column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Cinnamate'; column 'Km (uM)' = 54.4; column 'Vmax (pkat mg^-1)' = 300; column 'Kcat (min^-1)' = 1.02; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 312.

normalized_value_unit_evidence: Km: printed Table I cell 54.4 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 54.4 / 1000 = 0.0544 mM; the exported value is 0.0544 mM. kcat: printed Table I cell 1.02 min^-1 (the Kcat column header prints 'min^-1'); 1.02 / 60 = 0.017 s^(-1); the exported value is 1.02 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 312 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 312 / 1000 = 0.312 s^(-1)*mM^(-1); the exported value is 18.75 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Cinnamate': Km = 54.4 uM; Vmax = 300 pkat mg^-1; Kcat = 1.02 min^-1; printed Kenz = Kcat/Km = 312 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Cinnamate' (catalog accession Q6ZAC1)


enzyme_display_name: trans-feruloyl-CoA synthase

organism: Oryza sativa subsp. japonica

source_db: uniprot

verification_status: corrected

ki_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.

assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row '4-Coumarate'; column 'Km (uM)' = 10.3; column 'Vmax (pkat mg^-1)' = 830; column 'Kcat (min^-1)' = 2.88; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 4660.

normalized_value_unit_evidence: Km: printed Table I cell 10.3 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 10.3 / 1000 = 0.0103 mM; the exported value is 0.0103 mM. kcat: printed Table I cell 2.88 min^-1 (the Kcat column header prints 'min^-1'); 2.88 / 60 = 0.048 s^(-1); the exported value is 2.88 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 4660 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 4660 / 1000 = 4.66 s^(-1)*mM^(-1); the exported value is 279.6116504854369 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row '4-Coumarate': Km = 10.3 uM; Vmax = 830 pkat mg^-1; Kcat = 2.88 min^-1; printed Kenz = Kcat/Km = 4660 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row '4-Coumarate' (catalog accession Q6ZAC1)

data_origin: experimental

enzyme: trans-feruloyl-CoA synthase

status: corrected

source: uniprot


substrate_name: caffeate

column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Caffeate'; column 'Km (uM)' = 26.1; column 'Vmax (pkat mg^-1)' = 240; column 'Kcat (min^-1)' = 0.84; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 535.

normalized_value_unit_evidence: Km: printed Table I cell 26.1 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 26.1 / 1000 = 0.0261 mM; the exported value is 0.0261 mM. kcat: printed Table I cell 0.84 min^-1 (the Kcat column header prints 'min^-1'); 0.84 / 60 = 0.014 s^(-1); the exported value is 0.84 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 535 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 535 / 1000 = 0.535 s^(-1)*mM^(-1); the exported value is 32.183908045977006 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Caffeate': Km = 26.1 uM; Vmax = 240 pkat mg^-1; Kcat = 0.84 min^-1; printed Kenz = Kcat/Km = 535 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Caffeate' (catalog accession Q6ZAC1)

substrate: caffeate


substrate_name: ferulate

column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Ferulate'; column 'Km (uM)' = 6.9; column 'Vmax (pkat mg^-1)' = 590; column 'Kcat (min^-1)' = 2.04; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 4871.

normalized_value_unit_evidence: Km: printed Table I cell 6.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 6.9 / 1000 = 0.006900000000000001 mM; the exported value is 0.006900000000000001 mM. kcat: printed Table I cell 2.04 min^-1 (the Kcat column header prints 'min^-1'); 2.04 / 60 = 0.034 s^(-1); the exported value is 2.04 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 4871 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 4871 / 1000 = 4.871 s^(-1)*mM^(-1); the exported value is 295.65217391304344 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Ferulate': Km = 6.9 uM; Vmax = 590 pkat mg^-1; Kcat = 2.04 min^-1; printed Kenz = Kcat/Km = 4871 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Ferulate' (catalog accession Q6ZAC1)

substrate: ferulate


substrate_name: sinapate

column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Sinapate'; column 'Km (uM)' = 58.9; column 'Vmax (pkat mg^-1)' = 920; column 'Kcat (min^-1)' = 3.18; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 899.

normalized_value_unit_evidence: Km: printed Table I cell 58.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 58.9 / 1000 = 0.0589 mM; the exported value is 0.0589 mM. kcat: printed Table I cell 3.18 min^-1 (the Kcat column header prints 'min^-1'); 3.18 / 60 = 0.053000000000000005 s^(-1); the exported value is 3.18 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 899 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 899 / 1000 = 0.899 s^(-1)*mM^(-1); the exported value is 53.98981324278438 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Sinapate': Km = 58.9 uM; Vmax = 920 pkat mg^-1; Kcat = 3.18 min^-1; printed Kenz = Kcat/Km = 899 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Sinapate' (catalog accession Q6ZAC1)

substrate: sinapate


substrate_name: cinnamate

column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row 'Cinnamate'; column 'Km (uM)' = 9.4; column 'Vmax (pkat mg^-1)' = 100; column 'Kcat (min^-1)' = 0.37; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 663.

normalized_value_unit_evidence: Km: printed Table I cell 9.4 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 9.4 / 1000 = 0.0094 mM; the exported value is 0.0094 mM. kcat: printed Table I cell 0.37 min^-1 (the Kcat column header prints 'min^-1'); 0.37 / 60 = 0.006166666666666667 s^(-1); the exported value is 0.37 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 663 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 663 / 1000 = 0.663 s^(-1)*mM^(-1); the exported value is 39.36170212765957 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row 'Cinnamate': Km = 9.4 uM; Vmax = 100 pkat mg^-1; Kcat = 0.37 min^-1; printed Kenz = Kcat/Km = 663 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row 'Cinnamate' (catalog accession P17814)

substrate: cinnamate


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row '4-Coumarate'; column 'Km (uM)' = 11.9; column 'Vmax (pkat mg^-1)' = 130; column 'Kcat (min^-1)' = 0.49; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 681.

normalized_value_unit_evidence: Km: printed Table I cell 11.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 11.9 / 1000 = 0.0119 mM; the exported value is 0.0119 mM. kcat: printed Table I cell 0.49 min^-1 (the Kcat column header prints 'min^-1'); 0.49 / 60 = 0.008166666666666666 s^(-1); the exported value is 0.49 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 681 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 681 / 1000 = 0.681 s^(-1)*mM^(-1); the exported value is 41.17647058823529 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row '4-Coumarate': Km = 11.9 uM; Vmax = 130 pkat mg^-1; Kcat = 0.49 min^-1; printed Kenz = Kcat/Km = 681 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row '4-Coumarate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row 'Caffeate'; column 'Km (uM)' = 29.3; column 'Vmax (pkat mg^-1)' = 140; column 'Kcat (min^-1)' = 0.52; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 296.

normalized_value_unit_evidence: Km: printed Table I cell 29.3 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 29.3 / 1000 = 0.0293 mM; the exported value is 0.0293 mM. kcat: printed Table I cell 0.52 min^-1 (the Kcat column header prints 'min^-1'); 0.52 / 60 = 0.008666666666666666 s^(-1); the exported value is 0.52 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 296 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 296 / 1000 = 0.296 s^(-1)*mM^(-1); the exported value is 17.747440273037544 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row 'Caffeate': Km = 29.3 uM; Vmax = 140 pkat mg^-1; Kcat = 0.52 min^-1; printed Kenz = Kcat/Km = 296 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row 'Caffeate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row 'Ferulate'; column 'Km (uM)' = 8.3; column 'Vmax (pkat mg^-1)' = 110; column 'Kcat (min^-1)' = 0.41; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 824.

normalized_value_unit_evidence: Km: printed Table I cell 8.3 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 8.3 / 1000 = 0.0083 mM; the exported value is 0.0083 mM. kcat: printed Table I cell 0.41 min^-1 (the Kcat column header prints 'min^-1'); 0.41 / 60 = 0.006833333333333333 s^(-1); the exported value is 0.41 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 824 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 824 / 1000 = 0.824 s^(-1)*mM^(-1); the exported value is 49.39759036144578 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row 'Ferulate': Km = 8.3 uM; Vmax = 110 pkat mg^-1; Kcat = 0.41 min^-1; printed Kenz = Kcat/Km = 824 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row 'Ferulate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row 'Cinnamate'; column 'Km (uM)' = 21.7; column 'Vmax (pkat mg^-1)' = 299; column 'Kcat (min^-1)' = 1.13; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 867.

normalized_value_unit_evidence: Km: printed Table I cell 21.7 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 21.7 / 1000 = 0.0217 mM; the exported value is 0.0217 mM. kcat: printed Table I cell 1.13 min^-1 (the Kcat column header prints 'min^-1'); 1.13 / 60 = 0.01883333333333333 s^(-1); the exported value is 1.13 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 867 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 867 / 1000 = 0.867 s^(-1)*mM^(-1); the exported value is 52.073732718894 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row 'Cinnamate': Km = 21.7 uM; Vmax = 299 pkat mg^-1; Kcat = 1.13 min^-1; printed Kenz = Kcat/Km = 867 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row 'Cinnamate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row '4-Coumarate'; column 'Km (uM)' = 16.8; column 'Vmax (pkat mg^-1)' = 629; column 'Kcat (min^-1)' = 2.37; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 2351.

normalized_value_unit_evidence: Km: printed Table I cell 16.8 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 16.8 / 1000 = 0.016800000000000002 mM; the exported value is 0.016800000000000002 mM. kcat: printed Table I cell 2.37 min^-1 (the Kcat column header prints 'min^-1'); 2.37 / 60 = 0.0395 s^(-1); the exported value is 2.37 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 2351 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 2351 / 1000 = 2.351 s^(-1)*mM^(-1); the exported value is 141.07142857142856 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row '4-Coumarate': Km = 16.8 uM; Vmax = 629 pkat mg^-1; Kcat = 2.37 min^-1; printed Kenz = Kcat/Km = 2351 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row '4-Coumarate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row 'Caffeate'; column 'Km (uM)' = 27.6; column 'Vmax (pkat mg^-1)' = 708; column 'Kcat (min^-1)' = 2.67; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 1612.

