column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the H458A enzyme block, substrate row S-Me-L-Cys: column Km, mM = 2.32; column kcat, s-1 = 6.03; column kcat/Km , M-1 s-1 = 2.59 x 10^3. captured primary segment: Table 1, H458A enzyme block, substrate row S-Me-L-Cys | construct H458A mutant Proteus vulgaris tryptophan indole-lyase | substrate S-Me-L-Cys | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 2.32 mM | kcat 6.03 s-1 | kcat/Km 2.59 x 10^3 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 2.32 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 2.32 mM. kcat: printed Table 1 cell 6.03 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 6.03 s^(-1). kcat/Km: printed Table 1 cell 2.59 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2590.0 / 1000 = 2.59 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, H458A enzyme block, substrate row S-Me-L-Cys: Km = 2.32 mM; kcat = 6.03 s-1; printed kcat/Km = 2.59 x 10^3 M-1 s-1.


enzyme_display_name: tryptophanase

organism: Proteus vulgaris

substrate_name: S-Methyl-L-cysteine

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the wild type enzyme block, substrate row S-Me-L-Cys: column Km, mM = 16.8; column kcat, s-1 = 4.1; column kcat/Km , M-1 s-1 = 2.38 x 10^2. captured primary segment: Table 1, wild type enzyme block, substrate row S-Me-L-Cys | construct wild-type Proteus vulgaris tryptophan indole-lyase | substrate S-Me-L-Cys | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 16.8 mM | kcat 4.1 s-1 | kcat/Km 2.38 x 10^2 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 16.8 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 16.8 mM. kcat: printed Table 1 cell 4.1 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 4.1 s^(-1). kcat/Km: printed Table 1 cell 2.38 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 238.0 / 1000 = 0.23800000000000002 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, wild type enzyme block, substrate row S-Me-L-Cys: Km = 16.8 mM; kcat = 4.1 s-1; printed kcat/Km = 2.38 x 10^2 M-1 s-1.

table_label: Table 1: Steady-State Kinetic Parameters, wild type enzyme block (Biochemistry 2003, 42(38):11161-11169)

data_origin: experimental

enzyme: tryptophanase

substrate: S-Methyl-L-cysteine

status: corrected

source: oed


substrate_name: S-o-Nitrophenyl-L-cysteine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D133A to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines:
Proteus vulgaris
tryptophan indole-lyase
S-(o-nitrophenyl)-L-cysteine

substrate: S-o-Nitrophenyl-L-cysteine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H458A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADH

column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the wild type enzyme block, substrate row SOPC: column Km, mM = 0.18; column kcat, s-1 = 33.35; column kcat/Km , M-1 s-1 = 1.85 x 10^5. captured primary segment: Table 1, wild type enzyme block, substrate row SOPC | construct wild-type Proteus vulgaris tryptophan indole-lyase | substrate SOPC | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 0.18 mM | kcat 33.35 s-1 | kcat/Km 1.85 x 10^5 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 0.18 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 0.18 mM. kcat: printed Table 1 cell 33.35 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 33.35 s^(-1). kcat/Km: printed Table 1 cell 1.85 x 10^5 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 185000.0 / 1000 = 185.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, wild type enzyme block, substrate row SOPC: Km = 0.18 mM; kcat = 33.35 s-1; printed kcat/Km = 1.85 x 10^5 M-1 s-1.


enzyme_display_name: tyrosine phenol-lyase

organism: Citrobacter freundii

substrate_name: S-ethyl-L-cysteine

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S51A to reconstruct the assayed variant sequence.

enzyme: tyrosine phenol-lyase

substrate: S-ethyl-L-cysteine


substrate_name: S-methyl-L-cysteine

substrate: S-methyl-L-cysteine


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


substrate_name: L-Serine

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

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y72F to reconstruct the assayed variant sequence.

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

proof_lines:
Proteus vulgaris
tryptophan indole-lyase
L-serine

substrate: L-Serine


substrate_name: L-Tryptophan

column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the wild type enzyme block, substrate row L-Trp: column Km, mM = 0.28; column kcat, s-1 = 6.29; column kcat/Km , M-1 s-1 = 2.25 x 10^4. captured primary segment: Table 1, wild type enzyme block, substrate row L-Trp | construct wild-type Proteus vulgaris tryptophan indole-lyase | substrate L-Trp | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 0.28 mM | kcat 6.29 s-1 | kcat/Km 2.25 x 10^4 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 0.28 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 0.28 mM. kcat: printed Table 1 cell 6.29 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 6.29 s^(-1). kcat/Km: printed Table 1 cell 2.25 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 22500.0 / 1000 = 22.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, wild type enzyme block, substrate row L-Trp: Km = 0.28 mM; kcat = 6.29 s-1; printed kcat/Km = 2.25 x 10^4 M-1 s-1.

substrate: L-Tryptophan


substrate_name: S-Benzyl-L-cysteine

verification_status: unverified

substrate: S-Benzyl-L-cysteine

status: unverified


column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the wild type enzyme block, substrate row S-Bzl-L-Cys: column Km, mM = 0.8; column kcat, s-1 = 1.95; column kcat/Km , M-1 s-1 = 2.44 x 10^3. captured primary segment: Table 1, wild type enzyme block, substrate row S-Bzl-L-Cys | construct wild-type Proteus vulgaris tryptophan indole-lyase | substrate S-Bzl-L-Cys | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 0.8 mM | kcat 1.95 s-1 | kcat/Km 2.44 x 10^3 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 0.8 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 0.8 mM. kcat: printed Table 1 cell 1.95 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 1.95 s^(-1). kcat/Km: printed Table 1 cell 2.44 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2440.0 / 1000 = 2.44 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, wild type enzyme block, substrate row S-Bzl-L-Cys: Km = 0.8 mM; kcat = 1.95 s-1; printed kcat/Km = 2.44 x 10^3 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28796 and applied mutation signature H458A to reconstruct the assayed variant sequence.

column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the H458A enzyme block, substrate row S-Bzl-L-Cys: column Km, mM = 0.096; column kcat, s-1 = 10.9; column kcat/Km , M-1 s-1 = 1.13 x 10^5. captured primary segment: Table 1, H458A enzyme block, substrate row S-Bzl-L-Cys | construct H458A mutant Proteus vulgaris tryptophan indole-lyase | substrate S-Bzl-L-Cys | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 0.096 mM | kcat 10.9 s-1 | kcat/Km 1.13 x 10^5 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 0.096 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 0.096 mM. kcat: printed Table 1 cell 10.9 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 10.9 s^(-1). kcat/Km: printed Table 1 cell 1.13 x 10^5 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 112999.99999999999 / 1000 = 112.99999999999999 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, H458A enzyme block, substrate row S-Bzl-L-Cys: Km = 0.096 mM; kcat = 10.9 s-1; printed kcat/Km = 1.13 x 10^5 M-1 s-1.

table_label: Table 1: Steady-State Kinetic Parameters, H458A enzyme block (Biochemistry 2003, 42(38):11161-11169)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28796 and applied mutation signature D133A to reconstruct the assayed variant sequence.

column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the D133A enzyme block, substrate row beta-Cl-L-Ala: column Km, mM = 4.6; column kcat, s-1 = 10.8; column kcat/Km , M-1 s-1 = 2.35 x 10^3. captured primary segment: Table 1, D133A enzyme block, substrate row beta-Cl-L-Ala | construct D133A mutant Proteus vulgaris tryptophan indole-lyase | substrate beta-Cl-L-Ala | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 4.6 mM | kcat 10.8 s-1 | kcat/Km 2.35 x 10^3 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 4.6 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 4.6 mM. kcat: printed Table 1 cell 10.8 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 10.8 s^(-1). kcat/Km: printed Table 1 cell 2.35 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2350.0 / 1000 = 2.35 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, D133A enzyme block, substrate row beta-Cl-L-Ala: Km = 4.6 mM; kcat = 10.8 s-1; printed kcat/Km = 2.35 x 10^3 M-1 s-1.

table_label: Table 1: Steady-State Kinetic Parameters, D133A enzyme block (Biochemistry 2003, 42(38):11161-11169)


column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the H458A enzyme block, substrate row beta-Cl-L-Ala: column Km, mM = 5.6; column kcat, s-1 = 23.3; column kcat/Km , M-1 s-1 = 4.16 x 10^3. captured primary segment: Table 1, H458A enzyme block, substrate row beta-Cl-L-Ala | construct H458A mutant Proteus vulgaris tryptophan indole-lyase | substrate beta-Cl-L-Ala | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 5.6 mM | kcat 23.3 s-1 | kcat/Km 4.16 x 10^3 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 5.6 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 5.6 mM. kcat: printed Table 1 cell 23.3 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 23.3 s^(-1). kcat/Km: printed Table 1 cell 4.16 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4160.0 / 1000 = 4.16 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, H458A enzyme block, substrate row beta-Cl-L-Ala: Km = 5.6 mM; kcat = 23.3 s-1; printed kcat/Km = 4.16 x 10^3 M-1 s-1.


column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the wild type enzyme block, substrate row beta-Cl-L-Ala: column Km, mM = 9.36; column kcat, s-1 = 8.41; column kcat/Km , M-1 s-1 = 8.98 x 10^2. captured primary segment: Table 1, wild type enzyme block, substrate row beta-Cl-L-Ala | construct wild-type Proteus vulgaris tryptophan indole-lyase | substrate beta-Cl-L-Ala | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 9.36 mM | kcat 8.41 s-1 | kcat/Km 8.98 x 10^2 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 9.36 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 9.36 mM. kcat: printed Table 1 cell 8.41 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 8.41 s^(-1). kcat/Km: printed Table 1 cell 8.98 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 898.0 / 1000 = 0.898 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, wild type enzyme block, substrate row beta-Cl-L-Ala: Km = 9.36 mM; kcat = 8.41 s-1; printed kcat/Km = 8.98 x 10^2 M-1 s-1.


column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the H458A enzyme block, substrate row L-Ser: column Km, mM = 7.85; column kcat, s-1 = 1.3; column kcat/Km , M-1 s-1 = 1.65 x 10^2. captured primary segment: Table 1, H458A enzyme block, substrate row L-Ser | construct H458A mutant Proteus vulgaris tryptophan indole-lyase | substrate L-Ser | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 7.85 mM | kcat 1.3 s-1 | kcat/Km 1.65 x 10^2 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 7.85 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 7.85 mM. kcat: printed Table 1 cell 1.3 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 1.3 s^(-1). kcat/Km: printed Table 1 cell 1.65 x 10^2 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 165.0 / 1000 = 0.165 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, H458A enzyme block, substrate row L-Ser: Km = 7.85 mM; kcat = 1.3 s-1; printed kcat/Km = 1.65 x 10^2 M-1 s-1.


