column_label: PMID 8695641, article page 161, Figure 4 / Results section 3.3; isoform delta-C; metric calculated Km; value 0.13 mM.

normalized_value_unit_evidence: Km 0.13 mM; no unit conversion required; numerically matches current 0.12999999999999998 mM.

raw_value_unit_evidence: Results section 3.3 reports calculated Km for delta-C of 0.13 mM.

row_label: delta-C crystallin isoform

table_label: Figure 4 and Results section 3.3, article page 161


enzyme_display_name: argininosuccinate lyase

organism: Anas platyrhynchos

substrate_name: N(omega)-(L-Arginino)succinate

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

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

km_unit: mM

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

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

column_label: PMID 8695641, article page 161, Figure 4 / Results section 3.3; isoform delta-B; metric calculated Km; value 0.10 mM.

normalized_value_unit_evidence: Km 0.10 mM; no unit conversion required; numerically matches current 0.1 mM.

raw_value_unit_evidence: Results section 3.3 reports calculated Km for delta-B of 0.10 mM.

row_label: delta-B crystallin isoform

data_origin: experimental

enzyme: argininosuccinate lyase

substrate: N(omega)-(L-Arginino)succinate

status: verified


enzyme_display_name: adenylosuccinate lyase

organism: Bacillus subtilis

source_db: oed

verification_status: corrected

protein_accession_database: UniProt

source_license: CC BY 4.0

sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:P12047 and applied mutation signature I62E/D69E to reconstruct the assayed variant sequence.

column_label: Table I; row 5 I62E/D69E; kcat, Km, and kcat/Km columns; table header gives Km in uM and kcat/Km in M^-1 s^-1.

normalized_value_unit_evidence: normalized Table I values: kcat=0.08 s^-1; Km=0.0043 mM; kcat/Km=19 s^-1 mM^-1. Export has Km=0.004 mM and kcat/Km=20 s^-1 mM^-1.

table_label: Table I

enzyme: adenylosuccinate lyase

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24058 and applied mutation signature W9F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

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

mutation_type: substitution

assay_conditions_summary: pH 7.5; 298.15 K; buffer A (10 mM Tris-HCl

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, ddc2 Mutants block, mutant row W9F: Km (mM) = 0.111; kcat (s-1) = 0.909; kcat/Km (s-1 M-1) = 0.833 x 10^4; Vmax ((µmol/min)/mg) = 0.273; relative catalytic efficiency (%) = 11.3; Tm (°C) = 67.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.111 mM; the column is already in mM, so no unit conversion applies and the paper value is 0.111 mM. kcat: printed Table 1 kcat cell 0.909 s-1; the column is already per second, so no unit conversion applies and the paper value is 0.909 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.833 x 10^4 s-1 M-1, that is 8330.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8330.0 / 1000 = 8.33 s^(-1)*mM^(-1). Quotient disclosure for this line: 0.909 / 0.111 = 8.18918918918919 s^-1 mM^-1, against the printed catalytic-efficiency cell 8.33 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ddc2 Mutants block, mutant row W9F: Km = 0.111 mM; kcat = 0.909 s-1; printed kcat/Km = 0.833 x 10^4 s-1 M-1.

table_label: Table 1: Kinetic Parameters and Tm Values (Biochemistry 2005, 44, 9034-9044)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24058 and applied mutation signature W9M with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, ddc2 Mutants block, mutant row W9M: Km (mM) = 0.115; kcat (s-1) = 0.081; kcat/Km (s-1 M-1) = 0.076 x 10^4; Vmax ((µmol/min)/mg) = 0.024; relative catalytic efficiency (%) = 1.0; Tm (°C) = 67.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.115 mM; the column is already in mM, so no unit conversion applies and the paper value is 0.115 mM. kcat: printed Table 1 kcat cell 0.081 s-1; the column is already per second, so no unit conversion applies and the paper value is 0.081 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.076 x 10^4 s-1 M-1, that is 760.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 760.0 / 1000 = 0.76 s^(-1)*mM^(-1). Quotient disclosure for this line: 0.081 / 0.115 = 0.7043478260869566 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.76 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ddc2 Mutants block, mutant row W9M: Km = 0.115 mM; kcat = 0.081 s-1; printed kcat/Km = 0.076 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24058 and applied mutation signature W9R with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, ddc2 Mutants block, mutant row W9R: Km (mM) = 0.069; kcat (s-1) = 0.147; kcat/Km (s-1 M-1) = 0.220 x 10^4; Vmax ((µmol/min)/mg) = 0.044; relative catalytic efficiency (%) = 3.0; Tm (°C) = 67.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.069 mM; the column is already in mM, so no unit conversion applies and the paper value is 0.069 mM. kcat: printed Table 1 kcat cell 0.147 s-1; the column is already per second, so no unit conversion applies and the paper value is 0.147 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.220 x 10^4 s-1 M-1, that is 2200.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2200.0 / 1000 = 2.2 s^(-1)*mM^(-1). Quotient disclosure for this line: 0.147 / 0.069 = 2.1304347826086953 s^-1 mM^-1, against the printed catalytic-efficiency cell 2.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ddc2 Mutants block, mutant row W9R: Km = 0.069 mM; kcat = 0.147 s-1; printed kcat/Km = 0.220 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24058 and applied mutation signature W9Y with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, ddc2 Mutants block, mutant row W9Y: Km (mM) = 0.106; kcat (s-1) = 3.960; kcat/Km (s-1 M-1) = 3.640 x 10^4; Vmax ((µmol/min)/mg) = 1.188; relative catalytic efficiency (%) = 49.5; Tm (°C) = 67.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.106 mM; the column is already in mM, so no unit conversion applies and the paper value is 0.106 mM. kcat: printed Table 1 kcat cell 3.960 s-1; the column is already per second, so no unit conversion applies and the paper value is 3.96 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 3.640 x 10^4 s-1 M-1, that is 36400.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 36400.0 / 1000 = 36.4 s^(-1)*mM^(-1). Quotient disclosure for this line: 3.960 / 0.106 = 37.35849056603774 s^-1 mM^-1, against the printed catalytic-efficiency cell 36.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ddc2 Mutants block, mutant row W9Y: Km = 0.106 mM; kcat = 3.960 s-1; printed kcat/Km = 3.640 x 10^4 s-1 M-1.


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H141A/H68Q to reconstruct the assayed variant sequence.

proof_lines: Bacillus subtilis adenylosuccinate lyase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H141E/H68Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H141L/H68Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H141Q/H68A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H141Q/H68K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H141Q/H68Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H141Q/R67M/H68Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H141R/H68Q to reconstruct the assayed variant sequence.


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

sequence_source: multiple

assay_conditions_summary: pH 7

proof_lines: duck delta2-crystallin has maintained ASL activity

proof_lines: ASL activity is recovered in the DLM by changing Met-9 to Trp


proof_lines: duck delta1-crystallin is enzymatically inactive

proof_lines: the abstract distinguishes delta1 from delta2 crystallin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M9F/E115D to reconstruct the assayed variant sequence.

proof_lines: M9F is discussed only in the DLM-E115D background

proof_lines: the selected row is a plain d1 point-mutant context


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24057 and applied mutation signature M9W to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, DLM Mutants block, mutant row M9W: Km (mM) = 2.724; kcat (s-1) = 3.874; kcat/Km (s-1 M-1) = 0.144 x 10^4; Vmax ((µmol/min)/mg) = 1.162; relative catalytic efficiency (%) = 2.0; Tm (°C) = 71.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 2.724 mM; the column is already in mM, so no unit conversion applies and the paper value is 2.724 mM. kcat: printed Table 1 kcat cell 3.874 s-1; the column is already per second, so no unit conversion applies and the paper value is 3.874 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.144 x 10^4 s-1 M-1, that is 1440.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1440.0 / 1000 = 1.44 s^(-1)*mM^(-1). Quotient disclosure for this line: 3.874 / 2.724 = 1.422173274596182 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.44 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, DLM Mutants block, mutant row M9W: Km = 2.724 mM; kcat = 3.874 s-1; printed kcat/Km = 0.144 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24057 and applied mutation signature M9W/E115D to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, DLM Mutants block, mutant row M9W/E115D: Km (mM) = 0.294; kcat (s-1) = 3.585; kcat/Km (s-1 M-1) = 1.252 x 10^4; Vmax ((µmol/min)/mg) = 1.075; relative catalytic efficiency (%) = 17.0; Tm (°C) = 71.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.294 mM; the column is already in mM, so no unit conversion applies and the paper value is 0.294 mM. kcat: printed Table 1 kcat cell 3.585 s-1; the column is already per second, so no unit conversion applies and the paper value is 3.585 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 1.252 x 10^4 s-1 M-1, that is 12520.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12520.0 / 1000 = 12.52 s^(-1)*mM^(-1). Quotient disclosure for this line: 3.585 / 0.294 = 12.193877551020408 s^-1 mM^-1, against the printed catalytic-efficiency cell 12.52 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, DLM Mutants block, mutant row M9W/E115D: Km = 0.294 mM; kcat = 3.585 s-1; printed kcat/Km = 1.252 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24057 and applied mutation signature M9W/V14S to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, DLM Mutants block, mutant row M9W/V14S: Km (mM) = 3.159; kcat (s-1) = 4.459; kcat/Km (s-1 M-1) = 0.142 x 10^4; Vmax ((µmol/min)/mg) = 1.338; relative catalytic efficiency (%) = 1.9; Tm (°C) = 63.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 3.159 mM; the column is already in mM, so no unit conversion applies and the paper value is 3.159 mM. kcat: printed Table 1 kcat cell 4.459 s-1; the column is already per second, so no unit conversion applies and the paper value is 4.459 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.142 x 10^4 s-1 M-1, that is 1420.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1420.0 / 1000 = 1.42 s^(-1)*mM^(-1). Quotient disclosure for this line: 4.459 / 3.159 = 1.4115226337448559 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.42 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, DLM Mutants block, mutant row M9W/V14S: Km = 3.159 mM; kcat = 4.459 s-1; printed kcat/Km = 0.142 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24057 and applied mutation signature M9Y/E115D to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, DLM Mutants block, mutant row M9Y/E115D: Km (mM) = 0.610; kcat (s-1) = 2.460; kcat/Km (s-1 M-1) = 0.404 x 10^4; Vmax ((µmol/min)/mg) = 0.738; relative catalytic efficiency (%) = 5.5; Tm (°C) = 65.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.610 mM; the column is already in mM, so no unit conversion applies and the paper value is 0.61 mM. kcat: printed Table 1 kcat cell 2.460 s-1; the column is already per second, so no unit conversion applies and the paper value is 2.46 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.404 x 10^4 s-1 M-1, that is 4040.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4040.0 / 1000 = 4.04 s^(-1)*mM^(-1). Quotient disclosure for this line: 2.460 / 0.610 = 4.032786885245901 s^-1 mM^-1, against the printed catalytic-efficiency cell 4.04 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, DLM Mutants block, mutant row M9Y/E115D: Km = 0.610 mM; kcat = 2.460 s-1; printed kcat/Km = 0.404 x 10^4 s-1 M-1.


verification_status: unverified

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -9, so it is treated as a source-provided variant sequence.

