sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature T75A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row T75A / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row T75A: kcat 55 s^-1; K_M 0.154 mM; printed Table 2 kcat/K_M 360 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


enzyme_display_name: o-succinylbenzoate synthase

organism: Thermobifida fusca

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature T75L with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 2 / T. fusca OSBS / row T75L / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row T75L: kcat 18 s^-1; K_M 0.057 mM; printed Table 2 kcat/K_M 320 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.

table_label: Table 2

data_origin: experimental

enzyme: o-succinylbenzoate synthase

status: corrected

source: oed


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature V230L with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row V230L / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row V230L: kcat 29 s^-1; K_M 0.145 mM; printed Table 2 kcat/K_M 200 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.

status: verified


verification_status: unverified

mutation_signature: Unknown

kcat_over_km_origin: calculated

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

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature Y42A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row Y42A / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row Y42A: kcat 210 s^-1; K_M 0.588 mM; printed Table 2 kcat/K_M 360 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


enzyme_display_name: chondroitin-sulfate-ABC exolyase

organism: Vibrio hyugaensis

substrate_name: chondroitin sulfate C

source_db: brenda

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.

enzyme: chondroitin-sulfate-ABC exolyase

substrate: chondroitin sulfate C

source: brenda


substrate_name: chondroitin sulfate B

substrate: chondroitin sulfate B


organism: Proteus vulgaris

substrate_name: dermatan sulfate

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -14, so it is treated as a source-provided variant sequence.

proof_lines:
mutant R500A, pH 8.0
mutant R500A, pH 8.0, 37°C

substrate: dermatan sulfate


sequence_variant_note: Mutation signature H712A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 8


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H561A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official reviewed UniProtKB C7S340 sequence version 1 and applied mutation signature H452A to reconstruct the assayed variant sequence.

column_label: PMID 18849565 official PMC full article, Table 3, row H452A, Dermatan sulfate column block, columns Km (uM), kcat (min^-1), and kcat/Km (uM^-1 min^-1).

raw_value_unit_evidence: PMID 18849565 Table 3, row H452A, dermatan sulfate columns: Km 9.1 uM with SD 4.2 uM; kcat 4.3 min^-1 with SD 0.5 min^-1; printed kcat/Km 0.5 uM^-1 min^-1.

table_label: Table 3


sequence_variant_note: Resolved canonical sequence from official reviewed UniProtKB C7S340 sequence version 1 and applied mutation signature H456A to reconstruct the assayed variant sequence.

column_label: PMID 18849565 official PMC full article, Table 3, row H456A, Dermatan sulfate column block, columns Km (uM), kcat (min^-1), and kcat/Km (uM^-1 min^-1).

normalized_value_unit_evidence: Same-row central values normalize to Km 0.0076 mM, kcat 2.4 s^-1, and independently printed kcat/Km 316.6666666666666666666666666666667 s^-1 mM^-1.

raw_value_unit_evidence: PMID 18849565 Table 3, row H456A, dermatan sulfate columns: Km 7.6 uM with SD 1.9 uM; kcat 144 min^-1 with SD 17 min^-1; printed kcat/Km 19 uM^-1 min^-1.


proof_lines: wild type enzyme, in 50mM Tris/HCl, pH 8.0, at 37°C


enzyme_display_name: chondroitin B lyase

organism: Pedobacter heparinus

substrate_name: Dermatan sulfate

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

sequence_source: multiple

proof_lines: recombinant enzyme, pH 8.0, 30°C, dependent on expression system

enzyme: chondroitin B lyase

substrate: Dermatan sulfate


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature F16A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row F16A / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row F16A: kcat 4.4 s^-1; K_M 0.036 mM; printed Table 2 kcat/K_M 120 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature F39A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row F39A / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row F39A: kcat 163 s^-1; K_M 0.666 mM; printed Table 2 kcat/K_M 250 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature G254A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row G254A / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row G254A: kcat 16 s^-1; K_M 0.086 mM; printed Table 2 kcat/K_M 190 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature G254T with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row G254T / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row G254T: kcat 13 s^-1; K_M 0.668 mM; printed Table 2 kcat/K_M 19 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature N73A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row N73A / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row N73A: kcat 10 s^-1; K_M 0.322 mM; printed Table 2 kcat/K_M 31 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature N73A/T75L with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row N73A/T75L / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row N73A/T75L: kcat 5.1 s^-1; K_M 0.256 mM; printed Table 2 kcat/K_M 20 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature N73L/T75V with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row N73L/T75V / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row N73L/T75V: kcat 0.18 s^-1; K_M 0.3 mM; printed Table 2 kcat/K_M 0.61 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature R128M with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row R128M / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row R128M: kcat 104 s^-1; K_M 0.47 mM; printed Table 2 kcat/K_M 220 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R15G/F16G/R17G/G18G/I19G with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: Divergent Evolution of Ligand Binding in the o-Succinylbenzoate Synthase Family


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature R17A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row R17A / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row R17A: kcat 0.6 s^-1; K_M 0.007 mM; printed Table 2 kcat/K_M 86 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.


enzyme_display_name: oligo-alginate lyase

organism: Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)

substrate_name: alginate (at pH 6 and 40 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

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

proof_lines: kcat is 56.9 sec(-1) with low viscosity alginate as substrate. kcat is 62.4 sec(-1) with alginate trisaccharide as substrate (at pH 7.5 and 30 degrees Celsius).

enzyme: oligo-alginate lyase

source: uniprot


organism: Stenotrophomonas maltophilia (strain K279a)

substrate_name: alginate

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

assay_conditions_summary: pH 8.5; buffer pH 8

column_label: Table 1 WT column KM (mM) for row Alginate under pH 8.5 alginate-based polysaccharide assay.

raw_value_unit_evidence: Table 1 WT Alginate: kCAT 34.8 s^-1; KM 0.67 mM; kCAT/KM 52.2 s^-1*mM^-1

row_label: WT Alginate

table_label: Table 1 Kinetic parameters of WT and H208F mutant

substrate: alginate


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


enzyme_display_name: chondroitin-sulfate-ABC endolyase

substrate_name: chondroitin 4-sulfate

proof_lines:
presence of 1 M sorbitol, pH 6.8, 37°C
presence of 1 M trehalose, pH 6.8, 37°C
presence of 20% glycerol, pH 6.8, 37°C

source_databases_merged: brenda uniprot

enzyme: chondroitin-sulfate-ABC endolyase

substrate: chondroitin 4-sulfate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q140G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q140A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q140N to reconstruct the assayed variant sequence.


organism: Stenotrophomonas maltophilia

sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature H208F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer pH 8

column_label: Table 1 H208F columns kCAT (s^-1), KM (mM), and kCAT/KM for row Alginate under pH 8.5 alginate-based polysaccharide assay.

raw_value_unit_evidence: Table 1 H208F Alginate: kCAT 14.6 s^-1; KM 1.35 mM; kCAT/KM 10.8 s^-1*mM^-1

row_label: H208F Alginate


column_label: Table 1 WT columns kCAT (s^-1), KM (mM), and kCAT/KM for row Alginate under pH 8.5 alginate-based polysaccharide assay.


organism: Bacteroides thetaiotaomicron

substrate_name: Chondroitin 4-sulfate

assay_conditions_summary: pH 7.6; 310.15 K; buffer a 50 mM K-phosphate

column_label: Table III: Kinetic analysis of BactnABC and its mutants (Glycobiology 2008, volume 18, number 3, pages 270-277); each substrate block prints the column heads KM (uM), kcat (min^-1) and kcat/KM (uM^-1 min^-1). CS-A block, enzyme row WT; column KM (uM) = 67; column kcat (min^-1) = 15,792; column kcat/KM (uM^-1 min^-1) = 235.7. captured primary segment: Table III. Kinetic analysis of BactnABC and its mutants | CS-A | WT | KM 67 uM | kcat 15,792 min^-1 | kcat/KM 235.7 uM^-1 min^-1 | assay pH 7.6, 37 C

raw_value_unit_evidence: Table III, CS-A block, enzyme row WT: KM = 67 uM; kcat = 15,792 min^-1; printed kcat/KM = 235.7 uM^-1 min^-1.

row_label: Table III, CS-A block, enzyme row WT

substrate: Chondroitin 4-sulfate


substrate_name: chondroitin 6-sulfate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H561A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

substrate: chondroitin 6-sulfate


sequence_variant_note: Mutation signature H712A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +13, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y508F with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -14, so it is treated as a source-provided variant sequence.

