: isoamyl alcohol


proof_lines:
wild-type, pH 6.0
wild-type, pH 6.5, 4°C


substrate_name: Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys

substrate: Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys


enzyme_display_name: UniProt P31570

organism: Salmonella enterica

substrate_name: cob(II)inamide

enzyme: UniProt P31570

substrate: cob(II)inamide


substrate_name: ATP

substrate: ATP


enzyme_display_name: UniProt Q96EY8

organism: Homo sapiens

enzyme: UniProt Q96EY8


substrate_name: cob(I)alamin

substrate: cob(I)alamin


enzyme_display_name: UniProt Q9HIA7

organism: Thermoplasma acidophilum

substrate_name: Cobalamin

enzyme: UniProt Q9HIA7

substrate: Cobalamin


substrate_name: hydroxocobalamin

substrate: hydroxocobalamin


substrate_name: dATP

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

substrate: dATP


enzyme_display_name: glutathione transferase

organism: Chlamys islandica

substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

enzyme: glutathione transferase

substrate: glutathione


enzyme_display_name: UniProt M2QJS8

organism: Gelatoporia subvermispora

substrate_name: cumene hydroperoxide

enzyme: UniProt M2QJS8

substrate: cumene hydroperoxide


substrate_name: 4-methylumbelliferyl acetate

substrate: 4-methylumbelliferyl acetate


substrate_name: 5-chloromethylfluorescein diacetate

substrate: 5-chloromethylfluorescein diacetate


enzyme_display_name: UniProt O49235

organism: Glycine max

enzyme: UniProt O49235


enzyme_display_name: UniProt P30711

substrate_name: iodobutane

smiles: CCC(C)I

enzyme: UniProt P30711

substrate: iodobutane


substrate_name: iodohexane

smiles: CCCCCCI

substrate: iodohexane


substrate_name: iodomethane

smiles: CI

substrate: iodomethane


enzyme_display_name: UniProt P09211

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.4
Raw SKiD Env: Temp=25°C, pH=6.5
Raw SKiD Env: Temp=30°C, pH=6.5

enzyme: UniProt P09211


enzyme_display_name: UniProt A8R5V3

organism: Bombyx mori

enzyme: UniProt A8R5V3


smiles: CCCCCC(C=CC=O)O


substrate_name: Ethacrynic acid

substrate: Ethacrynic acid


proof_lines:
Raw SKiD Env: Temp=-----, pH=6.5
Raw SKiD Env: Temp=30°C, pH=6.5
Raw SKiD Env: Temp=25°C, pH=6.5


enzyme_display_name: UniProt Q5CCJ4

enzyme: UniProt Q5CCJ4


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=6.5


enzyme_display_name: UniProt Q9FQE8

enzyme: UniProt Q9FQE8


substrate_name: fluorodifen

substrate: fluorodifen


substrate_name: tert-butyl peroxide

smiles: CC(C)(C)OOC(C)(C)C

substrate: tert-butyl peroxide


organism: Isoptericola variabilis

substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


enzyme_display_name: UniProt Q9S400

organism: Streptococcus pneumoniae

substrate_name: phosphate

enzyme: UniProt Q9S400

substrate: phosphate


enzyme_display_name: UniProt P0A6D3

enzyme: UniProt P0A6D3


substrate_name: shikimate 3-phosphate

substrate: shikimate 3-phosphate


enzyme_display_name: UniProt P37268

substrate_name: farnesyl diphosphate

enzyme: UniProt P37268

substrate: farnesyl diphosphate


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

substrate_name: Unknown

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, competitive inhibition, substrate acetyl-CoA

proof_lines: pH 8.0, mixed inhibition, substrate acetoacetyl-CoA

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: Unknown


substrate_name: NADH

assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADH

proof_lines: using ubiquinone-2 as substrate, in 20 mM MOPS/KOH, 1 mM EDTA, 0.03% (v/v) Triton X-100, 200 mM KCl, pH 6.2, temperature not specified in the publication