normalized_value_unit_evidence: Km: printed Table I cell 27.6 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 27.6 / 1000 = 0.027600000000000003 mM; the exported value is 0.0216 mM. kcat: printed Table I cell 2.67 min^-1 (the Kcat column header prints 'min^-1'); 2.67 / 60 = 0.0445 s^(-1); the exported value is 2.67 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 1612 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 1612 / 1000 = 1.612 s^(-1)*mM^(-1); the exported value is 123.6111111111111 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row 'Caffeate': Km = 27.6 uM; Vmax = 708 pkat mg^-1; Kcat = 2.67 min^-1; printed Kenz = Kcat/Km = 1612 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row 'Caffeate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row 'Ferulate'; column 'Km (uM)' = 2.2; column 'Vmax (pkat mg^-1)' = 613; column 'Kcat (min^-1)' = 2.31; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 17295.

normalized_value_unit_evidence: Km: printed Table I cell 2.2 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 2.2 / 1000 = 0.0022 mM; the exported value is 0.0022 mM. kcat: printed Table I cell 2.31 min^-1 (the Kcat column header prints 'min^-1'); 2.31 / 60 = 0.0385 s^(-1); the exported value is 2.31 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 17295 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 17295 / 1000 = 17.295 s^(-1)*mM^(-1); the exported value is 1050.0 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row 'Ferulate': Km = 2.2 uM; Vmax = 613 pkat mg^-1; Kcat = 2.31 min^-1; printed Kenz = Kcat/Km = 17295 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row 'Ferulate' (catalog accession Q42982)


enzyme_display_name: ribose-5-phosphate isomerase

organism: Cyberlindnera jadinii

substrate_name: D-ribose 5-phosphate

source_db: brenda

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

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

proof_lines:
enzyme form III
enzyme form II
enzyme form I

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate

status: unverified

source: brenda


enzyme_display_name: UDP-glucose 4-epimerase

organism: Davallia divaricata

substrate_name: UDP-alpha-D-galactose

proof_lines: DdUGE1, pH and temperature not specified in the publication

proof_lines: DdUGE2, pH and temperature not specified in the publication

enzyme: UDP-glucose 4-epimerase

substrate: UDP-alpha-D-galactose


enzyme_display_name: 4-chlorobenzoate--CoA ligase

organism: Arthrobacter sp

verification_status: verified

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

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

column_label: PMID 15068371 abstract; enzyme 4-chlorobenzoate:CoA ligase; substrate 4-chlorobenzoate; metric apparent Km; raw value 3.5 microM; normalized value 0.0035 mM.

normalized_value_unit_evidence: 3.5 microM normalized to 0.0035 mM.

raw_value_unit_evidence: PubMed abstract reports apparent Km for 4-chlorobenzoate = 3.5 microM.

row_label: 4-chlorobenzoate:CoA ligase / 4-chlorobenzoate apparent Km

table_label: PubMed abstract prose (PMID 15068371)

enzyme: 4-chlorobenzoate--CoA ligase

status: verified


substrate_name: CoA

column_label: PMID 15068371 abstract; enzyme 4-chlorobenzoate:CoA ligase; substrate CoA; metric apparent Km; raw value 30 microM; normalized value 0.03 mM.

normalized_value_unit_evidence: 30 microM normalized to 0.03 mM.

raw_value_unit_evidence: PubMed abstract reports apparent Km for CoA = 30 microM.

row_label: 4-chlorobenzoate:CoA ligase / CoA apparent Km

substrate: CoA


substrate_name: ATP

column_label: PMID 15068371 abstract; enzyme 4-chlorobenzoate:CoA ligase; substrate ATP; metric apparent Km; raw value 238 microM; normalized value 0.238 mM.

normalized_value_unit_evidence: 238 microM normalized to 0.238 mM.

raw_value_unit_evidence: PubMed abstract reports apparent Km for ATP = 238 microM.

row_label: 4-chlorobenzoate:CoA ligase / ATP apparent Km

substrate: ATP


enzyme_display_name: maltose alpha-D-glucosyltransferase

organism: Deinococcus radiodurans

substrate_name: maltose

proof_lines: pH 7.6, 30°C, recombinant His6-tagged enzyme

enzyme: maltose alpha-D-glucosyltransferase

substrate: maltose


enzyme_display_name: cellobiose epimerase

organism: Dictyoglomus thermophilum

substrate_name: cellobiose

enzyme: cellobiose epimerase

substrate: cellobiose


organism: Dianthus caryophyllus

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Pyrobaculum neutrophilum


organism: Pseudomonas sp.

sequence_source: multiple

source_databases_merged: brenda uniprot


assay_conditions_summary: cofactor CoA


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

assay_conditions_summary: cofactor ATP


source_db: oed

kcat_over_km_origin: calculated

source: oed


substrate_name: Coenzyme A

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: Coenzyme A


substrate_name: Toluate

substrate: Toluate


substrate_name: benzoate

substrate: benzoate


enzyme_display_name: 3-hydroxypropionyl-CoA synthase

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

enzyme: 3-hydroxypropionyl-CoA synthase


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.3; 295.15 K; cofactor CoA

proof_lines: kcat is 7.1 sec(-1) for ligase activity with HIP. kcat is 7.5 sec(-1) for ligase activity with CoASH (at pH 7.3 and 22 degrees Celsius). kcat is 13 sec(-1) for ligase activity with 5alpha-OH HIP (at pH 7.3 and 22 degrees Celsius).


organism: Streptomyces carzinostaticus

substrate_name: 2-hydroxynaphthalene-1-carboxylic acid

proof_lines: pH and temperature not specified in the publication

substrate: 2-hydroxynaphthalene-1-carboxylic acid


substrate_name: Naphthalene-1-carboxylic acid

substrate: Naphthalene-1-carboxylic acid


proof_lines: kcat is 38 min(-1) with 2-hydroxy-7-methoxy-5-methyl-1-naphthoate as substrate. kcat is 8.1 min(-1) with 2-hydroxy-5-methyl-1-naphthoate as substrate. kcat is 93 min(-1) with 2,7-dihydroxy-5-methyl-1-naphthoate as substrate.


organism: Metallosphaera sedula

sequence_source: UniProt A4YDR9

smiles: O=C(O)CCCO

assay_conditions_summary: pH 7.9; 348.15 K; cofactor CoA


enzyme_display_name: 3-(methylthio)propionate--CoA ligase

organism: Ruegeria pomeroyi

substrate_name: Butyrate

sequence_source: UniProt Q5LRT0

smiles: CCCC(=O)O

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

enzyme: 3-(methylthio)propionate--CoA ligase

substrate: Butyrate


smiles: CSCCC(=O)O


substrate_name: propionate

substrate: propionate


substrate_name: Acrylate

substrate: Acrylate


organism: Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)

substrate_name: Unknown

km_display: Not reported

proof_lines: kcat is 16.2 sec(-1) for ligase activity with propionate as substrate. kcat is 8.4 sec(-1) for ligase activity with butyrate as substrate. kcat is 6.4 sec(-1) for ligase activity with acetate as substrate. kcat is 5.6 sec(-1) for ligase act

substrate: Unknown


proof_lines: kcat is 0.24 sec(-1) for ligase activity with 4HB as substrate. kcat is 0.23 sec(-1) for ligase activity with butyrate as substrate. kcat is 0.22 sec(-1) for ligase activity with valerate as substrate. kcat is 0.21 sec(-1) for ligase activi


enzyme_display_name: 3-oxocholest-4-en-26-oate--CoA ligase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

assay_conditions_summary: pH 7.3; cofactor CoA

proof_lines: kcat is 0.75 sec(-1) for 3-oxo-4-cholesten-26-oate--CoA ligase activity (at pH 7.3 and 22 degrees Celsius).

enzyme: 3-oxocholest-4-en-26-oate--CoA ligase


organism: Mycolicibacterium smegmatis

ki_unit: mM


substrate_name: 3-oxo-4-cholesten-26-oate (at pH 7.3 and 22 degrees Celsius)


organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)

proof_lines: kcat is 14.9 sec(-1) for ligase activity with MMPA as substrate. kcat is 7.2 sec(-1) for ligase activity with butyrate as substrate. kcat is 3.7 sec(-1) for ligase activity with propionate as substrate. kcat is 1 sec(-1) for ligase activity


enzyme_display_name: L-allo-isoleucine--holo-[CmaA peptidyl-carrier protein] ligase

organism: Pseudomonas savastanoi pv. glycinea

substrate_name: DL-coronamic acid (at pH 7.5 and 25 degrees Celsius)

proof_lines: kcat is 17 min(-1) for ligase activity with L-allo-isoleucine as substrate (at pH 7.5 and 25 degrees Celsius). kcat is 16 min(-1) for ligase activity with L-leucine as substrate (at pH 7.5 and 25 degrees Celsius). kcat is 12 min(-1) for lig