proof_lines:
mutant R500A, pH 8.0, 37°C
mutant R500A, pH 8.0


organism: Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1)

substrate_name: ulvan

substrate: ulvan


enzyme_display_name: pectate trisaccharide-lyase

organism: Thermotoga maritima

substrate_name: polygalacturonic acid

enzyme: pectate trisaccharide-lyase

substrate: polygalacturonic acid


enzyme_display_name: rhamnogalacturonan endolyase

organism: Bacillus subtilis (strain 168)

substrate_name: rhamnogalacturonan (RG) type I region of plant cell wall pectin

enzyme: rhamnogalacturonan endolyase


enzyme_display_name: rhamnogalacturonan exolyase

enzyme: rhamnogalacturonan exolyase

substrate: rhamnogalacturonan (RG) type I region of plant cell wall pectin


proof_lines: kcat is 34.8 sec(-1) with alginate as substrate. kcat is 62.2 sec(-1) with poly-ManA as substrate. kcat is 34.6 sec(-1) with poly-GulA as substrate. kcat is 22.2 sec(-1) with poly-MG as substrate. kcat is 0.4 sec(-1) with poly-GlcA as subst


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H208F to reconstruct the assayed variant sequence.

proof_lines:
mutant H208F, pH 8.0, 25°C
mutant H208F, pH 8.5, 25°C


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature H456A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H456A, in 50mM Tris/HCl, pH 8.0, at 37°C


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature H452A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H452A, in 50mM Tris/HCl, pH 8.0, at 37°C


enzyme_display_name: gellan lyase

organism: Geobacillus stearothermophilus

substrate_name: gellan

proof_lines: at 70°C, pH not specified in the publication

enzyme: gellan lyase

substrate: gellan


substrate_name: low viscosity alginate (at pH 7.5 and 30 degrees Celsius)


proof_lines:
wild-type, pH 8.5, 25°C
wild-type, pH 8.0, 25°C


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I19W/D297G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I19Y/D297G to reconstruct the assayed variant sequence.


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

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D297G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51981 and applied mutation signature D297G to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters fr OSBS and AEE Activities (Biochemistry 2005, 44, 11722-11729); printed column heads enzyme | kcat (s-1) | KM (M) | kcat/KM (M-1 s-1). Table 1, OSBS Activity block, mutant row D297G; column KM (M) = 1.8 x 10^-3; column kcat (s-1) = 1.3 x 10^-2; column kcat/KM (M-1 s-1) = 7.4. captured primary segment: Table 1, OSBS Activity block, mutant row D297G, substrate SHCHC: Km 1.8 x 10^-3 M | kcat 1.3 x 10^-2 s-1 | kcat/Km 7.4 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 1.8 x 10^-3 M; 1 M is 1000 mM, so 1.8 x 10^-3 x 1000 = 1.8 mM. kcat: printed Table 1 kcat cell 1.3 x 10^-2 s-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.013 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 7.4 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 7.4 / 1000 = 0.0074 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.013 / 1.8 = 0.007222222222222222 s^-1 mM^-1, against the printed efficiency cell 0.0074 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, OSBS Activity block, mutant row D297G: KM = 1.8 x 10^-3 M; kcat = 1.3 x 10^-2 s-1; printed kcat/KM = 7.4 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51981 and applied mutation signature I19A/D297G to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters fr OSBS and AEE Activities (Biochemistry 2005, 44, 11722-11729); printed column heads enzyme | kcat (s-1) | KM (M) | kcat/KM (M-1 s-1). Table 1, OSBS Activity block, mutant row I19A/D297G; column KM (M) = 8.9 x 10^-4; column kcat (s-1) = 2.1 x 10^-2; column kcat/KM (M-1 s-1) = 23. captured primary segment: Table 1, OSBS Activity block, mutant row I19A/D297G, substrate SHCHC: Km 8.9 x 10^-4 M | kcat 2.1 x 10^-2 s-1 | kcat/Km 23 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 8.9 x 10^-4 M; 1 M is 1000 mM, so 8.9 x 10^-4 x 1000 = 0.89 mM. kcat: printed Table 1 kcat cell 2.1 x 10^-2 s-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.021 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 23 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 23 / 1000 = 0.023 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.021 / 0.89 = 0.02359550561797753 s^-1 mM^-1, against the printed efficiency cell 0.023 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, OSBS Activity block, mutant row I19A/D297G: KM = 8.9 x 10^-4 M; kcat = 2.1 x 10^-2 s-1; printed kcat/KM = 23 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I19F/D297G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51981 and applied mutation signature I19H/D297G to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters fr OSBS and AEE Activities (Biochemistry 2005, 44, 11722-11729); printed column heads enzyme | kcat (s-1) | KM (M) | kcat/KM (M-1 s-1). Table 1, OSBS Activity block, mutant row I19H/D297G; column KM (M) = 1.1 x 10^-3; column kcat (s-1) = 1.1 x 10^-2; column kcat/KM (M-1 s-1) = 10.5. captured primary segment: Table 1, OSBS Activity block, mutant row I19H/D297G, substrate SHCHC: Km 1.1 x 10^-3 M | kcat 1.1 x 10^-2 s-1 | kcat/Km 10.5 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 1.1 x 10^-3 M; 1 M is 1000 mM, so 1.1 x 10^-3 x 1000 = 1.1 mM. kcat: printed Table 1 kcat cell 1.1 x 10^-2 s-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.011 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 10.5 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 10.5 / 1000 = 0.0105 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.011 / 1.1 = 0.009999999999999998 s^-1 mM^-1, against the printed efficiency cell 0.0105 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, OSBS Activity block, mutant row I19H/D297G: KM = 1.1 x 10^-3 M; kcat = 1.1 x 10^-2 s-1; printed kcat/KM = 10.5 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51981 and applied mutation signature I19L/D297G to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters fr OSBS and AEE Activities (Biochemistry 2005, 44, 11722-11729); printed column heads enzyme | kcat (s-1) | KM (M) | kcat/KM (M-1 s-1). Table 1, OSBS Activity block, mutant row I19L/D297G; column KM (M) = 1.9 x 10^-3; column kcat (s-1) = 3.2 x 10^-3; column kcat/KM (M-1 s-1) = 1.7. captured primary segment: Table 1, OSBS Activity block, mutant row I19L/D297G, substrate SHCHC: Km 1.9 x 10^-3 M | kcat 3.2 x 10^-3 s-1 | kcat/Km 1.7 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 1.9 x 10^-3 M; 1 M is 1000 mM, so 1.9 x 10^-3 x 1000 = 1.9 mM. kcat: printed Table 1 kcat cell 3.2 x 10^-3 s-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.0032 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 1.7 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 1.7 / 1000 = 0.0017 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.0032 / 1.9 = 0.0016842105263157896 s^-1 mM^-1, against the printed efficiency cell 0.0017 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, OSBS Activity block, mutant row I19L/D297G: KM = 1.9 x 10^-3 M; kcat = 3.2 x 10^-3 s-1; printed kcat/KM = 1.7 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51981 and applied mutation signature I19N/D297G to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters fr OSBS and AEE Activities (Biochemistry 2005, 44, 11722-11729); printed column heads enzyme | kcat (s-1) | KM (M) | kcat/KM (M-1 s-1). Table 1, OSBS Activity block, mutant row I19N/D297G; column KM (M) = 6.4 x 10^-4; column kcat (s-1) = 1.9 x 10^-2; column kcat/KM (M-1 s-1) = 29. captured primary segment: Table 1, OSBS Activity block, mutant row I19N/D297G, substrate SHCHC: Km 6.4 x 10^-4 M | kcat 1.9 x 10^-2 s-1 | kcat/Km 29 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 6.4 x 10^-4 M; 1 M is 1000 mM, so 6.4 x 10^-4 x 1000 = 0.64 mM. kcat: printed Table 1 kcat cell 1.9 x 10^-2 s-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.019 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 29 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 29 / 1000 = 0.029 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.019 / 0.64 = 0.0296875 s^-1 mM^-1, against the printed efficiency cell 0.029 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, OSBS Activity block, mutant row I19N/D297G: KM = 6.4 x 10^-4 M; kcat = 1.9 x 10^-2 s-1; printed kcat/KM = 29 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51981 and applied mutation signature I19S/D297G to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters fr OSBS and AEE Activities (Biochemistry 2005, 44, 11722-11729); printed column heads enzyme | kcat (s-1) | KM (M) | kcat/KM (M-1 s-1). Table 1, OSBS Activity block, mutant row I19S/D297G; column KM (M) = 1.0 x 10^-4; column kcat (s-1) = 6.1 x 10^-3; column kcat/KM (M-1 s-1) = 60. captured primary segment: Table 1, OSBS Activity block, mutant row I19S/D297G, substrate SHCHC: Km 1.0 x 10^-4 M | kcat 6.1 x 10^-3 s-1 | kcat/Km 60 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 1.0 x 10^-4 M; 1 M is 1000 mM, so 1.0 x 10^-4 x 1000 = 0.1 mM. kcat: printed Table 1 kcat cell 6.1 x 10^-3 s-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.0061 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 60 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 60 / 1000 = 0.06 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.0061 / 0.1 = 0.061 s^-1 mM^-1, against the printed efficiency cell 0.06 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, OSBS Activity block, mutant row I19S/D297G: KM = 1.0 x 10^-4 M; kcat = 6.1 x 10^-3 s-1; printed kcat/KM = 60 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I19T/D297G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51981 and applied mutation signature I19V/D297G to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters fr OSBS and AEE Activities (Biochemistry 2005, 44, 11722-11729); printed column heads enzyme | kcat (s-1) | KM (M) | kcat/KM (M-1 s-1). Table 1, OSBS Activity block, mutant row I19V/D297G; column KM (M) = 1.4 x 10^-3; column kcat (s-1) = 9.5 x 10^-3; column kcat/KM (M-1 s-1) = 7.0. captured primary segment: Table 1, OSBS Activity block, mutant row I19V/D297G, substrate SHCHC: Km 1.4 x 10^-3 M | kcat 9.5 x 10^-3 s-1 | kcat/Km 7.0 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 1.4 x 10^-3 M; 1 M is 1000 mM, so 1.4 x 10^-3 x 1000 = 1.4 mM. kcat: printed Table 1 kcat cell 9.5 x 10^-3 s-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.0095 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 7.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 7.0 / 1000 = 0.007 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.0095 / 1.4 = 0.0067857142857142855 s^-1 mM^-1, against the printed efficiency cell 0.007 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, OSBS Activity block, mutant row I19V/D297G: KM = 1.4 x 10^-3 M; kcat = 9.5 x 10^-3 s-1; printed kcat/KM = 7.0 M-1 s-1.