substrate: NADH


substrate_name: acetyl-CoA

proof_lines:
strain NCYC 366
isoamyl acetate synthesis
ethyl acetate synthesis

substrate: acetyl-CoA


enzyme_display_name: cytochrome-b5 reductase

organism: Rattus norvegicus

enzyme: cytochrome-b5 reductase


organism: Saccharomyces cerevisiae

proof_lines:
apparent value, at pH 7.5 and 30°C
at pH 7.5 and 25°C
competitive inhibition


enzyme_display_name: sterol 14alpha-demethylase

enzyme: sterol 14alpha-demethylase


enzyme_display_name: UniProt P58758

organism: Agrobacterium tumefaciens

enzyme: UniProt P58758


substrate_name: dimethylallyl diphosphate

smiles: CC(=CCOP(=O)(O)OP(=O)(O)O)C

substrate: dimethylallyl diphosphate


substrate_name: AMP

substrate: AMP


enzyme_display_name: geranylgeranyl diphosphate synthase

organism: Capsicum annuum

enzyme: geranylgeranyl diphosphate synthase


substrate_name: geranyl diphosphate

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

substrate: geranyl diphosphate


organism: Sinapis alba


substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


enzyme_display_name: UniProt Q12051

substrate_name: (2E,6E)-farnesyl diphosphate

enzyme: UniProt Q12051

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: UniProt Q94IE8

organism: Eucommia ulmoides

enzyme: UniProt Q94IE8


enzyme_display_name: UniProt P55984

organism: Helicobacter pylori

enzyme: UniProt P55984


enzyme_display_name: UniProt O82827

organism: Micrococcus luteus

substrate_name: (2Z,6E,10E)-geranylgeranyl diphosphate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.3
Raw SKiD Env: Temp=37°C, pH=7.5

enzyme: UniProt O82827

substrate: (2Z,6E,10E)-geranylgeranyl diphosphate


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.3
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.5


enzyme_display_name: ribonucleoside-diphosphate reductase

substrate_name: thioredoxin

enzyme: ribonucleoside-diphosphate reductase

substrate: thioredoxin


enzyme_display_name: malate synthase

substrate_name: glyoxylate

enzyme: malate synthase

substrate: glyoxylate


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: UDP-galactose

substrate: UDP-galactose


enzyme_display_name: UniProt Q50EL0

organism: Aspergillus fumigatus

substrate_name: L-tryptophan methyl ester

enzyme: UniProt Q50EL0

substrate: L-tryptophan methyl ester


substrate_name: L-o-tyrosine

substrate: L-o-tyrosine


substrate_name: L-abrine

substrate: L-abrine


substrate_name: L-m-tyrosine

substrate: L-m-tyrosine


substrate_name: cyclo-L-Trp-L-Trp

substrate: cyclo-L-Trp-L-Trp


substrate_name: cyclo-L-Trp-L-Pro

substrate: cyclo-L-Trp-L-Pro


enzyme_display_name: ferroxidase

smiles: O=O

enzyme: ferroxidase


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Serratia marcescens

substrate_name: ribostamycin

proof_lines:
full length enzyme, pH 7.5, 25°C
isolated AAC(6') domain, pH 7.5, 25°C

enzyme: aminoglycoside 6'-N-acetyltransferase

substrate: ribostamycin


enzyme_display_name: mercury(II) reductase

enzyme: mercury(II) reductase


organism: Solanum tuberosum


enzyme_display_name: monodehydroascorbate reductase (NADH)

substrate_name: monodehydroascorbate

enzyme: monodehydroascorbate reductase (NADH)

substrate: monodehydroascorbate


enzyme_display_name: catechol 2,3-dioxygenase

organism: Sphingomonas sp.

substrate_name: catechol

proof_lines:
hybrid enzyme, pH 7.5, 25°C
native enzyme, pH 7.5, 25°C

enzyme: catechol 2,3-dioxygenase

substrate: catechol


enzyme_display_name: ferredoxin hydrogenase

organism: Sporomusa sphaeroides

smiles: [HH]