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W424G with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

mutation_type: substitution


organism: Candidatus Pelagibacter ubique

column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column PU_DmdB1; row MMPA; columns kcat; kcat/Km; Km; kcat raw_value=29.4 raw_unit=s^-1; kcat/Km raw_value=735 raw_unit=s^-1*mM^-1; Km raw_value=0.04 +/- 0.01 raw_unit=mM

normalized_value_unit_evidence: kcat normalized_value=29.4 normalized_unit=s^-1; kcat/Km normalized_value=735 normalized_unit=s^-1*mM^-1; Km normalized_value=0.04 normalized_unit=mM

row_label: MMPA


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column PU_DmdB1; row Acrylate; columns kcat; kcat/Km; Km; kcat raw_value=22.3 raw_unit=s^-1; kcat/Km raw_value=50 raw_unit=s^-1*mM^-1; Km raw_value=0.44 +/- 0.04 raw_unit=mM

normalized_value_unit_evidence: kcat normalized_value=22.3 normalized_unit=s^-1; kcat/Km normalized_value=50 normalized_unit=s^-1*mM^-1; Km normalized_value=0.44 normalized_unit=mM

row_label: Acrylate


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column PU_DmdB1; row Butyrate; columns kcat; kcat/Km; Km; kcat raw_value=43.8 raw_unit=s^-1; kcat/Km raw_value=3,370 raw_unit=s^-1*mM^-1; Km raw_value=0.01 +/- 0.01 raw_unit=mM

normalized_value_unit_evidence: kcat normalized_value=43.8 normalized_unit=s^-1; kcat/Km normalized_value=3370 normalized_unit=s^-1*mM^-1; Km normalized_value=0.01 normalized_unit=mM

row_label: Butyrate


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column PU_DmdB1; row propionate; columns kcat; kcat/Km; Km; kcat raw_value=17.7 raw_unit=s^-1; kcat/Km raw_value=505 raw_unit=s^-1*mM^-1; Km raw_value=0.04 +/- 0.02 raw_unit=mM

normalized_value_unit_evidence: kcat normalized_value=17.7 normalized_unit=s^-1; kcat/Km normalized_value=505 normalized_unit=s^-1*mM^-1; Km normalized_value=0.04 normalized_unit=mM

row_label: propionate


organism: Candidatus Pelagibacter communis


assay_conditions_summary: pH 7.5; cofactor CoA

column_label: Table 4 row PU_DmdB1 with MMPA gives Km 0.04 mM, kcat 29.4 s^-1, and kcat/Km 735 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.04 normalized_unit=mM; kcat normalized_value=29.4 normalized_unit=s^-1; kcat/Km normalized_value=735 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=0.04 mM; kcat raw_value=29.4 s^-1; kcat/Km raw_value=735 s^-1 mM^-1

row_label: PU_DmdB1 / MMPA (3-(methylthio)propanoate)

table_label: Official PMC full-text Table 4: Apparent kinetic constants for DmdBs


smiles: CCCC(=O)[O-]


organism: Unknown prokaryotic organism

substrate_name: ferulate

column_label: Full text reports the FCS1 Km and Vmax values were 0.1 mM and 36.8 U/mg and Table 1 lists Km 0.1 for the unknown lignin consortium enzyme.

raw_value_unit_evidence: Km raw_value=0.1 mM raw_unit=mM

row_label: FCS1 feruloyl-CoA synthetase / ferulate

table_label: PMC full text Table 1 PMID 30802241

substrate: ferulate


organism: Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157)

substrate_name: MMPA

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

assay_conditions_summary: pH 8

column_label: Table 3. Km values of wild type DmdB and its mutants to different substrates; row Wild type DmdB / To MMPA; column Km to MMPA (mM); raw cell 0.2 +/- 0.02 mM; normalized Km 0.2 mM

normalized_value_unit_evidence: Km=0.2 mM

raw_value_unit_evidence: Wild type DmdB / To MMPA: Km to MMPA (mM)=0.2 +/- 0.02 mM

row_label: Wild type DmdB / To MMPA

substrate: MMPA


substrate_name: ATP

assay_conditions_summary: pH 8; cofactor ATP

column_label: Table 3. Km values of wild type DmdB and its mutants to different substrates; row Wild type DmdB / To ATP; column Km to ATP (mM); raw cell 0.8 +/- 0.05 mM; normalized Km 0.8 mM

normalized_value_unit_evidence: Km=0.8 mM

raw_value_unit_evidence: Wild type DmdB / To ATP: Km to ATP (mM)=0.8 +/- 0.05 mM

row_label: Wild type DmdB / To ATP


substrate_name: CoA

assay_conditions_summary: pH 8; cofactor CoA

column_label: Table 3. Km values of wild type DmdB and its mutants to different substrates; row Wild type DmdB / To CoA; column Km to CoA (mM); raw cell 0.4 +/- 0.01 mM; normalized Km 0.4 mM

normalized_value_unit_evidence: Km=0.4 mM

raw_value_unit_evidence: Wild type DmdB / To CoA: Km to CoA (mM)=0.4 +/- 0.01 mM

row_label: Wild type DmdB / To CoA


assay_conditions_summary: pH 7.5; 343.15 K; cofactor CoA


organism: Ruegeria lacuscaerulensis

smiles: CSCCC(=O)[O-]

assay_conditions_summary: pH 8; 313.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H231A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K526A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K434A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; 313.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G303P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W326A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D435A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W443A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G441P with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E474A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K438A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E442A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R432A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G440P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P333A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W235A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G302P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W424G with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 8; 297.15 K; cofactor ATP

column_label: PMID 17539640 main article, page 7729, Table 1; row label compound 11 (the 1-naphthoate source row); columns Km (microM), kcat (min^-1), and rel kcat/Km; raw cells 18 +/- 9, 6.7 +/- 1.4, and 5.8 x 10^-3.

normalized_value_unit_evidence: Km 18 microM = 0.018 mM; kcat 6.7 min^-1 / 60 = 0.1116666666666666666666666667 s^-1; the absolute kcat/Km from those same printed central cells is 0.1116666666666666666666666667 / 0.018 = 6.203703703703703703703703704 s^-1 mM^-1. The printed 5.8 x 10^-3 column is relative kcat/Km and is retained only as a row cross-check.

raw_value_unit_evidence: Main-article Table 1 row 11 prints Km 18 +/- 9 microM, kcat 6.7 +/- 1.4 min^-1, and relative kcat/Km 5.8 x 10^-3.

row_label: compound 11 / 1-naphthoate source identity

table_label: JACS 2007 Table 1, Naphthoic Acid Substrate Scope of the NcsB2 CoA Ligase


organism: Pseudomonas syringae

substrate_name: L-allo-isoleucine

column_label: Table 2: Kinetic parameters for CmaA-FLAG as determined by the forward PPi assay; row L-allo-Isoleucine; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); 0.04 +/- 0.01 mM; 0.09 +/- 0.00 min^-1; kcat/Km 2.3 min^-1 mM^-1.

enzyme: L-allo-isoleucine--holo-[CmaA peptidyl-carrier protein] ligase

substrate: L-allo-isoleucine


substrate_name: L-leucine

column_label: Table 2: Kinetic parameters for CmaA-FLAG as determined by the forward PPi assay; row L-Leucine; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); 1.5 +/- 0.1 mM; 1.8 +/- 0.1 min^-1; kcat/Km 1.2 min^-1 mM^-1.

row_label: L-Leucine; Km/kcat/kcat/Km columns

substrate: L-leucine


substrate_name: L-Valine

column_label: Table 2: Kinetic parameters for CmaA-FLAG as determined by the forward PPi assay; row L-Valine; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); 1.2 +/- 0.1 mM; 1.4 +/- 0.1 min^-1; kcat/Km 1.2 min^-1 mM^-1.

row_label: L-Valine; Km/kcat/kcat/Km columns

substrate: L-Valine


substrate_name: L-Isoleucine

column_label: Table 2: Kinetic parameters for CmaA-FLAG as determined by the forward PPi assay; row L-Isoleucine; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); 0.50 +/- 0.06 mM; 0.71 +/- 0.03 min^-1; kcat/Km 1.4 min^-1 mM^-1.

row_label: L-Isoleucine; Km/kcat/kcat/Km columns

substrate: L-Isoleucine


substrate_name: CoA (with MMPA)

substrate: CoA (with MMPA)


substrate_name: ATP (with MMPA)

substrate: ATP (with MMPA)


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column RPO_DmdB2; row MMPA; columns Km; Km raw_value=0.07 +/- 0.02 raw_unit=mM

raw_value_unit_evidence: Km raw_value=0.07 +/- 0.02 raw_unit=mM


substrate_name: butyrate

column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column RPO_DmdB2; row butyrate; columns Km; Km raw_value=0.12 +/- 0.03 raw_unit=mM

raw_value_unit_evidence: Km raw_value=0.12 +/- 0.03 raw_unit=mM

row_label: butyrate

substrate: butyrate


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column RPO_DmdB2; row propionate; columns Km; Km raw_value=3.11 +/- 1.13 raw_unit=mM

raw_value_unit_evidence: Km raw_value=3.11 +/- 1.13 raw_unit=mM


substrate_name: acrylate

column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column RPO_DmdB2; row acrylate; columns Km; Km raw_value=5.25 +/- 2.1 raw_unit=mM

raw_value_unit_evidence: Km raw_value=5.25 +/- 2.1 raw_unit=mM

row_label: acrylate

substrate: acrylate


enzyme_display_name: E1 ubiquitin-activating enzyme

organism: Homo sapiens

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

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, mutant enzyme D576E

proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, mutant enzyme D576E

enzyme: E1 ubiquitin-activating enzyme

substrate: ATP


substrate_name: ubiquitin

substrate: ubiquitin


substrate_name: ubiquitin carrier protein E2

substrate: ubiquitin carrier protein E2


proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, mutant enzyme D576N

proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, mutant enzyme D576N


proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, mutant enzyme K528A

proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, mutant enzyme K528A


proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, mutant enzyme D576A

proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, mutant enzyme D576A


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

proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, wild-type enzyme

proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, wild-type enzyme


substrate_name: Acrylate


substrate_name: propionate


assay_conditions_summary: pH 8.5; 318.15 K; cofactor ATP


substrate_name: Butyrate

substrate: Butyrate


substrate_name: valerate

smiles: CCCCC(=O)[O-]

substrate: valerate


substrate: propionate


substrate_name: acetate

substrate: acetate


substrate_name: Oregon Green-labeled ubiquitin

substrate: Oregon Green-labeled ubiquitin


substrate_name: ATP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


substrate_name: L-allo-isoleucine (at pH 7.5 and 25 degrees Celsius)