column_label: Table 1 prints, under each enzyme block, the three column heads Km, mM | kcat, s-1 | kcat/Km , M-1 s-1. The cited cells are the wild type enzyme block, substrate row L-Ser: column Km, mM = 50.9; column kcat, s-1 = 1.83; column kcat/Km , M-1 s-1 = 3.59 x 10^1. captured primary segment: Table 1, wild type enzyme block, substrate row L-Ser | construct wild-type Proteus vulgaris tryptophan indole-lyase | substrate L-Ser | condition 0.05 M potassium phosphate, pH 8, at 30 C | Km 50.9 mM | kcat 1.83 s-1 | kcat/Km 3.59 x 10^1 M-1 s-1

normalized_value_unit_evidence: Km: printed Table 1 cell 50.9 mM; the printed Km column head of this table is Km, mM, so no unit conversion applies and the paper value is 50.9 mM. kcat: printed Table 1 cell 1.83 s-1; the printed turnover column head is kcat, s-1, so no unit conversion applies and the paper value is 1.83 s^(-1). kcat/Km: printed Table 1 cell 3.59 x 10^1 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 35.9 / 1000 = 0.0359 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, wild type enzyme block, substrate row L-Ser: Km = 50.9 mM; kcat = 1.83 s-1; printed kcat/Km = 3.59 x 10^1 M-1 s-1.


organism: Fusobacterium nucleatum subsp. nucleatum

substrate_name: L-Dopa

proof_lines:
l-DOPA synthesis
Fn-TPL
specific activity of 2.69 U mg-1

substrate: L-Dopa


substrate_name: L-tyrosine

proof_lines:
l-tyrosine decomposition
kcat/Km value
Fn-TPL

substrate: L-tyrosine


substrate_name: phenol

proof_lines: reversible cleavage of l-tyrosine to phenol

substrate: phenol


organism: Vibrio cholerae O1

substrate_name: L-tryptophan

substrate: L-tryptophan


proof_lines: S-alkyl-L-cysteines tryptophanase Tyr72


proof_lines:
tryptophanase
small leaving groups
Tyr72


proof_lines: L-serine tryptophanase Y72F


substrate_name: S-Ethyl-L-cysteine

substrate: S-Ethyl-L-cysteine


enzyme_display_name: 3-hydroxy-D-aspartate aldolase

organism: Paracoccus denitrificans (strain Pd 1222)

substrate_name: glyoxylate

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

proof_lines: kcat is 91 sec(-1) for the condensation of glyoxylate and glycine. kcat is 33 sec(-1) for the cleavage of (3S)-3-hydroxy-D-aspartate. kcat is 76 sec(-1) for the cleavage of D-threonine into acetaldehyde and glycine (PubMed:31723261).

enzyme: 3-hydroxy-D-aspartate aldolase

substrate: glyoxylate

source: uniprot


substrate_name: glycine

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

substrate: glycine


substrate_name: D-threonine

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

substrate: D-threonine


organism: Pantoea agglomerans

substrate_name: pyruvate

source_db: brenda

assay_conditions_summary: pH 8

substrate: pyruvate

source: brenda


smiles: N


enzyme_display_name: anthranilate synthase

organism: Escherichia coli (strain K12)

substrate_name: chorismate (at pH 7.5)

enzyme: anthranilate synthase

substrate: chorismate (at pH 7.5)


substrate_name: glutamine (at pH 7.5)

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

substrate: glutamine (at pH 7.5)


enzyme_display_name: 4-hydroxy-2-oxohexanoate aldolase

organism: Paraburkholderia xenovorans

substrate_name: glycolaldehyde

smiles: C(C=O)O

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM HEPES

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', BphI column group; column 'Km,app (mM)' = 124.6; column 'kcat,app (s-1)' = 0.40; column '(kcat/Km)app (M-1 s-1)' = 3.7.

normalized_value_unit_evidence: Km: printed cell 124.6 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 124.6 mM. kcat: printed cell 0.40 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 0.4 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 3.7 M^-1 s^-1 under the printed column head (kcat/Km)app (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.7 / 1000 = 0.0037 s^-1 mM^-1. Quotient disclosure for this cell group: 0.40 / 124.6 = 0.003210272873194222 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', BphI column group: Km,app = 124.6 mM; kcat,app = 0.40 s^-1; printed (kcat/Km)app = 3.7 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, glycolaldehyde row, BphI column group

table_label: Table 2: Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction (Biochemistry 2010, 49, 3774-3782); the HpaI column group prints Km,app (mM), kcat,app (s-1) and (kcat/Km)app in (10^3 M-1 s-1) and the BphI column group prints Km,app (mM), kcat,app (s-1) and (kcat/Km)app in (M-1 s-1)

enzyme: 4-hydroxy-2-oxohexanoate aldolase

substrate: glycolaldehyde


substrate_name: acetaldehyde

smiles: CC=O

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines: app. kcat-value with pyruvate as carbonyl donor, pH 8.0 and 25°C

proof_lines: app. Km-value with pyruvate as carbonyl donor, pH 8.0 and 25°C

proof_lines: steady-state kinetic parameter, pH 8.0 and 25°C

source_databases_merged: brenda uniprot

substrate: acetaldehyde


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


substrate_name: propionaldehyde

verification_status: verified

smiles: CCC=O

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM HEPES; cofactor NADH

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'propionaldehyde', BphI column group; column 'Km,app (mM)' = 135.9; column 'kcat,app (s-1)' = 1.79; column '(kcat/Km)app (M-1 s-1)' = 13.2.

normalized_value_unit_evidence: Km: printed cell 135.9 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 135.9 mM. kcat: printed cell 1.79 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 1.79 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 13.2 M^-1 s^-1 under the printed column head (kcat/Km)app (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 13.2 / 1000 = 0.0132 s^-1 mM^-1. Quotient disclosure for this cell group: 1.79 / 135.9 = 0.013171449595290655 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'propionaldehyde', BphI column group: Km,app = 135.9 mM; kcat,app = 1.79 s^-1; printed (kcat/Km)app = 13.2 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, propionaldehyde row, BphI column group

substrate: propionaldehyde

status: verified


enzyme_display_name: methylisocitrate lyase

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

substrate_name: magnesium

smiles: [Mg]

proof_lines:
2-methylisocitrate lyase
A. nidulans
threo-2-methylisocitrate

enzyme: methylisocitrate lyase

substrate: magnesium


substrate_name: isocitrate

proof_lines:
2-methylisocitrate lyase
isocitrate
A. nidulans

substrate: isocitrate


substrate_name: ammonia (at 37 degrees Celsius and at pH 7.6)


organism: Arabidopsis thaliana

substrate_name: chorismate

substrate: chorismate


organism: Citrobacter intermedius


organism: Prevotella intermedia

substrate_name: S-ethyl-L-cysteine

substrate: S-ethyl-L-cysteine


substrate_name: S-methyl-L-cysteine

substrate: S-methyl-L-cysteine


organism: Aspergillus nidulans

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

sequence_source: multiple


organism: [Bacillus] caldotenax

assay_conditions_summary: pH 9

column_label: Prose reports the Km values for NH4Cl and chorismate were 46 mM and 38 uM, respectively, and kcat was 2.3 x 10^4 min^-1.

raw_value_unit_evidence: Km raw_value=46 raw_unit=mM

row_label: Bacillus caldotenax anthranilate synthase I kinetic properties

table_label: Results and Discussion: Purification and Characterization of Wild Type ASI


organism: Escherichia coli

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


organism: Paracoccus denitrificans

proof_lines:
D-3-hydroxyaspartate aldolase
Paracoccus denitrificans IFO 13301
D-3-hydroxyaspartate


proof_lines: The catalytic efficiency is similar when using 4-hydroxy-2-oxopentanoate or 4-hydroxy-2-oxohexanoate as substrate, but is 10-fold lower with 4-hydroxy-2-oxoheptanoate. It is also 25-fold higher when NADH is present than the value obtained w


enzyme_display_name: 2,3-dimethylmalate lyase

organism: Eubacterium barkeri

enzyme: 2,3-dimethylmalate lyase


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

substrate_name: HMG-CoA (at pH 6.7 and 37 degrees Celsius)

assay_conditions_summary: 310.15 K; cofactor CoA


substrate_name: catechol

substrate: catechol


enzyme_display_name: 3-hydroxybenzoate synthase

organism: Streptomyces sp.

km_display: Not reported

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

enzyme: 3-hydroxybenzoate synthase


organism: Thermus thermophilus

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


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


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

proof_lines:
methylisocitrate lyase
Aspergillus nidulans
methylisocitrate


organism: Citrobacter freundii

substrate_name: S-methyl-L-Cys

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

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

proof_lines: mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C

substrate: S-methyl-L-Cys


proof_lines: mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C


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


substrate_name: S-benzyl-L-Cys

substrate: S-benzyl-L-Cys


substrate_name: S-(o-nitrophenyl)-L-Cys

substrate: S-(o-nitrophenyl)-L-Cys


substrate_name: L-Phe

ki_unit: mM

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

proof_lines: wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate

proof_lines: wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate

substrate: L-Phe


substrate_name: L-Met

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

substrate: L-Met


assay_conditions_summary: pH 8; cofactor NADH

column_label: Table 2 row 4-hydroxy-2-oxohexanoate confirms Km and kcat but reports kcat/Km as 2.1 x10^4 M^-1 s^-1, normalized to 21 s^-1*mM^-1.

normalized_value_unit_evidence: Km 0.18 mM; kcat 3.8 s^-1; paper kcat/Km 21 s^-1*mM^-1

row_label: BphI / 4-hydroxy-2-oxohexanoate

table_label: Table 2


substrate_name: oxaloacetate

column_label: Table 2 row oxaloacetate exactly supports all required metrics after unit normalization.

normalized_value_unit_evidence: Km 7.5 mM; kcat 16.5 s^-1; paper kcat/Km 2.2 s^-1*mM^-1

row_label: BphI / oxaloacetate

substrate: oxaloacetate


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


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


column_label: Table 2 row 4-hydroxy-2-oxopentanoate confirms Km and kcat but reports kcat/Km as 1.9 x10^4 M^-1 s^-1, normalized to 19 s^-1*mM^-1.

normalized_value_unit_evidence: Km 0.22 mM; kcat 4.1 s^-1; paper kcat/Km 19 s^-1*mM^-1

row_label: BphI / 4-hydroxy-2-oxopentanoate


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: S-ethyl-L-Cys

substrate: S-ethyl-L-Cys


substrate_name: S-(o-nitrophenyl)-L-cysteine

substrate: S-(o-nitrophenyl)-L-cysteine


proof_lines: mutant enzyme M379A, pH and temperature not specified in the publication