enzyme: ferredoxin hydrogenase


enzyme_display_name: UniProt P49366

organism: Homo sapiens

substrate_name: spermidine

smiles: C(CCNCCCN)CN

enzyme: UniProt P49366

substrate: spermidine


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: UniProt A8YBP8

organism: Microcystis aeruginosa

substrate_name: O-acetyl-L-serine

smiles: CC(=O)OCC(C(=O)O)N

enzyme: UniProt A8YBP8

substrate: O-acetyl-L-serine


enzyme_display_name: UniProt A8YBS4

enzyme: UniProt A8YBS4


enzyme_display_name: UniProt D2Z027

organism: Streptomyces lavendulae

substrate_name: thiosulfate

enzyme: UniProt D2Z027

substrate: thiosulfate


enzyme_display_name: Cysteine synthase A

organism: Escherichia coli (strain K12)

smiles: C(C(C(=O)O)N)Cl

enzyme: Cysteine synthase A


substrate_name: thioglycolate

substrate: thioglycolate


organism: Spinacia oleracea

substrate_name: O-acetylserine

substrate: O-acetylserine


substrate_name: sulfide

substrate: sulfide


enzyme_display_name: cystathionine gamma-synthase

organism: Lysinibacillus sphaericus

substrate_name: O-succinyl-L-homoserine

smiles: C(COC(=O)CCC(=O)O)C(C(=O)O)N

enzyme: cystathionine gamma-synthase

substrate: O-succinyl-L-homoserine


substrate_name: O-acetyl-L-homoserine

smiles: CC(=O)OCCC(C(=O)O)N

substrate: O-acetyl-L-homoserine


enzyme_display_name: NADPH:quinone reductase

organism: Staphylococcus aureus

enzyme: NADPH:quinone reductase


enzyme_display_name: ectoine hydroxylase

organism: Stutzerimonas stutzeri

substrate_name: L-homoectoine

enzyme: ectoine hydroxylase

substrate: L-homoectoine


enzyme_display_name: nitric oxide reductase (cytochrome c)

substrate_name: Unknown

enzyme: nitric oxide reductase (cytochrome c)

substrate: Unknown


enzyme_display_name: catechol 1,2-dioxygenase

proof_lines: pH 8.5, temperature not specified in the publication

enzyme: catechol 1,2-dioxygenase


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

organism: Sus scrofa

substrate_name: acetyl-CoA

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: acetyl-CoA


enzyme_display_name: biflaviolin synthase

organism: Streptomyces coelicolor

substrate_name: flaviolin

column_label: PMID 15659395 page 11601, Results section 'An Endogenous Function and Probable Biological Role of CYP158A2'; metric label turnover number for flaviolin oxidation.

raw_value_unit_evidence: Results prose reports turnover number 1.4 min^-1 for flaviolin oxidation.

enzyme: biflaviolin synthase

substrate: flaviolin


enzyme_display_name: N-acetyllactosamine synthase

substrate_name: N-acetylglucosamine

smiles: CC(=O)NC(C=O)C(C(C(CO)O)O)O

enzyme: N-acetyllactosamine synthase

substrate: N-acetylglucosamine


enzyme_display_name: beta-pyrazolylalanine synthase

organism: Citrullus lanatus

enzyme: beta-pyrazolylalanine synthase


substrate_name: pyrazole

substrate: pyrazole


enzyme_display_name: UniProt G3XCJ9

organism: Pseudomonas aeruginosa

substrate_name: D-erythrose 4-phosphate

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

enzyme: UniProt G3XCJ9

substrate: D-erythrose 4-phosphate


enzyme_display_name: UniProt P0AB91

organism: Escherichia coli

substrate_name: phosphoenolpyruvate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=6.8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P0AB91

substrate: phosphoenolpyruvate


enzyme_display_name: UniProt Q9K169

organism: Neisseria meningitidis

proof_lines:
Raw SKiD Env: Temp=25°C, pH=6.8
Raw SKiD Env: Temp=30°C, pH=6.8

enzyme: UniProt Q9K169


enzyme_display_name: UniProt O66496

organism: Aquifex aeolicus

proof_lines:
Raw SKiD Env: Temp=40°C, pH=7.5
Raw SKiD Env: Temp=40°C, pH=5
Raw SKiD Env: Temp=60°C, pH=7.5

enzyme: UniProt O66496


substrate_name: D-arabinose 5-phosphate

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=40°C, pH=7.5
Raw SKiD Env: Temp=40°C, pH=5