enzyme_display_name: heparin lyase

substrate_name: Heparin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R141A to reconstruct the assayed variant sequence.

proof_lines:
Heparinase I
Flavobacterium heparinum
K199A

enzyme: heparin lyase

substrate: Heparin


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

proof_lines:
Heparinase I
Flavobacterium heparinum


enzyme_display_name: UniProt Q5SL02

organism: Thermus thermophilus

substrate_name: O-phospho-L-homoserine

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt Q5SL02

substrate: O-phospho-L-homoserine

source: skid


substrate_name: L-Vinylglycine

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

substrate: L-Vinylglycine


substrate_name: phosphate

substrate: phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K132A to reconstruct the assayed variant sequence.

proof_lines:
Heparinase I
Flavobacterium heparinum
K132A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K198A to reconstruct the assayed variant sequence.

proof_lines:
Heparinase I
Flavobacterium heparinum
K198A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K198A/K199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K198D to reconstruct the assayed variant sequence.

proof_lines:
Heparinase I
Flavobacterium heparinum
K198D


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K198R/K199R to reconstruct the assayed variant sequence.

proof_lines:
Heparinase I
Flavobacterium heparinum
K198R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K208A/K209A to reconstruct the assayed variant sequence.

proof_lines:
Heparinase I
Flavobacterium heparinum
KK208AA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K208D/K209D to reconstruct the assayed variant sequence.

proof_lines:
Heparinase I
Flavobacterium heparinum
KK208DD


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K208R/K209R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N200A to reconstruct the assayed variant sequence.

proof_lines:
Heparinase I
Flavobacterium heparinum
N200A


enzyme_display_name: 3-hydroxypropionyl-CoA dehydratase

organism: Metallosphaera sedula

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

assay_conditions_summary: pH 7.8; 338.15 K; cofactor CoA

column_label: Table 4 Msed_2001 columns; row (S)-3-Hydroxybutyryl-CoA; Km (mM) column = 0.034 +/- 0.004.

raw_value_unit_evidence: Table 4 row Msed_2001 (S)-3-Hydroxybutyryl-CoA reports Km = 0.034 +/- 0.004 mM.

row_label: Msed_2001 / (S)-3-Hydroxybutyryl-CoA

table_label: Table 4: Catalytic properties of Msed_2001 and homologs

source_databases_merged: brenda skid uniprot

enzyme: 3-hydroxypropionyl-CoA dehydratase


substrate_name: acryloyl-CoA

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

assay_conditions_summary: pH 7.8; cofactor CoA

substrate: acryloyl-CoA


substrate_name: (E)-octenoyl-CoA

column_label: Table 4 Msed_2001 columns; row (E)-2-Octenoyl-CoA; Km (mM) column = 0.048 +/- 0.005.

raw_value_unit_evidence: Table 4 row Msed_2001 (E)-2-Octenoyl-CoA reports Km = 0.048 +/- 0.005 mM.

row_label: Msed_2001 / (E)-2-Octenoyl-CoA

substrate: (E)-octenoyl-CoA


substrate_name: crotonyl-CoA

column_label: Table 4 Msed_2001 columns; row crotonyl-CoA; Km (mM) column = 0.08 +/- 0.01.

raw_value_unit_evidence: Table 4 row Msed_2001 crotonyl-CoA reports Km = 0.08 +/- 0.01 mM.

row_label: Msed_2001 / crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: methacrylyl-CoA

substrate: methacrylyl-CoA


enzyme_display_name: tetracenomycin F2 cyclase

organism: Streptomyces glaucescens

substrate_name: tetracenomycin F2

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature D27N to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'D27N'; column 'Km (uM)' = 1.05 x 10^3; column 'Vmax (umol min^-1 mg^-1)' = 0.0948; column 'Relative activity' = 14; column 'kcat (s^-1)' = 0.0198; column 'Kcat/Km (M^-1 s^-1)' = 18.8.

normalized_value_unit_evidence: Km: printed Table I cell 1.05 x 10^3 uM; 1.05 x 10^3 uM / 1000 = 1.05 mM; the exported value is 1.05 mM. kcat: printed Table I cell 0.0198 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0198 s^(-1). kcat/Km: printed Table I cell 18.8 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 18.8 M^-1 s^-1 / 1000 = 0.0188 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'D27N': Km = 1.05 x 10^3 uM; Vmax = 0.0948 umol min^-1 mg^-1; relative activity = 14; kcat = 0.0198 s^-1; printed Kcat/Km = 18.8 M^-1 s^-1.

row_label: Table I, variant row 'D27N'

table_label: Table I: Kinetic data for the TcmI active site mutants (J. Biol. Chem. 2004, 279(36):37956-37963)

enzyme: tetracenomycin F2 cyclase

substrate: tetracenomycin F2


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature H26A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'H26A'; column 'Km (uM)' = 732; column 'Vmax (umol min^-1 mg^-1)' = 0.0920; column 'Relative activity' = 15; column 'kcat (s^-1)' = 0.0192; column 'Kcat/Km (M^-1 s^-1)' = 26.2.

normalized_value_unit_evidence: Km: printed Table I cell 732 uM; 732 uM / 1000 = 0.732 mM; the exported value is 0.732 mM. kcat: printed Table I cell 0.0192 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0192 s^(-1). kcat/Km: printed Table I cell 26.2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 26.2 M^-1 s^-1 / 1000 = 0.0262 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'H26A': Km = 732 uM; Vmax = 0.0920 umol min^-1 mg^-1; relative activity = 15; kcat = 0.0192 s^-1; printed Kcat/Km = 26.2 M^-1 s^-1.

row_label: Table I, variant row 'H26A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature H26Q to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'H26Q'; column 'Km (uM)' = 203; column 'Vmax (umol min^-1 mg^-1)' = 0.627; column 'Relative activity' = 91; column 'kcat (s^-1)' = 0.131; column 'Kcat/Km (M^-1 s^-1)' = 645.

normalized_value_unit_evidence: Km: printed Table I cell 203 uM; 203 uM / 1000 = 0.203 mM; the exported value is 0.203 mM. kcat: printed Table I cell 0.131 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.131 s^(-1). kcat/Km: printed Table I cell 645 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 645 M^-1 s^-1 / 1000 = 0.645 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'H26Q': Km = 203 uM; Vmax = 0.627 umol min^-1 mg^-1; relative activity = 91; kcat = 0.131 s^-1; printed Kcat/Km = 645 M^-1 s^-1.

row_label: Table I, variant row 'H26Q'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature H51A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'H51A'; column 'Km (uM)' = 892; column 'Vmax (umol min^-1 mg^-1)' = 0.105; column 'Relative activity' = 16; column 'kcat (s^-1)' = 0.0219; column 'Kcat/Km (M^-1 s^-1)' = 24.5.

normalized_value_unit_evidence: Km: printed Table I cell 892 uM; 892 uM / 1000 = 0.892 mM; the exported value is 0.892 mM. kcat: printed Table I cell 0.0219 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0219 s^(-1). kcat/Km: printed Table I cell 24.5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 24.5 M^-1 s^-1 / 1000 = 0.0245 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'H51A': Km = 892 uM; Vmax = 0.105 umol min^-1 mg^-1; relative activity = 16; kcat = 0.0219 s^-1; printed Kcat/Km = 24.5 M^-1 s^-1.

row_label: Table I, variant row 'H51A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature H51Q to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'H51Q'; column 'Km (uM)' = 191; column 'Vmax (umol min^-1 mg^-1)' = 0.651; column 'Relative activity' = 96; column 'kcat (s^-1)' = 0.136; column 'Kcat/Km (M^-1 s^-1)' = 712.