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

proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme

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

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


substrate_name: L-Dopa

substrate: L-Dopa


proof_lines:
recombinant mutant S51A, pH 8.0, 30°C
mutant enzyme S51A, at pH 8.0 and 30°C


substrate_name: S-Benzyl-L-cysteine

substrate: S-Benzyl-L-cysteine


substrate_name: beta-chloro-L-alanine

substrate: beta-chloro-L-alanine


substrate_name: D-Ala

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

substrate: D-Ala


substrate_name: S-benzoyl-L-Cys

substrate: S-benzoyl-L-Cys


substrate_name: L-Ser

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

substrate: L-Ser


substrate_name: L-Tyr

substrate: L-Tyr


proof_lines: wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C


substrate_name: S-benzylcysteine

substrate: S-benzylcysteine


substrate_name: O-benzylserine

substrate: O-benzylserine


substrate_name: alpha,beta-diaminopropionic acid

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

substrate: alpha,beta-diaminopropionic acid


substrate_name: S-ethylcysteine

substrate: S-ethylcysteine


substrate_name: O-methylserine

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

substrate: O-methylserine


substrate_name: cysteine sulfinic acid

substrate: cysteine sulfinic acid


organism: Proteus vulgaris

substrate_name: Trp

substrate: Trp


substrate_name: S-methyl-L-Cys

substrate: S-methyl-L-Cys


substrate_name: S-ethyl-L-cysteine

substrate: S-ethyl-L-cysteine


substrate_name: beta-chloroalanine

substrate: beta-chloroalanine


substrate_name: S-o-nitrophenyl-L-Cys

substrate: S-o-nitrophenyl-L-Cys


substrate_name: L-tryptophan

substrate: L-tryptophan


proof_lines: recombinant wild-type enzyme, pH 7.8, 22°C


substrate_name: Unknown

substrate: Unknown


substrate_name: indole

substrate: indole


substrate_name: Cys

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

substrate: Cys


substrate_name: pyruvate

substrate: pyruvate


substrate_name: L-Ser

substrate: L-Ser


substrate_name: S-ethyl-L-Cys

substrate: S-ethyl-L-Cys


substrate_name: S-benzyl-L-Cys

substrate: S-benzyl-L-Cys


proof_lines:
pH 8.0, 25°C
strain B/1t7-A, 37°C


assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.8), at 25°C


assay_conditions_summary: pH 8; 298.15 K; buffer 0.1 M potassium phosphate

proof_lines: in the presence of Hfq protein, in 0.1 M potassium phosphate buffer (pH 7.8), at 37°C

proof_lines: in the absence of Hfq protein, in 0.1 M potassium phosphate buffer (pH 7.8), at 37°C


organism: Daucus carota

substrate_name: chorismate

substrate: chorismate


substrate_name: L-Gln

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

substrate: L-Gln


organism: Photobacterium profundum


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


substrate_name: L-Met

substrate: L-Met


substrate_name: L-Phe

substrate: L-Phe


organism: Salmonella enterica


organism: Archaeoglobus fulgidus

proof_lines: pH 8.0, 60°C, with or without 2 M KCl and 25% glycerol

proof_lines: pH 8.0, 60°C, with 25% glycerol and 2 M KCl


organism: Providencia rettgeri

substrate_name: L-Cys

substrate: L-Cys


substrate_name: S-methyl-L-Cys

substrate: S-methyl-L-Cys


proof_lines:
beta-replacement reaction
reverse of alpha,beta-elimination


organism: Aspergillus fumigatus

substrate_name: methylisocitrate

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

substrate: methylisocitrate


proof_lines: L521F/S523T mutant protein, pH not specified in the publication, temperature not specified in the publication


proof_lines: S523T mutant protein, pH not specified in the publication, temperature not specified in the publication


proof_lines: L521F mutant protein, pH not specified in the publication, temperature not specified in the publication


organism: Fusobacterium nucleatum subsp. nucleatum

substrate_name: phenol

proof_lines: recombinant enzyme, L-tyrosine formation is measured from phenol, pyruvate, and ammonium, pH 8.5, 20°C

substrate: phenol


substrate_name: L-Dopa

substrate: L-Dopa


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: pyrocatechol

proof_lines: recombinant enzyme, L-DOPA formation is measured from dicatechol, pyruvate, and ammonium, pH 8.5, 20°C

substrate: pyrocatechol


organism: Oryza sativa

proof_lines: reconstituted enzyme OASA2-OASB1, cosubstrate: NH4+


proof_lines: alpha-subunit OASA1D (N323D, cosubstrate: NH4+)

proof_lines: reconstituted enzyme OASA1D(N323D)-OASB1, cosubstrate: NH4+

proof_lines: reconstituted enzyme OASA1D(N323D)-OASB1, cosubstrate: L-Gln


substrate_name: Unknown

proof_lines: reconstituted enzyme OASA2-OASB1, cosubstrate: L-Gln

proof_lines: reconstituted enzyme OASA1-OASB1, cosubstrate: L-Gln

substrate: Unknown


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines: pH 7.7, 25°C, mutant enzyme Y455(o-nitrobenzyl-O-tyrosine)

proof_lines: pH 7.7, 25°C, mutant enzyme K50(o-nitrobenzyl-O-tyrosine)


assay_conditions_summary: pH 8; 303.15 K; buffer 0.1 M potassium phosphate

proof_lines: wild type enzyme, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C

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


proof_lines: mutant enzyme T15A, in 0.1 M potassium phosphate buffer (pH 8.0) at 30°C


proof_lines: wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 7.5; 333.15 K; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.5), 20 mM L-glutamine, and 10 mM MgCl2, at 60°C


assay_conditions_summary: pH 8; 333.15 K; buffer 50 mM Tris

proof_lines: in 50 mM Tris buffer (pH 8.0), 50 mM NH4Cl, and 10 mM MgCl2, at 60°C


smiles: N


organism: Streptomyces venezuelae


substrate_name: L-glutamine

substrate: L-glutamine


organism: Escherichia coli


substrate_name: L-tryptophan

proof_lines: recombinant wild-type enzyme, pH 7.8, 22°C

substrate: L-tryptophan


organism: Thermococcus kodakarensis

proof_lines:
75°C, glutamine-dependent activity
75°C, ammonia-dependent activity


proof_lines: 75°C, ammonia-dependent activity, competitive to chorismate

proof_lines: 75°C, glutamine-dependent activity, competitive to chorismate


organism: Pseudomonas putida

proof_lines: enzyme component ASI, with Gln as cosubstrate


substrate_name: Gln

substrate: Gln


organism: Vibrio cholerae O1

substrate_name: S-Benzyl-L-cysteine

proof_lines: recombinant His-tagged wild-type enzyme, pH 7.8, 37°C

substrate: S-Benzyl-L-cysteine


substrate_name: S-methyl-L-cysteine

substrate: S-methyl-L-cysteine


organism: Citrobacter freundii


substrate_name: S-benzyl-L-Cys

substrate: S-benzyl-L-Cys


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


organism: Claviceps sp.

substrate_name: chorismate

substrate: chorismate


organism: Cupriavidus necator


substrate_name: glutamine

substrate: glutamine


enzyme_display_name: (4S)-4-hydroxy-2-oxoglutarate aldolase

enzyme: (4S)-4-hydroxy-2-oxoglutarate aldolase


proof_lines: pH 8.4, temperature not specified in the publication


substrate_name: S-(o-nitrophenyl)-L-cysteine

substrate: S-(o-nitrophenyl)-L-cysteine


proof_lines: pH 8.3, 32°C, wild-type enzyme, anthranilate synthase alpha-subunit OASA2


proof_lines: pH 8.3, 32°C, Y367A/L530D mutant anthranilate synthase alpha-subunit OASA2


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: pyruvate

substrate: pyruvate


organism: Ruta graveolens

proof_lines:
cell line R-15
cell line R-20


proof_lines:
cell line R-20
cell line R-15


organism: Proteus vulgaris


organism: Aeromonas hydrophila

substrate_name: L-Trp

substrate: L-Trp


organism: Aspergillus nidulans

assay_conditions_summary: pH 7


proof_lines: reaction of component I, with NH4+ as cosubstrate


proof_lines: inhibition with respect to chorismate binding, pH 7.8, 25°C

proof_lines: inhibitor binding to the enzyme-chorismate complex, pH 7.8, 25°C


proof_lines:
25°C, pH 7.8
pH 8.0, 30°C, recombinant enzyme
pH 8.0, 30°C


substrate_name: D-Ala

substrate: D-Ala


assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM phosphate

proof_lines: wild-type, at 25°C, in 100 mM phosphate buffer, pH 7.0, with 20 mM L-glutamine and 5 mM MgCl2


proof_lines: mutant Q147K, at 25°C, in 100 mM phosphate buffer, pH 7.0, with 20 mM L-glutamine and 5 mM MgCl2


organism: Morganella morganii


organism: Mycobacterium tuberculosis


organism: Paenibacillus alvei


substrate_name: S-methyl-L-Cys

substrate: S-methyl-L-Cys


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Paracoccus denitrificans

assay_conditions_summary: pH 8; buffer 0.02 mM HEPES


organism: Providencia rettgeri


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Serratia marcescens

proof_lines: pH and temperature not specified in the publication


substrate_name: oxindolyl-L-alanine

substrate: oxindolyl-L-alanine


proof_lines:
pH 7.0, 25°C
with NH4+ as cosubstrate
with Gln as cosubstrate


organism: Symbiobacterium thermophilum


organism: Zea mays

substrate_name: NH3; Chorismate

substrate: NH3; Chorismate


organism: Salmonella typhimurium


organism: Yarrowia lipolytica


enzyme_display_name: UniProt Q54735

organism: Synechocystis sp. PCC 6803 / Kazusa

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q54735

source: skid


enzyme_display_name: UniProt C0QRB5

organism: Persephonella marina

enzyme: UniProt C0QRB5


enzyme_display_name: UniProt Q16790

organism: Homo sapiens

enzyme: UniProt Q16790


enzyme_display_name: UniProt Q9ULX7

enzyme: UniProt Q9ULX7


enzyme_display_name: UniProt P05042

organism: Escherichia coli

substrate_name: (S)-malate

enzyme: UniProt P05042

substrate: (S)-malate


substrate_name: (S,S)-Tartrate

substrate: (S,S)-Tartrate


enzyme_display_name: aconitate hydratase

organism: Saccharomycopsis lipolytica

substrate_name: cis-aconitate

enzyme: aconitate hydratase

substrate: cis-aconitate


substrate_name: isocitrate

substrate: isocitrate


substrate_name: 2-methyl cis-aconitate

substrate: 2-methyl cis-aconitate


substrate_name: methylisocitrate

substrate: methylisocitrate


enzyme_display_name: carbonic anhydrase

organism: Acipenser gueldenstaedtii

enzyme: carbonic anhydrase


substrate_name: Unknown

proof_lines: pH 7.4, 30°C, inhibition of CO2 hydration activity

proof_lines: pH 9.0, 30°C, inhibition of esterase activity with 4-nitrophenyl acetate

substrate: Unknown


enzyme_display_name: fumarate hydratase

organism: Euglena gracilis

substrate_name: fumarate

enzyme: fumarate hydratase

substrate: fumarate


organism: Methanothermobacter thermautotrophicus

proof_lines: pH 8.5, 25°C, mutant R36A, imidazole buffer


proof_lines: pH 8.5, 25°C, mutant D34A/R36A, MOPS buffer

proof_lines: pH 8.5, 25°C, mutant D34A/R36A, imidazole buffer


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


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


organism: Sinapis alba


substrate_name: citrate

substrate: citrate


organism: Leishmania chagasi


substrate_name: Fumarate; H2O

substrate: Fumarate; H2O


substrate_name: L-Malate

substrate: L-Malate


substrate_name: H2O; Fumarate

substrate: H2O; Fumarate


organism: Brucella suis

assay_conditions_summary: pH 8.3; 293.15 K; buffer and 20 mM NaCl

proof_lines: isozyme bsCAII, pH 8.3, temperature not specified in the publication

proof_lines: isozyme bsCAI, pH 8.3, temperature not specified in the publication

proof_lines: at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl


proof_lines: pH 8.3, temperature not specified in the publication, isozyme bsCA II