substrate: D-arabinose 5-phosphate


enzyme_display_name: UniProt P0A715

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.3

enzyme: UniProt P0A715


enzyme_display_name: UniProt Q9JZ55

enzyme: UniProt Q9JZ55


substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


substrate_name: UDP-GalNAc

substrate: UDP-GalNAc


substrate_name: Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro

substrate: Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: 1-linoleoyl lysophosphatidylcholine

proof_lines: inhibition of the ferric form of 12-lipoxygenase, free enzyme

proof_lines: inhibition of the ferric form of 12-lipoxygenase, substrate-bound form of enzyme

enzyme: arachidonate 12-lipoxygenase

substrate: 1-linoleoyl lysophosphatidylcholine


enzyme_display_name: NADPH-hemoprotein reductase

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: kidney spleen

enzyme: NADPH-hemoprotein reductase

substrate: NADPH


substrate_name: linoleic acid

smiles: CCCCCC=CCC=CCCCCCCCC(=O)O

substrate: linoleic acid


substrate_name: GDP-L-fucose

substrate: GDP-L-fucose


organism: Taeniopygia guttata

substrate_name: GAGADDDYAVTPGPDDDAGAG

proof_lines: pH and temperature not specified in the publication

substrate: GAGADDDYAVTPGPDDDAGAG


organism: Takifugu rubripes

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


substrate_name: deglycosylated swine trachea mucin

substrate: deglycosylated swine trachea mucin


smiles: CCCCCCC=CC=CCC=CCC=CCCCC(=O)O


enzyme_display_name: UniProt P9WP53

organism: Mycobacterium tuberculosis

substrate_name: O-phospho-L-serine

enzyme: UniProt P9WP53

substrate: O-phospho-L-serine


enzyme_display_name: nitrite reductase (NO-forming)

organism: uncultured bacterium

substrate_name: nitrite

enzyme: nitrite reductase (NO-forming)

substrate: nitrite


enzyme_display_name: trihydroxystilbene synthase

organism: Vitis vinifera

substrate_name: Unknown

proof_lines:
pH 4.0, 30°C, uncompetitive inhibition
pH 4.0, 30°C, competitive inhibition

enzyme: trihydroxystilbene synthase

substrate: Unknown


enzyme_display_name: sterol 3beta-glucosyltransferase

organism: Zea mays

enzyme: sterol 3beta-glucosyltransferase


enzyme_display_name: fatty-acid synthase system

organism: Mus musculus

substrate_name: palmitoyl-CoA

assay_conditions_summary: 298.15 K; cofactor CoA

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

enzyme: fatty-acid synthase system

substrate: palmitoyl-CoA


substrate_name: methylmalonyl-CoA

substrate: methylmalonyl-CoA


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


substrate_name: malonyl-CoA

proof_lines: didomain construct bearing mutation R606A, pH not specified in the publication, 25°C

substrate: malonyl-CoA


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


enzyme_display_name: nitrate reductase (NADH)

substrate_name: nitrate

enzyme: nitrate reductase (NADH)

substrate: nitrate


organism: Homo sapiens

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

substrate: NADPH


proof_lines: mutant enzyme A635G/R636S, at pH 7.5 and 25°C


enzyme_display_name: cytochrome-b5 reductase

substrate_name: NADH

enzyme: cytochrome-b5 reductase

substrate: NADH


substrate_name: ferricytochrome b5

substrate: ferricytochrome b5


substrate_name: ferricyanide

substrate: ferricyanide


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH

proof_lines: lysosome- and detergent-solubilized enzyme


assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM potassium phosphate; cofactor NADH

proof_lines: wild type enzyme, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


enzyme_display_name: NADPH:quinone reductase

smiles: CCCCCCC=CC=O

enzyme: NADPH:quinone reductase


smiles: CC(=O)C=C


smiles: CCC=CC=O


smiles: CC=CC(=O)C


smiles: CCCCCC=CC(=O)C


smiles: CCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCC(C=CC=O)O


substrate_name: propenal

smiles: C=CC=O

substrate: propenal


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


enzyme_display_name: UniProt P9WFF7

substrate_name: neryl diphosphate

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

enzyme: UniProt P9WFF7

substrate: neryl diphosphate


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


enzyme_display_name: Dehydrodolichyl diphosphate synthase 1

organism: Arabidopsis thaliana

substrate_name: farnesyl diphosphate (FPP)