normalized_value_unit_evidence: Km: printed Table I cell 191 uM; 191 uM / 1000 = 0.191 mM; the exported value is 0.191 mM. kcat: printed Table I cell 0.136 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.136 s^(-1). kcat/Km: printed Table I cell 712 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 712 M^-1 s^-1 / 1000 = 0.712 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'H51Q': Km = 191 uM; Vmax = 0.651 umol min^-1 mg^-1; relative activity = 96; kcat = 0.136 s^-1; printed Kcat/Km = 712 M^-1 s^-1.

row_label: Table I, variant row 'H51Q'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature R40G to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'R40G'; column 'Km (uM)' = 1.20 x 10^3; column 'Vmax (umol min^-1 mg^-1)' = 0.0703; column 'Relative activity' = 10; column 'kcat (s^-1)' = 0.0146; column 'Kcat/Km (M^-1 s^-1)' = 12.1.

normalized_value_unit_evidence: Km: printed Table I cell 1.20 x 10^3 uM; 1.20 x 10^3 uM / 1000 = 1.2 mM; the exported value is 1.2 mM. kcat: printed Table I cell 0.0146 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0146 s^(-1). kcat/Km: printed Table I cell 12.1 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12.1 M^-1 s^-1 / 1000 = 0.0121 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'R40G': Km = 1.20 x 10^3 uM; Vmax = 0.0703 umol min^-1 mg^-1; relative activity = 10; kcat = 0.0146 s^-1; printed Kcat/Km = 12.1 M^-1 s^-1.

row_label: Table I, variant row 'R40G'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature R40K to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'R40K'; column 'Km (uM)' = 816; column 'Vmax (umol min^-1 mg^-1)' = 0.108; column 'Relative activity' = 16; column 'kcat (s^-1)' = 0.0250; column 'Kcat/Km (M^-1 s^-1)' = 30.6.

normalized_value_unit_evidence: Km: printed Table I cell 816 uM; 816 uM / 1000 = 0.816 mM; the exported value is 0.816 mM. kcat: printed Table I cell 0.0250 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.025 s^(-1). kcat/Km: printed Table I cell 30.6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 30.6 M^-1 s^-1 / 1000 = 0.0306 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'R40K': Km = 816 uM; Vmax = 0.108 umol min^-1 mg^-1; relative activity = 16; kcat = 0.0250 s^-1; printed Kcat/Km = 30.6 M^-1 s^-1.

row_label: Table I, variant row 'R40K'


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

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'Wild type'; column 'Km (uM)' = 155; column 'Vmax (umol min^-1 mg^-1)' = 0.680; column 'Relative activity' = 100; column 'kcat (s^-1)' = 0.142; column 'Kcat/Km (M^-1 s^-1)' = 916.

normalized_value_unit_evidence: Km: printed Table I cell 155 uM; 155 uM / 1000 = 0.155 mM; the exported value is 0.155 mM. kcat: printed Table I cell 0.142 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.142 s^(-1). kcat/Km: printed Table I cell 916 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 916 M^-1 s^-1 / 1000 = 0.916 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'Wild type': Km = 155 uM; Vmax = 0.680 umol min^-1 mg^-1; relative activity = 100; kcat = 0.142 s^-1; printed Kcat/Km = 916 M^-1 s^-1.

row_label: Table I, variant row 'Wild type'


substrate_name: Dermatan sulfate

proof_lines:
Bacteroides thetaiotaomicron
chondroitinase ABC
dermatan sulfate

substrate: Dermatan sulfate


substrate_name: Chondroitin 4-sulfate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C5G6D7 and applied mutation signature H453A to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic analysis of BactnABC and its mutants (Glycobiology 2008, volume 18, number 3, pages 270-277); each substrate block prints the column heads KM (uM), kcat (min^-1) and kcat/KM (uM^-1 min^-1). CS-A block, enzyme row H453A; column KM (uM) = 38; column kcat (min^-1) = 1,057; column kcat/KM (uM^-1 min^-1) = 27.8. captured primary segment: Table III. Kinetic analysis of BactnABC and its mutants | CS-A | H453A | KM 38 uM | kcat 1,057 min^-1 | kcat/KM 27.8 uM^-1 min^-1 | assay pH 7.6, 37 C

raw_value_unit_evidence: Table III, CS-A block, enzyme row H453A: KM = 38 uM; kcat = 1,057 min^-1; printed kcat/KM = 27.8 uM^-1 min^-1.

row_label: Table III, CS-A block, enzyme row H453A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C5G6D7 and applied mutation signature H344A to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic analysis of BactnABC and its mutants (Glycobiology 2008, volume 18, number 3, pages 270-277); each substrate block prints the column heads KM (uM), kcat (min^-1) and kcat/KM (uM^-1 min^-1). CS-A block, enzyme row H344A; column KM (uM) = 202; column kcat (min^-1) = 5,560; column kcat/KM (uM^-1 min^-1) = 27.5. captured primary segment: Table III. Kinetic analysis of BactnABC and its mutants | CS-A | H344A | KM 202 uM | kcat 5,560 min^-1 | kcat/KM 27.5 uM^-1 min^-1 | assay pH 7.6, 37 C

raw_value_unit_evidence: Table III, CS-A block, enzyme row H344A: KM = 202 uM; kcat = 5,560 min^-1; printed kcat/KM = 27.5 uM^-1 min^-1.

row_label: Table III, CS-A block, enzyme row H344A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C5G6D7 and applied mutation signature Q173A to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic analysis of BactnABC and its mutants (Glycobiology 2008, volume 18, number 3, pages 270-277); each substrate block prints the column heads KM (uM), kcat (min^-1) and kcat/KM (uM^-1 min^-1). CS-A block, enzyme row Q173A; column KM (uM) = 102; column kcat (min^-1) = 7,389; column kcat/KM (uM^-1 min^-1) = 72.4. captured primary segment: Table III. Kinetic analysis of BactnABC and its mutants | CS-A | Q173A | KM 102 uM | kcat 7,389 min^-1 | kcat/KM 72.4 uM^-1 min^-1 | assay pH 7.6, 37 C

raw_value_unit_evidence: Table III, CS-A block, enzyme row Q173A: KM = 102 uM; kcat = 7,389 min^-1; printed kcat/KM = 72.4 uM^-1 min^-1.

row_label: Table III, CS-A block, enzyme row Q173A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C5G6D7 and applied mutation signature R267A to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic analysis of BactnABC and its mutants (Glycobiology 2008, volume 18, number 3, pages 270-277); each substrate block prints the column heads KM (uM), kcat (min^-1) and kcat/KM (uM^-1 min^-1). CS-A block, enzyme row R267A; column KM (uM) = 109; column kcat (min^-1) = 12,320; column kcat/KM (uM^-1 min^-1) = 113.0. captured primary segment: Table III. Kinetic analysis of BactnABC and its mutants | CS-A | R267A | KM 109 uM | kcat 12,320 min^-1 | kcat/KM 113.0 uM^-1 min^-1 | assay pH 7.6, 37 C

raw_value_unit_evidence: Table III, CS-A block, enzyme row R267A: KM = 109 uM; kcat = 12,320 min^-1; printed kcat/KM = 113.0 uM^-1 min^-1.

row_label: Table III, CS-A block, enzyme row R267A


column_label: Table III: Kinetic analysis of BactnABC and its mutants (Glycobiology 2008, volume 18, number 3, pages 270-277); each substrate block prints the column heads KM (uM), kcat (min^-1) and kcat/KM (uM^-1 min^-1). DS block, enzyme row H453A; column KM (uM) = 44; column kcat (min^-1) = 352; column kcat/KM (uM^-1 min^-1) = 8.0. captured primary segment: Table III. Kinetic analysis of BactnABC and its mutants | DS | H453A | KM 44 uM | kcat 352 min^-1 | kcat/KM 8.0 uM^-1 min^-1 | assay pH 7.6, 37 C

raw_value_unit_evidence: Table III, DS block, enzyme row H453A: KM = 44 uM; kcat = 352 min^-1; printed kcat/KM = 8.0 uM^-1 min^-1.

row_label: Table III, DS block, enzyme row H453A


column_label: Table III: Kinetic analysis of BactnABC and its mutants (Glycobiology 2008, volume 18, number 3, pages 270-277); each substrate block prints the column heads KM (uM), kcat (min^-1) and kcat/KM (uM^-1 min^-1). DS block, enzyme row Q173A; column KM (uM) = 71; column kcat (min^-1) = 408; column kcat/KM (uM^-1 min^-1) = 5.7. captured primary segment: Table III. Kinetic analysis of BactnABC and its mutants | DS | Q173A | KM 71 uM | kcat 408 min^-1 | kcat/KM 5.7 uM^-1 min^-1 | assay pH 7.6, 37 C

raw_value_unit_evidence: Table III, DS block, enzyme row Q173A: KM = 71 uM; kcat = 408 min^-1; printed kcat/KM = 5.7 uM^-1 min^-1.