organism: Porphyromonas gingivalis

proof_lines: pH 8.3, 22°C, recombinant His-tagged enzyme


organism: Bacillus cereus

substrate_name: Isocitrate

proof_lines:
isoenzyme II
isoenzyme I

substrate: Isocitrate


substrate_name: Citrate

substrate: Citrate


enzyme_display_name: arabinonate dehydratase

organism: Herbaspirillum huttiense

substrate_name: L-fuconate

enzyme: arabinonate dehydratase

substrate: L-fuconate


substrate_name: D-idonate

substrate: D-idonate


substrate_name: L-xylonate

substrate: L-xylonate


organism: Bos taurus

substrate_name: 4-nitrophenyl acetate

proof_lines: pH 7.4, 20°C, outer peripheral isoenzyme

substrate: 4-nitrophenyl acetate


organism: Pelotomaculum thermopropionicum

substrate_name: (S)-malate

substrate: (S)-malate


proof_lines:
at pH 7.0 and 20°C
pH 7.4, 25°C, bCA IV
pH 7.4, 25°C, isozyme bCA IV


organism: Conticribra weissflogii


organism: Corynebacterium flavescens


proof_lines: pH 7.9, temperature not specified in the publication, the activities depended on culture conditions, ranging between 20/sec and 150/sec

proof_lines: measured with hydration of CO2 activity assay, pH 7.5-8.3, 0°C


proof_lines:
0.1 M NaCl
without NaCl
pH 7.5, 20°C


proof_lines: pH and temperature not specified in the publication

proof_lines: isozyme CA VII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4

proof_lines: pH 7.5, catalytic domain of cloned isoenzyme


proof_lines: isoform carbonic anhydrase III, at pH 7.4 and 25°C


organism: Elephas trogontherii

substrate_name: p-nitrophenyl acetate

proof_lines:
integral isoenzyme
inner peripheral isoenzyme
outer peripheral isoenzyme

substrate: p-nitrophenyl acetate


organism: Macropus eugenii desmarest


organism: Acer pseudoplatanus

substrate_name: cis-aconitate

substrate: cis-aconitate


proof_lines: 20°C, pH not specified in the publication


organism: Methanosarcina thermophila

proof_lines: 20°C, pH not specified in the publication, Zn2+-containing enzyme

proof_lines: 20°C, pH not specified in the publication, Co2+-containing enzyme


organism: Sander vitreus


organism: Mus musculus


organism: Solanum tuberosum

proof_lines:
chloroplastic isoenzyme
cytosolic isoenzyme


organism: Stylophora pistillata

assay_conditions_summary: pH 7.5; 293.15 K; buffer 10 mM HEPES

proof_lines: isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication

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


proof_lines:
isoenzyme mCA XIII catalytic domain
pH 7.5, 25°C, mCA XIII
isoenzyme mCA XIII


organism: Sulfurihydrogenibium yellowstonense


organism: Tectona grandis


proof_lines: in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C


organism: Rattus norvegicus

proof_lines:
cytoplasmic isoenzyme
mitochondrial isoenzyme


organism: Helicobacter pylori

proof_lines:
isoenzyme hpalphaCA
isoenzyme hpbetaCA
isoenzyme hpbetaCA, i.e. daranide


substrate_name: isocitrate

proof_lines:
cytoplasmic isoenzyme
mitochondrial enzyme

substrate: isocitrate


organism: Rattus rattus

proof_lines: mitochondrial enzyme, with isocitrate as substrate

proof_lines: cytosolic enzyme, with isocitrate as substrate


organism: Teladorsagia circumcincta

assay_conditions_summary: cofactor NADP+


organism: Escherichia coli

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:
enzyme form FUMC
Raw SKiD Env: Temp=-----, pH=7.9
Raw SKiD Env: Temp=37°C, pH=6.9

source_databases_merged: sabio_rk brenda skid uniprot


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

source_databases_merged: brenda skid uniprot


source_databases_merged: sabio_rk brenda uniprot


organism: Escherichia coli (strain K12)

proof_lines: kcat is 3000 sec(-1) for the hydration of fumarate and 300 sec(-1) for the isomerization of enol-oxaloacetate.


substrate_name: enol-oxaloacetate

substrate: enol-oxaloacetate


organism: Schistosoma mansoni

proof_lines: kcat is 19 sec(-1) for the conversion of L-malate into fumarate (at pH 7.5 and in the presence of 150 mM KCl). kcat is 49 sec(-1) for the conversion of fumarate into L-malate (at pH 7.5 and in the presence of 150 mM KCl).


substrate_name: fumarate (at pH 7.5 and in the presence of 150 mM KCl)


enzyme_display_name: cyclopenase

organism: Aspergillus nidulans

substrate_name: (-)-cyclopenine

assay_conditions_summary: pH 5.5; 303.15 K; buffer –)-cyclopenine in MES Na

proof_lines:
pH 5.5, 30°C
presence of Zn2+, pH 5.5, 30°C

enzyme: cyclopenase

substrate: (-)-cyclopenine


organism: Arabidopsis thaliana


organism: Corynebacterium glutamicum


organism: Homo sapiens


organism: Cryptococcus neoformans

assay_conditions_summary: pH 8.3; buffer and 20 mM NaClO4

proof_lines: Can2, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine


substrate_name: H2O; CO2

substrate: H2O; CO2


organism: Enterobacter sp. B13

substrate_name: Unknown

proof_lines: pH 8.3, 20°C, recombinant His-tagged enzyme

substrate: Unknown


organism: Gyrodactylus salaris


enzyme_display_name: 3'-dehydrocarminate deglycosidase

organism: Microbacterium sp

proof_lines: kcat is 23 min(-1) with 3'-dehydrocarminate as substrate. kcat is 0.12 min(-1) with 3''-dehydropuerarin as substrate. kcat is 0.024 min(-1) with 3''-dehydroisoorientin as substrate. kcat is 0.16 min(-1) with 3'-dehydromangiferin as substrat

enzyme: 3'-dehydrocarminate deglycosidase


organism: Candida albicans

substrate_name: CO2; H2O

substrate: CO2; H2O


organism: Chionodraco hamatus


organism: Coccomyxa sp.


organism: Halothiobacillus neapolitanus

assay_conditions_summary: pH 8

proof_lines: kcat is 8.9 x 10(4) sec(-1) for CO(2) hydration at pH 8.0, and 4.6 x 10(4) sec(-1) for hydrogencarbonate dehydration at pH 7.0.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F198L/C183S/C188S with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y7F to reconstruct the assayed variant sequence.


organism: Lathyrus oleraceus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H208A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines:
pH 6.2, 25°C, mutant H208A
pH 7.3, 25°C, mutant H208A
pH 8.8, 25°C, mutant H208A


organism: Malassezia globosa


organism: Malassezia pachydermatis

proof_lines: at pH 8.3, temperature not specified in the publication


organism: Malassezia restricta


organism: Methanosarcina thermophila

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.5


organism: Rattus norvegicus

substrate_name: H2O; Fumarate


organism: Escherichia coli

substrate_name: H2O; cis-Aconitate

column_label: Table 1; row cis-Aconitate; method EH; AcnB columns Km and Vmax.

raw_value_unit_evidence: Table 1 cis-Aconitate AcnB EH cell: Km 0.018 mM; Vmax 40.9 units mg^-1.

row_label: cis-Aconitate / AcnB / EH

table_label: Table 1

substrate: H2O; cis-Aconitate


organism: Helicobacter pylori


organism: Sulfolobus acidocaldarius


organism: Micropterus salmoides


organism: Mus musculus


organism: Nakaseomyces glabratus

substrate_name: histamine

proof_lines: at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine

substrate: histamine


organism: Neisseria gonorrhoeae


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.


organism: Microbacterium sp


organism: Persephonella marina

smiles: O=C=O


organism: Plasmodium falciparum

mutation_signature: truncated form PfCA1 / truncated form PfCA1

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation

proof_lines: pH 7.5, 22°C, truncated form PfCA1, CO2 hydration reaction


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

proof_lines: pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA26

proof_lines: pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA37

proof_lines: pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA38


mutation_signature: truncated form PfCA1


proof_lines: pH 7.5, 22°C, long enzyme form PfCAdom, CO2 hydration reaction


mutation_signature: truncated mutant PfCA1


organism: Spinacia oleracea


organism: Arabidopsis thaliana

substrate_name: fumarate (at pH 8.0)

column_label: PMID 29688630 Table 1, row AtFUM1, FH activity columns pH and Km (mM): pH 8.0 and Km 0.7 +/- 0.1 mM. FH activity uses fumarate as substrate.

raw_value_unit_evidence: Table 1, AtFUM1, FH activity: pH 8.0; Km 0.7 +/- 0.1 mM.

row_label: AtFUM1; FH activity; pH 8.0

table_label: Table 1. Kinetic parameters of AtFUM1 and AtFUM2

substrate: fumarate (at pH 8.0)


substrate_name: (S)-malate (at pH 8.0)

column_label: PMID 29688630 Table 1, row AtFUM1, MD activity columns pH and Km (mM): pH 8.0 and Km 1.8 +/- 0.2 mM. MD activity uses L-malate as substrate.

raw_value_unit_evidence: Table 1, AtFUM1, MD activity: pH 8.0; Km 1.8 +/- 0.2 mM.

row_label: AtFUM1; MD activity; pH 8.0

substrate: (S)-malate (at pH 8.0)


substrate_name: fumarate (at pH 7.7)

column_label: PMID 29688630 Table 1, row AtFUM2, FH activity columns pH and Km (mM): pH 7.7 and Km 0.4 +/- 0.1 mM. FH activity uses fumarate as substrate.

raw_value_unit_evidence: Table 1, AtFUM2, FH activity: pH 7.7; Km 0.4 +/- 0.1 mM.

row_label: AtFUM2; FH activity; pH 7.7

substrate: fumarate (at pH 7.7)


substrate_name: (S)-malate (at pH 7.7)

column_label: PMID 29688630 Table 1, row AtFUM2, MD activity columns pH and Km (mM): pH 7.7 and Km 0.6 +/- 0.1 mM. MD activity uses L-malate as substrate.

raw_value_unit_evidence: Table 1, AtFUM2, MD activity: pH 7.7; Km 0.6 +/- 0.1 mM.

row_label: AtFUM2; MD activity; pH 7.7

substrate: (S)-malate (at pH 7.7)


substrate_name: Dihydrogen carbonate

substrate: Dihydrogen carbonate


smiles: O=C(O)O


organism: Sulfurihydrogenibium azorense

proof_lines: pH 7.5, 20°C, recombinant His-tagged enzyme


organism: Sulfurihydrogenibium sp. YO3AOP1


organism: Trematomus bernacchii


proof_lines: kcat is 3000 sec(-1) for the hydration of fumarate and 300 sec(-1) for the isomerization of enol-oxaloacetate.

substrate: H2O; Fumarate


proof_lines: kcat is 1149 sec(-1) for fumarate (at pH 7.9). kcat is 595.2 sec(-1) for S-malate (at pH 7.9).