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


substrate_name: L-leucine (at pH 7.5 and 25 degrees Celsius)

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


substrate_name: L-valine (at pH 7.5 and 25 degrees Celsius)

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


organism: Dictyoglomus turgidum

substrate_name: lactose

proof_lines: purified recombinant His-tagged enzyme, pH 7.0, 70°C

proof_lines: pH and temperature not specified in the publication

substrate: lactose


enzyme_display_name: D-psicose 3-epimerase

organism: Dorea sp. CAG:317

substrate_name: D-fructose

enzyme: D-psicose 3-epimerase

substrate: D-fructose


organism: Diospyros kaki

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Dirofilaria immitis

proof_lines: in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C

proof_lines: recombinant His-tagged enzyme, pH 7.5, 30°C


organism: Echinococcus granulosus

substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


substrate_name: L-allo-isoleucine

proof_lines: pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH

substrate: L-allo-isoleucine


substrate_name: L-valine

substrate: L-valine


substrate_name: L-leucine

substrate: L-leucine


organism: Mycobacterium tuberculosis

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


organism: Dyadobacter fermentans


enzyme_display_name: UniProt Q8TBC4

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q8TBC4

source: skid


substrate_name: diphosphate

substrate: diphosphate


enzyme_display_name: L-firefly luciferin--CoA ligase

organism: Zophobas atratus

substrate_name: L-firefly luciferin

proof_lines: at pH 8.5, temperature not specified in the publication

enzyme: L-firefly luciferin--CoA ligase

substrate: L-firefly luciferin


assay_conditions_summary: pH 8.5; cofactor ATP

substrate: ATP


organism: Aquatica lateralis

substrate_name: Ketoprofen

substrate: Ketoprofen


organism: Photinus pyralis

assay_conditions_summary: 298.15 K; cofactor CoA

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


enzyme_display_name: (hydroxyamino)benzene mutase

organism: Ectopseudomonas oleovorans

substrate_name: (hydroxylamino)benzene

assay_conditions_summary: pH 7

enzyme: (hydroxyamino)benzene mutase

substrate: (hydroxylamino)benzene


organism: Enterobacter cloacae

substrate_name: N-acetylglucosamine 6-phosphate

substrate: N-acetylglucosamine 6-phosphate


organism: Pseudomonas aeruginosa (strain UCBPP-PA14)

substrate_name: L-cysteine

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

proof_lines: kcat is 415 min(-1) with L-cysteine as substrate.

substrate: L-cysteine


proof_lines: kcat is 38 min(-1) with L-cysteine as substrate.


enzyme_display_name: UniProt P10378

organism: Escherichia coli

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.8
Raw SKiD Env: Temp=37°C, pH=8

enzyme: UniProt P10378


organism: Pseudomonas syringae pv. syringae

substrate_name: L-serine

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

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

proof_lines: kcat is 29.1 min(-1) with L-threonine as substrate. kcat is 1.23 min(-1) with L-serine as substrate.

substrate: L-serine


substrate_name: L-threonine

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

substrate: L-threonine


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

substrate_name: MbtL-holo

assay_conditions_summary: pH 7.8; 298.15 K; buffer that applies to every line of the table; cofactor ATP

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'MbtL-holo'; column 'Km (uM)' = 106; column 'kcat (min^-1)' = 2.0; column 'kcat/Km (uM^-1 min^-1)' = 0.018. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 106 uM; 1 uM is one thousandth of 1 mM, so 106 / 1000 = 0.106 mM; the exported value is 0.106 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 2.0 min^-1; the printed head is per minute, so 2.0 / 60 = 0.03333333333333333 s^(-1); the proposed kcat is 0.03333333333333333 s^(-1). kcat/Km: printed Table 2 cell 0.018 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.018 times 1000 divided by 60 = 0.3 s^(-1)*mM^(-1); the proposed kcat/Km is 0.3 s^(-1)*mM^(-1). The live catalog row for this substrate holds no kcat/Km value, so the printed efficiency cell is recorded here as evidence only.

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'MbtL-holo': Km cell = 106 uM; kcat cell = 2.0 min^-1; printed kcat/Km cell = 0.018 uM^-1 min^-1.

table_label: Table 2: acyl chain length selectivity and kinetic parameters of FadD33 (J. Biol. Chem. 2013, 288(39):28116-28125), PDF page 5 of 10; printed column heads Enzyme/Substrate, Km (uM), kcat (min^-1) and kcat/Km (uM^-1 min^-1)

substrate: MbtL-holo


organism: Pseudomonas aeruginosa

substrate_name: L-Cysteine

substrate: L-Cysteine


enzyme_display_name: thioglycine synthase

organism: Methanosarcina acetivorans

substrate_name: RLGFFGFDLQD

enzyme: thioglycine synthase

substrate: RLGFFGFDLQD


organism: Streptomyces coelicolor

substrate_name: L-proline

substrate: L-proline


organism: Bacillus cereus

substrate_name: ATP

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


substrate_name: L-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C269A to reconstruct the assayed variant sequence.

substrate: L-alanine


substrate_name: D-Alanine

substrate: D-Alanine


enzyme_display_name: malonate--CoA ligase

organism: Rhizobium leguminosarum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H206L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: pH 7.0, 30°C, mutant enzyme H206L, cosubstrate: malonate

enzyme: malonate--CoA ligase


substrate_name: malonate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9ZIP5 and applied mutation signature H206L to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-state kinetic constants for MCS activities of the wild type and mutant GST-MCS enzymes (Biochem. J. 1999, 344, 159-166, journal page 162), printed substrate column heads Malonate | ATP | CoA and printed metric row heads Km (uM) | kcat (s-1) | kcat/Km (mM-1 s-1); enzyme block 'H206L', Malonate column: Km cell = 8700 +/- 980; kcat cell = 0.53 +/- 0.28; kcat/Km cell = 0.11.

normalized_value_unit_evidence: Km: printed Table 2 cell 8700 uM; 8700 / 1000 = 8.7 mM; the exported value is 8.7 mM. kcat: printed Table 2 cell 0.53 s-1; the printed unit s-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 0.53 s^(-1); the exported value is 0.53 s^(-1). kcat/Km: printed Table 2 cell 0.11 under the column head kcat/Km (mM-1 s-1); mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.11 s^(-1)*mM^(-1); the exported value is 0.060919540229885064 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 2, enzyme block 'H206L', Malonate column: Km = 8700 +/- 980 uM; kcat = 0.53 +/- 0.28 s-1; kcat/Km = 0.11 under the printed column head kcat/Km (mM-1 s-1).

row_label: Table 2, enzyme block 'H206L', Malonate substrate column

substrate: malonate


substrate_name: CoA

substrate: CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K170M to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme K170M, cosubstrate: methylmalonate

proof_lines: pH 7.0, 30°C, mutant enzyme K170M, cosubstrate: malonate


substrate_name: methylmalonate

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

source_databases_merged: brenda oed

substrate: methylmalonate


assay_conditions_summary: pH 7; 303.15 K; buffer Assay condition: 100 mM potassium phosphate; cofactor ATP

column_label: Table 3  Steady-state kinetic constants for methyl MCS activities of the wild type and mutant GST-MCS enzymes; enzyme-form block 'Wild type'; column 'Methylmalonate'; metric line 'Km (uM)' = 373 +/- 19; metric line 'kcat (s^-1)' = 2.7 +/- 0.1; metric line 'kcat/Km (mM^-1 . s^-1)' = 7.2.

normalized_value_unit_evidence: kcat: paper cell 2.7 +/- 0.1 s^-1 -> 2.7 s^(-1) (no conversion); catalog holds 2.7 s^(-1). Km: paper cell 373 +/- 19 uM / 1000 = 0.373 mM; catalog holds 0.373 mM. kcat/Km: catalog 7.238605898123325 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells; the printed rounded cell 7.2 mM^-1 . s^-1 is documented in prose.

raw_value_unit_evidence: Table 3, Wild type block, Methylmalonate column: Km (uM) = 373 +/- 19; kcat (s^-1) = 2.7 +/- 0.1; kcat/Km (mM^-1 . s^-1) = 7.2 (rounded printed cell).

row_label: Table 3, enzyme-form block 'Wild type', column 'Methylmalonate'


proof_lines: pH 7.0, 30°C, wild-type enzyme, cosubstrate: methylmalonate

proof_lines: pH 7.0, 30°C, wild-type enzyme, cosubstrate: malonate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R168G/K170M to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme R168G/K170M, cosubstrate: malonate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R168G to reconstruct the assayed variant sequence.


proof_lines: pH 7.0, 30°C, mutant enzyme R168G, cosubstrate: methylmalonate

proof_lines: pH 7.0, 30°C, mutant enzyme R168G, cosubstrate: malonate


column_label: Table 2  Steady-state kinetic constants for MCS activities of the wild type and mutant GST-MCS enzymes; enzyme-form block 'Wild type'; column 'Malonate'; metric line 'Km (uM)' = 208 +/- 6; metric line 'kcat (s^-1)' = 19 +/- 0.3; metric line 'kcat/Km (mM^-1 . s^-1)' = 91.