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24058 and applied mutation signature D115E with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, ddc2 Mutants block, mutant row D115E: Km (mM) = 0.273; kcat (s-1) = 8.532; kcat/Km (s-1 M-1) = 3.134 x 10^4; Vmax ((µmol/min)/mg) = 2.559; relative catalytic efficiency (%) = 42.6; Tm (°C) = 71.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.273 mM; the column is already in mM, so no unit conversion applies and the paper value is 0.273 mM. kcat: printed Table 1 kcat cell 8.532 s-1; the column is already per second, so no unit conversion applies and the paper value is 8.532 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 3.134 x 10^4 s-1 M-1, that is 31340.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 31340.0 / 1000 = 31.34 s^(-1)*mM^(-1). Quotient disclosure for this line: 8.532 / 0.273 = 31.252747252747252 s^-1 mM^-1, against the printed catalytic-efficiency cell 31.34 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ddc2 Mutants block, mutant row D115E: Km = 0.273 mM; kcat = 8.532 s-1; printed kcat/Km = 3.134 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24058 and applied mutation signature W9A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters and Tm Values) prints one mutant-label column followed by the column heads Vmax ((µmol/min)/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1 M-1) | relative catalytic efficiency (%) | Tm (°C), and its mutant lines are grouped under the block headings DLM Mutants and dδc2 Mutants. The cited cell set is Table 1, ddc2 Mutants block, mutant row W9A: Km (mM) = 0.112; kcat (s-1) = 0.155; kcat/Km (s-1 M-1) = 0.136 x 10^4; Vmax ((µmol/min)/mg) = 0.040; relative catalytic efficiency (%) = 1.9; Tm (°C) = 67.

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.112 mM; the column is already in mM, so no unit conversion applies and the paper value is 0.112 mM. kcat: printed Table 1 kcat cell 0.155 s-1; the column is already per second, so no unit conversion applies and the paper value is 0.155 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.136 x 10^4 s-1 M-1, that is 1360.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1360.0 / 1000 = 1.36 s^(-1)*mM^(-1). Quotient disclosure for this line: 0.155 / 0.112 = 1.3839285714285714 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.36 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ddc2 Mutants block, mutant row W9A: Km = 0.112 mM; kcat = 0.155 s-1; printed kcat/Km = 0.136 x 10^4 s-1 M-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D293N to reconstruct the assayed variant sequence.

proof_lines:
duck delta2 crystallin
argininosuccinate lyase
site-directed mutagenesis


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D33N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K325N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N116D with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S29A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T161S to reconstruct the assayed variant sequence.

proof_lines:
Thr-161
site-directed mutagenesis
duck delta2 crystallin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T281V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I123R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I123W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M10L 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 T367R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T367S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:P12047 and applied mutation signature D65R to reconstruct the assayed variant sequence.

column_label: Table I; row 7 D65R; kcat, Km, and kcat/Km columns; table header gives Km in uM and kcat/Km in M^-1 s^-1.

normalized_value_unit_evidence: normalized Table I values: kcat=1.07 s^-1; Km=0.0046 mM; kcat/Km=231 s^-1 mM^-1. Export has Km=0.005 mM and kcat/Km=214 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12047 and applied mutation signature D65R/D69E to reconstruct the assayed variant sequence.

column_label: Table I (Kinetics of wild type and mutant B. subtilis adenylosuccinate lyases), numbered enzyme line '8. D65R/D69E'; column 'kcat (s^-1)' = 0.20; column 'Km (uM)' = 2.0; column 'kcat/Km (M^-1 s^-1)' = 1.00 x 10^5. The same line also carries a 'Vmax (umol min^-1 mg^-1)' cell, which is specific activity and is outside the exported metric set for this catalog row.

normalized_value_unit_evidence: kcat: printed Table I cell 0.20 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the normalized value is 0.2 s^(-1). Km: printed Table I cell 2.0 uM; 1 uM is 0.001 mM, so 2.0 / 1000 = 0.002 mM. kcat/Km: printed Table I cell 1.00 x 10^5 M^-1 s^-1, that is 100000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 100000 / 1000 = 100.0 s^-1 mM^-1.

raw_value_unit_evidence: Table I, numbered enzyme line '8. D65R/D69E': kcat = 0.20 s^-1; Km = 2.0 uM; printed kcat/Km = 1.00 x 10^5 M^-1 s^-1.

table_label: Table I: Kinetics of wild type and mutant B. subtilis adenylosuccinate lyases (J. Biol. Chem. 2004, 279(51):53789-53797)


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:P12047 and applied mutation signature D69E to reconstruct the assayed variant sequence.

column_label: Table I; row 4 D69E; kcat, Km, and kcat/Km columns; table header gives Km in uM and kcat/Km in M^-1 s^-1.

normalized_value_unit_evidence: normalized Table I values: kcat=0.34 s^-1; Km=0.0013 mM; kcat/Km=264 s^-1 mM^-1. Export has Km=0.001 mM and kcat/Km=340 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12047 and applied mutation signature I62D to reconstruct the assayed variant sequence.

column_label: Table I (Kinetics of wild type and mutant B. subtilis adenylosuccinate lyases), numbered enzyme line '3. I62D'; column 'kcat (s^-1)' = 0.03; column 'Km (uM)' = 55.1; column 'kcat/Km (M^-1 s^-1)' = 0.005 x 10^5. The same line also carries a 'Vmax (umol min^-1 mg^-1)' cell, which is specific activity and is outside the exported metric set for this catalog row.

normalized_value_unit_evidence: kcat: printed Table I cell 0.03 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the normalized value is 0.03 s^(-1). Km: printed Table I cell 55.1 uM; 1 uM is 0.001 mM, so 55.1 / 1000 = 0.0551 mM. kcat/Km: printed Table I cell 0.005 x 10^5 M^-1 s^-1, that is 500 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 500 / 1000 = 0.5 s^-1 mM^-1.

raw_value_unit_evidence: Table I, numbered enzyme line '3. I62D': kcat = 0.03 s^-1; Km = 55.1 uM; printed kcat/Km = 0.005 x 10^5 M^-1 s^-1.

row_label: Table I, numbered enzyme line '3. I62D'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12047 and applied mutation signature I62D/D65R to reconstruct the assayed variant sequence.

column_label: Table I (Kinetics of wild type and mutant B. subtilis adenylosuccinate lyases), numbered enzyme line '11. I62D/D65R'; column 'kcat (s^-1)' = 0.05; column 'Km (uM)' = 48.8; column 'kcat/Km (M^-1 s^-1)' = 0.01 x 10^5. The same line also carries a 'Vmax (umol min^-1 mg^-1)' cell, which is specific activity and is outside the exported metric set for this catalog row.

normalized_value_unit_evidence: kcat: printed Table I cell 0.05 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the normalized value is 0.05 s^(-1). Km: printed Table I cell 48.8 uM; 1 uM is 0.001 mM, so 48.8 / 1000 = 0.0488 mM. kcat/Km: printed Table I cell 0.01 x 10^5 M^-1 s^-1, that is 1000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1000 / 1000 = 1.0 s^-1 mM^-1.

raw_value_unit_evidence: Table I, numbered enzyme line '11. I62D/D65R': kcat = 0.05 s^-1; Km = 48.8 uM; printed kcat/Km = 0.01 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12047 and applied mutation signature I62D/D65R/D69E to reconstruct the assayed variant sequence.

column_label: Table I (Kinetics of wild type and mutant B. subtilis adenylosuccinate lyases), numbered enzyme line '12. I62D/D65R/D69E'; column 'kcat (s^-1)' = 0.06; column 'Km (uM)' = 10.7; column 'kcat/Km (M^-1 s^-1)' = 0.05 x 10^5. The same line also carries a 'Vmax (umol min^-1 mg^-1)' cell, which is specific activity and is outside the exported metric set for this catalog row.

normalized_value_unit_evidence: kcat: printed Table I cell 0.06 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the normalized value is 0.06 s^(-1). Km: printed Table I cell 10.7 uM; 1 uM is 0.001 mM, so 10.7 / 1000 = 0.0107 mM. kcat/Km: printed Table I cell 0.05 x 10^5 M^-1 s^-1, that is 5000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5000 / 1000 = 5.0 s^-1 mM^-1.

raw_value_unit_evidence: Table I, numbered enzyme line '12. I62D/D65R/D69E': kcat = 0.06 s^-1; Km = 10.7 uM; printed kcat/Km = 0.05 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I62D/D69E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12047 and applied mutation signature I62E to reconstruct the assayed variant sequence.

column_label: Table I (Kinetics of wild type and mutant B. subtilis adenylosuccinate lyases), numbered enzyme line '2. I62E'; column 'kcat (s^-1)' = 0.07; column 'Km (uM)' = 17.5; column 'kcat/Km (M^-1 s^-1)' = 0.03 x 10^5. The same line also carries a 'Vmax (umol min^-1 mg^-1)' cell, which is specific activity and is outside the exported metric set for this catalog row.

normalized_value_unit_evidence: kcat: printed Table I cell 0.07 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the normalized value is 0.07 s^(-1). Km: printed Table I cell 17.5 uM; 1 uM is 0.001 mM, so 17.5 / 1000 = 0.0175 mM. kcat/Km: printed Table I cell 0.03 x 10^5 M^-1 s^-1, that is 3000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3000 / 1000 = 3.0 s^-1 mM^-1.

raw_value_unit_evidence: Table I, numbered enzyme line '2. I62E': kcat = 0.07 s^-1; Km = 17.5 uM; printed kcat/Km = 0.03 x 10^5 M^-1 s^-1.

row_label: Table I, numbered enzyme line '2. I62E'


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:P12047 and applied mutation signature I62E/D65R to reconstruct the assayed variant sequence.

column_label: Table I; row 9 I62E/D65R; kcat, Km, and kcat/Km columns; table footnote a says this is the humanized normal B. subtilis enzyme.

normalized_value_unit_evidence: normalized Table I values: kcat=0.48 s^-1; Km=0.0181 mM; kcat/Km=26 s^-1 mM^-1. Export has Km=0.018 mM and kcat/Km=26.666666666666668 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:P12047 and applied mutation signature I62E/D65R/D69E to reconstruct the assayed variant sequence.

column_label: Table I; row 10 I62E/D65R/D69E; kcat, Km, and kcat/Km columns; table footnote b says this 69 mutant mimics the human defect at 87.

normalized_value_unit_evidence: normalized Table I values: kcat=0.23 s^-1; Km=0.0061 mM; kcat/Km=37 s^-1 mM^-1. Export has Km=0.006 mM and kcat/Km=38.333333333333336 s^-1 mM^-1.


organism: Homo sapiens

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


organism: Nostoc sp. PCC 7120 = FACHB-418

source_db: brenda

proof_lines: kcat is 8.71 sec(-1) with argininosuccinate as substrate.

source_databases_merged: brenda uniprot

source: brenda


organism: Delftia sp.