organism: Leishmania major

proof_lines: kcat is 204.2 sec(-1) for fumarate (in anaerobic conditions) (PubMed:22569531). kcat is 48.6 sec(-1) for fumarate (in aerobic conditions) (PubMed:22569531). kcat is 151.4 sec(-1) for (S)-malate (in anaerobic conditions) (PubMed:22569531). k


proof_lines: kcat is 28.3 sec(-1) for fumarate (in anaerobic conditions) (PubMed:22569531). kcat is 1.9 sec(-1) for fumarate (in aerobic conditions) (PubMed:22569531). kcat is 12.9 sec(-1) for (S)-malate (in anaerobic conditions) (PubMed:22569531). kcat


organism: Synechocystis sp. 6803

substrate_name: (S)-malate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A314E with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

substrate: (S)-malate


substrate_name: fumarate

substrate: fumarate


organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

substrate_name: cis-aconitate (at pH 8)

assay_conditions_summary: pH 8; buffer 100 mM Tris-HCl

column_label: ScienceDirect Table 4 row cis-Aconitate, column Km (uM); caption states assays in 100 mM Tris-HCl buffer pH 8.0.

row_label: cis-Aconitate

table_label: Table 4: Kinetic parameters of aconitase from C. glutamicum

substrate: cis-aconitate (at pH 8)


substrate_name: citrate (at pH 8)

column_label: ScienceDirect Table 4 row Citrate, column Km (uM); caption states assays in 100 mM Tris-HCl buffer pH 8.0.

row_label: Citrate

substrate: citrate (at pH 8)


substrate_name: isocitrate (at pH 8)

column_label: ScienceDirect Table 4 row Isocitrate, column Km (uM); caption states assays in 100 mM Tris-HCl buffer pH 8.0.

row_label: Isocitrate

substrate: isocitrate (at pH 8)


organism: Dioscorea japonica

substrate_name: dehydroascorbate (DHA) (at ph 7.0 and 30 degrees Celsius)

proof_lines: kcat is 0.0152 min(-1) for DHA. kcat is 30500 min(-1) for sodium bicarbonate.


substrate_name: sodium bicarbonate (at ph 7.1 and 4 degrees Celsius)


organism: Halothiobacillus neapolitanus (strain ATCC 23641 / DSM 15147 / CIP 104769 / NCIMB 8539 / c2)

smiles: [Co]


organism: Rattus norvegicus


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V62N with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.

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

proof_lines: pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62N

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


substrate_name: L-Malate

proof_lines: kcat is 280 sec(-1) with L-malate (at pH 8.5) (PubMed:30761759). kcat is 170 sec(-1) with fumarate (at pH 8.5) (PubMed:30761759).

source_databases_merged: sabio_rk skid uniprot

substrate: L-Malate


substrate_name: fumarate (at pH 8.5)

substrate: fumarate (at pH 8.5)


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

substrate_name: CO(2) at pH 7.5, 25 degrees Celsius, for N-terminal 209 residue fragment


organism: Escherichia coli

substrate_name: L-malate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E315Q to reconstruct the assayed variant sequence.

substrate: L-malate


organism: Escherichia coli (strain K12)

substrate_name: D-tartrate

substrate: D-tartrate


substrate_name: Unknown

proof_lines: with (S)-malate as substrate, pH and temperature not specified in the publication

proof_lines: with fumarate as substrate, pH and temperature not specified in the publication

substrate: Unknown


organism: Saccharomyces cerevisiae

substrate_name: Fumarate; H2O

substrate: Fumarate; H2O


organism: Sus scrofa


proof_lines: kcat is 19.6 sec(-1) for aconitase activity with citrate as substrate (at pH 8). kcat is 28.9 sec(-1) for aconitase activity with isocitrate as substrate (at pH 8). kcat is 71 sec(-1) for aconitase activity with cis-aconitate as substrate (


organism: Mycobacterium smegmatis

substrate_name: H2O; cis-Aconitate

substrate: H2O; cis-Aconitate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Rhizopus arrhizus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D162K with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D162M with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D162W with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H159S with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H159V with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H159Y with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N161E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N161F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N161R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P160A to reconstruct the assayed variant sequence.


proof_lines: human carbonic anhydrase structural context


proof_lines: CA II catalytic activity is supported qualitatively


proof_lines: human carbonic anhydrase XIII structural context


substrate_name: Citrate

substrate: Citrate


substrate_name: D-Isocitrate

substrate: D-Isocitrate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P160H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P160T to reconstruct the assayed variant sequence.


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: fumarate (in anaerobic conditions)

substrate: fumarate (in anaerobic conditions)


substrate_name: (S)-malate (in anaerobic conditions)

substrate: (S)-malate (in anaerobic conditions)


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


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


organism: Corynebacterium glutamicum


substrate_name: Fumarate

substrate: Fumarate


organism: Plasmodium falciparum

substrate_name: mesaconate

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

column_label: Table 2 columns are Organism/enzyme name, Substrate, Km, kcat, kcat/Km, and Refs.; caption states units are mM, s^-1, and s^-1 M^-1; PfFHDelta40 mesaconate row cells are 3.2 +/- 0.3, 60 +/- 2, and 1.9 x 10^4.

normalized_value_unit_evidence: Km 3.2 mM; kcat 60 s^-1; printed kcat/Km 1.9 x 10^4 s^-1 M^-1 = 19.0 s^-1 mM^-1. Export expected kcat/Km 18.75 is within table precision/rounding.

raw_value_unit_evidence: Table 2 PfFHDelta40 mesaconate: Km 3.2 +/- 0.3 mM, kcat 60 +/- 2 s^-1, kcat/Km 1.9 x 10^4 s^-1 M^-1.

row_label: PfFHDelta40 / Mesaconate

table_label: Table 2, Kinetic parameters of PfFHDelta40 and other class I FH

substrate: mesaconate


substrate_name: (S)-malate

column_label: Table 2 columns are Organism/enzyme name, Substrate, Km, kcat, kcat/Km, and Refs.; caption states units are mM, s^-1, and s^-1 M^-1; PfFHDelta40 malate row cells are 1.2 +/- 0.1, 159 +/- 9, and 1.3 x 10^5.

normalized_value_unit_evidence: Km 1.2 mM; kcat 159 s^-1; printed kcat/Km 1.3 x 10^5 s^-1 M^-1 = 130.0 s^-1 mM^-1. Export expected kcat/Km 132.5 is within table precision/rounding.

row_label: PfFHDelta40 / Malate

substrate: (S)-malate


substrate_name: fumarate

column_label: Table 2 columns are Organism/enzyme name, Substrate, Km, kcat, kcat/Km, and Refs.; caption states units are mM, s^-1, and s^-1 M^-1; PfFHDelta40 fumarate row cells are 2.6 +/- 0.3, 182 +/- 8, and 7.0 x 10^4.

normalized_value_unit_evidence: Km 2.6 mM; kcat 182 s^-1; printed kcat/Km 7.0 x 10^4 s^-1 M^-1 = 70.0 s^-1 mM^-1. Export expected kcat/Km 70.0 matches the converted primary table metric.

raw_value_unit_evidence: Table 2 PfFHDelta40 fumarate: Km 2.6 +/- 0.3 mM, kcat 182 +/- 8 s^-1, kcat/Km 7.0 x 10^4 s^-1 M^-1.

row_label: PfFHDelta40 / Fumarate

substrate: fumarate


substrate_name: Isocitrate

substrate: Isocitrate


source_databases_merged: skid uniprot


organism: Arabidopsis thaliana

substrate_name: L-Malate

substrate: L-Malate


organism: Sulfolobus acidocaldarius

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

column_label: Prose reports that using the coupled assay system, apparent Km values decreased and citrate was 358 +/- 36 uM.

raw_value_unit_evidence: apparent Km citrate = 358 +/- 36 uM in coupled assay

row_label: S. acidocaldarius; citrate under coupled assay

table_label: Results prose after Table 2; coupled assay system with enriched endogenous ICDH


column_label: Table 2 row S. acidocaldarius, column Km isocitrate (uM): 370 +/- 45.

raw_value_unit_evidence: Km isocitrate = 370 +/- 45 uM

row_label: S. acidocaldarius; isocitrate

table_label: Table 2. Comparison of Km values of aconitase from S. acidocaldarius; direct assay


substrate_name: cis-aconitate

column_label: Table 2 row S. acidocaldarius, column Km cis-aconitate (uM): 108 +/- 13.

raw_value_unit_evidence: Km cis-aconitate = 108 +/- 13 uM

row_label: S. acidocaldarius; cis-aconitate

substrate: cis-aconitate


organism: Cyanidioschyzon merolae

column_label: Table 1 row CmFUM/Fumarate; columns Km, kcat, kcat/Km

row_label: CmFUM / Fumarate

table_label: Table 1. Kinetic parameters of CmFUM and TeFum


column_label: Table 1 row CmFUM/L-malate; columns Km, kcat, kcat/Km

row_label: CmFUM / L-malate


organism: Helianthus annuus

substrate_name: L-malate

proof_lines: isoform Fum2, pH 7.5, temperature not specified in the publication

substrate: L-malate


proof_lines: isoform Fum1, pH 7.5, temperature not specified in the publication


organism: Thermosynechococcus vestitus

column_label: Table 1 row TeFum/L-malate; columns Km, kcat, kcat/Km

normalized_value_unit_evidence: Km 0.20 mM; kcat 15 s^-1; kcat/Km 75.0 s^-1 mM^-1 from 15/0.20; table reports 76

row_label: TeFum / L-malate


column_label: Table 1 row TeFum/Fumarate; columns Km, kcat, kcat/Km

row_label: TeFum / Fumarate


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


organism: Aspergillus nidulans


organism: Synechocystis sp. PCC 6803

substrate_name: citrate

proof_lines:
at pH 9.0 and 45°C
at pH 9.0 and 30°C
at pH 8.0 and 45°C

substrate: citrate


substrate_name: isocitrate

proof_lines:
at pH 9.0 and 53°C
at pH 7.0 and 53°C
at pH 7.0 and 45°C

substrate: isocitrate


organism: Homo sapiens


organism: Malassezia restricta


organism: Petroselinum crispum

proof_lines: 25°C, pH 7.07, high activity carbonic anhydrase


organism: Methanosarcina thermophila

proof_lines:
CamH homolog from M. thermophila
interconversion of CO2 and HCO3(-)


organism: Escherichia coli


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

substrate_name: (-)-Cyclopeptin

column_label: The paper maps compound 5 to (-)-Cyclopeptin and reports AsqI with 5 Km 0.068 +/- 0.0089 mM.

raw_value_unit_evidence: Km raw_value=0.068 +/- 0.0089 raw_unit=mM

row_label: AsqI with compound 5 / (-)-Cyclopeptin

table_label: Main-text steady-state kinetic analysis paragraph; Supplementary Fig. 6a

substrate: (-)-Cyclopeptin


organism: Helicobacter pylori

column_label: Table 1 row Fumarase lists substrates Fumarate/Malate with Km 121/7.3 mM and Vmax 4100/10800 nmol min-1 mg-1; surrounding fumarase paragraph gives malate Vmax as 10.8 umol min-1 mg-1.

raw_value_unit_evidence: Fumarase malate Km = 7.3 +/- 0.4 mM and Vmax = 10.8 +/- 0.2 umol min-1 mg-1 in prose/Table 1.