normalized_value_unit_evidence: kcat: paper cell 19 +/- 0.3 s^-1 -> 19.0 s^(-1) (no conversion); catalog holds 19.0 s^(-1). Km: paper cell 208 +/- 6 uM / 1000 = 0.208 mM; catalog holds 0.208 mM. kcat/Km: catalog 91.34615384615385 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells; the printed rounded cell 91 mM^-1 . s^-1 is documented in prose.

raw_value_unit_evidence: Table 2, Wild type block, Malonate column: Km (uM) = 208 +/- 6; kcat (s^-1) = 19 +/- 0.3; kcat/Km (mM^-1 . s^-1) = 91 (rounded printed cell).

row_label: Table 2, enzyme-form block 'Wild type', column 'Malonate'


enzyme_display_name: indoleacetate--CoA ligase

organism: Aromatoleum aromaticum

substrate_name: phenyl acetate

proof_lines: pH and temperature not specified in the publication

enzyme: indoleacetate--CoA ligase

substrate: phenyl acetate


substrate_name: 2-naphthyl acetate

substrate: 2-naphthyl acetate


organism: Methanocaldococcus jannaschii

substrate_name: GGRLGFYGYDLQD

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

column_label: Full text reports MjYcaO had KM 59.9 uM and kcat 5.3 x 10^-2 s^-1 for the 11-mer peptide substrate in Figure 2b.

normalized_value_unit_evidence: kcat normalized_value=0.053 normalized_unit=s^-1; Km normalized_value=0.0599 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=5.3 x 10^-2 s^-1 raw_unit=s^-1; Km raw_value=59.9 uM raw_unit=uM

row_label: MjYcaO thioamidation reaction / 11-mer peptide substrate

table_label: PMC full text Figure 2b kinetic prose PMID 31139720

substrate: GGRLGFYGYDLQD


organism: Escherichia coli (strain K12)

substrate_name: D-pantetheine (at pH 7.8 and 25 degrees Celsius)

smiles: CC(C)(CO)C(C(=O)NCCC(=O)NCCS)O

assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines: kcat is 0.3 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with 3-hydroxybenzoate as substrate (at pH 7.8 and 25 degrees Celsius). kcat is 0.8 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with salicylate as substrate (at pH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature N235A to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row N235A, substrate column DHB (the variant label prints its footnote letter e); column kcat (min-1) = 1.0; column Km (uM) = 5.2; column kcat/Km (mM-1 min-1) = 188; column specificity = 0.14; column specificity switch = 0.5.

normalized_value_unit_evidence: Km: printed cell 5.2 uM; 1 uM is 1/1000 mM, so 5.2 / 1000 = 0.0052 mM. kcat: printed cell 1.0 min^-1; the printed turnover column is per minute, so 1.0 / 60 = 0.016666666666666666 s^(-1). kcat/Km: printed cell 188 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 188 / 60 = 3.1333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row N235A, substrate column DHB (the variant label prints its footnote letter e): kcat = 1.0 min^-1; Km = 5.2 uM; kcat/Km = 188 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature N340C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row N340C, substrate column DHB; column kcat (min-1) = 0.97; column Km (uM) = 2.7; column kcat/Km (mM-1 min-1) = 365; column specificity = 2; column specificity switch = 8.

normalized_value_unit_evidence: Km: printed cell 2.7 uM; 1 uM is 1/1000 mM, so 2.7 / 1000 = 0.0027 mM. kcat: printed cell 0.97 min^-1; the printed turnover column is per minute, so 0.97 / 60 = 0.016166666666666666 s^(-1). kcat/Km: printed cell 365 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 365 / 60 = 6.083333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row N340C, substrate column DHB: kcat = 0.97 min^-1; Km = 2.7 uM; kcat/Km = 365 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature S240C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row S240C, substrate column DHB (the variant label prints its footnote letter d); column kcat (min-1) = 10; column Km (uM) = 364; column kcat/Km (mM-1 min-1) = 28; column specificity = 8; column specificity switch = 26.

normalized_value_unit_evidence: Km: printed cell 364 uM; 1 uM is 1/1000 mM, so 364 / 1000 = 0.364 mM. kcat: printed cell 10 min^-1; the printed turnover column is per minute, so 10 / 60 = 0.16666666666666666 s^(-1). kcat/Km: printed cell 28 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 28 / 60 = 0.4666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row S240C, substrate column DHB (the variant label prints its footnote letter d): kcat = 10 min^-1; Km = 364 uM; kcat/Km = 28 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature V339I to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row V339I, substrate column DHB; column kcat (min-1) = 1.8; column Km (uM) = 6.1; column kcat/Km (mM-1 min-1) = 298; column specificity = 5; column specificity switch = 18.

normalized_value_unit_evidence: Km: printed cell 6.1 uM; 1 uM is 1/1000 mM, so 6.1 / 1000 = 0.0061 mM. kcat: printed cell 1.8 min^-1; the printed turnover column is per minute, so 1.8 / 60 = 0.03 s^(-1). kcat/Km: printed cell 298 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 298 / 60 = 4.966666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row V339I, substrate column DHB: kcat = 1.8 min^-1; Km = 6.1 uM; kcat/Km = 298 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature V339L to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row V339L, substrate column DHB; column kcat (min-1) = 1.5; column Km (uM) = 4.9; column kcat/Km (mM-1 min-1) = 318; column specificity = 4; column specificity switch = 12.

normalized_value_unit_evidence: Km: printed cell 4.9 uM; 1 uM is 1/1000 mM, so 4.9 / 1000 = 0.0049 mM. kcat: printed cell 1.5 min^-1; the printed turnover column is per minute, so 1.5 / 60 = 0.025 s^(-1). kcat/Km: printed cell 318 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 318 / 60 = 5.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row V339L, substrate column DHB: kcat = 1.5 min^-1; Km = 4.9 uM; kcat/Km = 318 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature Y236F to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F, substrate column DHB; column kcat (min-1) = 1.6; column Km (uM) = 7.1; column kcat/Km (mM-1 min-1) = 218; column specificity = 5; column specificity switch = 17.

normalized_value_unit_evidence: Km: printed cell 7.1 uM; 1 uM is 1/1000 mM, so 7.1 / 1000 = 0.0071 mM. kcat: printed cell 1.6 min^-1; the printed turnover column is per minute, so 1.6 / 60 = 0.02666666666666667 s^(-1). kcat/Km: printed cell 218 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 218 / 60 = 3.6333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F, substrate column DHB: kcat = 1.6 min^-1; Km = 7.1 uM; kcat/Km = 218 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y236F/S240C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature Y236F/S240C/N340C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F/S240C/N340C, substrate column DHB; column kcat (min-1) = 8.0; column Km (uM) = 318; column kcat/Km (mM-1 min-1) = 25; column specificity = 7; column specificity switch = 23.

normalized_value_unit_evidence: Km: printed cell 318 uM; 1 uM is 1/1000 mM, so 318 / 1000 = 0.318 mM. kcat: printed cell 8.0 min^-1; the printed turnover column is per minute, so 8.0 / 60 = 0.13333333333333333 s^(-1). kcat/Km: printed cell 25 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 25 / 60 = 0.4166666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F/S240C/N340C, substrate column DHB: kcat = 8.0 min^-1; Km = 318 uM; kcat/Km = 25 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature Y236F/S240C/V339I/N340C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F/S240C/V339I/N340C, substrate column DHB; column kcat (min-1) = 8.8; column Km (uM) = 417; column kcat/Km (mM-1 min-1) = 21; column specificity = 14; column specificity switch = 45.

normalized_value_unit_evidence: Km: printed cell 417 uM; 1 uM is 1/1000 mM, so 417 / 1000 = 0.417 mM. kcat: printed cell 8.8 min^-1; the printed turnover column is per minute, so 8.8 / 60 = 0.14666666666666667 s^(-1). kcat/Km: printed cell 21 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 21 / 60 = 0.35 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F/S240C/V339I/N340C, substrate column DHB: kcat = 8.8 min^-1; Km = 417 uM; kcat/Km = 21 under the printed column head kcat/Km (mM-1 min-1).


substrate_name: salicylate

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row N235A, substrate column Sal (the variant label prints its footnote letter e); column kcat (min-1) = 2.2; column Km (uM) = 80; column kcat/Km (mM-1 min-1) = 27; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 80 uM; 1 uM is 1/1000 mM, so 80 / 1000 = 0.08 mM. kcat: printed cell 2.2 min^-1; the printed turnover column is per minute, so 2.2 / 60 = 0.03666666666666667 s^(-1). kcat/Km: printed cell 27 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 27 / 60 = 0.45 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row N235A, substrate column Sal (the variant label prints its footnote letter e): kcat = 2.2 min^-1; Km = 80 uM; kcat/Km = 27 under the printed column head kcat/Km (mM-1 min-1).

substrate: salicylate


substrate_name: holo-EntB (at pH 8.8 and 37 degrees Celsius)

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


organism: Arabidopsis thaliana

substrate_name: Unknown

substrate: Unknown


organism: Bradyrhizobium japonicum


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row N340C, substrate column Sal; column kcat (min-1) = 7.8; column Km (uM) = 8.9; column kcat/Km (mM-1 min-1) = 879; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 8.9 uM; 1 uM is 1/1000 mM, so 8.9 / 1000 = 0.0089 mM. kcat: printed cell 7.8 min^-1; the printed turnover column is per minute, so 7.8 / 60 = 0.13 s^(-1). kcat/Km: printed cell 879 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 879 / 60 = 14.65 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row N340C, substrate column Sal: kcat = 7.8 min^-1; Km = 8.9 uM; kcat/Km = 879 under the printed column head kcat/Km (mM-1 min-1).