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:
Table II
D-threo-3-hydroxyaspartate
pH 8.5

source_databases_merged: sabio_rk brenda skid


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: 2-amino-2-deoxy-D-gluconate 6-phosphate

proof_lines:
weak competitive inhibitors
Ki values near 30 mM
alpha-glycerophosphate

substrate: 2-amino-2-deoxy-D-gluconate 6-phosphate


organism: Streptomyces venezuelae

proof_lines:
Streptomyces venezuelae
DesII
TDP-4-amino-4,6-dideoxy-D-glucose


organism: Synechocystis sp. PCC 6803

proof_lines: kcat is 6.78 sec(-1) with argininosuccinate as substrate.


organism: Schistosoma mansoni

substrate_name: adenylosuccinate (ADS) (at 25 degrees Celsius)

source_db: uniprot

assay_conditions_summary: buffer the same NaH2PO4/NaCl/MgCl2

column_label: Table 2 lists ADS Km 17.2 +/- 2.3 uM for SmADSL; Figure 1 caption repeats ADS consumption Km 17.2 +/- 2.3 uM.

raw_value_unit_evidence: Km raw_value=17.2 +/- 2.3 raw_unit=uM

row_label: ADS -> AMP + fumarate / SmADSL

table_label: Table 2, kinetic parameters for adenylosuccinate (ADS) and SAICAR

source: uniprot


organism: Rattus norvegicus

column_label: Abstract reports in rat liver the apparent Km values for ASase and arginase were respectively 1.25 and 13.5 mM.

raw_value_unit_evidence: Km raw_value=1.25 mM raw_unit=mM

row_label: rat liver argininosuccinate lyase / argininosuccinate

table_label: PubMed XML abstract PMID 2085183


organism: Chlamydomonas reinhardtii

column_label: Abstract states: The Km for argininosuccinate at 37 degrees C and pH 7.5 is 0.26 mM.

raw_value_unit_evidence: Km raw_value=0.26 raw_unit=mM

row_label: Chlamydomonas reinhardtii argininosuccinate lyase with argininosuccinate substrate

table_label: PubMed/PMC abstract PMID 3593239


enzyme_display_name: ureidoglycolate lyase

organism: Burkholderia cepacia

substrate_name: (-)-Ureidoglycolate

enzyme: ureidoglycolate lyase

substrate: (-)-Ureidoglycolate


organism: Mycolicibacterium smegmatis

substrate_name: succinyladenosine monophosphate

substrate: succinyladenosine monophosphate


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


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C441S to reconstruct the assayed variant sequence.


substrate_name: adenylsuccinate

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

substrate: adenylsuccinate


proof_lines: mutant D65R/D69E, 50 mM HEPES, pH 7.0, 25°C


proof_lines: mutant I62E/D69E, 50 mM HEPES, pH 7.0, 25°C


proof_lines: mutant I62E/D65R/D69E, 50 mM HEPES, pH 7.0, 25°C


proof_lines: mutant I62D/D65R/D69E, 50 mM HEPES, pH 7.0, 25°C


proof_lines: mutant I62D/D69E, 50 mM HEPES, pH 7.0, 25°C


proof_lines: mutant I62E/D65R, 50 mM HEPES, pH 7.0, 25°C


proof_lines: mutant I62D/D65R, 50 mM HEPES, pH 7.0, 25°C


enzyme_display_name: phenylalanine ammonia-lyase

organism: Petroselinum crispum

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

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

enzyme: phenylalanine ammonia-lyase


substrate_name: L-styrylalanine

substrate: L-styrylalanine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


proof_lines:
pH 8.8, 30°C, mutant enzyme F137V
mutant F137V, pH 10, 30°C


substrate_name: argininosuccinate

substrate: argininosuccinate


substrate_name: adenylosuccinate

substrate: adenylosuccinate


proof_lines:
wild-type enzyme
wild type, 50 mM HEPES, pH 7.0, 25°C


enzyme_display_name: peptidylamidoglycolate lyase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E707Q to reconstruct the assayed variant sequence.

column_label: Table 2; row E707Q; Km (uM) column.

normalized_value_unit_evidence: normalized Km=0.0102 mM from 10.2 uM.

table_label: Table 2

enzyme: peptidylamidoglycolate lyase


column_label: Table 2; row PALcc; Km (uM) column.

normalized_value_unit_evidence: normalized Km=0.0139 mM from 13.9 uM.

row_label: PALcc


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H690A to reconstruct the assayed variant sequence.

column_label: Table 2; row H690A; Km (uM) column.

normalized_value_unit_evidence: normalized Km=0.0156 mM from 15.6 uM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D705N to reconstruct the assayed variant sequence.

column_label: Table 2; row D705N; Km (uM) column.

normalized_value_unit_evidence: normalized Km=0.0214 mM from 21.4 uM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H585A to reconstruct the assayed variant sequence.

column_label: Table 2; row H585A; Km (uM) column.

normalized_value_unit_evidence: normalized Km=0.0231 mM from 23.1 uM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H786A to reconstruct the assayed variant sequence.

column_label: Table 2; row H786A; Km (uM) column.

normalized_value_unit_evidence: normalized Km=0.0985 mM from 98.5 uM.


proof_lines: pH and temperature not specified in the publication, mutant enzyme I460T


proof_lines: pH and temperature not specified in the publication, mutant enzyme I460V


organism: Bambusa oldhamii

substrate_name: L-Tyr

substrate: L-Tyr


substrate_name: L-Phe

substrate: L-Phe


substrate_name: 2-amino-3-(3-thienyl)propanoic acid

substrate: 2-amino-3-(3-thienyl)propanoic acid


substrate_name: 2-amino-3-(2-furyl)propanoic acid

substrate: 2-amino-3-(2-furyl)propanoic acid


substrate_name: 2-amino-3-(2-thienyl)propanoic acid

substrate: 2-amino-3-(2-thienyl)propanoic acid


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

enzyme: 6-pyruvoyltetrahydropterin synthase


enzyme_display_name: aspartate ammonia-lyase

organism: Lacticaseibacillus paracasei

substrate_name: L-tyrosine

enzyme: aspartate ammonia-lyase

substrate: L-tyrosine


substrate_name: fumarate

substrate: fumarate


substrate_name: L-aspartate

substrate: L-aspartate


organism: Arabidopsis thaliana

assay_conditions_summary: pH 9

column_label: Table 1. Steady-State Kinetic Parameters of TALs and PALs Investigated in This Study (Underlined) with Tyrosine and Phenylalanine as Substrates.; row A. thaliana PAL1 / Tyrosine; Km column Km [uM] raw 1049 +/- 67.2; kcat column kcat [s^-1] raw 0.084 +/- 0.0038; kcat/Km column kcat/Km [M^-1 s^-1] raw 80

normalized_value_unit_evidence: Km normalized_value=1.049 normalized_unit=mM; kcat normalized_value=0.084 normalized_unit=s^-1; kcat/Km normalized_value=0.08007626310772165 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1049 +/- 67.2 raw_unit=uM; kcat raw_value=0.084 +/- 0.0038 raw_unit=s^-1; kcat/Km raw_value=80 raw_unit=M^-1 s^-1

row_label: A. thaliana PAL1 / Tyrosine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35510 and applied mutation signature F144H with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

column_label: Table 1. Steady-State Kinetic Parameters of TALs and PALs Investigated in This Study (Underlined) with Tyrosine and Phenylalanine as Substrates.; row A. thaliana PAL1 F144H / Tyrosine; Km column Km [uM] raw 532.6 +/- 27.7; kcat column kcat [s^-1] raw 0.75 +/- 0.15; kcat/Km column kcat/Km [M^-1 s^-1] raw 1410

normalized_value_unit_evidence: Km normalized_value=0.532 normalized_unit=mM; kcat normalized_value=0.75 normalized_unit=s^-1; kcat/Km normalized_value=1.4097744360902256 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=532.6 +/- 27.7 raw_unit=uM; kcat raw_value=0.75 +/- 0.15 raw_unit=s^-1; kcat/Km raw_value=1410 raw_unit=M^-1 s^-1

row_label: A. thaliana PAL1 F144H / Tyrosine


column_label: Table 1. Steady-State Kinetic Parameters of TALs and PALs Investigated in This Study (Underlined) with Tyrosine and Phenylalanine as Substrates.; row A. thaliana PAL1 F144H / Phenylalanine; Km column Km [uM] raw 1386 +/- 162.9; kcat column kcat [s^-1] raw 47.3 +/- 2.4; kcat/Km column kcat/Km [M^-1 s^-1] raw 3.4 x 10^4

normalized_value_unit_evidence: Km normalized_value=1.386 normalized_unit=mM; kcat normalized_value=47.3 normalized_unit=s^-1; kcat/Km normalized_value=34.12698412698413 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1386 +/- 162.9 raw_unit=uM; kcat raw_value=47.3 +/- 2.4 raw_unit=s^-1; kcat/Km raw_value=3.4 x 10^4 raw_unit=M^-1 s^-1

row_label: A. thaliana PAL1 F144H / Phenylalanine


column_label: Table 1. Steady-State Kinetic Parameters of TALs and PALs Investigated in This Study (Underlined) with Tyrosine and Phenylalanine as Substrates.; row A. thaliana PAL1 / Phenylalanine; Km column Km [uM] raw 42.8 +/- 1.3; kcat column kcat [s^-1] raw 115.8 +/- 2.1; kcat/Km column kcat/Km [M^-1 s^-1] raw 2.7 x 10^6

normalized_value_unit_evidence: Km normalized_value=0.0428 normalized_unit=mM; kcat normalized_value=115.8 normalized_unit=s^-1; kcat/Km normalized_value=2705.607476635514 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=42.8 +/- 1.3 raw_unit=uM; kcat raw_value=115.8 +/- 2.1 raw_unit=s^-1; kcat/Km raw_value=2.7 x 10^6 raw_unit=M^-1 s^-1

row_label: A. thaliana PAL1 / Phenylalanine


enzyme_display_name: methanogen homoaconitase

organism: Methanocaldococcus jannaschii

substrate_name: (R)-homocitrate

proof_lines: pH 8.5, 60°C, recombinant enzyme, dehydratase reaction

enzyme: methanogen homoaconitase

substrate: (R)-homocitrate


proof_lines: pH 9.0, 60°C, recombinant enzyme, hydrolase reaction


substrate_name: cis-homoaconitate

substrate: cis-homoaconitate


substrate_name: Maleate

substrate: Maleate


enzyme_display_name: xanthan lyase

organism: Microbacterium sp. XT11

substrate_name: Xanthan

enzyme: xanthan lyase

substrate: Xanthan


proof_lines:
native enzyme, at pH 6.0 and 30°C
recombinant enzyme, at pH 6.0 and 30°C


enzyme_display_name: heparin lyase

organism: Pedobacter heparinus

substrate_name: heparin

proof_lines: wild type recombinant enzyme, pH 7.0 30°C

enzyme: heparin lyase

substrate: heparin


enzyme_display_name: histidine ammonia-lyase

organism: Pseudomonas sp.