enzyme: Dehydrodolichyl diphosphate synthase 1

substrate: farnesyl diphosphate (FPP)


substrate_name: geranylgeranyl diphosphate (GGPP)

substrate: geranylgeranyl diphosphate (GGPP)


substrate_name: isopentenyl diphosphate (IPP)

smiles: CC(=C)CCOP(=O)(O)OP(=O)(O)O

substrate: isopentenyl diphosphate (IPP)


enzyme_display_name: UniProt P0AD57

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

enzyme: UniProt P0AD57


substrate_name: dimethylallyl diphosphate

smiles: CC(=CCOP(=O)(O)OP(=O)(O)O)C

substrate: dimethylallyl diphosphate


substrate_name: isopentenyl diphosphate

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

substrate: isopentenyl diphosphate


enzyme_display_name: UniProt B8XA40

organism: Solanum habrochaites

enzyme: UniProt B8XA40


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: with 0.08 mM 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.5 and 25°C

proof_lines: with 0.06 mM 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.5 and 25°C


proof_lines: with NADPH as cosubstrate, at pH 7.5 and 25°C


enzyme_display_name: xanthine oxidase

organism: Bos taurus

enzyme: xanthine oxidase


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Sus scrofa


enzyme_display_name: demethylphylloquinol methyltransferase

substrate_name: menadione

enzyme: demethylphylloquinol methyltransferase

substrate: menadione


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

proof_lines: recombinant NAD(P)H:quinone acceptor oxidoreductase 2

enzyme: NAD(P)H dehydrogenase (quinone)


substrate_name: Methyl red

proof_lines: recombinant NAD(P)H:quinone acceptor oxidoreductase 1

substrate: Methyl red


organism: Gluconobacter oxydans


substrate_name: (2E,6E,10E)-geranylgeranyl diphosphate

substrate: (2E,6E,10E)-geranylgeranyl diphosphate


proof_lines:
pH 7.5, 37°C, mutant enzyme A197V
mutant A197V, pH 7.5, 37°C


substrate_name: NADPH

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: mutant N143A, pH 7.5, temperature not specified in the publication

substrate: NADPH


proof_lines: mutant N143L, pH 7.5, temperature not specified in the publication


proof_lines: mutant W139A, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, pH 7.5, temperature not specified in the publication


proof_lines: mutant W139F, pH 7.5, temperature not specified in the publication


proof_lines: mutant Y140F, pH 7.5, temperature not specified in the publication


proof_lines: mutant W139I, pH 7.5, temperature not specified in the publication


proof_lines:
pH 7.5, 37°C, mutant enzyme F190W
mutant F190W, pH 7.5, 37°C


proof_lines:
pH 7.5, 37°C, mutant enzyme F190A
mutant F190A, pH 7.5, 37°C


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


proof_lines:
pH 7.5, 37°C, mutant enzyme A70V
mutant A70V, pH 7.5, 37°C


proof_lines:
pH 7.5, 37°C, mutant enzyme A70G
mutant A70G, pH 7.5, 37°C


enzyme_display_name: UniProt A0A1B0UHJ4

organism: Aspergillus terreus

enzyme: UniProt A0A1B0UHJ4


substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


substrate_name: (2E,6Z)-farnesyl diphosphate

substrate: (2E,6Z)-farnesyl diphosphate


enzyme_display_name: UniProt P29848

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: thiosulfate

enzyme: UniProt P29848

substrate: thiosulfate


substrate_name: O-acetyl-L-serine

smiles: CC(=O)OCC(C(=O)O)N

substrate: O-acetyl-L-serine


organism: Thermotoga maritima


enzyme_display_name: all-trans-nonaprenyl diphosphate synthase [geranyl-diphosphate specific]

organism: Micrococcus luteus


substrate_name: farnesyl diphosphate

enzyme: all-trans-nonaprenyl diphosphate synthase [geranyl-diphosphate specific]