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row S240C, substrate column Sal (the variant label prints its footnote letter d); column kcat (min-1) = 12; column Km (uM) = 54; column kcat/Km (mM-1 min-1) = 226; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 54 uM; 1 uM is 1/1000 mM, so 54 / 1000 = 0.054 mM. kcat: printed cell 12 min^-1; the printed turnover column is per minute, so 12 / 60 = 0.2 s^(-1). kcat/Km: printed cell 226 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 226 / 60 = 3.7666666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row S240C, substrate column Sal (the variant label prints its footnote letter d): kcat = 12 min^-1; Km = 54 uM; kcat/Km = 226 under the printed column head kcat/Km (mM-1 min-1).


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row V339I, substrate column Sal; column kcat (min-1) = 8.9; column Km (uM) = 5.5; column kcat/Km (mM-1 min-1) = 1616; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 5.5 uM; 1 uM is 1/1000 mM, so 5.5 / 1000 = 0.0055 mM. kcat: printed cell 8.9 min^-1; the printed turnover column is per minute, so 8.9 / 60 = 0.14833333333333334 s^(-1). kcat/Km: printed cell 1616 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 1616 / 60 = 26.933333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row V339I, substrate column Sal: kcat = 8.9 min^-1; Km = 5.5 uM; kcat/Km = 1616 under the printed column head kcat/Km (mM-1 min-1).


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row V339L, substrate column Sal; column kcat (min-1) = 9.3; column Km (uM) = 8.0; column kcat/Km (mM-1 min-1) = 1170; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 8.0 uM; 1 uM is 1/1000 mM, so 8.0 / 1000 = 0.008 mM. kcat: printed cell 9.3 min^-1; the printed turnover column is per minute, so 9.3 / 60 = 0.155 s^(-1). kcat/Km: printed cell 1170 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 1170 / 60 = 19.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row V339L, substrate column Sal: kcat = 9.3 min^-1; Km = 8.0 uM; kcat/Km = 1170 under the printed column head kcat/Km (mM-1 min-1).


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F, substrate column Sal; column kcat (min-1) = 6.9; column Km (uM) = 6.1; column kcat/Km (mM-1 min-1) = 1139; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 6.1 uM; 1 uM is 1/1000 mM, so 6.1 / 1000 = 0.0061 mM. kcat: printed cell 6.9 min^-1; the printed turnover column is per minute, so 6.9 / 60 = 0.115 s^(-1). kcat/Km: printed cell 1139 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 1139 / 60 = 18.983333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F, substrate column Sal: kcat = 6.9 min^-1; Km = 6.1 uM; kcat/Km = 1139 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature Y236F/S240C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F/S240C, substrate column Sal; column kcat (min-1) = 8.3; column Km (uM) = 39; column kcat/Km (mM-1 min-1) = 216; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 39 uM; 1 uM is 1/1000 mM, so 39 / 1000 = 0.039 mM. kcat: printed cell 8.3 min^-1; the printed turnover column is per minute, so 8.3 / 60 = 0.13833333333333334 s^(-1). kcat/Km: printed cell 216 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 216 / 60 = 3.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F/S240C, substrate column Sal: kcat = 8.3 min^-1; Km = 39 uM; kcat/Km = 216 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Mutation signature Y236F/S240C/N340C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y236F/S240C/V339I/N340C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y236F/S240C/V339L/N340C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Vibrio cholerae


assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP


substrate: ATP


assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADH

column_label: Table 1: Kinetic Parameters of EntE1 (decoded plain-numeral transcription of the printed table). Substrate row 'salicylic acid'; column 'Km (uM)' = 70 +/- 4; column 'kcat (s^-1)' = 0.8 +/- 0.1; column 'kcat/Km (M^-1 s^-1)' = 1.1 x 10^4.

normalized_value_unit_evidence: Km: printed Table 1 cell 70 +/- 4 uM; the catalog unit is mM and 1 uM is 0.001 mM, so 70 / 1000 = 0.07 mM; the exported value is 0.028 mM. kcat: printed Table 1 cell 0.8 +/- 0.1 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.8 s^(-1). kcat/Km: printed Table 1 cell 1.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11000 x 0.001 = 11 s^-1 mM^-1; the exported value is 28.571428571428573 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, decoded plain-numeral transcription (Biochemistry 2010, volume 49, issue 17, pages 3648-3657), substrate row 'salicylic acid': Km = 70 +/- 4 uM; kcat = 0.8 +/- 0.1 s^-1; printed kcat/Km = 1.1 x 10^4 M^-1 s^-1.

row_label: Table 1, substrate row 'salicylic acid'


column_label: Table 1: Kinetic Parameters of EntE (Biochemistry 2010, 49(17):3648-3657), substrate row '3-hydroxybenzoic acid', wild-type EntE; column 'Km (uM)' = 70; column 'kcat (s-1)' = 0.30; column 'kcat/Km (M-1 s-1)' = 4.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.30 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.3 s^(-1); the exported value is 0.3 s^(-1). Km: printed Table 1 cell 70 uM; 70 / 1000 = 0.07 mM; the paper value is 0.07 mM; the exported value is 0.07 mM. kcat/Km: printed Table 1 cell 4.6 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.6 x 10^3 / 1000 = 4.6 s^-1 mM^-1; the paper value is 4.6 s^(-1)*mM^(-1); the exported value is 4.285714285714286 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row '3-hydroxybenzoic acid', wild-type EntE: Km = 70 uM; kcat = 0.30 s-1; printed kcat/Km = 4.6 x 10^3 M-1 s-1.


organism: Amycolatopsis mediterranei

substrate_name: benzoate

assay_conditions_summary: pH 7.2; cofactor NADPH

substrate: benzoate


assay_conditions_summary: pH 7.2; 303.15 K; cofactor NADPH


assay_conditions_summary: pH 8.4; cofactor ATP


column_label: Abstract reports Km for malonate was 200 microM.

raw_value_unit_evidence: Km raw_value=200 microM raw_unit=microM

row_label: Rhizobium japonicum malonyl-CoA synthetase / malonate

table_label: PubMed XML abstract PMID 1847615


substrate_name: hexanoic acid

smiles: CCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Hexanoic acid (C6)'; column 'Km (uM)' = 129; column 'kcat (min^-1)' = 0.11; column 'kcat/Km (uM^-1 min^-1)' = 0.0008. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 129 uM; 1 uM is one thousandth of 1 mM, so 129 / 1000 = 0.129 mM; the exported value is 0.129 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 0.11 min^-1; the printed head is per minute, so 0.11 / 60 = 0.0018333333333333333 s^(-1); the proposed kcat is 0.0018333333333333333 s^(-1). kcat/Km: printed Table 2 cell 0.0008 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.0008 times 1000 divided by 60 = 0.013333333333333334 s^(-1)*mM^(-1); the proposed kcat/Km is 0.013333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Hexanoic acid (C6)': Km cell = 129 uM; kcat cell = 0.11 min^-1; printed kcat/Km cell = 0.0008 uM^-1 min^-1.

substrate: hexanoic acid


substrate_name: decanoic acid

smiles: CCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Decanoic acid (C10)'; column 'Km (uM)' = 121; column 'kcat (min^-1)' = 1.5; column 'kcat/Km (uM^-1 min^-1)' = 0.012. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 121 uM; 1 uM is one thousandth of 1 mM, so 121 / 1000 = 0.121 mM; the exported value is 0.121 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 1.5 min^-1; the printed head is per minute, so 1.5 / 60 = 0.025 s^(-1); the proposed kcat is 0.025 s^(-1). kcat/Km: printed Table 2 cell 0.012 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.012 times 1000 divided by 60 = 0.2 s^(-1)*mM^(-1); the proposed kcat/Km is 0.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Decanoic acid (C10)': Km cell = 121 uM; kcat cell = 1.5 min^-1; printed kcat/Km cell = 0.012 uM^-1 min^-1.

substrate: decanoic acid


substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Lauric acid (C12)'; column 'Km (uM)' = 21; column 'kcat (min^-1)' = 2.4; column 'kcat/Km (uM^-1 min^-1)' = 0.110. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 21 uM; 1 uM is one thousandth of 1 mM, so 21 / 1000 = 0.021 mM; the exported value is 0.021 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 2.4 min^-1; the printed head is per minute, so 2.4 / 60 = 0.04 s^(-1); the proposed kcat is 0.04 s^(-1). kcat/Km: printed Table 2 cell 0.110 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.110 times 1000 divided by 60 = 1.8333333333333335 s^(-1)*mM^(-1); the proposed kcat/Km is 1.8333333333333335 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Lauric acid (C12)': Km cell = 21 uM; kcat cell = 2.4 min^-1; printed kcat/Km cell = 0.110 uM^-1 min^-1.

substrate: lauric acid


substrate_name: palmitic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Palmitic acid (C16)'; column 'Km (uM)' = 1.9; column 'kcat (min^-1)' = 4.2; column 'kcat/Km (uM^-1 min^-1)' = 2.3. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.9 uM; 1 uM is one thousandth of 1 mM, so 1.9 / 1000 = 0.0019 mM; the exported value is 0.0019 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 4.2 min^-1; the printed head is per minute, so 4.2 / 60 = 0.07 s^(-1); the proposed kcat is 0.07 s^(-1). kcat/Km: printed Table 2 cell 2.3 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 2.3 times 1000 divided by 60 = 38.333333333333336 s^(-1)*mM^(-1); the proposed kcat/Km is 38.333333333333336 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Palmitic acid (C16)': Km cell = 1.9 uM; kcat cell = 4.2 min^-1; printed kcat/Km cell = 2.3 uM^-1 min^-1.