proof_lines:
in the presence of 0.1 mM CdCl2
in the presence of 1 mM EDTA

enzyme: histidine ammonia-lyase


substrate_name: DL-histidine

proof_lines: oxidized enzyme, in the absence of added metal

substrate: DL-histidine


substrate_name: Urocanate

substrate: Urocanate


enzyme_display_name: D-serine ammonia-lyase

organism: Saccharomyces cerevisiae

substrate_name: beta-Chloro-D-alanine

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

proof_lines:
untreated
EDTA-treated + 2.5 microM ZnCl2
EDTA-treated

enzyme: D-serine ammonia-lyase

substrate: beta-Chloro-D-alanine


substrate_name: D-threonine

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

proof_lines:
EDTA-treated + 2.5 microM ZnCl2
untreated

substrate: D-threonine


substrate_name: D-serine

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

proof_lines:
EDTA-treated
EDTA-treated + 2.5 microM ZnCl2
untreated

substrate: D-serine


substrate_name: beta-Cl-D-alanine

substrate: beta-Cl-D-alanine


enzyme_display_name: delta-guaiene synthase

organism: Aquilaria crassna

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

proof_lines: mutant enzyme Y110S/W144R/V241E/P296S/H337Y, in Tris-HCl (25 mM, pH 7.0), at 30°C

enzyme: delta-guaiene synthase

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


proof_lines: mutant enzyme Y110S/V241E/P296S/H337Y, in Tris-HCl (25 mM, pH 7.0), at 30°C


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


enzyme_display_name: L-serine ammonia-lyase

organism: Mus musculus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: wild-type, alpha,beta-elimination, pH 7.4, 37°C

proof_lines: wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C

enzyme: L-serine ammonia-lyase


proof_lines: mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C

proof_lines: mutant Q155D, presence of ATP, pH 7.4, 37°C


enzyme_display_name: threonine ammonia-lyase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: L-Thr

enzyme: threonine ammonia-lyase

substrate: L-Thr


substrate_name: L-Ser

substrate: L-Ser


enzyme_display_name: hyaluronate lyase

organism: Streptococcus pneumoniae

substrate_name: hyaluronan

enzyme: hyaluronate lyase

substrate: hyaluronan


substrate_name: hyaluronan hexasaccharide

proof_lines: recombinant wild-type enzyme, pH 6.0, 22°C

proof_lines: recombinant wild-type enzyme and mutant Y408F, pH 6.0, 22°C

substrate: hyaluronan hexasaccharide


proof_lines: recombinant mutants H399A and N580A, pH 6.0, 22°C


enzyme_display_name: pectate lyase

organism: Bacillus subtilis

substrate_name: Polygalacturonate

km_display: Not reported

enzyme: pectate lyase

substrate: Polygalacturonate


substrate_name: L-histidine

substrate: L-histidine


enzyme_display_name: argininosuccinate lyase

organism: Bos taurus

substrate_name: difluorofumarate

enzyme: argininosuccinate lyase

substrate: difluorofumarate


substrate_name: fumarate

substrate: fumarate


substrate_name: monofluorofumarate

substrate: monofluorofumarate


enzyme_display_name: alpha-farnesene synthase

proof_lines: accession Wassilewskija, 30°C, pH not specified in the publication

proof_lines: accession Columbia, 30°C, pH not specified in the publication

enzyme: alpha-farnesene synthase


enzyme_display_name: (E)-beta-ocimene synthase

enzyme: (E)-beta-ocimene synthase


substrate_name: geranyl diphosphate

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

substrate: geranyl diphosphate


organism: Caldicellulosiruptor bescii

substrate_name: Pectin

mutation_signature: CbCBM66-truncated mutant of CbPL9

mutation_type: truncation

proof_lines: pH 9.0, 85°C, CbCBM66-truncated mutant of CbPL9

substrate: Pectin


proof_lines:
pH 9.0, 85°C, wild-type enzyme CbPL9
pH 9.0, 85°C, wild-type enzyme CbPL3


mutation_signature: CbCBM66-truncated mutant of CbPL3

proof_lines: pH 9.0, 85°C, CbCBM66-truncated mutant of CbPL3


enzyme_display_name: 3-aminobutyryl-CoA ammonia-lyase

organism: Clostridium sp.

assay_conditions_summary: cofactor CoA

enzyme: 3-aminobutyryl-CoA ammonia-lyase


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


smiles: N


enzyme_display_name: tyrosine ammonia-lyase

organism: Cereibacter sphaeroides

substrate_name: L-tyrosinol

enzyme: tyrosine ammonia-lyase

substrate: L-tyrosinol


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


enzyme_display_name: methylaspartate ammonia-lyase

organism: Citrobacter amalonaticus

substrate_name: L-aspartate

enzyme: methylaspartate ammonia-lyase

substrate: L-aspartate


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


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: UniProt P18417

organism: Catharanthus roseus

substrate_name: tryptamine

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P18417

substrate: tryptamine

source: skid


enzyme_display_name: UniProt P68175

organism: Rauvolfia serpentina

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=35°C, pH=7

enzyme: UniProt P68175


substrate_name: serotonin

substrate: serotonin


substrate_name: secologanin

substrate: secologanin


enzyme_display_name: aspartate ammonia-lyase

organism: Escherichia coli

enzyme: aspartate ammonia-lyase


proof_lines:
wild-type, pH 7.0
wild type
pH 8.5, 30°C, wild-type enzyme


proof_lines:
native enzyme
30°C
N-ethylmaleimide-modified enzyme


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


organism: Cytophaga sp.


enzyme_display_name: (R)-2-hydroxyglutaryl-CoA dehydratase

organism: [Clostridium] symbiosum

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

proof_lines: strictly anaerobic conditions, 25°C, Tris-HCl buffer, pH 8.0, (R)-2-hydroxyglutaryl-CoA dehydratase activator protein from Acidaminococcus fermentans

enzyme: (R)-2-hydroxyglutaryl-CoA dehydratase


substrate_name: (E)-glutaconyl-CoA

substrate: (E)-glutaconyl-CoA


enzyme_display_name: trichodiene synthase

organism: Fusarium sporotrichioides

substrate_name: (Z,E)-farnesyl diphosphate

enzyme: trichodiene synthase

substrate: (Z,E)-farnesyl diphosphate


substrate_name: (3R)-nerolidyl diphosphate

substrate: (3R)-nerolidyl diphosphate


substrate_name: (7S)-6,7-dihydrofarnesyl diphosphate

proof_lines: apparent inhibition constant of PPi in the prensence of BTAC

proof_lines: induced inhibition constant for BTAC in the presence of PPi

substrate: (7S)-6,7-dihydrofarnesyl diphosphate


organism: Hafnia alvei

substrate_name: fumarate

proof_lines:
25°C, pH 7.0, in presence of Mg2+
25°C, pH 7.0, in absence of Mg2+

substrate: fumarate


substrate_name: aspartate

proof_lines:
25°C, pH 7.0, in presence of Mg2+
25°C, pH 7.0, in absence of Mg2+
40°C, pH 7.85, acetylated enzyme

substrate: aspartate


proof_lines:
25°C, pH 7.0, in absence of Mg2+
25°C, pH 7.0, in presence of Mg2+


enzyme_display_name: gamma-glutamylamine cyclotransferase

organism: Glycine max

substrate_name: gamma-glutamyldansylcadaverine

proof_lines: pH 8.6, pH not specified in the publication, temperature not specified in the publication

enzyme: gamma-glutamylamine cyclotransferase

substrate: gamma-glutamyldansylcadaverine


organism: Oryctolagus cuniculus

substrate_name: L-gamma-glutamylcyclopentylamine

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

substrate: L-gamma-glutamylcyclopentylamine


substrate_name: L-gamma-glutamyl-beta-alanine

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

substrate: L-gamma-glutamyl-beta-alanine


substrate_name: L-gamma-glutamylneohexylamine

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

substrate: L-gamma-glutamylneohexylamine


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


substrate_name: Nepsilon-(L-gamma-glutamyl)-L-lysine

substrate: Nepsilon-(L-gamma-glutamyl)-L-lysine


substrate_name: S-(n-butylcarbamyl)-L-cysteine

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

substrate: S-(n-butylcarbamyl)-L-cysteine


substrate_name: L-gamma-glutamylbenzylamine

substrate: L-gamma-glutamylbenzylamine


enzyme_display_name: gamma-glutamylcyclotransferase

organism: Ralstonia solanacearum

substrate_name: glutathione

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

enzyme: gamma-glutamylcyclotransferase

substrate: glutathione


enzyme_display_name: Transferred entry: 3.5.99.13

enzyme: Transferred entry: 3.5.99.13


substrate_name: tryptamine

substrate: tryptamine


organism: Rattus norvegicus

proof_lines: isoenzyme with pI 5.1, in extract, Km increases 4-10fold during purification


substrate_name: epsilon-(gamma-L-glutamyl)-L-lysine

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

substrate: epsilon-(gamma-L-glutamyl)-L-lysine


enzyme_display_name: 3-ketovalidoxylamine C-N-lyase

organism: Stenotrophomonas maltophilia

enzyme: 3-ketovalidoxylamine C-N-lyase


organism: Flavobacterium saccharophilum

proof_lines: pH 9.5, 30°C, 10% glycerol, second order kinetics


enzyme_display_name: imidazole glycerol-phosphate synthase

organism: Thermotoga maritima

proof_lines: pH 8.5, 25°C, ammonia-dependent reaction of isolated HisF subunit, wild-type

enzyme: imidazole glycerol-phosphate synthase


substrate_name: L-glutamine

substrate: L-glutamine


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


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: palmitoyl-CoA

proof_lines: kcat is 0.037 sec(-1) with palmitoyl-CoA as substrate. kcat is 0.019 sec(-1) with stearoyl-CoA as substrate. kcat is 0.015 sec(-1) with lauroyl-CoA as substrate. kcat is 0.012 sec(-1) with hexanoyl-CoA as substrate.