row_label: Fumarase / Malate

table_label: European Journal of Biochemistry Table 1, TCA cycle enzyme activities of H. pylori


organism: Escherichia coli (strain K12)

substrate_name: D-tartrate

proof_lines:
FumB
D-tartrate to oxaloacetate

substrate: D-tartrate


organism: Pisum sativum


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: Mycobacterium tuberculosis fumarate hydratase


organism: Sus scrofa


organism: Rattus norvegicus


column_label: Results prose adjacent to Table 3; PrpD substrate (2S,3S)-methylcitrate; metric Km

normalized_value_unit_evidence: normalized: Km=0.44 mM

raw_value_unit_evidence: paper text: Km=440 uM for enzymatically produced (2S,3S)-methylcitrate; Table 3 row (2S,3S)-Methylcitrate shows 1.0 mM substrate and 11.4 U mg^-1 activity

row_label: PrpD / (2S,3S)-methylcitrate

table_label: Table 3 plus Results prose


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

substrate_name: malate (at pH 7.5 and at 70 degrees Celsius)

proof_lines:
fumarate hydratase
Saccharolobus solfataricus
malate


column_label: PMID 17384188 kinetic paragraph, Acn monomer row/segment, Km (isocitrate) = 0.56 +/- 0.1 mM.

raw_value_unit_evidence: Km (isocitrate) for the monomer was 0.56 +/- 0.1 mM.

row_label: Acn monomer / isocitrate

table_label: Kinetic paragraph comparing monomer and trimer M. tuberculosis Acn


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

proof_lines: pH 7.5, 25°C, variant E84C, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84A and E84K, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84S and E84Y, 50 mM MOPS buffer


organism: Trypanosoma brucei brucei


organism: Saccharolobus solfataricus

substrate_name: D-Arabinonate

column_label: PMID 16849334 JBC Table 1, AraD column, substrate specificity/turnover number row: D-Arabinonate (1.8).

raw_value_unit_evidence: Table 1 AraD column lists Substrate specificity, turnover number (s^-1): D-Arabinonate (1.8).

row_label: AraD / D-arabinonate dehydratase / D-Arabinonate

table_label: Table 1. Properties of the D-Ara degrading enzymes of S. solfataricus

substrate: D-Arabinonate


organism: Leishmania major

proof_lines: isoform FH-2 mutant R173A, at pH 8.5 and 23°C


proof_lines: isoform FH-2 mutant R471A, at pH 8.5 and 23°C


proof_lines: isoform FH-2 mutant T467A, at pH 8.5 and 23°C


proof_lines: isoform FH-2 mutant D135A, at pH 8.5 and 23°C


proof_lines: isoform FH-2 mutant R421A, at pH 8.5 and 23°C


proof_lines: isoform FH-2 mutant H334A, at pH 8.5 and 23°C


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

proof_lines: wild type isoform FH-1, at pH 8.5 and 23°C

proof_lines: wild type isoform FH-2, at pH 8.5 and 23°C


organism: Rhizopus arrhizus


proof_lines: pH 7.5, 25°C, variant E62Y, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62A/E84A, 50 mM MOPS buffer


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

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

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


proof_lines: pH 7.5, 25°C, variant E62Q, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84Y, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84C and E62A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS-Ac buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM IMID buffer


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


proof_lines: pH 7.5, 25°C, variant E62C, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62H, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84S, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84Q, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84K, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62D/E84D, 50 mM MOPS buffer


proof_lines:
pH 5.7-9.5, 25°C, wild-type
pH 6.5, 25°C, wild-type, D2O
pH 7.5, 25°C, wild-type, D2O


proof_lines: pH 7.5, 25°C, variant E84H, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62D, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84D, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E88A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E89A, 50 mM MOPS buffer


organism: Homo sapiens

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

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

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


proof_lines: pH 8.88, TAPS buffer, carbonic anhydrase I mutant H200T

proof_lines: pH 7.21, 1-methylimidazole buffer, carbonic anhydrase I mutant H200T

proof_lines: pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H200T


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

proof_lines: pH 7.23, 1-methylimidazole buffer, carbonic anhydrase I mutant H67N

proof_lines: pH 8.75, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H67N


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

proof_lines: pH 8.88, TAPS buffer, carbonic anhydrase I mutant V62N,H67N

proof_lines: pH 8.72, 1,2-dimethyimidazole buffer, carbonic anhydrase I mutant V62N,H67N


proof_lines: pH 8.72, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62B, H67B

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant H67B

proof_lines: pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N67HV


proof_lines: pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant T200H


proof_lines: pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N62V


proof_lines: pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N67H


proof_lines: pH 7.5, 37°C, variant R59A, 100 mM imidazole


proof_lines: pH 7.5, 37°C, variant R59Q, without guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59Q, 100 mM guanidine hydrochloride


proof_lines: pH 7.5, 37°C, variant R59A, 100 mM 1.3-diaminoguanidine, variant R59H plus 100 mM guanidine hydrochloride


proof_lines: pH 7.5, 37°C, variant R59M, without guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59M, 100 mM guanidine hydrochloride


proof_lines: pH 7.5, 37°C, variant R59H, without guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59H, 100 mM guanidine hydrochloride


proof_lines: pH 7.5, 37°C, variant R59E, without guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59E, 100 mM guanidine hydrochloride


proof_lines: pH 7.5, 37°C, variant R59C, 100 mM ethylguanidine

proof_lines: pH 7.5, 37°C, variant R59C, 100 mM aminoguanidine


proof_lines: pH 7.5, 37°C, variant R59K, 100 mM guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59K, without guanidine hydrochloride


proof_lines: pH 7.5, 37°C, variant R59C, 100 mM methylguanidine, variant R59Q, 100 mM guanidine hydrochloride


substrate_name: L-threo-chloromalate

substrate: L-threo-chloromalate


substrate_name: fluorofumarate

substrate: fluorofumarate


substrate_name: chlorofumarate

substrate: chlorofumarate


substrate_name: L-Tartrate

substrate: L-Tartrate


proof_lines:
25°C, pH 7.5, mutant enzyme W19N
25°C, pH 8.8, mutant enzyme W19N


proof_lines:
25°C, pH 7.5, mutant enzyme W19F
25°C, pH 8.8, mutant enzyme W19F


proof_lines:
25°C, pH 7.5, mutant enzyme W19A
25°C, pH 8.8, mutant enzyme W19A


proof_lines:
25°C, pH 7.5, mutant enzyme Y200S
25°C, pH 8.8, mutant enzyme Y200S


proof_lines:
25°C, pH 7.5, mutant enzyme Y200A
25°C, pH 8.8, mutant enzyme Y200A


proof_lines:
25°C, pH 7.5, mutant enzyme Y200F
25°C, pH 8.8, mutant enzyme Y200F


organism: Mus musculus


substrate_name: Unknown

substrate: Unknown


organism: Escherichia coli O157:H7

substrate_name: mesaconate

substrate: mesaconate


substrate_name: (S)-malate

substrate: (S)-malate


substrate_name: fumarate

substrate: fumarate


substrate_name: (S)-citramalate

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

substrate: (S)-citramalate


organism: Escherichia coli K-12


organism: Paraburkholderia xenovorans


proof_lines: pH 6.3, MES buffer, wild-type carbonic anhydrase I


organism: Bos taurus

substrate_name: cis-aconitate

proof_lines:
liver enzyme
heart enzyme


substrate_name: methylisocitrate

substrate: methylisocitrate


substrate_name: citrate


organism: Microbacterium sp. 5-2b


organism: Bacillus subtilis

substrate_name: 4-nitrophenyl acetate

assay_conditions_summary: pH 8.3; 310.15 K; buffer 0.1 M Tris-HCl

proof_lines: in 0.1 M Tris-HCl buffer, pH 8.3, and 37°C

substrate: 4-nitrophenyl acetate


organism: Bacteria


substrate_name: L-malate

substrate: L-malate


organism: Colwellia psychrerythraea


proof_lines: pH 8.3, 22°C, inhibition of CO2 hydration activity


organism: Escherichia coli

proof_lines:
fumarase A
pH 6.9, 37°C
enzyme form FUMA


proof_lines:
fumarase A
pH 7.9, native enzyme
pH 6.9, 37°C


substrate_name: acetylene dicarboxylate

substrate: acetylene dicarboxylate


organism: Corynebacterium glutamicum

substrate: cis-aconitate


substrate: citrate


substrate_name: isocitrate

substrate: isocitrate


organism: Drosophila melanogaster


proof_lines:
pH 8.3, 20°C
above, pH 8.3, 20°C


organism: Entamoeba histolytica


assay_conditions_summary: pH 6

proof_lines:
MES-NaOH buffer, pH 6.0
phosphate buffer, pH 6.0
MES-NaOH buffer, pH 7.0


proof_lines:
MES-NaOH buffer, pH 6.0
MES-NaOH buffer, pH 7.0
phosphate buffer, pH 6.0


organism: Nostoc commune


proof_lines: pH 7.5, 20°C, inhibition of CO2 hydration activity


organism: Oryctolagus cuniculus


organism: Pseudoalteromonas haloplanktis ANT/505


proof_lines: pH 8.3, 20°C, inhibition of CO2 hydration activity


organism: Anguilla anguilla


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Arabidopsis thaliana

proof_lines: presence of 3 mM oxalacetate, pH 8.0, 30°C

proof_lines: presence of 3 mM oxaloacetate, pH 8.0, 30°C


organism: Candida albicans

assay_conditions_summary: pH 8.3; 293.15 K; buffer and 20 mM NaClO4

proof_lines: at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4

proof_lines: CaNce103, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine


organism: Ascaris suum

proof_lines:
pH 7.3, 30°C, recombinant enzyme
pH 7.3, 30°C, worm enzyme


organism: Pyrococcus furiosus


substrate_name: D-Tartrate

substrate: D-Tartrate


organism: Homo sapiens


organism: Astrosclera willeyana


organism: Campylobacter jejuni


organism: Bos taurus


substrate_name: COS

substrate: COS


organism: Danio rerio

proof_lines: carbonate dehydratase activity, recombinant enzyme, pH and temperature not specified in the publication


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


organism: Columba livia


organism: Cryptococcus neoformans

assay_conditions_summary: pH 8.3; 293.15 K; buffer 20 mM Tris


organism: Escherichia coli


organism: Flaveria bidentis


proof_lines:
at pH 6.5 and 25°C
at pH 7.0 and 25°C
at pH 7.5 and 25°C


proof_lines:
at pH 9.0 and 25°C
at pH 6.0 and 25°C
at pH 8.5 and 25°C


organism: Lacticaseibacillus rhamnosus


organism: Halomonas sp.