substrate: farnesyl diphosphate


substrate_name: farnesyl phosphosulfate

smiles: CCC(C)CCCC(C)CCCC(C)COS(=O)(=O)OP(=O)=O

substrate: farnesyl phosphosulfate


substrate_name: Geranyl phosphosulfate

smiles: CC(=CCCC(=CC(=O)OS(=O)(=O)OP(=O)=O)C)C

substrate: Geranyl phosphosulfate


enzyme_display_name: 4-O-dimethylallyl-L-tyrosine synthase

organism: Aspergillus niger

enzyme: 4-O-dimethylallyl-L-tyrosine synthase


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: D-tyrosine

proof_lines:
at pH 7.5 and 37°C
pH 7.5, 37°C

substrate: D-tyrosine


substrate_name: alpha-methyl-L-tyrosine

substrate: alpha-methyl-L-tyrosine


substrate_name: dimethylallyl diphosphate

proof_lines: with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C

substrate: dimethylallyl diphosphate


substrate_name: geranylgeranyl diphosphate

protein_accession_database: NCBI Protein

sequence_source: GenBank AB006850.1 (protein_id BAA32241.1)

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

substrate: geranylgeranyl diphosphate


substrate_name: (2E,6E)-farnesyl diphosphate

proof_lines:
pH 7.5, 37°C, mutant enzyme N193A
mutant N193A, pH 7.5, 37°C

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]

organism: Trypanosoma cruzi


substrate_name: isopentenyl diphosphate

proof_lines: pH 7.4, 37°C, cosubstrate: farnesyl diphosphate

proof_lines: pH 7.4, 37°C, cosubstrate: geranyl diphosphate

proof_lines: pH 7.4, 37°C, cosubstrate: geranylgeranyl diphosphate

enzyme: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]

substrate: isopentenyl diphosphate


organism: Paracoccus denitrificans


substrate_name: all-E-geranylgeranyl diphosphate

substrate: all-E-geranylgeranyl diphosphate


organism: Plenodomus lingam

substrate_name: (2Z)-3-chlorobut-2-en-1-yl diphosphate

proof_lines: cosubstrate 4-hydroxyphenylalanine, pH 7.5, 37°C

proof_lines: cosubstrate 4-aminophenylalanine, pH 7.5, 37°C

substrate: (2Z)-3-chlorobut-2-en-1-yl diphosphate


proof_lines: with L-tyrosine as cosubstrate, at pH 7.5 and 35°C


organism: Cereibacter sphaeroides

substrate_name: (2E,6E,10E)-geranylgeranyl diphosphate

substrate: (2E,6E,10E)-geranylgeranyl diphosphate


substrate_name: geranyl geranyl diphosphate

substrate: geranyl geranyl diphosphate


substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


enzyme_display_name: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]

organism: Thermococcus kodakarensis


enzyme: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]


proof_lines: 65°C, cosubstrate: dimethylallyl diphosphate


enzyme_display_name: geranylfarnesyl diphosphate synthase

enzyme: geranylfarnesyl diphosphate synthase


substrate_name: all-trans-farnesyl diphosphate

proof_lines: pH 7.7, 37°C, in presence of high molecular mass faction

proof_lines: pH 7.7, 37°C, in absence of high molecular mass fraction

substrate: all-trans-farnesyl diphosphate


organism: Solanum lycopersicum


column_label: Table 2 columns Km, kcat, and kcat/Km for At-SPS2-delta / FPP give 6.89, 3.77, and 0.547.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 3.77 s^-1; Km 0.00689 mM; kcat/Km 547 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row At-SPS2-delta FPP: Km 6.89 +/- 0.74 microM; kcat 3.77 +/- 0.15 s^-1; kcat/Km 0.547 s^-1 microM^-1.

row_label: At-SPS2-delta / FPP / 500 microM IPP

table_label: Table 2. Kinetic Parameters of At-SPS2 and At-SPS2-delta


column_label: Table 2 columns Km, kcat, and kcat/Km for At-SPS2-delta / GGPP give 0.843, 2.33, and 2.77.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 2.33 s^-1; Km 0.000843 mM; kcat/Km 2770 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row At-SPS2-delta GGPP: Km 0.843 +/- 0.157 microM; kcat 2.33 +/- 0.13 s^-1; kcat/Km 2.77 s^-1 microM^-1.