substrate: palmitoyl-CoA


substrate_name: stearoyl-CoA

column_label: Table 1: Kinetic Parameters of Mtb FcoT with a Series of Different Fatty Acyl-CoAs as Substrates; row Stearoyl-CoA (C18:0); Km column; Stearoyl-CoA (C18:0): kcat = 1.90E-02 s^-1; Km = 10.28 uM; kcat/Km = 1.85 uM^-1 s^-1.

row_label: Stearoyl-CoA (C18:0); Km column

substrate: stearoyl-CoA


substrate_name: lauroyl-CoA

substrate: lauroyl-CoA


substrate_name: hexanoyl-CoA

column_label: Table 1: Kinetic Parameters of Mtb FcoT with a Series of Different Fatty Acyl-CoAs as Substrates; row Hexanoyl-CoA (C6:0); Km column; Hexanoyl-CoA (C6:0): kcat = 1.20E-02 s^-1; Km = 63.18 uM; kcat/Km = 0.19 uM^-1 s^-1.

row_label: Hexanoyl-CoA (C6:0); Km column

substrate: hexanoyl-CoA


organism: Homo sapiens


organism: Escherichia coli (strain K12)


substrate_name: gamma-glutamyl-L-alanine

substrate: gamma-glutamyl-L-alanine


organism: Mus musculus

substrate_name: Unknown

substrate: Unknown


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Ovis aries

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


organism: Arabidopsis thaliana


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K258A to reconstruct the assayed variant sequence.

proof_lines: Substrate-Induced Changes in the Ammonia Channel for Imidazole Glycerol Phosphate Synthase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K258R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K360A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K360R with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R239A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R239H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R239K to reconstruct the assayed variant sequence.


substrate_name: Reduced glutathione

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

substrate: Reduced glutathione


organism: Anas sp.

substrate_name: argininosuccinate

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

proof_lines: wild type, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA

substrate: argininosuccinate


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

proof_lines: mutant W9R, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant TRUN1-8, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA

proof_lines: mutant TRUN1-9, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant W9Y, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant W9F, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant W9A, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant W9M, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: 211-chimera, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant M9F/E115D, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant D115A, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant D115E, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant M9W/E115D, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant M9Y/E115D, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


proof_lines: mutant M9W/V14S, 25°C, 10 mM Tris-HCl, pH 7.5, 1 mM EDTA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D98A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V12A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V48A to reconstruct the assayed variant sequence.


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: PRFAR

substrate: PRFAR


substrate_name: glutamine

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

substrate: glutamine


organism: Escherichia coli

proof_lines: pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF


proof_lines: pH 8.0, 30°C, IGP synthase enzyme with a E46G mutant subunit HisF


proof_lines: pH 8.0, 30°C, IGP synthase enzyme with a C124R mutant subunit HisF


proof_lines: pH 8.0, 30°C, IGP synthase enzyme enzyme with a E46G mutant subunit HisF


proof_lines: pH 8.0, 30°C, IGP synthase enzyme with a Q123R mutant subunit HisF


substrate_name: reduced glutathione

substrate: reduced glutathione


proof_lines: pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A

proof_lines: pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A


proof_lines: pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A

proof_lines: pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A


proof_lines: pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A

proof_lines: pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A


proof_lines: pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A

proof_lines: pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A


proof_lines: pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A

proof_lines: pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A


proof_lines: pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme

proof_lines: pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme


organism: Oryctolagus cuniculus

proof_lines: kcat below 0.001 s-1, pH and temperature not specified in the publication


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

proof_lines: pH and temperature not specified in the publication


substrate_name: S-(n-propylcarbamyl)-L-cysteine

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

substrate: S-(n-propylcarbamyl)-L-cysteine


substrate_name: S-(n-butylcarbamyl)-L-cysteine

substrate: S-(n-butylcarbamyl)-L-cysteine


substrate_name: O-(n-butylcarbamyl)-L-serine

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

substrate: O-(n-butylcarbamyl)-L-serine


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

proof_lines: kcat above 0.012 s-1, pH and temperature not specified in the publication


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


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature V12A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: pH 8.0, 37°C, HisF mutant enzyme V12A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D98A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, HisF mutant enzyme D98A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide


proof_lines: pH 8.0, 37°C, HisF mutant enzyme V48A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature K19A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, HisF mutant enzyme K19A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide


substrate_name: glutathione

substrate: glutathione


enzyme_display_name: phenylalanine ammonia-lyase

organism: Lycoris radiata

substrate_name: L-phenylalanine

enzyme: phenylalanine ammonia-lyase

substrate: L-phenylalanine


enzyme_display_name: adenylosuccinate lyase

organism: Leishmania donovani

enzyme: adenylosuccinate lyase


substrate_name: AMP

substrate: AMP


proof_lines:
pH 8.0, 30°C, cosubstrate: NH4+
pH 8.0, 30°C, cosubstrate: L-glutamine


substrate_name: L-glutamine

substrate: L-glutamine


enzyme_display_name: UniProt P0A6L2

substrate_name: L-aspartate 4-semialdehyde

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

enzyme: UniProt P0A6L2

substrate: L-aspartate 4-semialdehyde


enzyme_display_name: UniProt Q9I4W3

organism: Pseudomonas aeruginosa

enzyme: UniProt Q9I4W3


organism: Plasmodium falciparum


substrate_name: fumarate

substrate: fumarate


substrate_name: succinyladenosine monophosphate

substrate: succinyladenosine monophosphate


enzyme_display_name: peptidoglycan lytic transglycosylase

substrate_name: insoluble peptidoglycan

enzyme: peptidoglycan lytic transglycosylase

substrate: insoluble peptidoglycan


enzyme_display_name: threonine ammonia-lyase

organism: Mycolicibacterium smegmatis

substrate_name: L-allo-threonine

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

enzyme: threonine ammonia-lyase

substrate: L-allo-threonine


substrate_name: beta-chloro-L-alanine

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

substrate: beta-chloro-L-alanine


substrate_name: L-serine

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

substrate: L-serine


enzyme_display_name: pyridoxal 5'-phosphate synthase (glutamine hydrolyzing)

organism: Bacillus subtilis

substrate_name: Glyceraldehyde 3-phosphate; Ribose 5-phosphate; L-Glutamine


substrate_name: Pyruvate; L-Aspartate 4-semialdehyde

substrate: Pyruvate; L-Aspartate 4-semialdehyde


substrate_name: pyruvate

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

substrate: pyruvate


enzyme_display_name: DNA-(apurinic or apyrimidinic site) lyase

organism: Homo sapiens

substrate_name: DNA containing 5-OH-C/A

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

proof_lines: + G 212 mutant, pH 7.5, 37°C, presence of Mg2+

proof_lines: + G 212 mutant, pH 7.5, 37°C, presence of EDTA

proof_lines: G212 mutant, pH 7.5, 37°C, presence of EDTA

substrate: DNA containing 5-OH-C/A


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

proof_lines: P211R mutant, pH 7.5, 37°C, presence of Mg2+

proof_lines: P211R mutant, pH 7.5, 37°C, presence of EDTA

enzyme: DNA-(apurinic or apyrimidinic site) lyase


proof_lines: wild-type, pH 7.5, 37°C, presence of Mg2+

proof_lines: wild-type, pH 7.5, 37°C, presence of EDTA


enzyme_display_name: mimosinase

organism: Arthrobacter sp. Ryudai-S1

substrate_name: mimosine

enzyme: mimosinase

substrate: mimosine


enzyme_display_name: heparin-sulfate lyase

organism: Pedobacter heparinus

substrate_name: heparan sulfate

enzyme: heparin-sulfate lyase

substrate: heparan sulfate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature H36A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature H469A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


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


proof_lines:
isoform DHDPS1, at pH and 30°C
isoform DHDPS1, at pH 8.0 and 30°C


organism: Bacillus anthracis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L170E/G191E with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

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, 30°C, recombinant mutant DELTAAsp237

proof_lines: pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp171


proof_lines: pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168


proof_lines: pH not specified in the publication, 30°C, recombinant wild-type enzyme

proof_lines: pH not specified in the publication, 45°C, recombinant wild-type enzyme


organism: Rhizobium meliloti


substrate_name: pyruvate (at 30 degrees Celsius)

proof_lines: kcat is 136 sec(-1) and 465 sec(-1) at 30 and 45 degrees Celsius, respectively.

substrate: pyruvate (at 30 degrees Celsius)


substrate_name: L-aspartate-4-semialdehyde (at 30 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Escherichia coli (strain K12)

substrate_name: glutathione

substrate: glutathione


organism: Mimosa pudica

substrate_name: cystathionine

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

assay_conditions_summary: pH 8.5; 308.15 K; buffer 100 mM Britton-Robinson

column_label: Table 2 (Enzyme kinetics of mimosinase and CBL cloned from M. pudica for mimosine and cystathionine), substrate block 'Cystathionine', enzyme column 'Mimosinase'; column head 'Km (× 10−3 M)' = 0.05; column head 'kcat (s−1)' = 310; column head 'kcat/Km (mM−1 s−1)' = 6,200. The same column's 'Optimum pH' and 'Optimum temperature' entries are enzyme properties, not kinetic constants.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.05 under the column head Km (× 10−3 M); 10−3 M is the millimolar unit, so the cell reads 0.05 mM and the exported value is 0.05 mM. kcat: printed Table 2 cell 310 under the column head kcat (s−1); the cell is already in s^-1 and no unit conversion applies, so the exported value is 310.0 s^(-1). kcat/Km: printed Table 2 cell 6,200 under the column head kcat/Km (mM−1 s−1); mM−1 s−1 is already the canonical s^-1 mM^-1 unit and no unit conversion applies, so the exported value is 6200.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate block 'Cystathionine', enzyme column 'Mimosinase': Km = 0.05 (column head Km (× 10−3 M)); kcat = 310 s−1; printed kcat/Km = 6,200 mM−1 s−1.

row_label: Table 2, Cystathionine block, Mimosinase column

table_label: Table 2: Enzyme kinetics of mimosinase and CBL cloned from M. pudica for mimosine and cystathionine (Journal of Plant Research 2019, 132(5):667-680)

substrate: cystathionine


substrate_name: L,L-cystathionine

proof_lines: kcat is 12180 sec(-1) with L-mimosine as substrate (PubMed:31368041). kcat is 310 sec(-1) with L,L-cystathionine as substrate (PubMed:31368041).