proof_lines: pH 7.5, 20°C, inhibition of CO2 hydration reaction


organism: Leishmania major

substrate_name: S-malate

proof_lines: pH 8.7, temperature not specified in the publication, aerobic condition

proof_lines: pH 8.7, temperature not specified in the publication, anaerobic condition

proof_lines: pH 9, temperature not specified in the publication, aerobic condition

substrate: S-malate


organism: Oryza sativa


organism: Mesorhizobium loti

assay_conditions_summary: pH 6.3; 277.15 K; buffer a MES/KOH pH 6.3

proof_lines: recombinant enzyme, at 4°C in a MES/KOH pH 6.3 buffer


proof_lines: recombinant enzyme, at 4°C in a HEPES/NaOH, pH 7.5


organism: Ovis aries


proof_lines:
pH 8.5, 35°C
pH 7.4, 25°C, purified enzyme


organism: Python bivittatus

proof_lines: pH not specified in the publication, 4°C, assay using the delta pH method


organism: Rhizopus arrhizus


organism: Mus musculus


mutation_signature: truncated form of carbonic anhydrase VII lacking the amino-terminal 23 residues of recombinant enzyme truncated form of carbonic anhydrase VII lacking the amino


organism: Salmo trutta Labrax Coruhensis


organism: Saccharomyces cerevisiae

proof_lines: at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-

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


organism: Saccharolobus solfataricus


organism: Mytilus galloprovincialis

proof_lines: CO2 hydration, pH 8.3, 22°C, native enzyme

proof_lines: CO2 hydration, pH 8.3, 22°C, recombinant enzyme


organism: Sordaria macrospora


proof_lines:
20°C, pH 8.3
value above, 20°C, pH 8.3


organism: Schistosoma mansoni


organism: Trichomonas vaginalis

proof_lines:
at pH 7.5 and 20°C
at pH 7.5 and 25°C


proof_lines:
at pH 7.5 and 20°C
at pH 7.5 and 25°C
Ki above 0.01 mM, at pH 7.5 and 20°C


organism: Vibrio cholerae serotype O1


organism: Struthio camelus


organism: Trypanosoma cruzi


organism: Arabidopsis thaliana


enzyme_display_name: porphobilinogen synthase

organism: Ictalurus punctatus

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

enzyme: porphobilinogen synthase


organism: Zea mays

substrate_name: DL-isocitrate

proof_lines: substrate isocitrate, isoform Aco1, pH 8.0, 25°C

substrate: DL-isocitrate


proof_lines:
isoform Aco1, at pH 8.0 and 25°C
isoform Aco4, pH 8.0, 25°C
isoform Aco2, at pH 8.0 and 25°C


organism: Bos taurus

substrate_name: cis-Aconitate; H2O

substrate: cis-Aconitate; H2O


organism: Caenorhabditis elegans

proof_lines: purified recombinant CAH-4a, pH 7.5, 4°C


organism: Synechocystis sp. PCC 6803 / Kazusa

proof_lines: recombinant full-length CcaA274 enzyme, pH 7.5, 25°C, CO2 hydration reaction

proof_lines: recombinant full-length CcaA274 enzyme, pH 9.5, 25°C, CO2 hydration reaction


mutation_signature: recombinant truncated CcaA220 enzyme / CO2 hydration reaction recombinant truncated CcaA220 enzyme

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

proof_lines: recombinant truncated CcaA220 enzyme, pH 9.5, 25°C, CO2 hydration reaction


organism: Clostridium perfringens

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


proof_lines: 0.5°C, pH 7.1, high activity carbonic anhydrase

proof_lines: 25°C, pH 7.0, high activity carbonic anhydrase

proof_lines: 25°C, pH 7.2, low activity carbonic anhydrase


organism: Cavia porcellus

proof_lines: 0°C, pH 7.2, high activity carbonic anhydrase

proof_lines: 0°C, pH 7.2, low activity carbonic anhydrase


organism: Dunaliella salina

proof_lines:
without NaCl
0.5 M NaCl
pH 6.8, in absence of NaCl


organism: Cyprinus carpio


organism: Escherichia coli


proof_lines: pH 8, 37°C, Vmax: 2.3 micromol/minute/mg/

proof_lines: pH 8, 37°C, Vmax: 9.2 micromol/minute/mg/


organism: Felis catus

proof_lines:
pH 6-8
above pH 8


enzyme_display_name: tryptophan synthase

substrate_name: (3-Indolyl)-glycerol phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M101I to reconstruct the assayed variant sequence.

enzyme: tryptophan synthase

substrate: (3-Indolyl)-glycerol phosphate


substrate_name: Indole

sequence_variant_note: Mutation signature P98S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Indole


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P21S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M101T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A67V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q65R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N104S to reconstruct the assayed variant sequence.


organism: Helicobacter pylori


organism: Homo sapiens


substrate_name: 4-nitrophenyl phosphate

proof_lines: isoform carbonic anhydrase I, at pH 7.4 and 25°C

proof_lines: isoform carbonic anhydrase II, at pH 7.4 and 25°C

substrate: 4-nitrophenyl phosphate


proof_lines: pH 7.6, temperature not specified in the publication, mutant A23C/L203C/C206S


organism: Glycine max


proof_lines:
carbonic anhydrase IV
carbonic anhydrase II


proof_lines: isoform CA II mutant A65T/N67Q/F130Y/V134Q/L203T, at pH 7.5 and 23°C


organism: Lathyrus oleraceus

proof_lines: pH 6.2, 25°C, wild-type, term extrapolated from the highest substrate concentrations, due to curved Eadie?Hofstee plots


substrate_name: Unknown

proof_lines: Ki less than 0.000001 mM wild type carbonic anhydrase II

substrate: Unknown


organism: Mycobacterium tuberculosis


organism: Methanosarcina thermophila

proof_lines: pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and aerobically purified

proof_lines: pH 7.5, 25°C, recombinant enzyme expressed from Methanosarcina acetivorans and anaerobically purified

proof_lines: pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and anaerobically purified


proof_lines: at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl

proof_lines: at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl


organism: Mus musculus

proof_lines: isoform carbonic anhydrase XIII, at pH 7.4 and 25°C


proof_lines: pH 7.5, 25°C, enzyme cultured with supplemental zinc


organism: Oncorhynchus mykiss


assay_conditions_summary: pH 9; 298.15 K; buffer 0.05 M Tris-SO4

proof_lines: in 0.05 M Tris-SO4 buffer, at pH 9.0 and 25°C


proof_lines: isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl


organism: Nostoc sp.


organism: Oryctolagus cuniculus

proof_lines: enzyme from red muscle sarcoplasmic reticulum

proof_lines: enzyme from red muscle sarcolemmal membranes

proof_lines: enzyme from white muscle sarcoplasmic reticulum


organism: Persephonella marina


organism: Populus tremula

assay_conditions_summary: pH 6.6; buffer pH 6

proof_lines:
pH 6.6, MES buffer
pH 8.8, TAPS buffer


organism: Rattus norvegicus


proof_lines: 25°C, pH 7.0, low activity carbonic anhydrase

proof_lines: 0°C, pH 7.0, high activity carbonic anhydrase


organism: Rhodospirillum rubrum


organism: Saccharomyces cerevisiae

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

proof_lines: at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-


organism: Streptomyces lividans


organism: Sus scrofa

proof_lines: reversible inhibition after brief exposure


organism: Thalassiosira pseudonana

proof_lines: pH 7.9, temperature not specified in the publication, the activities depended on culture conditions, ranging between 80/sec and 200/sec


organism: Stylophora pistillata

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

proof_lines: in the absence of L-Trp and D-Trp, at 25°C and pH 7.5

proof_lines: in the presence of 0.01 mM D-Trp, at 25°C and pH 7.5


organism: Thermovibrio ammonificans


organism: Trypanosoma brucei


organism: Thermus thermophilus

substrate_name: (S)-malate

assay_conditions_summary: pH 6.5; buffer pH 6

proof_lines:
pH 6.5, 50 mM MOPS-NaOH buffer
pH 7.0, 50 mM MOPS-NaOH buffer
pH 7.5, 50 mM MOPS-NaOH buffer

substrate: (S)-malate


organism: Escherichia coli

substrate_name: L-Malate

proof_lines: pH 8, 37°C, Vmax: 490 micromol/minute/mg/

substrate: L-Malate


organism: Zea mays

proof_lines: pH 6.5 cytosolic form, Vmax: 4.5 micromol/min/mg, temperature not specified in the publication

proof_lines: pH 7 mitochondrial, Vmax: 0.3 micromol/min/mg, temperature not specified in the publication


organism: Arabidopsis thaliana

substrate_name: CO2; H2O

substrate: CO2; H2O


organism: Mycobacterium tuberculosis


organism: Penicillium chrysogenum


organism: Trypanosoma brucei brucei

substrate_name: Citrate

proof_lines: cytoplasm and mitochondrion localization

substrate: Citrate


organism: Mycobacterium smegmatis


organism: Mycobacterium bovis

substrate_name: H2O; cis-Aconitate

substrate: H2O; cis-Aconitate


organism: Plasmodium falciparum

substrate_name: cis-aconitate

substrate: cis-aconitate


proof_lines:
isoform Aco1, pH 8.0, 25°C
isoform Aco4, pH 8.0, 25°C


enzyme_display_name: phenylserine aldolase

organism: Caulobacter vibrioides

substrate_name: L-threo-phenylserine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D176E with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

enzyme: phenylserine aldolase

substrate: L-threo-phenylserine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D95C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D95G/E96G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D95L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D95M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D95N/E96S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D95W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D95Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D95Y/E96T to reconstruct the assayed variant sequence.


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


enzyme_display_name: 3-deoxy-D-manno-octulosonate aldolase

organism: Microbacterium barkeri

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

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

enzyme: 3-deoxy-D-manno-octulosonate aldolase


organism: Enterobacter cloacae


organism: Pseudomonas putida

proof_lines:
pH 8.5, 30°C, cyclized enzyme
pH 8.5, 30°C, linear enzyme
pH 8.5, 30°C


enzyme_display_name: dimethylaniline-N-oxide aldolase

organism: Sus scrofa

substrate_name: N,N-dimethylnaphthylamine N-oxide

proof_lines: in presence of N,N-dimethylcyclohexylamine

enzyme: dimethylaniline-N-oxide aldolase

substrate: N,N-dimethylnaphthylamine N-oxide


substrate_name: N,N-Dimethylaniline N-oxide

substrate: N,N-Dimethylaniline N-oxide


substrate_name: L-Thr

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

substrate: L-Thr


substrate_name: L-allo-Thr

substrate: L-allo-Thr


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


substrate_name: N-acetyl-D-mannosamine

substrate: N-acetyl-D-mannosamine


substrate_name: L-arabinose

substrate: L-arabinose


enzyme_display_name: D-galactonate dehydratase

organism: Escherichia coli (strain K12)

substrate_name: D-galactonate

enzyme: D-galactonate dehydratase

substrate: D-galactonate


enzyme_display_name: mannonate dehydratase

organism: Thermoplasma acidophilum

enzyme: mannonate dehydratase


substrate_name: D-mannonate

substrate: D-mannonate


enzyme_display_name: UniProt A4VVI4

organism: Streptococcus suis

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

enzyme: UniProt A4VVI4


enzyme_display_name: UniProt P24215

organism: Escherichia coli

enzyme: UniProt P24215


enzyme_display_name: dihydroneopterin aldolase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 7,8-dihydroneopterin in the aldolase reaction

proof_lines: kcat is 0.0054 sec(-1) for the aldolase reaction with 7,8-dihydroneopterin as substrate. kcat is 0.006 sec(-1) for the aldolase reaction with 7,8-dihydromonapterin as substrate. kcat is 0.0015 sec(-1) for the epimerization of 7,8-dihydroneo

enzyme: dihydroneopterin aldolase


organism: Pneumocystis carinii

substrate_name: Unknown


substrate_name: 7,8-dihydroneopterin in aldolase reaction


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

substrate: 7,8-dihydroneopterin in aldolase reaction


enzyme_display_name: altronate dehydratase

organism: Paracidovorax avenae

substrate_name: D-idonate

enzyme: altronate dehydratase

substrate: D-idonate


substrate_name: L-fuconate

substrate: L-fuconate


substrate_name: L-xylonate

substrate: L-xylonate


organism: Mycobacterium tuberculosis


enzyme_display_name: galactonate dehydratase

organism: Aspergillus terreus

enzyme: galactonate dehydratase


organism: Methanocaldococcus jannaschii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q61A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y78F with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H35N to reconstruct the assayed variant sequence.