row_label: Table III, DS block, enzyme row Q173A


column_label: Table III: Kinetic analysis of BactnABC and its mutants (Glycobiology 2008, volume 18, number 3, pages 270-277); each substrate block prints the column heads KM (uM), kcat (min^-1) and kcat/KM (uM^-1 min^-1). DS block, enzyme row R267A; column KM (uM) = 71; column kcat (min^-1) = 250; column kcat/KM (uM^-1 min^-1) = 3.5. captured primary segment: Table III. Kinetic analysis of BactnABC and its mutants | DS | R267A | KM 71 uM | kcat 250 min^-1 | kcat/KM 3.5 uM^-1 min^-1 | assay pH 7.6, 37 C

raw_value_unit_evidence: Table III, DS block, enzyme row R267A: KM = 71 uM; kcat = 250 min^-1; printed kcat/KM = 3.5 uM^-1 min^-1.

row_label: Table III, DS block, enzyme row R267A


column_label: Table III: Kinetic analysis of BactnABC and its mutants (Glycobiology 2008, volume 18, number 3, pages 270-277); each substrate block prints the column heads KM (uM), kcat (min^-1) and kcat/KM (uM^-1 min^-1). DS block, enzyme row WT; column KM (uM) = 61; column kcat (min^-1) = 2,307; column kcat/KM (uM^-1 min^-1) = 37.8. captured primary segment: Table III. Kinetic analysis of BactnABC and its mutants | DS | WT | KM 61 uM | kcat 2,307 min^-1 | kcat/KM 37.8 uM^-1 min^-1 | assay pH 7.6, 37 C

raw_value_unit_evidence: Table III, DS block, enzyme row WT: KM = 61 uM; kcat = 2,307 min^-1; printed kcat/KM = 37.8 uM^-1 min^-1.

row_label: Table III, DS block, enzyme row WT


organism: Fusarium oxysporum

substrate_name: Gum arabic

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

substrate: Gum arabic


enzyme_display_name: threonine synthase

organism: Lemna aequinoctialis

proof_lines: at saturating S-adenosylmethionine concentrations

enzyme: threonine synthase


enzyme_display_name: ethanolamine-phosphate phospho-lyase

organism: Achromobacter sp.

substrate_name: Ethanolamine phosphate

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

enzyme: ethanolamine-phosphate phospho-lyase

substrate: Ethanolamine phosphate


organism: Homo sapiens

assay_conditions_summary: pH 7.4; buffer pH 7; cofactor NADPH

column_label: Table 2 row Glu-P-1 / Wild-type lists KM 4 uM.

raw_value_unit_evidence: Km raw_value=4 raw_unit=uM

row_label: Glu-P-1 / Wild-type

table_label: Table 2. Kinetic data for P450 1A2 variants.


column_label: Table 2 row IQ / Wild-type lists KM 21 uM.

raw_value_unit_evidence: Km raw_value=21 raw_unit=uM

row_label: IQ / Wild-type


column_label: Table 2 row MeIQx / Wild-type lists KM 27 uM.

raw_value_unit_evidence: Km raw_value=27 raw_unit=uM

row_label: MeIQx / Wild-type


column_label: Table 2 row PhIP / Wild-type lists KM 71 uM.

raw_value_unit_evidence: Km raw_value=71 raw_unit=uM

row_label: PhIP / Wild-type


substrate_name: phenacetin

column_label: Table 2 row Phenacetin / Wild-type lists KM 25 uM.

raw_value_unit_evidence: Km raw_value=25 raw_unit=uM

row_label: Phenacetin / Wild-type

substrate: phenacetin


organism: Flavobacterium rhenanum


organism: Microbacterium arborescens


enzyme_display_name: methylglyoxal synthase

organism: Saccharomyces cerevisiae

substrate_name: dihydroxyacetone phosphate

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

enzyme: methylglyoxal synthase

substrate: dihydroxyacetone phosphate


enzyme_display_name: chorismate synthase

organism: Euglena gracilis

substrate_name: 5-enolpyruvylshikimate 3-phosphate

enzyme: chorismate synthase

substrate: 5-enolpyruvylshikimate 3-phosphate


organism: Beta vulgaris

substrate_name: O-Phospho-L-homoserine; H2O

substrate: O-Phospho-L-homoserine; H2O


substrate_name: O-phosphohomoserine

substrate: O-phosphohomoserine


enzyme_display_name: 2-methylfumaryl-CoA hydratase

organism: Haloarcula hispanica

column_label: PDF Table 4 row Mesaconyl-C4-CoA / 3-methylfumaryl-CoA; Km column reports Km 0.18 +/- 0.01 mM, matching the exported Km-only record.

row_label: Mesaconyl-C4-CoA / 3-methylfumaryl-CoA

table_label: Table 4. Catalytic properties of recombinant Mch from H. hispanica

enzyme: 2-methylfumaryl-CoA hydratase


substrate_name: (S)-malyl-CoA

column_label: PMC5592240 Table 4 reports (S)-Malyl-CoA Km = 0.32 +/- 0.05 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=0.32 +/- 0.05 mM raw_unit=mM

row_label: Row: (S)-Malyl-CoA

table_label: PMC5592240 Table 4

substrate: (S)-malyl-CoA


column_label: PDF Table 4 row Mesaconyl-C1-CoA / 2-methylfumaryl-CoA; Km column reports Km 1.0 +/- 0.1 mM, matching the exported Km-only record.

row_label: Mesaconyl-C1-CoA / 2-methylfumaryl-CoA


organism: Solanum lycopersicum

proof_lines:
isozyme MatCS1
isozyme MatCS2


enzyme_display_name: 3-dehydroquinate synthase

organism: Providencia alcalifaciens

enzyme: 3-dehydroquinate synthase


enzyme_display_name: chondroitin-sulfate-ABC exolyase

organism: Proteus vulgaris

substrate_name: dermatan sulfate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y508F with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

enzyme: chondroitin-sulfate-ABC exolyase

substrate: dermatan sulfate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +13, so it is treated as a source-provided variant sequence.


enzyme_display_name: chondroitin B lyase

organism: Pedobacter heparinus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E333A to reconstruct the assayed variant sequence.

enzyme: chondroitin B lyase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H272A to reconstruct the assayed variant sequence.


proof_lines: recombinant wild-type enzyme, pH 8.0, 30°C, in presence of 0.01 mM Ca2+

proof_lines: recombinant wild-type enzyme, pH 8.0, 30°C, in presence of 5 mM Ca2+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R363A to reconstruct the assayed variant sequence.


organism: Thermus sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R97E to reconstruct the assayed variant sequence.

proof_lines: mutant R97E, Hill coefficient 3.7, presence of 1 mM phosphate, pH 6.5, 60°C

proof_lines: mutant R97E, Hill coefficient 3.4, pH 6.5, 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature ΔR97 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: mutant DELTAR97, Hill coefficient 5.2, presence of 1 mM phosphate, pH 6.5, 60°C

proof_lines: mutant DELTAR97, Hill coefficient 3.3, pH 6.5, 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R97K to reconstruct the assayed variant sequence.

proof_lines: mutant R97K, Hill coefficient 1.5, presence of 1 mM phosphate, pH 6.5, 60°C

proof_lines: mutant R97K, Hill coefficient 1.55, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: mutant R97K, Hill coefficient 1.5, pH 6.5, 60°C


organism: Oryctolagus cuniculus

substrate_name: dihydroxyacetone phosphate (at pH 7.9)

proof_lines: The kcat is 900 sec(-1) for the isomerization of dihydroxyacetone phosphate (PubMed:2021650). The kcat is 0.011 sec(-1) for the production of methylglyoxal via the elimination reaction (PubMed:2021650). Produces methylglyoxal with a calcula

substrate: dihydroxyacetone phosphate (at pH 7.9)


organism: Escherichia coli

substrate_name: Glycerone phosphate

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

proof_lines: kcat is 220 sec(-1) with dihydroxyacetone phosphate as substrate.

source_databases_merged: sabio_rk skid uniprot

substrate: Glycerone phosphate


proof_lines: carrying two additional His residues between residues Arg22 and His23, Hill coefficient 2.12, pH 6.2, 60°C

proof_lines: carrying one additional His residue between residues Arg22 and His23, Hill coefficient 1.58, pH 6.2, 60°C

source_databases_merged: brenda skid


organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 0.87 sec(-1) for chorismate formation.