substrate: palmitic acid


substrate_name: ATP

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'ATP'; column 'Km (uM)' = 15; column 'kcat (min^-1)' = 1.3; column 'kcat/Km (uM^-1 min^-1)' = 0.085. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 15 uM; 1 uM is one thousandth of 1 mM, so 15 / 1000 = 0.015 mM; the exported value is 0.015 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 1.3 min^-1; the printed head is per minute, so 1.3 / 60 = 0.021666666666666667 s^(-1); the proposed kcat is 0.021666666666666667 s^(-1). kcat/Km: printed Table 2 cell 0.085 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.085 times 1000 divided by 60 = 1.416666666666667 s^(-1)*mM^(-1); the proposed kcat/Km is 1.416666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'ATP': Km cell = 15 uM; kcat cell = 1.3 min^-1; printed kcat/Km cell = 0.085 uM^-1 min^-1.


organism: Pseudomonas fluorescens

substrate_name: L-proline

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

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

source_databases_merged: brenda skid

substrate: L-proline


organism: Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)

substrate_name: D-alanine

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

substrate: D-alanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H206L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K170M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R168G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R168G/K170M to reconstruct the assayed variant sequence.


column_label: Table 2  Steady-state kinetic constants for MCS activities of the wild type and mutant GST-MCS enzymes; enzyme-form block 'Wild type'; column 'ATP'; metric line 'Km (uM)' = 52 +/- 4.5; metric line 'kcat (s^-1)' = 20 +/- 0.4; metric line 'kcat/Km (mM^-1 . s^-1)' = 384.

normalized_value_unit_evidence: kcat: paper cell 20 +/- 0.4 s^-1 -> 20.0 s^(-1) (no conversion); catalog holds 20.0 s^(-1). Km: paper cell 52 +/- 4.5 uM / 1000 = 0.052 mM; catalog holds 0.052 mM. kcat/Km: catalog 384.61538461538464 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells; the printed rounded cell 384 mM^-1 . s^-1 is documented in prose.

raw_value_unit_evidence: Table 2, Wild type block, ATP column: Km (uM) = 52 +/- 4.5; kcat (s^-1) = 20 +/- 0.4; kcat/Km (mM^-1 . s^-1) = 384 (rounded printed cell).

row_label: Table 2, enzyme-form block 'Wild type', column 'ATP'


substrate_name: CoA

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA


assay_conditions_summary: pH 6.9; cofactor ATP


substrate_name: malonate

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


column_label: Table 2  Steady-state kinetic constants for MCS activities of the wild type and mutant GST-MCS enzymes; enzyme-form block 'Wild type'; column 'Malonate'; metric line 'Km (uM)' = 208 +/- 6; metric line 'kcat (s^-1)' = 19 +/- 0.3; metric line 'kcat/Km (mM^-1 . s^-1)' = 91.

normalized_value_unit_evidence: kcat: paper cell 19 +/- 0.3 s^-1 -> 19.0 s^(-1) (no conversion); catalog holds 19.0 s^(-1). Km: paper cell 208 +/- 6 uM / 1000 = 0.208 mM; catalog holds 0.208 mM. kcat/Km: catalog 91.34615384615385 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells; the printed rounded cell 91 mM^-1 . s^-1 is documented in prose.

raw_value_unit_evidence: Table 2, Wild type block, Malonate column: Km (uM) = 208 +/- 6; kcat (s^-1) = 19 +/- 0.3; kcat/Km (mM^-1 . s^-1) = 91 (rounded printed cell).


organism: Aromatoleum aromaticum (strain DSM 19018 / LMG 30748 / EbN1)

substrate_name: indoleacetate

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

proof_lines: kcat is 4.3 sec(-1) with indoleacetate as substrate. kcat is 4.7 sec(-1) with (2-naphthyl)acetate as substrate. kcat is 0.48 sec(-1) with phenylacetate as substrate.

substrate: indoleacetate


substrate_name: phenylacetate

substrate: phenylacetate


substrate_name: ATP (in the presence of 0.6 mM indoleacetate)

assay_conditions_summary: cofactor ATP


substrate_name: CoA (in the presence of 0.6 mM indoleacetate)

assay_conditions_summary: cofactor CoA


substrate_name: L-serine

substrate: L-serine


substrate: CoA


substrate: malonate


column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row 'L-Serine': column 'Km (mM)' = 0.26; column 'kcat (min^-1)' = 760; column 'kcat/Km' = 2,900.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 760 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 760 / 60 = 12.666666666667 s^(-1). The exported value is 760.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 0.26 mM, already the export unit; the exported value is 0.26 mM. kcat/Km: the printed Table 2 cell is 2,900 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 2,900 / 60 = 48.333333333333 s^(-1)*mM^(-1); the exported value is 2923.076923076923 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

row_label: Table 2, substrate row 'L-Serine'


column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row 'ATP': column 'Km (mM)' = 0.75; column 'kcat (min^-1)' = 660; column 'kcat/Km' = 880.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 660 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 660 / 60 = 11 s^(-1). The exported value is 660.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 0.75 mM, already the export unit; the exported value is 0.75 mM. kcat/Km: the printed Table 2 cell is 880 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 880 / 60 = 14.666666666667 s^(-1)*mM^(-1); the exported value is 880.0 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

row_label: Table 2, substrate row 'ATP'


substrate_name: O-acetyl-L-serine

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

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row '(O)Ac-L-serine': column 'Km (mM)' = 5.0; column 'kcat (min^-1)' = 720; column 'kcat/Km' = 150.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 720 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 720 / 60 = 12 s^(-1). The exported value is 720.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 5.0 mM, already the export unit; the exported value is 5.0 mM. kcat/Km: the printed Table 2 cell is 150 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 150 / 60 = 2.5 s^(-1)*mM^(-1); the exported value is 144.0 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

row_label: Table 2, substrate row '(O)Ac-L-serine'

substrate: O-acetyl-L-serine


substrate_name: L-beta-chloroalanine

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

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row 'beta-Cl-L-alanine': column 'Km (mM)' = 8.0; column 'kcat (min^-1)' = 870; column 'kcat/Km' = 110.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 870 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 870 / 60 = 14.5 s^(-1). The exported value is 870.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 8.0 mM, already the export unit; the exported value is 8.0 mM. kcat/Km: the printed Table 2 cell is 110 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 110 / 60 = 1.833333333333 s^(-1)*mM^(-1); the exported value is 108.75 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

substrate: L-beta-chloroalanine


substrate_name: S-methyl-L-cysteine

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

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row '(S)methyl-L-cysteine': column 'Km (mM)' = 3.1; column 'kcat (min^-1)' = 38; column 'kcat/Km' = 12.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 38 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 38 / 60 = 0.633333333333 s^(-1). The exported value is 38.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 3.1 mM, already the export unit; the exported value is 3.1 mM. kcat/Km: the printed Table 2 cell is 12 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 12 / 60 = 0.2 s^(-1)*mM^(-1); the exported value is 12.258064516129032 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

substrate: S-methyl-L-cysteine


substrate_name: malonate (at pH 7.5)

substrate: malonate (at pH 7.5)


organism: Escherichia coli

row_label: Table 1, substrate row '3-hydroxybenzoic acid', wild-type EntE

table_label: Table 1: Kinetic Parameters of EntE (Biochemistry 2010, 49(17):3648-3657)

source_databases_merged: skid uniprot


substrate_name: salicylate

normalized_value_unit_evidence: Km: printed Table 1 cell 70 +/- 4 uM; the catalog unit is mM and 1 uM is 0.001 mM, so 70 / 1000 = 0.07 mM; the exported value is 0.0055 mM. kcat: printed Table 1 cell 0.8 +/- 0.1 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.8 s^(-1). kcat/Km: printed Table 1 cell 1.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11000 x 0.001 = 11 s^-1 mM^-1; the exported value is 145.45454545454547 s^(-1)*mM^(-1).

table_label: Table 1: Kinetic Parameters of EntE1 (decoded plain-numeral transcription of the printed table)

substrate: salicylate


substrate: ATP


enzyme_display_name: E1 NEDD8-activating enzyme

organism: Homo sapiens

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

proof_lines: chimeric Ub1, pH not specified in the publication, temperature not specified in the publication

enzyme: E1 NEDD8-activating enzyme


mutation_type: deletion

proof_lines: mutant DELTA946, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant DELTA348, pH not specified in the publication, temperature not specified in the publication