proof_lines:
wild type enzyme, at pH 7.6 and 25°C
wild type enzyme, at pH 7.6 and 70°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y111F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E25Q with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: Km above 0.25 mM, mutant enzyme E25Q, at pH 7.6 and 70°C

proof_lines: Km below 2.7 1/sec*mM, mutant enzyme E25Q, at pH 7.6 and 70°C


organism: Rhizobium leguminosarum bv. trifolii (strain WSM2304)

substrate_name: L-arabinonate

proof_lines: kcat is 728 min(-1) with L-arabinonate as substrate. kcat is 1377 min(-1) with D-galactonate as substrate. kcat is 2949 min(-1) with D-fuconate as substrate. kcat is 349 min(-1) with D-xylonate as substrate. kcat is 431 min(-1) with D-gluco

substrate: L-arabinonate


substrate_name: D-fuconate

substrate: D-fuconate


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate: Unknown


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

proof_lines: kcat is 10.4 sec(-1) for gluconate and 1.08 sec(-1) for galactonate (at 70 degrees Celsius and pH 6). kcat is 12.6 sec(-1) for gluconate (at 78 degrees Celsius and pH 7).


organism: Caulobacter sp. (strain K31)


organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)


enzyme_display_name: dihydroxy-acid dehydratase

proof_lines: kcat is 112 min(-1) with (2R)-2,3-dihydroxy-3-methylbutanoate as substrate.

enzyme: dihydroxy-acid dehydratase


organism: Salmonella gallinarum (strain 287/91 / NCTC 13346)


organism: Sphingomonas sp. (strain SKA58)


organism: Streptomyces sp. (strain SPB78)


organism: Xanthomonas oryzae pv. oryzicola (strain BLS256)


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


organism: Escherichia coli (strain K12)

substrate_name: racemic 2,3-dihydroxy-3-methylbutanoate

proof_lines: Since only one of the isomers present in the racemic substrate is active, the corrected Km would be 0.75 mM.

substrate: racemic 2,3-dihydroxy-3-methylbutanoate


organism: Cellvibrio japonicus (strain Ueda107)


organism: Chromohalobacter israelensis (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)

proof_lines: kcat is 0.02 sec(-1) with D-mannonate. kcat is 0.04 sec(-1) with D-gluconate.


organism: Enterobacter sp. (strain 638)


organism: Escherichia albertii (strain TW07627)


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


organism: Escherichia coli (strain MS 21-1)


organism: Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)

proof_lines: kcat is 0.03 sec(-1) with D-mannonate. kcat is 0.05 sec(-1) with D-gluconate.


organism: Marinomonas sp. (strain MWYL1)


organism: Musicola paradisiaca (strain Ech703)

proof_lines: kcat is 0.04 sec(-1) with D-mannonate. kcat is 0.03 sec(-1) with D-gluconate.


organism: Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 / F199)


organism: Pectobacterium carotovorum subsp. carotovorum (strain PC1)


organism: Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1)


organism: Synechocystis sp. PCC 6803


organism: Pneumocystis carinii

assay_conditions_summary: pH 8.2; buffer 50 mM Tris

column_label: Abstract states the Km value for 6-hydroxymethyl-7,8-dihydropterin was 3.6 microM in 50 mM Tris buffer, pH 8.2.

raw_value_unit_evidence: Km raw_value=3.6 raw_unit=microM

row_label: Pneumocystis carinii recombinant PPPK with 6-hydroxymethyl-7,8-dihydropterin

table_label: PubMed abstract PMID 7950384


enzyme_display_name: Cyanide hydratase

organism: Aspergillus niger

substrate_name: cyanide

enzyme: Cyanide hydratase

substrate: cyanide


substrate_name: fumaronitrile

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

substrate: fumaronitrile


organism: Fusarium solani


organism: Haemophilus influenzae


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: galactonate (at 60 degrees Celsius and pH 6.2)

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


substrate_name: gluconate (at 60 degrees Celsius and pH 6.2)


organism: Streptococcus suis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H311A to reconstruct the assayed variant sequence.


organism: Pseudomonas sp.

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


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

substrate_name: 7,8-dihydroneopterin (at 25 degrees Celsius)

proof_lines: kcat is 0.07 sec(-1) at 25 degrees Celsius. kcat is 1.0 sec(-1) at 70 degrees Celsius.


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

substrate_name: L-threonate

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

column_label: PMC3445565 results prose reports recombinant AfIlv3A had a Km for threonate of 10.1 mM.

raw_value_unit_evidence: Results prose reports AfIlv3A had Km raw_value=10.1 raw_unit=mM for threonate.

row_label: Recombinant A. fumigatus AfIlv3A/IlvC assayed with L-threonate

table_label: PMC3445565 results prose and Figure 5B

substrate: L-threonate


substrate_name: D-galactonate

assay_conditions_summary: pH 7

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


organism: Methanococcus aeolicus


organism: Mycobacterium butyricum


enzyme_display_name: D-fuconate dehydratase

enzyme: D-fuconate dehydratase


substrate_name: L-arabonate

substrate: L-arabonate


enzyme_display_name: trans-L-3-hydroxyproline dehydratase

organism: Rattus norvegicus

enzyme: trans-L-3-hydroxyproline dehydratase


enzyme_display_name: UniProt Q67A25

organism: Thalictrum flavum

enzyme: UniProt Q67A25


organism: Yarrowia lipolytica (strain CLIB 122 / E 150)


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

substrate_name: galactonate (at 70 degrees Celsius and pH 6)


organism: Arabidopsis thaliana

proof_lines: kcat is 1.2 sec(-1) with (2R)-2,3-dihydroxy-3-methylbutanoate as substrate.


organism: Escherichia coli (strain K12)


organism: Escherichia coli

assay_conditions_summary: pH 8.3; buffer Tris-HCl / EDTA / DTT

proof_lines: mutant enzyme E21A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)


proof_lines: mutant enzyme K98A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)


proof_lines: mutant enzyme E73A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)


proof_lines: wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)


proof_lines:
E. coli D-sialic acid aldolase
L-KDO
directed evolution


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N4G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N4C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N4A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N4E to reconstruct the assayed variant sequence.


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


column_label: Table 1: Kinetics parameters of wild-type and evolved sialic acid aldolase (PNAS 2005, 102(26):9122-9126); enzyme row 'Wild type', substrate row 'D-KDO'; column 'Km, mM' = 13.8 (1.1); column 'kcat, s^-1' = 1.2 (0.15); column 'kcat/Km, mM^-1 s^-1' = 0.087

normalized_value_unit_evidence: Km: printed cell 13.8 mM is already the canonical unit, so no unit conversion applies and the value is 13.8 mM. kcat: printed cell 1.2 s^-1 is already the canonical unit, so no unit conversion applies and the value is 1.2 s^(-1). kcat/Km: printed cell 0.087 mM^-1 s^-1 is the canonical ratio unit written in the other order, so no unit conversion applies and the value is 0.087 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'Wild type', substrate row 'D-KDO': printed Km cell 13.8 (1.1) in the column head 'Km, mM'; printed kcat cell 1.2 (0.15) in the column head 'kcat, s^-1'; printed kcat/Km cell 0.087 in the column head 'kcat/Km, mM^-1 s^-1'. The parenthetical figures are the printed standard errors of the curve fitting.


column_label: Table 1: Kinetics parameters of wild-type and evolved sialic acid aldolase (PNAS 2005, 102(26):9122-9126); enzyme row 'Wild type', substrate row 'L-KDO'; column 'Km, mM' = 7.5 (1.2); column 'kcat, s^-1' = 1.1 (0.2); column 'kcat/Km, mM^-1 s^-1' = 0.15 ; column '[kcat/Km (L-KDO)]/[kcat/Km (D-sialic acid)]' = 0.036

normalized_value_unit_evidence: Km: printed cell 7.5 mM is already the canonical unit, so no unit conversion applies and the value is 7.5 mM. kcat: printed cell 1.1 s^-1 is already the canonical unit, so no unit conversion applies and the value is 1.1 s^(-1). kcat/Km: printed cell 0.15 mM^-1 s^-1 is the canonical ratio unit written in the other order, so no unit conversion applies and the value is 0.15 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'Wild type', substrate row 'L-KDO': printed Km cell 7.5 (1.2) in the column head 'Km, mM'; printed kcat cell 1.1 (0.2) in the column head 'kcat, s^-1'; printed kcat/Km cell 0.15 in the column head 'kcat/Km, mM^-1 s^-1'. The parenthetical figures are the printed standard errors of the curve fitting.


substrate_name: D-mannonate


organism: Saccharolobus solfataricus

substrate_name: D-gluconate

proof_lines: mutant enzyme I161M/Y145S/G205K, at pH 7.5 and 70°C

substrate: D-gluconate


substrate_name: D-glycerate

substrate: D-glycerate


proof_lines: mutant enzyme I161M/Y145S, at pH 7.5 and 70°C


organism: Spinacia oleracea


enzyme_display_name: nitrile hydratase

organism: Rhodococcus rhodochrous

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y68T to reconstruct the assayed variant sequence.

smiles: N#CCCCCC(=N)O

enzyme: nitrile hydratase


substrate_name: cyanoacetamide

smiles: N#CCC(=N)O

substrate: cyanoacetamide


organism: Staphylococcus aureus

proof_lines: mutant enzyme K100A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)


proof_lines: mutant enzyme K100Q, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)


proof_lines: mutant enzyme E22A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)


organism: Campylobacter jejuni

proof_lines: initially purified enzyme, at pH 8.5 and 37°C


substrate_name: Unknown


proof_lines: pH 7, 50°C, enzyme activated by 2-mercaptoethanol


organism: Neurospora crassa

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


substrate_name: Threonate

substrate: Threonate


substrate_name: D-erythronate

substrate: D-erythronate


organism: Klebsiella pneumoniae

substrate: D-galactonate


substrate_name: D-fuconate


proof_lines:
mitochondrial enzyme
supernatant enzyme


proof_lines:
supernatant enzyme
mitochondrial enzyme


organism: Streptococcus suis

substrate: D-mannonate


proof_lines:
wild type enzyme, at pH 7.5 and 37°C
wild type enzyme, at pH 7.5


substrate_name: D-altronate

substrate: D-altronate


proof_lines: cleavage epimerization


proof_lines: pH 8.0, Tris buffer, since only one of the isomers present in the racemic substrate is active, the corrected Km would be 0.75 mM


enzyme_display_name: UniProt Q4K977

organism: Pseudomonas fluorescens

substrate_name: 2-naphthyl isocyanide

enzyme: UniProt Q4K977

substrate: 2-naphthyl isocyanide