row_label: At-SPS2-delta / GGPP / 100 microM IPP


smiles: C=C(C)CCOP(=O)(O)OP(=O)(O)O

column_label: Table 2 separates At-SPS2-delta IPP and At-SPS2 IPP rows; the exported tuple combines metrics across those rows.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 2.83 s^-1; Km 0.182 mM; kcat/Km 15.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 At-SPS2-delta IPP with 20 microM FPP: Km 182 +/- 30 microM, kcat 2.83 +/- 0.21 s^-1, kcat/Km 0.0155 s^-1 microM^-1. Full-length At-SPS2 IPP with 20 microM FPP: Km 248 +/- 40 microM and no kcat.

row_label: At-SPS2-delta IPP / 20 microM FPP vs At-SPS2 IPP / 20 microM FPP


organism: Homo sapiens

substrate_name: Isopentenyl diphosphate; trans,trans-Farnesyl diphosphate


enzyme_display_name: adenosyl-chloride synthase

organism: Streptomyces noursei

substrate_name: S-adenosyl-L-methionine

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

enzyme: adenosyl-chloride synthase

substrate: S-adenosyl-L-methionine


enzyme_display_name: (2Z,6Z)-farnesyl diphosphate synthase

organism: Plasmodium falciparum

proof_lines: pH 7.5, 37°C, recombinant enzyme, with dimethylallyl diphosphate

enzyme: (2Z,6Z)-farnesyl diphosphate synthase


proof_lines: pH 7.5, 37°C, recombinant enzyme, with isopentenyl diphosphate


substrate_name: methylallyl diphosphate

substrate: methylallyl diphosphate


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Umezawaea tangerina


organism: uncultured bacterium

proof_lines:
isoform ClA2, at pH 7.8 and 37°C
isoform ClA1, at pH 7.8 and 37°C


proof_lines:
isoform ClA1, at pH 7.8 and 37°C
isoform ClA2, at pH 7.8 and 37°C


organism: Streptantibioticus cattleyicolor

proof_lines: 37°C, direct displacement reaction in the absence of L-methionine or S-adenosyl-L-methionine, pH not specified in the publication


substrate_name: L-o-tyrosine

substrate: L-o-tyrosine


enzyme_display_name: aspartate transaminase

organism: Bubalus bubalis

substrate_name: L-aspartate

enzyme: aspartate transaminase

substrate: L-aspartate


enzyme_display_name: UniProt P00509

organism: Escherichia coli

substrate_name: L-glutamate

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

enzyme: UniProt P00509

substrate: L-glutamate


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=8


substrate_name: L-cysteine

smiles: C(C(C(=O)O)N)S

substrate: L-cysteine


substrate_name: L-Phe

assay_conditions_summary: pH 8

substrate: L-Phe


enzyme_display_name: UniProt Q4D080

enzyme: UniProt Q4D080


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-methionine

smiles: CSCCC(C(=O)O)N

substrate: L-methionine


enzyme_display_name: Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase

organism: Comamonas testosteroni


enzyme_display_name: UniProt P52894

organism: Hordeum vulgare

substrate_name: pyruvate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=20°C, pH=8

enzyme: UniProt P52894

substrate: pyruvate


substrate_name: L-alanine

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

substrate: L-alanine


enzyme_display_name: UniProt H8WR05

organism: Variovorax paradoxus

substrate_name: (S)-beta-phenylalanine

enzyme: UniProt H8WR05

substrate: (S)-beta-phenylalanine


organism: Streptomyces sp.