substrate: L,L-cystathionine


organism: Arabidopsis thaliana

substrate_name: L-glutamine

enzyme: pyridoxal 5'-phosphate synthase (glutamine hydrolyzing)

substrate: L-glutamine


organism: Bacillus subtilis (strain 168)

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

column_label: Figure 5B text states R5P/Ru5P kcat values 0.040/0.042 min^-1 and Km values 0.053/3.18 mM respectively

raw_value_unit_evidence: Km raw_value=0.053 raw_unit=mM

row_label: R5P assay; free Pdx1/Pdx2

table_label: PMID 17189272 Results / Figure 5B


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

proof_lines: kcat is 0.040 min(-1) with ribose-5-phosphate as substrate. kcat is 0.042 min(-1) with ribulose-5-phosphate as substrate.


column_label: Results prose states varying glutamine produced Michaelis-Menten kinetics with kcat 7.60 +/- 0.01 min^-1 and Km 0.99 +/- 0.01 mM

raw_value_unit_evidence: Km raw_value=0.99 +/- 0.01 raw_unit=mM

row_label: YaaE glutaminase assay; glutamine varied

table_label: PMID 16030023 Results / supplemental data statement


organism: Caldanaerobacter subterraneus subsp. tengcongensis

proof_lines: by adding 2 mM (S)-aspartate 4-semialdehyde, at 60°C


organism: Plasmodium falciparum (isolate 3D7)


organism: Escherichia coli

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

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

source_databases_merged: skid uniprot


organism: Priestia megaterium

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
kcat is 46.7 sec(-1).


enzyme_display_name: indigoidine synthase

organism: Streptomyces lavendulae

proof_lines: kcat is 324 min(-1) with L-glutamine as substrate.

enzyme: indigoidine synthase


organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)

column_label: Table 1 reports N. meningitidis Km(ASA) (mM) = 0.052+/-0.003.

raw_value_unit_evidence: Km(ASA) raw_value=0.052+/-0.003 mM raw_unit=mM

row_label: N. meningitidis DHDPS row / Km(ASA) column

table_label: ScienceDirect PMID 19236959 Table 1


organism: Staphylococcus aureus (strain MRSA252)

column_label: Abstract reports K(m)(ASA)=0.22+/-0.02 mm.

raw_value_unit_evidence: Km raw_value=0.22 mm raw_unit=mM

row_label: MRSA-DHDPS / ASA

table_label: PubMed XML abstract PMID 18684709


organism: Staphylococcus aureus

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
kcat is 70 sec(-1).


column_label: Table 3(b) row DHDPS with (S)-ASA reports K mASA 0.11 +/- 0.01 mM.

raw_value_unit_evidence: Km raw_value=0.11 +/- 0.01 mM raw_unit=mM

row_label: DHDPS with (S)-ASA

table_label: Table 3(b), PMID 14580236 PDF


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: Unknown

substrate: Unknown


substrate_name: (S)-aspartate 4-semialdehyde

proof_lines: modeled with substrate inhibition, at 60°C

substrate: (S)-aspartate 4-semialdehyde


substrate_name: L-Aspartate 4-semialdehyde; Pyruvate

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

source_databases_merged: sabio_rk skid uniprot

substrate: L-Aspartate 4-semialdehyde; Pyruvate


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


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)


organism: Leucaena leucocephala


substrate_name: ribose 5-phosphate

column_label: Table 3 reports ScPdx1.1 ribose 5-phosphate Km (mM) = 0.11+/-0.05.

raw_value_unit_evidence: Km raw_value=0.11+/-0.05 mM raw_unit=mM

row_label: ScPdx1.1 row / Ribose 5-phosphate Km column

table_label: ScienceDirect PMID 19523954 Table 3

substrate: ribose 5-phosphate


substrate_name: glyceraldehyde 3-phosphate

column_label: Table 3 reports ScPdx1.1 glyceraldehyde 3-phosphate Km (mM) = 0.30+/-0.09.

raw_value_unit_evidence: Km raw_value=0.30+/-0.09 mM raw_unit=mM

row_label: ScPdx1.1 row / Glyceraldehyde 3-phosphate Km column

substrate: glyceraldehyde 3-phosphate


organism: Pseudomonas aeruginosa


organism: Saccharomyces cerevisiae

substrate_name: NH3; Glyceraldehyde 3-phosphate; Ribose 5-phosphate


organism: Agrobacterium tumefaciens

substrate_name: Pyruvate; L-Aspartate 4-semialdehyde


organism: Zea mays


organism: Bacillus subtilis (strain 168)

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


organism: Neisseria meningitidis

substrate_name: pyruvate


substrate_name: glutamine

column_label: Abstract reports the complex showed glutaminase activity with Km of 3.4 mm for glutamine.

raw_value_unit_evidence: Km raw_value=3.4 mm raw_unit=mM

row_label: Sno1p/Snz1p complex / glutamine

table_label: PubMed XML abstract PMID 14764090

substrate: glutamine


proof_lines:
Pseudomonas aeruginosa
dihydrodipicolinate synthase
EC 4.2.1.52


organism: Agrobacterium fabrum (strain C58 / ATCC 33970)


organism: Staphylococcus aureus (strain COL)

assay_conditions_summary: pH 8; cofactor NADH

column_label: Results prose reports K m for ASA = 0.33 +/- 0.025 mM.

raw_value_unit_evidence: Km raw_value=0.33 +/- 0.025 mM raw_unit=mM

row_label: S. aureus DHDPS prose kinetic fit

table_label: Wiley FEBS Letters PMID 18671976 Results prose / Fig. 3


enzyme_display_name: UniProt Q5HG25

column_label: Results prose reports K m for pyruvate = 0.12 +/- 0.01 mM, not the exported 0.114891252930761 mM.

raw_value_unit_evidence: Km raw_value=0.12 +/- 0.01 mM raw_unit=mM

enzyme: UniProt Q5HG25


proof_lines: 30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258A

proof_lines: 30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258A


proof_lines: 30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258R

proof_lines: 30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258R


proof_lines: 30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239A

proof_lines: 30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239A


proof_lines: 30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239H

proof_lines: 30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239H


proof_lines: 30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360A

proof_lines: 30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360A


proof_lines: 30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360R

proof_lines: 30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360R


proof_lines: 30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239K

proof_lines: 30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239K


proof_lines: 30°C, pH 7.0, cosubstrate: NH4+, wild-type enzyme

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


substrate_name: mimosine

column_label: Abstract reports apparent Km and Vmax values of 1.16x10(-4) M and 5.05x10(-5) mol s(-1) mg(-1), respectively.

raw_value_unit_evidence: Km raw_value=1.16e-4 M raw_unit=M

row_label: recombinant Leucaena leucocephala mimosinase / mimosine

table_label: PubMed XML abstract PMID 24351687


organism: Bacillus subtilis

substrate_name: D-ribose 5-phosphate

proof_lines: pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C

substrate: D-ribose 5-phosphate


proof_lines: pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C

proof_lines: pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C


proof_lines: pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C

proof_lines: Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C


proof_lines: Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C


proof_lines: pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C


organism: Escherichia coli

substrate_name: L-aspartate 4-semialdehyde

substrate: L-aspartate 4-semialdehyde


substrate: pyruvate


proof_lines: mutant D193A, with respect to (S)-aspartate 4-semialdehyde


proof_lines: mutant Q196D, with respect to (S)-aspartate 4-semialdehyde


proof_lines:
mutant Y107F, pH 8.0, 30°C
Y107F mutant


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


assay_conditions_summary: pH 8; 303.15 K; buffer 100 mM HEPES; cofactor NADPH

proof_lines: mutant K161A, at 30°C, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR

proof_lines: mutant K161A, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR


assay_conditions_summary: pH 8; buffer 100 mM HEPES; cofactor NADPH

proof_lines: mutant K161R, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR


proof_lines: mutant K161A, with pyruvate as substrate

proof_lines: mutant K161A, with L-aspartate 4-semialdehyde as substrate


proof_lines: mutant K161R, with pyruvate as substrate

proof_lines: mutant K161R, with L-aspartate 4-semialdehyde as substrate


organism: Campylobacter jejuni


organism: Mycobacterium tuberculosis


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


proof_lines: pH 8.0, 37°C, free pyridoxal 5'-phosphate synthase subunit (Pdx1)


substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


proof_lines: recombinant mutant H56K, pH 8.0, temperature not specified in the publication


proof_lines: recombinant mutant E84T, pH 8.0, temperature not specified in the publication


organism: Geobacillus kaustophilus


assay_conditions_summary: pH 8; 303.15 K; buffer 100 mM HEPES


proof_lines: with (S)-aspartate 4-semialdehyde as substrate


organism: Geobacillus sp. H6a


enzyme_display_name: cyclohexyl-isocyanide hydratase

organism: Pseudomonas fluorescens

substrate_name: 2-naphthyl isocyanide

enzyme: cyclohexyl-isocyanide hydratase

substrate: 2-naphthyl isocyanide


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

organism: Rattus norvegicus

substrate_name: 7,8-dihydroneopterin triphosphate

proof_lines:
mutant E133Q pH 7.4, 37°C
mutant enzyme E133Q

enzyme: 6-pyruvoyltetrahydropterin synthase

substrate: 7,8-dihydroneopterin triphosphate


proof_lines:
mutant H89N pH 7.4, 37°C
mutant enzyme H89N


enzyme_display_name: enoyl-CoA hydratase 2

substrate_name: crotonyl-CoA

enzyme: enoyl-CoA hydratase 2

substrate: crotonyl-CoA


substrate_name: AMP

substrate: AMP


substrate_name: fumarate

substrate: fumarate


enzyme_display_name: hyaluronate lyase

organism: Streptococcus pneumoniae

substrate_name: hyaluronan

enzyme: hyaluronate lyase

substrate: hyaluronan


enzyme_display_name: aspartate ammonia-lyase

organism: Yersinia pestis

substrate_name: L-aspartate

proof_lines:
recombinant enzyme
recmbinant enzyme

enzyme: aspartate ammonia-lyase

substrate: L-aspartate


enzyme_display_name: mannuronate-specific alginate lyase

organism: Alteromonas sp.