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D10N to reconstruct the assayed variant sequence.

proof_lines: mutant carrying C-terminal extension YQRYLADRLK C-terminal extension YQRYLADRLK plus mutation D10N, pH 6.0, 60°C, Hill coefficient 1.5

proof_lines: mutant D10N, pH 6.0, 60°C, Hill coefficient 1.5


organism: Arabidopsis thaliana


substrate_name: H2O; Ethanolamine phosphate

substrate: H2O; Ethanolamine phosphate


organism: Actinidia chinensis


organism: Pyrococcus furiosus


organism: Aspergillus nidulans

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R130K with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Neurospora crassa

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S16A to reconstruct the assayed variant sequence.


organism: Homo sapiens

substrate_name: Unknown

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

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G56S to reconstruct the assayed variant sequence.

smiles: O=C(CO)COP(=O)(O)O


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G56S to reconstruct the assayed variant sequence.

proof_lines: mutant G56S, Hill coefficient 2.8, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: mutant G56S, Hill coefficient 2.3, pH 6.5, 60°C


organism: Escherichia coli (strain K12)

proof_lines: kcat is 16.5 sec(-1) for phospholyase activity with EPSP as substrate. kcat is 27 sec(-1) for phospholyase activity with EPSP as substrate.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S127A to reconstruct the assayed variant sequence.


organism: Thermus sp. GH5

substrate_name: glycerone phosphate

substrate: glycerone phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D100V with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80I with inferred residue-numbering offset -39 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D100N with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80K with inferred residue-numbering offset -39 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80D/D100R with inferred residue-numbering offset -39 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R80D/D100R, at pH 6.2 and 60°C


proof_lines: wild-type, Hill coefficient 1.5, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: wild-type, Hill coefficient 2.2, pH 6.2, 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G56A to reconstruct the assayed variant sequence.

proof_lines: mutant G56A, Hill coefficient 1.6, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: mutant G56A, Hill coefficient 2, pH 6.5, 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V101I to reconstruct the assayed variant sequence.

proof_lines: mutant V101I, Hill coefficient 1.4, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: mutant V101I, Hill coefficient 1.44, pH 6.5, 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S55K to reconstruct the assayed variant sequence.

proof_lines: mutant S55K, Hill coefficient 1.3, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: mutant S55K, Hill coefficient 1.3, pH 6.5, 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V101S to reconstruct the assayed variant sequence.

proof_lines: mutant V101S, Hill coefficient 1.22, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: mutant V101S, Hill coefficient 1.3, pH 6.5, 60°C


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

proof_lines: mutant mutant carrying C-terminus of Escherichia coli enzyme, Hill coefficient 1.99, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: mutant carrying C-terminus of Escherichia coli enzyme, Hill coefficient 0.87, pH 6.5, 60°C

proof_lines: mutant carrying C-terminal extension YQRYLADRLK, pH 6.0, 60°C, Hill coefficient 1.5


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V101A to reconstruct the assayed variant sequence.

proof_lines: mutant V101A, Hill coefficient 1.45, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: mutant V101A, Hill coefficient 1, pH 6.5, 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S55D to reconstruct the assayed variant sequence.

proof_lines: mutant S55D, Hill coefficient 1.2, presence of 1.5 mM phosphate, pH 6.5, 60°C

proof_lines: mutant S55D, Hill coefficient 1, pH 6.5, 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D101E to reconstruct the assayed variant sequence.

proof_lines:
methylglyoxal synthase
Asp 101
kcat/Km


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D101N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A731 and applied mutation signature D20E to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic Constants for wt and Mutant MGS at 0.0 mM Pi (Biochemistry 1998, 37, 10074-10086); enzyme form row 'D20E'; column 'KM (mM)' = 0.18; column 'kcat (s-1)' = 0.959; column 'kcat/KM (mM-1 s-1)' = 5.3; column 'fold inactivation' = 2.1 x 10^2. The title of the table fixes 0.0 mM Pi for every row it lists.

normalized_value_unit_evidence: Km: printed cell 0.18 mM; the printed unit is already the canonical unit, so the value carries over as 0.18 mM. kcat: printed cell 0.959 s^-1; the printed unit is already the canonical unit, so the value carries over as 0.959 s^(-1). kcat/Km: the exported efficiency is the full-precision quotient of those same two printed cells, 0.959 / 0.18 = 5.3277777777777775 s^(-1)*mM^(-1), and the paper's own efficiency cell 5.3 mM^-1 s^-1 is that quotient rendered at the table's two-digit printed precision (5.3 s^(-1)*mM^(-1) in canonical units).

raw_value_unit_evidence: Table 5, enzyme form row 'D20E': KM = 0.18 mM; kcat = 0.959 s^-1; kcat/KM = 5.3 mM^-1 s^-1.

row_label: Table 5, enzyme form row 'D20E', the DHAP kinetic cells of that row


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D71E with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines:
methylglyoxal synthase
Asp 71
kcat/Km


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D71N with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A731 and applied mutation signature D91E to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic Constants for wt and Mutant MGS at 0.0 mM Pi (Biochemistry 1998, 37, 10074-10086); enzyme form row 'D91E'; column 'KM (mM)' = 0.41; column 'kcat (s-1)' = 0.564; column 'kcat/KM (mM-1 s-1)' = 1.4; column 'fold inactivation' = 7.9 x 10^2. The title of the table fixes 0.0 mM Pi for every row it lists.

normalized_value_unit_evidence: Km: printed cell 0.41 mM; the printed unit is already the canonical unit, so the value carries over as 0.41 mM. kcat: printed cell 0.564 s^-1; the printed unit is already the canonical unit, so the value carries over as 0.564 s^(-1). kcat/Km: the exported efficiency is the full-precision quotient of those same two printed cells, 0.564 / 0.41 = 1.3756097560975609 s^(-1)*mM^(-1), and the paper's own efficiency cell 1.4 mM^-1 s^-1 is that quotient rendered at the table's two-digit printed precision (1.4 s^(-1)*mM^(-1) in canonical units).

raw_value_unit_evidence: Table 5, enzyme form row 'D91E': KM = 0.41 mM; kcat = 0.564 s^-1; kcat/KM = 1.4 mM^-1 s^-1.

row_label: Table 5, enzyme form row 'D91E', the DHAP kinetic cells of that row


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A731 and applied mutation signature D91N to reconstruct the assayed variant sequence.

column_label: Table 6: Apparent Kinetic Constants for wt and Mutant Methylglyoxal Synthase in the Presence of Pi (Biochemistry 1998, 37, 10074-10086); enzyme form row 'D91N'; column 'KM (mM)' = 0.56; column 'kcat (s-1)' = 1.60; the 'Hill coefficient' cell of this row is empty and the 'equation used' cell reads 1. Table 6 prints no efficiency column. The spanning column head fixes 0.3 mM Pi for every row it lists.

normalized_value_unit_evidence: Km: printed cell 0.56 mM; the printed unit is already the canonical unit, so the value carries over as 0.56 mM. kcat: printed cell 1.60 s^-1; the printed unit is already the canonical unit, so the value carries over as 1.6 s^(-1). kcat/Km: the paper prints no efficiency cell for this row, so the efficiency is the full-precision quotient of the same measurement's own two printed cells, 1.60 / 0.56 = 2.857142857142857 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 6, enzyme form row 'D91N': KM = 0.56 mM; kcat = 1.60 s^-1; the table prints no efficiency cell.

row_label: Table 6, enzyme form row 'D91N', the DHAP kinetic cells of that row


substrate_name: EPSP

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

proof_lines: kcat is 16.5 sec(-1) for phospholyase activity with EPSP as substrate. kcat is 27 sec(-1) for phospholyase activity with EPSP as substrate.

substrate: EPSP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D100N with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D100V with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R80D/D100R with inferred residue-numbering offset -19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R80I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R80K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +13, so it is treated as a source-provided variant sequence.


organism: Capnoides sempervirens


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R97K to reconstruct the assayed variant sequence.

proof_lines:
methylglyoxal synthase
Thermus sp. GH5
Arg-97


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B3VH91 and applied mutation signature G56A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of the wild-type TMGS and the mutant enzymes), enzyme row 'G56A', sub-row with column 'Phosphate concentration (mM)' = 0; column 'kcat (s^-1)' = 1.3 x 10^-4; column 'Km (mM)' = 2.40; column 'kcat/Km' = 5.4 x 10^-5; column 'nH' = 2.

normalized_value_unit_evidence: kcat: printed Table I cell 1.3 x 10^-4 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.00013 s^(-1). Km: printed Table I cell 2.40 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 2.4 mM. kcat/Km: printed Table I cell 5.4 x 10^-5 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 0.000054 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme row 'G56A', phosphate concentration 0 mM sub-row: kcat = 1.3 x 10^-4 s^-1; Km = 2.40 mM; printed kcat/Km = 5.4 x 10^-5 s^-1 mM^-1.

table_label: Table I: Kinetic parameters of the wild-type TMGS and the mutant enzymes (Protein Engineering, Design & Selection 2013, 26(7):445-452)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B3VH91 and applied mutation signature S55D to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of the wild-type TMGS and the mutant enzymes), enzyme row 'S55D', sub-row with column 'Phosphate concentration (mM)' = 0; column 'kcat (s^-1)' = 300; column 'Km (mM)' = 2.76; column 'kcat/Km' = 110; column 'nH' = 1.