column_label: Table 1. Steady-state kinetic parameters of Fur7; row 1,3-DHN / GPP; column(s) kcat x 10^3; Aromatic substrate Km; kcat/Km computed from exact table kcat and Km cells plus rounded M^-1 s^-1 table value

normalized_value_unit_evidence: kcat normalized_value=0.00013 normalized_unit=s^-1; Km normalized_value=0.32 normalized_unit=mM; kcat/Km normalized_value=0.00040625 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.13 +/- 0.05 in kcat x 10^3 s^-1 raw_unit=s^-1; Km raw_value=0.32 +/- 0.02 raw_unit=mM; kcat/Km raw_value=0.41 M^-1 s^-1 raw_unit=s^-1*mM^-1; kcat/Km computed_from_table_kcat_km=0.00013/0.32 raw_unit=s^-1*mM^-1

row_label: 1,3-DHN / GPP


column_label: Table 1. Steady-state kinetic parameters of Fur7; row compound 4 (2-methoxy-3-methylflaviolin) / GPP; Table 1 first row printed as Fur-P1; column(s) kcat x 10^3; Aromatic substrate Km; kcat/Km computed from exact table kcat and Km cells plus rounded M^-1 s^-1 table value

normalized_value_unit_evidence: kcat normalized_value=0.00066 normalized_unit=s^-1; Km normalized_value=0.054 normalized_unit=mM; kcat/Km normalized_value=0.0122222222222222 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.66 +/- 0.02 in kcat x 10^3 s^-1 raw_unit=s^-1; Km raw_value=0.054 +/- 0.005 raw_unit=mM; kcat/Km raw_value=12 M^-1 s^-1 raw_unit=s^-1*mM^-1; kcat/Km computed_from_table_kcat_km=0.00066/0.054 raw_unit=s^-1*mM^-1


substrate_name: flaviolin

column_label: Table 1. Steady-state kinetic parameters of Fur7; row Flaviolin 1 / GPP; column(s) kcat x 10^3; Aromatic substrate Km; kcat/Km computed from exact table kcat and Km cells plus rounded M^-1 s^-1 table value

normalized_value_unit_evidence: kcat normalized_value=0.028 normalized_unit=s^-1; Km normalized_value=0.048 normalized_unit=mM; kcat/Km normalized_value=0.583333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=28 +/- 3 in kcat x 10^3 s^-1 raw_unit=s^-1; Km raw_value=0.048 +/- 0.002 raw_unit=mM; kcat/Km raw_value=580 M^-1 s^-1 raw_unit=s^-1*mM^-1; kcat/Km computed_from_table_kcat_km=0.028/0.048 raw_unit=s^-1*mM^-1

row_label: Flaviolin 1 / GPP

substrate: flaviolin


substrate_name: geranyl diphosphate

column_label: Table 1. Steady-state kinetic parameters of Fur7; row Flaviolin 1 / GPP; column(s) Prenyl donor Km for GPP

raw_value_unit_evidence: Km raw_value=0.059 +/- 0.010 raw_unit=mM

substrate: geranyl diphosphate


substrate_name: dimethylallyl diphosphate

column_label: Table 1. Steady-state kinetic parameters of Fur7; row Flaviolin 1 / DMAPP; column(s) Prenyl donor Km for DMAPP

raw_value_unit_evidence: Km raw_value=0.72 +/- 0.06 raw_unit=mM

row_label: Flaviolin 1 / DMAPP

substrate: dimethylallyl diphosphate


organism: Solanum habrochaites

proof_lines:
pH 7.6, 30°C, mutant zFPS-M2
pH 7.6, 30°C, mutant zFPS-M10


substrate_name: isopentenyl diphosphate

proof_lines:
pH 7.6, 30°C, mutant zFPS-M10
pH 7.6, 30°C, mutant zFPS-M2

substrate: isopentenyl diphosphate


substrate_name: neryl diphosphate

substrate: neryl diphosphate


enzyme_display_name: Polyamine aminopropyltransferase

organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: norspermidine (at pH 9 and 37 degrees Celsius)

smiles: C(CN)CNCCCN

assay_conditions_summary: pH 9

proof_lines: kcat is 0.73 sec(-1) for aminopropyl transferase activity with S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees Celsius). kcat is 0.65 sec(-1) for aminopropyl transferase activity with spermidine as substrate (at pH 9 and 37 de

enzyme: Polyamine aminopropyltransferase


substrate_name: S-adenosylmethioninamine (at pH 9 and 37 degrees Celsius)


substrate_name: spermidine (at pH 9 and 37 degrees Celsius)

smiles: C(CCNCCCN)CN


substrate_name: mitsubishine (at pH 9 and 37 degrees Celsius)

smiles: C(CN)CN(CCCN)CCCN