substrate_name: tetra-alpha1,4-L-guluronic acid

enzyme: mannuronate-specific alginate lyase

substrate: tetra-alpha1,4-L-guluronic acid


enzyme_display_name: guluronate-specific alginate lyase

proof_lines: pH 8.5, 30°C, 100 mM glycine in 0.1 N NaCl and 0.1 N NaOH

enzyme: guluronate-specific alginate lyase


enzyme_display_name: 3-dehydroquinate synthase

organism: Actinidia chinensis

enzyme: 3-dehydroquinate synthase


organism: Agrobacterium tumefaciens

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: UniProt Q30W70

organism: Oleidesulfovibrio alaskensis

substrate_name: choline

smiles: C[N+](C)(C)CCO

enzyme: UniProt Q30W70

substrate: choline


enzyme_display_name: UniProt B6K8Y1

organism: Toxoplasma gondii

substrate_name: L-cystathionine

enzyme: UniProt B6K8Y1

substrate: L-cystathionine


substrate_name: djenkolic acid

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

substrate: djenkolic acid


substrate_name: L-cysteine

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

substrate: L-cysteine


enzyme_display_name: UniProt Q5LT18

organism: Ruegeria pomeroyi

substrate_name: dimethylsulfoniopropionate

enzyme: UniProt Q5LT18

substrate: dimethylsulfoniopropionate


substrate_name: diethylsulfoniopropionate

substrate: diethylsulfoniopropionate


enzyme_display_name: pyridoxal 5'-phosphate synthase (glutamine hydrolyzing)

organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 0.040 min(-1) with ribose-5-phosphate as substrate. kcat is 0.042 min(-1) with ribulose-5-phosphate as substrate.


substrate_name: L-glutamine

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

proof_lines: kcat is 7.60 min(-1) for glutaminase activity.

substrate: L-glutamine


enzyme_display_name: phenylalanine ammonia-lyase

organism: Anthoceros agrestis

substrate_name: L-tyrosine

enzyme: phenylalanine ammonia-lyase

substrate: L-tyrosine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


enzyme_display_name: threonine synthase

organism: Thermus thermophilus

substrate_name: phosphate

enzyme: threonine synthase

substrate: phosphate


substrate_name: L-Vinylglycine

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

substrate: L-Vinylglycine


substrate_name: O-phospho-L-homoserine

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

substrate: O-phospho-L-homoserine


organism: Arabidopsis thaliana


substrate_name: trans-cinnamate

substrate: trans-cinnamate


organism: Pseudomonas aeruginosa

sequence_source: UniProt Q9HTD7


substrate_name: fumarate

substrate: fumarate


enzyme_display_name: cystathionine gamma-lyase

enzyme: cystathionine gamma-lyase


enzyme_display_name: dimethylpropiothetin dethiomethylase

organism: Synechocystis sp.

substrate_name: L-Djenkolic acid

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NADH

column_label: Table I; row L-Djenkolic acid; columns Km, kcat, and kcat/Km confirm required row metrics

normalized_value_unit_evidence: normalized: Km=0.7 mM; kcat=50 s^-1; printed kcat/Km=71 mM^-1 s^-1; row-derived central quotient=50/0.7=71.42857142857143 s^-1 mM^-1

raw_value_unit_evidence: Table I cells: substrate=L-Djenkolic acid; stoichiometric yield=2.0 mol pyruvate/mol substrate; Km=0.7 mM; kcat=50 s^-1; kcat/Km=71 mM^-1 s^-1

row_label: L-Djenkolic acid

table_label: Table I

enzyme: dimethylpropiothetin dethiomethylase

substrate: L-Djenkolic acid


substrate_name: Decarboxycystine

smiles: NCCSSCCN

column_label: Table I; row Decarboxycystine; columns Km, kcat, and kcat/Km confirm required row metrics

normalized_value_unit_evidence: normalized: Km=0.8 mM; kcat=14 s^-1; printed kcat/Km=18 mM^-1 s^-1; row-derived central quotient=14/0.8=17.5 s^-1 mM^-1

raw_value_unit_evidence: Table I cells: substrate=Decarboxycystine; stoichiometric yield=1.1 mol pyruvate/mol substrate; Km=0.8 mM; kcat=14 s^-1; kcat/Km=18 mM^-1 s^-1

row_label: Decarboxycystine

substrate: Decarboxycystine


substrate_name: L-Cystine

column_label: Table I; row L-Cystine; columns Km, kcat, and kcat/Km confirm required row metrics

normalized_value_unit_evidence: normalized: Km=1.0 mM; kcat=36 s^-1; printed kcat/Km=36 mM^-1 s^-1; row-derived central quotient=36/1.0=36 s^-1 mM^-1

raw_value_unit_evidence: Table I cells: substrate=L-Cystine; stoichiometric yield=2.0 mol pyruvate/mol substrate; Km=1.0 mM; kcat=36 s^-1; kcat/Km=36 mM^-1 s^-1

row_label: L-Cystine

substrate: L-Cystine


substrate_name: Desaminocystine

column_label: Table I; row Desaminocystine; columns Km, kcat, and kcat/Km confirm required row metrics

normalized_value_unit_evidence: normalized: Km=0.5 mM; kcat=29 s^-1; printed kcat/Km=58 mM^-1 s^-1; row-derived central quotient=29/0.5=58 s^-1 mM^-1

raw_value_unit_evidence: Table I cells: substrate=Desaminocystine; stoichiometric yield=1.0 mol pyruvate/mol substrate; Km=0.5 mM; kcat=29 s^-1; kcat/Km=58 mM^-1 s^-1

row_label: Desaminocystine

substrate: Desaminocystine


substrate_name: L-Cystathionine

column_label: Table I; row L-Cystathionine; columns Km, kcat, and kcat/Km confirm required row metrics

normalized_value_unit_evidence: normalized: Km=1.2 mM; kcat=7 s^-1; printed kcat/Km=6 mM^-1 s^-1; row-derived central quotient=7/1.2=5.833333333333334 s^-1 mM^-1

raw_value_unit_evidence: Table I cells: substrate=L-Cystathionine; stoichiometric yield=1.0 mol pyruvate/mol substrate; Km=1.2 mM; kcat=7 s^-1; kcat/Km=6 mM^-1 s^-1

row_label: L-Cystathionine

substrate: L-Cystathionine


substrate_name: S-Ethyl-L-cysteine

column_label: Table I; row S-Ethyl-L-cysteine; columns Km, kcat, and kcat/Km confirm required row metrics

normalized_value_unit_evidence: normalized: Km=7.3 mM; kcat=37 s^-1; printed kcat/Km=5 mM^-1 s^-1; row-derived central quotient=37/7.3=5.068493150684931 s^-1 mM^-1

raw_value_unit_evidence: Table I cells: substrate=S-Ethyl-L-cysteine; stoichiometric yield=1.1 mol pyruvate/mol substrate; Km=7.3 mM; kcat=37 s^-1; kcat/Km=5 mM^-1 s^-1

row_label: S-Ethyl-L-cysteine

substrate: S-Ethyl-L-cysteine


substrate_name: S-Methyl-L-cysteine

column_label: Table I; row S-Methyl-L-cysteine; columns Km, kcat, and kcat/Km confirm required row metrics

normalized_value_unit_evidence: normalized: Km=5.7 mM; kcat=20 s^-1; printed kcat/Km=3.5 mM^-1 s^-1; row-derived central quotient=20/5.7=3.508771929824561 s^-1 mM^-1

raw_value_unit_evidence: Table I cells: substrate=S-Methyl-L-cysteine; stoichiometric yield=1.2 mol pyruvate/mol substrate; Km=5.7 mM; kcat=20 s^-1; kcat/Km=3.5 mM^-1 s^-1

row_label: S-Methyl-L-cysteine

substrate: S-Methyl-L-cysteine


substrate_name: Meso-Cystine

column_label: Table I; row Meso-cystine; columns Km, kcat, and kcat/Km confirm required row metrics

normalized_value_unit_evidence: normalized: Km=2.2 mM; kcat=29 s^-1; printed kcat/Km=13 mM^-1 s^-1; row-derived central quotient=29/2.2=13.18181818181818 s^-1 mM^-1

raw_value_unit_evidence: Table I cells: substrate=Meso-cystine; stoichiometric yield=1.0 mol pyruvate/mol substrate; Km=2.2 mM; kcat=29 s^-1; kcat/Km=13 mM^-1 s^-1

row_label: Meso-cystine

substrate: Meso-Cystine


organism: Treponema denticola

substrate_name: beta-chloro-L-alanine

proof_lines: Y123F/Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C

substrate: beta-chloro-L-alanine


proof_lines: Y123F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C


substrate_name: D-alanine

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

proof_lines: racemization, Y123F/Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C

substrate: D-alanine


proof_lines: wild type, 20 mM potassium phosphate buffer, pH 7.4, 25°C


proof_lines: Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C


substrate_name: L-alanine

proof_lines: racemization, wild type, 20 mM potassium phosphate buffer, pH 7.4, 25°C

substrate: L-alanine


proof_lines: racemization, Y123F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C


proof_lines: racemization, Y124F mutant, 20 mM potassium phosphate buffer, pH 7.4, 25°C


substrate_name: H2O; L-Cystine

substrate: H2O; L-Cystine


enzyme_display_name: amorpha-4,11-diene synthase

organism: Artemisia annua

substrate_name: geranyl diphosphate

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

proof_lines:
presence of Mn2+, pH 7.5, 30°C
presence of Mn2+, pH 6.5, 30°C

enzyme: amorpha-4,11-diene synthase

substrate: geranyl diphosphate


substrate_name: farnesyl diphosphate

proof_lines:
presence of Co2+, pH 7.5, 30°C
presence of Co2+, pH 6.5, 30°C
presence of Mg2+, pH 7.5, 30°C

substrate: farnesyl diphosphate


enzyme_display_name: alliin lyase

organism: Petiveria alliacea

enzyme: alliin lyase


substrate_name: propiin

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

substrate: propiin


substrate_name: petiveriin

substrate: petiveriin


substrate_name: methiin

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

substrate: methiin


substrate_name: alliin

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

substrate: alliin


organism: Streptococcus anginosus

substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-cystine

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

substrate: L-cystine


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


substrate_name: DL-cystathionine / L-cystathionine

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

substrate: DL-cystathionine / L-cystathionine


substrate_name: S-methyl-L-cysteine

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

substrate: S-methyl-L-cysteine


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


organism: Citrobacter freundii


substrate_name: ethiin

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

substrate: ethiin


proof_lines:
mutant C115H, pH 8.0, 30°C
mutant C115H, pH pH 8.0, 30°C


substrate_name: L-Aspartate

substrate: L-Aspartate


substrate_name: Oxaloacetate

substrate: Oxaloacetate


organism: Phaeobacter inhibens

substrate_name: methylpropylsulfoniopropionate

proof_lines: 30°C, pH not specified in the publication

substrate: methylpropylsulfoniopropionate


substrate_name: diethylsulfoniopropionate

substrate: diethylsulfoniopropionate


organism: Streptococcus gordonii


substrate_name: L-cystathionine

substrate: L-cystathionine


organism: Streptococcus oralis


organism: Streptococcus mutans


organism: Streptococcus salivarius


organism: Celeribacter halophilus

substrate_name: S,S-dimethyl-beta-propiothetin

substrate: S,S-dimethyl-beta-propiothetin


substrate_name: dimethylsulfoxonium propionate

substrate: dimethylsulfoxonium propionate


organism: Streptococcus sobrinus


organism: Aspergillus carneus

substrate_name: DL-cystathionine

proof_lines: protein bound to polyethylene glycol, pH not specified in the publication, temperature not specified in the publication