normalized_value_unit_evidence: kcat: printed Table I cell 300 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 300 s^(-1). Km: printed Table I cell 2.76 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 2.76 mM. kcat/Km: printed Table I cell 110 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 110 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme row 'S55D', phosphate concentration 0 mM sub-row: kcat = 300 s^-1; Km = 2.76 mM; printed kcat/Km = 110 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B3VH91 and applied mutation signature S55K to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of the wild-type TMGS and the mutant enzymes), enzyme row 'S55K', sub-row with column 'Phosphate concentration (mM)' = 0; column 'kcat (s^-1)' = 1.0; column 'Km (mM)' = 0.08; column 'kcat/Km' = 12; column 'nH' = 1.3.

normalized_value_unit_evidence: kcat: printed Table I cell 1.0 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 1 s^(-1). Km: printed Table I cell 0.08 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 0.08 mM. kcat/Km: printed Table I cell 12 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 12 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme row 'S55K', phosphate concentration 0 mM sub-row: kcat = 1.0 s^-1; Km = 0.08 mM; printed kcat/Km = 12 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B3VH91 and applied mutation signature V101A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of the wild-type TMGS and the mutant enzymes), enzyme row 'V101A', sub-row with column 'Phosphate concentration (mM)' = 0; column 'kcat (s^-1)' = 338; column 'Km (mM)' = 1.03; column 'kcat/Km' = 330; column 'nH' = 1.0.

normalized_value_unit_evidence: kcat: printed Table I cell 338 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 338 s^(-1). Km: printed Table I cell 1.03 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 1.03 mM. kcat/Km: printed Table I cell 330 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 330 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme row 'V101A', phosphate concentration 0 mM sub-row: kcat = 338 s^-1; Km = 1.03 mM; printed kcat/Km = 330 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B3VH91 and applied mutation signature V101I to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of the wild-type TMGS and the mutant enzymes), enzyme row 'V101I', sub-row with column 'Phosphate concentration (mM)' = 0; column 'kcat (s^-1)' = 0.75; column 'Km (mM)' = 1.44; column 'kcat/Km' = 0.52; column 'nH' = 1.44.

normalized_value_unit_evidence: kcat: printed Table I cell 0.75 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.75 s^(-1). Km: printed Table I cell 1.44 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 1.44 mM. kcat/Km: printed Table I cell 0.52 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 0.52 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme row 'V101I', phosphate concentration 0 mM sub-row: kcat = 0.75 s^-1; Km = 1.44 mM; printed kcat/Km = 0.52 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B3VH91 and applied mutation signature V101S to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of the wild-type TMGS and the mutant enzymes), enzyme row 'V101S', sub-row with column 'Phosphate concentration (mM)' = 0; column 'kcat (s^-1)' = 1.4; column 'Km (mM)' = 1.65; column 'kcat/Km' = 0.86; column 'nH' = 1.3.

normalized_value_unit_evidence: kcat: printed Table I cell 1.4 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 1.4 s^(-1). Km: printed Table I cell 1.65 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 1.65 mM. kcat/Km: printed Table I cell 0.86 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 0.86 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, enzyme row 'V101S', phosphate concentration 0 mM sub-row: kcat = 1.4 s^-1; Km = 1.65 mM; printed kcat/Km = 0.86 s^-1 mM^-1.


enzyme_display_name: guluronate-specific alginate lyase

organism: Saccharophagus degradans

substrate_name: sodium alginate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H202L with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

enzyme: guluronate-specific alginate lyase

substrate: sodium alginate


sequence_variant_note: Mutation signature Q149A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R260A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R438A 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.

column_label: Table 2 row Wild type; columns Km, kcat, kcat/Km

row_label: Wild type Alg17c

table_label: PMCID PMC3961687 Table 2


enzyme_display_name: enoyl-CoA hydratase 2

organism: Aeromonas caviae

assay_conditions_summary: cofactor CoA

proof_lines: trans-2-enoyl-CoA substrates with four to six carbon atoms

enzyme: enoyl-CoA hydratase 2


enzyme_display_name: 3-dehydroshikimate dehydratase

organism: Bacillus anthracis

enzyme: 3-dehydroshikimate dehydratase


enzyme_display_name: chondroitin-sulfate-ABC endolyase

organism: Proteus vulgaris

substrate_name: chondroitin 4-sulfate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q140A to reconstruct the assayed variant sequence.

proof_lines:
chondroitinase ABC I
Q140A
activity

enzyme: chondroitin-sulfate-ABC endolyase

substrate: chondroitin 4-sulfate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q140G to reconstruct the assayed variant sequence.

proof_lines:
chondroitinase ABC I
Q140G
activity


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q140N to reconstruct the assayed variant sequence.

proof_lines:
chondroitinase ABC I
Q140N
activity


proof_lines:
chondroitinase ABC I
wild type
Q140G


enzyme_display_name: oligo-alginate lyase

organism: Stenotrophomonas maltophilia

substrate_name: (Alginate)n

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

column_label: Table 1 WT columns kCAT (s^-1), KM (mM), and kCAT/KM for row Alginate under pH 8.5 alginate-based polysaccharide assay.

raw_value_unit_evidence: Table 1 WT Alginate: kCAT 34.8 s^-1; KM 0.67 mM; kCAT/KM 52.2 s^-1*mM^-1

row_label: WT Alginate

enzyme: oligo-alginate lyase

substrate: (Alginate)n


substrate_name: alginate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H208F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: alginate


assay_conditions_summary: pH 8; 298.15 K; buffer pH 8


enzyme_display_name: Casbene synthase, chloroplastic

organism: Ricinus communis

substrate_name: geranylgeranyl diphosphate

enzyme: Casbene synthase, chloroplastic

substrate: geranylgeranyl diphosphate


enzyme_display_name: UniProt P27213

organism: Rattus norvegicus

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.4

enzyme: UniProt P27213


enzyme_display_name: UniProt Q39761

organism: Gossypium arboreum

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

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

enzyme: UniProt Q39761

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


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

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


substrate_name: nerolidyl diphosphate

substrate: nerolidyl diphosphate


enzyme_display_name: 3-hydroxypropionyl-CoA dehydratase

organism: Metallosphaera sedula

column_label: Table 3 reports apparent Km for (S)-3-hydroxybutyryl-CoA as 75 uM; adjacent prose reports the apparent Km value was 75 uM and the extrapolated Vmax was 34 umol min^-1 mg^-1.

normalized_value_unit_evidence: Km normalized_value=0.075 normalized_unit=mM; Vmax normalized_value=0.0005666667 normalized_unit=mol*s^(-1)*g^(-1)

raw_value_unit_evidence: Km raw_value=75 raw_unit=uM; Vmax raw_value=34 raw_unit=umol/min/mg

row_label: M. sedula 3-hydroxypropionyl-CoA dehydratase acting on (S)-3-hydroxybutyryl-CoA

table_label: Table 3 plus adjacent dehydratase properties prose

enzyme: 3-hydroxypropionyl-CoA dehydratase


enzyme_display_name: sabinene-hydrate synthase

organism: Origanum majorana

substrate_name: (3S)-linalyl diphosphate

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

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

enzyme: sabinene-hydrate synthase

substrate: (3S)-linalyl diphosphate


substrate_name: geranyl diphosphate

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

substrate: geranyl diphosphate


substrate_name: 6,7-dihydrogeranyl diphosphate

substrate: 6,7-dihydrogeranyl diphosphate


enzyme_display_name: L-lyxonate dehydratase

organism: Roseibium aggregatum

substrate_name: D-gulonate

enzyme: L-lyxonate dehydratase

substrate: D-gulonate


substrate_name: L-lyxonate

substrate: L-lyxonate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y216F to reconstruct the assayed variant sequence.


enzyme_display_name: (-)-endo-fenchol synthase

organism: Anethum foeniculum

enzyme: (-)-endo-fenchol synthase


substrate_name: 2,3-cyclopropylgeranyl diphosphate

substrate: 2,3-cyclopropylgeranyl diphosphate


enzyme_display_name: colneleate synthase

organism: Solanum tuberosum

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

enzyme: colneleate synthase


smiles: CCC=CCC=CC=CC(CCCCCCCC(=O)[O-])OO


organism: Bacteroides thetaiotaomicron

substrate_name: Chondroitin 4-sulfate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H344Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines:
Bacteroides thetaiotaomicron ChonABC
broad chondroitin sulfate activity
dermatan sulfate activity

substrate: Chondroitin 4-sulfate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H345N with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines:
His345 general base
Bacteroides thetaiotaomicron ChonABC
broad chondroitin sulfate activity


substrate_name: Dermatan sulfate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H344N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines:
Bacteroides thetaiotaomicron ChonABC
dermatan sulfate activity
broad chondroitin sulfate specificity

substrate: Dermatan sulfate


enzyme_display_name: aristolochene synthase

organism: Escherichia coli

substrate_name: farnesyl diphosphate

enzyme: aristolochene synthase

substrate: farnesyl diphosphate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 2-methylisocitrate dehydratase

organism: Escherichia coli (strain K12)

substrate_name: citrate

column_label: Table 1; row Citrate; method LB; AcnB column Km.