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

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

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


substrate_name: ubiquitin

substrate: ubiquitin


substrate_name: 2-hydroxybenzoic acid

substrate: 2-hydroxybenzoic acid


substrate_name: 2,5-dihydroxybenzoic acid

substrate: 2,5-dihydroxybenzoic acid


substrate_name: 2,3-Dihydroxybenzoic acid

substrate: 2,3-Dihydroxybenzoic acid


substrate_name: 2,4-dihydroxybenzoic acid

substrate: 2,4-dihydroxybenzoic acid


substrate_name: diphosphate

substrate: diphosphate


proof_lines: mutant enzyme Y352H, pH and temperature not specified in the publication


substrate_name: ATP

proof_lines: mutant enzyme I310N, pH and temperature not specified in the publication


proof_lines: acceptor aryl-carrier protein domain of SrfB1, pH 7.5, 37°C

proof_lines: acceptor aryl-carrier protein domain of EntB, pH 7.5, 37°C


proof_lines: acceptor holo-[L-seryl-carrier protein domain of Ybt], pH 7.5, 37°C

proof_lines: acceptor holo-[L-seryl-carrier protein domain of SrfB1], pH 7.5, 37°C


organism: Bacillus subtilis

substrate_name: Unknown

substrate: Unknown


substrate_name: malonate

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: pH 7.5, temperature not specified in the publication


substrate_name: D-Ala

assay_conditions_summary: pH 7.2; 310.15 K; cofactor CoA

proof_lines: wild-type, thiol assay, presence of coenzyme A, pH 7.2, temperature not specified in the publication

proof_lines: wild-type, diphosphate assay, presence of coenzyme A, pH 7.2, temperature not specified in the publication

substrate: D-Ala


proof_lines: mutant C269A, diphosphate assay, presence of coenzyme A, pH 7.2, temperature not specified in the publication


enzyme_display_name: glutamate racemase

organism: Enterococcus faecalis

substrate_name: D-glutamate

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

enzyme: glutamate racemase

substrate: D-glutamate


organism: Dinoroseobacter shibae

smiles: CSCCC(=O)[O-]


organism: Bacillus cereus


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


proof_lines: pH and temperature not specified in the publication


organism: Enterococcus faecium

substrate_name: L-glutamate / D-glutamate

substrate: L-glutamate / D-glutamate


enzyme_display_name: alanine racemase

substrate_name: D-alanine

enzyme: alanine racemase

substrate: D-alanine


organism: Enterocloster bolteae

substrate_name: D-tagatose

substrate: D-tagatose


enzyme_display_name: dTDP-4-dehydrorhamnose 3,5-epimerase

enzyme: dTDP-4-dehydrorhamnose 3,5-epimerase


enzyme_display_name: UDP-glucose 4-epimerase

enzyme: UDP-glucose 4-epimerase


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-galactose

enzyme: aldose 1-epimerase

substrate: alpha-D-galactose


enzyme_display_name: chorismate mutase

proof_lines: 30°C, pH 7.5, chorismate mutase domain of P-protein

enzyme: chorismate mutase


enzyme_display_name: L-arabinose isomerase

substrate_name: D-galactose

proof_lines:
at pH 7.0 and 50°C
pH 7.0-7.5, 45-50°C, recombinant enzyme
at pH 7.0 and 40°C

enzyme: L-arabinose isomerase

substrate: D-galactose


enzyme_display_name: bisphosphoglycerate mutase

organism: Equus caballus

substrate_name: Glycerate 1,3-bisphosphate

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

enzyme: bisphosphoglycerate mutase

substrate: Glycerate 1,3-bisphosphate


enzyme_display_name: glucuronate isomerase

substrate_name: D-tagaturonate

enzyme: glucuronate isomerase

substrate: D-tagaturonate


proof_lines: in 50 mM potassium phosphate buffer pH 7.4, at 30°C


enzyme_display_name: arabinose-5-phosphate isomerase

substrate_name: D-arabinose 5-phosphate

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

enzyme: arabinose-5-phosphate isomerase

substrate: D-arabinose 5-phosphate


substrate_name: D-glucuronate

proof_lines:
in absence of added metal or chelator
reconstituted with Co2+, 30°C, pH 8
in presence of 0.01 mM Zn2+

substrate: D-glucuronate


proof_lines:
apo and Zn2+ reconstituted enzyme
Zn2+ reconstituted enzyme
apo enzyme


enzyme_display_name: S-ribosylhomocysteine lyase

substrate_name: S-ribosylhomocysteine

enzyme: S-ribosylhomocysteine lyase

substrate: S-ribosylhomocysteine


enzyme_display_name: tRNA pseudouridine(32) synthase

substrate_name: tRNA uridine32

proof_lines: pH 7.5, 37°C, anticodon stem-loop of Escherichia coli tRNAPhe (17-mer)

enzyme: tRNA pseudouridine(32) synthase

substrate: tRNA uridine32


enzyme_display_name: aspartate-ammonia ligase

organism: Lactiplantibacillus plantarum

enzyme: aspartate-ammonia ligase

substrate: ATP


substrate_name: L-Asp

substrate: L-Asp


enzyme_display_name: glutamine synthetase

organism: Methylococcus capsulatus

substrate_name: ADP

enzyme: glutamine synthetase

substrate: ADP


substrate_name: ATP


enzyme_display_name: UniProt P12425

smiles: N

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

enzyme: UniProt P12425


enzyme_display_name: lactoylglutathione lyase

proof_lines:
in the presence of Fe2+
in the presence of Mn2+
in the presence of Cd2+

enzyme: lactoylglutathione lyase


enzyme_display_name: tRNA pseudouridine(13) synthase

substrate_name: tRNA uridine13

enzyme: tRNA pseudouridine(13) synthase

substrate: tRNA uridine13


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


enzyme_display_name: lysine 2,3-aminomutase

substrate_name: L-Lys

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

enzyme: lysine 2,3-aminomutase

substrate: L-Lys


enzyme_display_name: glutamate racemase

substrate_name: L-glutamate

proof_lines: in presence of 0.0065 mM of the activator UDP-N-acetylmuramyl-L-Ala

enzyme: glutamate racemase

substrate: L-glutamate


organism: Arabidopsis thaliana

proof_lines:
mutant A174S of isoenzyme GLN1,4
mutant A174S of isoenzyme GLN1,3


substrate_name: L-Glu

substrate: L-Glu


proof_lines:
mutant K49Q/A174S of isoenzyme GLN1,4
mutant K49Q/A174S of isoenzyme GLN1,3


proof_lines:
isoenzyme GLN1,4
isoenzyme GLN1,3
pH 7.8, 30°C, below, isoenzyme GLN1,1


proof_lines:
isoenzyme GLN1,4
isoenzyme GLN1,3
pH 7.8, 30°C, isoenzyme GLN1,4


proof_lines:
mutant K49Q of isoenzyme GLN1,4
mutant K49Q of isoenzyme GLN1,3


enzyme_display_name: isochorismate synthase

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication, inhibition of isochorismate synthase activity

proof_lines: pH and temperature not specified in the publication, inhibition of salicylate synthase activity

enzyme: isochorismate synthase

substrate: Unknown


enzyme_display_name: glutamate--ethylamine ligase

substrate_name: L-cysteine

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

enzyme: glutamate--ethylamine ligase

substrate: L-cysteine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


organism: Clarias batrachus

assay_conditions_summary: cofactor ADP


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


organism: Sphagnum fallax


organism: Xylanibacter ruminicola

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP

proof_lines: isozyme GSIII-1, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity

proof_lines: isozyme GSIII-2, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity

proof_lines: isozyme GSI, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity


proof_lines: isozyme GSIII-2, pH 7.5, 37°C, glutamine synthetase activity

proof_lines: isozyme GSIII-1, pH 7.5, 37°C, glutamine synthetase activity


substrate_name: L-glutamine

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

substrate: L-glutamine


organism: Oryza sativa Japonica Group

proof_lines:
30°C, isoenzyme OsGLN1,1
30°C, isoenzyme OsGLN1,2


assay_conditions_summary: 303.15 K; cofactor ATP


substrate_name: NH3; L-Glutamate; ATP

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

substrate: NH3; L-Glutamate; ATP


substrate_name: ATP; L-Glutamate; NH3

substrate: ATP; L-Glutamate; NH3


substrate_name: NH3; ATP; L-Glutamate

substrate: NH3; ATP; L-Glutamate


organism: Camellia sinensis


organism: Beta vulgaris


organism: Bradyrhizobium japonicum


enzyme_display_name: aspartate--ammonia ligase (ADP-forming)

organism: Solanum tuberosum

enzyme: aspartate--ammonia ligase (ADP-forming)


organism: Hordeum vulgare

proof_lines:
isozyme GS1
isozyme GS2


organism: Spinacia oleracea


organism: Senna obtusifolia


assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP

proof_lines:
pH 7.8, 30°C, isoenzyme GLN1,1
pH 7.8, 30°C, isoenzyme GLN1,4
pH 7.8, 30°C, isoenzyme GLN1,3


enzyme_display_name: NAD(+) synthase

organism: Herbaspirillum seropedicae

enzyme: NAD(+) synthase


organism: Zea mays


organism: Exiguobacterium sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E60A/R64G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor ADP

proof_lines: pH 6.0, 35°C, recombinant mutant E60A/R64G


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C4L2T5 and applied mutation signature E60A to reconstruct the assayed variant sequence.

column_label: Table 1: The kinetic parameters of the wild-type ExiGS and its mutants (Appl Microbiol Biotechnol 2017, volume 101, pages 3653-3661); printed row heads Km | Vmax (mM x min-1) | kcat (s-1) | kcat/Km (s-1 x uM-1); substrate blocks ADP (uM), Gln (mM) and Hydroxylamine (mM). Table 1, ADP block, enzyme column E60A; column Km = 4.61 uM; column kcat (s-1) = 4.76; column kcat/Km (s-1 x uM-1) = 1.03. captured primary segment: ADP block | E60A | Km 4.61 uM | kcat 4.76 s^-1 | kcat/Km 1.03 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 4.61 uM under the ADP block head ADP (uM); 1 uM is 1/1000 mM, so 4.61 / 1000 = 0.00461 mM. kcat: printed Table 1 cell 4.76 s^-1 under the printed row head kcat (s-1); the printed turnover column is per second and no unit conversion applies, so the normalized value is 4.76 s^(-1). kcat/Km: printed Table 1 cell 1.03 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.03 x 1000 = 1030.0 s^-1 mM^-1..

raw_value_unit_evidence: Table 1, ADP block, enzyme column E60A: Km = 4.61 uM; kcat = 4.76 s^-1; printed kcat/Km = 1.03 s^-1 uM^-1.

row_label: Table 1, ADP block, enzyme column E60A