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

substrate: DL-cystathionine


organism: Ferrimonas balearica


substrate_name: Cys

substrate: Cys


organism: Acinetobacter bereziniae

substrate_name: beta-dimethylsulfoniopropanoate

substrate: beta-dimethylsulfoniopropanoate


enzyme_display_name: homocysteine desulfhydrase

organism: Trichomonas vaginalis

substrate_name: homocysteine

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

enzyme: homocysteine desulfhydrase

substrate: homocysteine


organism: Candidatus Pelagibacter communis


organism: Bacillus sp.

substrate_name: H2O; L-Djenkolic acid

substrate: H2O; L-Djenkolic acid


organism: Spinacia oleracea

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

proof_lines:
higher plants
Chenopodiaceae
L-ASA Km 1.0 mM


organism: Fusarium lateritium

substrate_name: dimethylsulfoniopropionate

substrate: dimethylsulfoniopropionate


organism: Halodesulfovibrio aestuarii


organism: Oceanimonas doudoroffii


organism: Ulva curvata


substrate_name: H2O; L-Cystathionine

substrate: H2O; L-Cystathionine


organism: Phaeobacter inhibens


organism: Allium altyncolicum

substrate_name: L-(+)-alliin

substrate: L-(+)-alliin


organism: Allium jesdianum

substrate_name: (+)-S-(2-propenyl)-L-cysteine sulfoxide

substrate: (+)-S-(2-propenyl)-L-cysteine sulfoxide


organism: Allium obliquum


organism: Allium sphaerocephalon


organism: Allium saxatile


organism: Allium stipitatum


organism: Allium victorialis


organism: Allium subhirsutum


organism: Citrobacter freundii

substrate_name: (+-)-propiin

substrate: (+-)-propiin


organism: Cupriavidus necator

substrate_name: alliin

substrate: alliin


organism: Acinetobacter bereziniae


organism: Ensifer adhaerens

substrate_name: (-)-alliin

proof_lines:
about, below, pH 7.0, 30°C
pH 7.0, 30°C

substrate: (-)-alliin


organism: Lentinula edodes

substrate_name: desglutamyl-lentinic acid

substrate: desglutamyl-lentinic acid


organism: Penicillium hirsutum

substrate_name: S-allyl-L-Cys sulfoxide

substrate: S-allyl-L-Cys sulfoxide


organism: Tulbaghia violacea

substrate_name: S-ethyl-L-Cys sulfoxide

substrate: S-ethyl-L-Cys sulfoxide


organism: Homo sapiens

substrate_name: L-cystathionine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32929 and applied mutation signature Q240E to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232); the printed table is transposed: each printed column is one enzyme form and each printed line inside a substrate block is one parameter. Table 1, substrate block 'Csta', printed variant column 'Q240E'; row 'KM, mM' = 0.72; row 'kcat, s-1' = 0.02; row 'kcat/KM' = 0.028. captured primary segment: Table 1 | substrate Csta | human CGL Q240E | KM 0.72 mM | kcat 0.02 s-1 | kcat/KM 0.028 mM-1 s-1 | assay DTNB cysteine release from cystathionine, at 37 °C

normalized_value_unit_evidence: KM: printed Table 1 cell 0.72 mM; the printed row head is 'KM, mM', so no unit conversion applies and the paper value is 0.72 mM. kcat: printed Table 1 cell 0.02 s-1; the printed row head is 'kcat, s-1', already per second, so no unit conversion applies and the paper value is 0.02 s^(-1). kcat/KM: printed Table 1 cell 0.028 mM-1 s-1; footnote c states that kcat/KM is expressed in units of mM-1 s-1, which is the canonical unit, so no unit conversion applies and the printed cell is 0.028 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.02 / 0.72 = 0.02777777777777778 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.028 mM-1 s-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 1, substrate block 'Csta', printed variant column 'Q240E': kcat = 0.02 s-1; KM = 0.72 mM; printed kcat/KM = 0.028 mM-1 s-1.

row_label: Table 1, substrate block 'Csta' (cystathionine), printed variant column 'Q240E'

substrate: L-cystathionine


substrate_name: L-cysteine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32929 and applied mutation signature T67I to reconstruct the assayed variant sequence.

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

column_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232); the printed table is transposed: each printed column is one enzyme form and each printed line inside a substrate block is one parameter. Table 1, substrate block 'Cys', printed variant column 'T67I'; row 'KM, mM' = 4.1; row 'kcat, s-1' = 0.30; row 'kcat/KM' = 0.07. captured primary segment: Table 1 | substrate Cys | human CGL T67I | KM 4.1 mM | kcat 0.30 s-1 | kcat/KM 0.07 mM-1 s-1 | assay 40 mM borate pH 7.0 lead acetate H2S release, at 37 °C

normalized_value_unit_evidence: KM: printed Table 1 cell 4.1 mM; the printed row head is 'KM, mM', so no unit conversion applies and the paper value is 4.1 mM. kcat: printed Table 1 cell 0.30 s-1; the printed row head is 'kcat, s-1', already per second, so no unit conversion applies and the paper value is 0.3 s^(-1). kcat/KM: printed Table 1 cell 0.07 mM-1 s-1; footnote c states that kcat/KM is expressed in units of mM-1 s-1, which is the canonical unit, so no unit conversion applies and the printed cell is 0.07 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.30 / 4.1 = 0.07317073170731708 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.07 mM-1 s-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 1, substrate block 'Cys', printed variant column 'T67I': kcat = 0.30 s-1; KM = 4.1 mM; printed kcat/KM = 0.07 mM-1 s-1.

row_label: Table 1, substrate block 'Cys' (cysteine), printed variant column 'T67I'

substrate: L-cysteine


column_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232); the printed table is transposed: each printed column is one enzyme form and each printed line inside a substrate block is one parameter. Table 1, substrate block 'Csta', printed variant column 'T67I'; row 'KM, mM' = 0.6; row 'kcat, s-1' = 0.45; row 'kcat/KM' = 0.86. captured primary segment: Table 1 | substrate Csta | human CGL T67I | KM 0.6 mM | kcat 0.45 s-1 | kcat/KM 0.86 mM-1 s-1 | assay DTNB cysteine release from cystathionine, at 37 °C

normalized_value_unit_evidence: KM: printed Table 1 cell 0.6 mM; the printed row head is 'KM, mM', so no unit conversion applies and the paper value is 0.6 mM. kcat: printed Table 1 cell 0.45 s-1; the printed row head is 'kcat, s-1', already per second, so no unit conversion applies and the paper value is 0.45 s^(-1). kcat/KM: the paper's own printed efficiency cell 0.86 mM-1 s-1 is already in the canonical unit, so the paper value for this metric is 0.86 s^(-1)*mM^(-1). The quotient of the two printed component cells is 0.45 / 0.6 = 0.75 s^-1 mM^-1, which falls outside the rounding interval of the printed cell 0.86 at every place value that literal could carry, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 1, substrate block 'Csta', printed variant column 'T67I': kcat = 0.45 s-1; KM = 0.6 mM; printed kcat/KM = 0.86 mM-1 s-1.

row_label: Table 1, substrate block 'Csta' (cystathionine), printed variant column 'T67I'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32929 and applied mutation signature S403I to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232); the printed table is transposed: each printed column is one enzyme form and each printed line inside a substrate block is one parameter. Table 1, substrate block 'Cys', printed variant column 'I403'; row 'KM, mM' = 3.4; row 'kcat, s-1' = 0.67; row 'kcat/KM' = 0.20. captured primary segment: Table 1 | substrate Cys | human CGL I403 | KM 3.4 mM | kcat 0.67 s-1 | kcat/KM 0.20 mM-1 s-1 | assay 40 mM borate pH 7.0 lead acetate H2S release, at 37 °C

normalized_value_unit_evidence: KM: printed Table 1 cell 3.4 mM; the printed row head is 'KM, mM', so no unit conversion applies and the paper value is 3.4 mM. kcat: printed Table 1 cell 0.67 s-1; the printed row head is 'kcat, s-1', already per second, so no unit conversion applies and the paper value is 0.67 s^(-1). kcat/KM: printed Table 1 cell 0.20 mM-1 s-1; footnote c states that kcat/KM is expressed in units of mM-1 s-1, which is the canonical unit, so no unit conversion applies and the printed cell is 0.2 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.67 / 3.4 = 0.1970588235294118 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.20 mM-1 s-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 1, substrate block 'Cys', printed variant column 'I403': kcat = 0.67 s-1; KM = 3.4 mM; printed kcat/KM = 0.20 mM-1 s-1.

row_label: Table 1, substrate block 'Cys' (cysteine), printed variant column 'I403'


substrate_name: L-homocysteine

column_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232); the printed table is transposed: each printed column is one enzyme form and each printed line inside a substrate block is one parameter. Table 1, substrate block 'Hcy', printed variant column 'T67I'; row 'KM, mM' = 8.0; row 'kcat, s-1' = 0.82; row 'kcat/KM' = 0.10. captured primary segment: Table 1 | substrate Hcy | human CGL T67I | KM 8.0 mM | kcat 0.82 s-1 | kcat/KM 0.10 mM-1 s-1 | assay 40 mM borate pH 7.0 lead acetate H2S release, at 37 °C

normalized_value_unit_evidence: KM: printed Table 1 cell 8.0 mM; the printed row head is 'KM, mM', so no unit conversion applies and the paper value is 8.0 mM. kcat: printed Table 1 cell 0.82 s-1; the printed row head is 'kcat, s-1', already per second, so no unit conversion applies and the paper value is 0.82 s^(-1). kcat/KM: printed Table 1 cell 0.10 mM-1 s-1; footnote c states that kcat/KM is expressed in units of mM-1 s-1, which is the canonical unit, so no unit conversion applies and the printed cell is 0.1 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.82 / 8.0 = 0.1025 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.10 mM-1 s-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 1, substrate block 'Hcy', printed variant column 'T67I': kcat = 0.82 s-1; KM = 8.0 mM; printed kcat/KM = 0.10 mM-1 s-1.

row_label: Table 1, substrate block 'Hcy' (homocysteine), printed variant column 'T67I'

substrate: L-homocysteine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S403I to reconstruct the assayed variant sequence.

proof_lines:
for variante S403
for variante I403
for variant S403


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

assay_conditions_summary: pH 8.2; 310.15 K; buffer 50 mM sodium phosphate

proof_lines: wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E339K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E339Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E339A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C