raw_value_unit_evidence: Table 1 Citrate AcnB LB cell: Km 11.0 mM.

row_label: Citrate / AcnB / LB

table_label: Table 1

enzyme: 2-methylisocitrate dehydratase

substrate: citrate


substrate_name: cis-aconitate

column_label: Table 1; row cis-Aconitate; method LB; AcnB column Km.

raw_value_unit_evidence: Table 1 cis-Aconitate AcnB LB cell: Km 0.016 mM.

row_label: cis-Aconitate / AcnB / LB

substrate: cis-aconitate


substrate_name: isocitrate (using 0.01-0.8 mM substrate)

column_label: Table 1; row Isocitrate; method LB; AcnB lower-value Km column.

raw_value_unit_evidence: Table 1 Isocitrate AcnB LB lower-value cell: Km 0.051 mM.

row_label: Isocitrate / AcnB / LB / lower-value solution


enzyme_display_name: (+)-delta-cadinene synthase

organism: Phyla dulcis

enzyme: (+)-delta-cadinene synthase


organism: Nicotiana tabacum


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


substrate_name: anilinogeranyl diphosphate

substrate: anilinogeranyl diphosphate


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

proof_lines: in 200 mM Tris-HCl (pH 7.5), 40 mM MgCl2, at 22°C


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

substrate_name: sepiapterin

enzyme: 6-pyruvoyltetrahydropterin synthase

substrate: sepiapterin


enzyme_display_name: pentalenene synthase

organism: Streptomyces exfoliatus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W308F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W308F, pH and temperature not specified in the publication

enzyme: pentalenene synthase

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H309A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H309A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H309S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H309S, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F77Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F77Y, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H309C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H309C, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H309F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H309F, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D84E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D84E, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D81E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D81E, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D80E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D80E, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N219D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N219D, pH and temperature not specified in the publication


organism: Penicillium roqueforti

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature V88F with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant V88F, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L108A to reconstruct the assayed variant sequence.

proof_lines: mutant L108A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T89F to reconstruct the assayed variant sequence.

proof_lines: mutant T89F, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Mutation signature V88A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant V88A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L108F to reconstruct the assayed variant sequence.

proof_lines: mutant L108F, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L108V to reconstruct the assayed variant sequence.

proof_lines: mutant L108V, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T89A to reconstruct the assayed variant sequence.

proof_lines: mutant T89A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L108S to reconstruct the assayed variant sequence.

proof_lines: mutant L108S, pH not specified in the publication, temperature not specified in the publication


substrate_name: trans,trans-Farnesyl diphosphate

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

proof_lines: assay under normal conditions and in D2O, 20 mM Tris, 5 mM MgCl2, 5 mM 2-mercaptoethanol and 15% glycerol

source_databases_merged: sabio_rk brenda skid uniprot

substrate: trans,trans-Farnesyl diphosphate


substrate_name: trans,trans-farnesyl diphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature N244D with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

substrate: trans,trans-farnesyl diphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E252Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y92F to reconstruct the assayed variant sequence.

proof_lines:
pH 8.0, 30°C, mutant enzyme Y92F
pH 7.5, 30°C, mutant enzyme Y92F


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D116E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S248A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D116N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E252D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E119Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E119D with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D115E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W334H to reconstruct the assayed variant sequence.

proof_lines: mutant W334H, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W334L to reconstruct the assayed variant sequence.

proof_lines: mutant W334L, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W334F to reconstruct the assayed variant sequence.

proof_lines: mutant W334F, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W334Y to reconstruct the assayed variant sequence.

proof_lines: mutant W334Y, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: chorismate synthase

organism: Neurospora crassa

substrate_name: NADPH

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

proof_lines: FMN:NADPH oxidoreductase activity, wild-type enzyme

enzyme: chorismate synthase

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H17A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: FMN:NADPH oxidoreductase activity, mutant enzyme H17A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H106A to reconstruct the assayed variant sequence.

proof_lines: FMN:NADPH oxidoreductase activity, mutant enzyme H106A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R200K to reconstruct the assayed variant sequence.

proof_lines: mutant R200K, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D203L to reconstruct the assayed variant sequence.

proof_lines: mutant D203L, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R340K to reconstruct the assayed variant sequence.

proof_lines: mutant R340K, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K251Q to reconstruct the assayed variant sequence.

proof_lines: mutant K251Q, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y341F to reconstruct the assayed variant sequence.

proof_lines: mutant Y341F, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K251R to reconstruct the assayed variant sequence.

proof_lines: mutant K251R, pH not specified in the publication, temperature not specified in the publication


organism: Mus musculus

substrate_name: dihydroneopterin triphosphate

proof_lines: kcat is 0.27 (-1) with dihydroneopterin triphosphate as substrate.

substrate: dihydroneopterin triphosphate


enzyme_display_name: casbene synthase

organism: Ricinus communis

substrate_name: geranylgeranyl diphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H171Q/C519W to reconstruct the assayed variant sequence.

enzyme: casbene synthase

substrate: geranylgeranyl diphosphate


enzyme_display_name: threonine synthase

substrate_name: L-Serine

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

enzyme: threonine synthase

substrate: L-Serine


column_label: The abstract states L-serine (Km = 150 mM, V = 4.7 min-1).

raw_value_unit_evidence: Official PubMed abstract: L-serine; Km=150 mM; V=4.7 min^-1.

row_label: L-serine

table_label: PubMed PMID 7907888 abstract


substrate_name: O-Phospho-L-homoserine

column_label: The abstract states HSerP (Km = 0.5 mM, V = 440 min-1).

raw_value_unit_evidence: Official PubMed abstract: HSerP; Km=0.5 mM; V=440 min^-1.

row_label: L-homoserine phosphate (HSerP)

substrate: O-Phospho-L-homoserine


proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme


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

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

proof_lines: in presence of 0.25 mM inorganic disphosphate, pH and temperature not specified in the publication


organism: Homo sapiens


organism: Aspergillus terreus


proof_lines:
pH 8.0, 30°C, native enzyme
pH 8.0, 30°C, recombinant enzyme
Raw SKiD Env: Temp=30°C, pH=8


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N219D with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UR08 and applied mutation signature N219D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer H (20 mM Hepes pH 8

column_label: Table 2 (Aristolochene Synthase Mutants: Kinetic Parameters and Product Ratios), protein row 'AT-N219D'; column 'kcat (10-3 s-1)' = 0.076; column 'Km (uM)' = 3.9; column 'kcat/Km (s-1 M-1)' = 19.5; column 'aristolochene (4)' = 44; column 'valencene (5)' = ND; column 'germacrene A (2)' = 56.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.076 in the column headed kcat (10-3 s-1), i.e. 0.076 x 10^-3 s^-1 = 0.000076 s^-1. Km: printed Table 2 cell 3.9 uM; 3.9 / 1000 = 0.0039 mM. kcat/Km: printed Table 2 cell 19.5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 19.5 / 1000 = 0.0195 s^(-1)*mM^(-1). The three values this record carries for the row are those three printed cells.

raw_value_unit_evidence: Table 2, protein row 'AT-N219D': kcat = 0.076 in units of 10^-3 s^-1; Km = 3.9 uM; printed kcat/Km = 19.5 M^-1 s^-1.

row_label: Table 2, protein row 'AT-N219D'

table_label: Table 2: Aristolochene Synthase Mutants: Kinetic Parameters and Product Ratios (J. Am. Chem. Soc. 2004, 126(23):7212-7221)


organism: Gossypium arboreum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W279D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W279A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W279E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W279L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W279M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W279Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W279Y to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UR08 and applied mutation signature N299A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer triplicate on a 100-uL scale in assay

column_label: Table 2 (Steady-state kinetic parameters for ATAS mutants), body row 'N299A'; column 'kcat (s-1)' = 0.012; column 'KM (uM)' = 0.41; column 'kcat/KM (M-1s-1)' = 2.9 x 10^4. The value printed after the plus/minus sign beside the kcat and KM cells of this line is the printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.012 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.012 s^(-1). KM: printed Table 2 cell 0.41 in a column headed KM (uM); 1 uM is 0.001 mM, so 0.41 / 1000 = 0.00041 mM. kcat/KM: printed Table 2 cell 2.9 x 10^4 in a column headed kcat/KM (M-1s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^4 / 1000 = 29.0 s^(-1)*mM^(-1). The exported values are kcat 0.012 s^(-1), Km 0.00041 mM and kcat_over_km 29.26829268292683 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'N299A': kcat = 0.012 in a column headed kcat (s-1); KM = 0.41 in a column headed KM (uM); printed kcat/KM = 2.9 x 10^4 in a column headed kcat/KM (M-1s-1).

row_label: Table 2, row N299A

table_label: Table 2: Steady-state kinetic parameters for ATAS mutants (Biochemistry 2016, 55(20):2864-2874). Printed column heads: Mutant; kcat (s-1); KM (uM); kcat/KM (M-1s-1).